Released this past November, the list is based on data collected from the Web of Science and highlights some of the world’s most influential scientific minds by naming the researchers whose publications over the previous decade have included a high number of Highly Cited Papers placing them among the top 1% most-cited.
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We wish to congratulate all of the researchers named and especially our authors on this amazing accomplishment! We are happy and proud to share in their success!
IntechOpen is proud to announce that 191 of our authors have made the Clarivate™ Highly Cited Researchers List for 2020, ranking them among the top 1% most-cited.
\n\n
Throughout the years, the list has named a total of 261 IntechOpen authors as Highly Cited. Of those researchers, 69 have been featured on the list multiple times.
\n\n\n\n
Released this past November, the list is based on data collected from the Web of Science and highlights some of the world’s most influential scientific minds by naming the researchers whose publications over the previous decade have included a high number of Highly Cited Papers placing them among the top 1% most-cited.
\n\n
We wish to congratulate all of the researchers named and especially our authors on this amazing accomplishment! We are happy and proud to share in their success!
Note: Edited in March 2021
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1. Introduction
There are over 3700 extant snake species, but only approximately 200 in 600 venomous snake species, belonging to families Viperidae, Elapidae, Atractaspididae, and some of Colubridae, are considered medically important on public health aspects of snakebite [https://www.who.int/snakebites/disease/en/; http://www.reptile-database.org/, Accessed: 2019-11-22]. The World Health Organization (WHO) has recognized snakebite envenomation as a neglected tropical disease and has characterized a subset of venomous snake species as being of higher medical importance in the four geographical areas of the world snakebite is most frequent. The definition of highest medical importance to human public health (category 1) is “highly venomous snakes which are common or widespread and cause numerous snakebites, resulting in high levels of morbidity, disability, or mortality” [1]. These species are predominately from Elapidae and Viperidae families, but the majority of these species are from the family Viperidae (vipers and pit vipers). Viperidae species consist of approximately 50–100% of listed species in each geographical area and make up just over 60% of the entire list (Table 1).
Venomous snakes of highest medical importance (category 1); The table was modified classified sub-area in each of four broad geographical regions in tables 3-6 of Fifty-ninth report/WHO Expert Committee.
Venom variation results in pharmacological and clinical symptomology differences across venomous snake species, primarily varying in the extent of snakebite tissue damage and toxicity. In recent years, venom has been investigated using comprehensive venomics approaches, combining proteomics, transcriptomics, and genomics, in an attempt to better understand venom components responsible for variation. Next-generation sequencing (NGS) has greatly accelerated the pace of venomics, making high-throughput outputs possible; several venom gland transcriptomes can be sequenced together using multiplexed barcoded libraries, with little difference in cost, and third-generation longer read technologies, such as Oxford Nanopore (minION), are now available to correct transcriptome assembly errors [2]. Venom characterization that integrates both transcriptomics with proteomics has optimized proteomics by providing a species-specific database (venom gland transcriptome) for toxin identification, an ideal method to better distinguish unique toxins present in each species [3]. Current venom gland transcriptomes, completed using NGS technologies (Illumina and Roche) and E. coli, generated cDNA clone libraries, and assembled genomes of venomous snakes categorized as of highest medical importance are listed in Table 2. In our investigation, completed transcriptomes in snake species in category 1 are only about 20% despite the advance in increasing sequencing data. Additionally, on the completed snake genome, sequences are also less than 10% limited number.
Venom gland transcriptomes and currently completed snake genomes of species in category 1.
Transcriptome and proteome analyses of Viperidae species have consistently found that snake venom metalloproteinases (SVMPs), phospholipases A2 (PLA2s), serine proteinases, and L-amino acid oxidases are the most abundant toxins in these venoms [39]. These toxins are all enzymatic, providing immobilization and digestive roles in prey capture. Snakebites from these species result in local tissue damage, hemorrhage, and impaired coagulation symptoms in humans, which can lead to disability and mortality [40].
To date, the only effective snakebite treatment is intravenous administration of antibodies (often called antivenom), which come from animals immunized with toxins. However, using heterologous antibodies generated from numerous venom components has inherent weaknesses, such as an increased likelihood of an allergic reaction or life-threatening anaphylactic shock. Further, antivenom does not abolish local tissue damage, as it is intravenous and is usually not administered quickly enough. Thus, there is the issue of incomplete neutralization because of geographic venom variation, and high manufacturing costs and regulations have resulted in a struggle to properly match antivenom to venomous snakes of each locality and maintain antivenom stock [40]. To alleviate these issues, specific toxin inhibitors are actively being characterized and evaluated that neutralize snake venom toxicity and would work as an alternative antivenom snakebite therapy [41, 42, 43]. The challenge still remains to investigate the safety and efficiency of these toxin inhibitors to treat snakebite envenoming in humans.
Venomous snakes have endogenous inhibitors circulating in their plasma that provide resistance to their own venoms. These inhibitors can suppress the activity of enzymatic venom components, such as SVMPs, with high specificity. SVMPs are key venom components in viper venoms that contribute to hemorrhage and tissue damage; therefore, targeting these enzymes would greatly reduce human morbidity and mortality from snakebite. In this review, an overview of SVMPs is provided, with a focus on structure-function relationships within the various classes of SVMPS across snake families, and is followed by insights into how snake endogenous inhibitors function to abolish SVMP activity. The goal of our group is to design peptide inhibitors that bind to hemorrhagic SVMPs with high affinity and effectively neutralize these toxins. This chapter deeply understands the target SVMP behaviors on the snakebite issue and is a summary of our current work with historical studies in endogenous inhibitor of venomous snake.
2. Metalloproteinases
Metalloproteinases (MPs) are one of the most functionally diverse proteases in more than 50 families characterized in the MEROP database [44]. MPs play a significant role in organism homeostasis, and are involved in, cell invasion, cell fertilization, self-defense, and reproduction. Metalloproteinases are classified into two subgroups known by their enzyme commission numbers (ECNs), exopeptidases (ECN 3.4.17), and endopeptidases (ECN 3.4.24). The second group are enzymes from the metzincin family and include serralysins, astacins, adamalysins (a disintegrin and metalloproteinase domain; ADAMs), and matrix metalloproteinases (MMPs). There have been many studies documenting endogenous metalloproteinase dysregulation in cancer cells [45], especially mammalian ADAMs. ADAM proteins and SVMPs belonged to the same M12 family [46], and similar domain features are present for both. For SVMPs, three-dimensional structures and well-characterized effects on animal models in vivo have been published. Thus, the functional and structural insights provided by SVMPs have been useful for human ADAM inferences.
2.1 Structural classification of snake venom metalloproteinases (SVMPs)
All SVMP genes exhibit a conserved signal peptide region and a pro-(pre) domain. The number of domains following these conserved N-terminal regions varies, and the arrangements of the domains have resulted in the categorization of SVMPs into three main classes. SVMPs of the P-III class consist of the metalloproteinase domain (MD), disintegrin-like domain (DID), and cysteine-rich domain (CRD). P-IIs have a MD and DID, and P-I has only a MD. Further, each class has subclasses classified for different representation forms (P-Ia, P-IIa-e, P-IIIa-d). These subclasses include dimeric or truncate isoforms that have only been observed within the venom and are generated mainly by post-translational modifications.
There have been many observations of gene neofunctionalization generating large families of venom proteins with multiple functionalities, and the SVMP gene family is an example of this. SVMPs originated from the gene duplication of an ancestral ADAM gene. The ADAM 28 precursor gene is the closed SVMP homolog present in nonvenomous snakes and is also present in mammalian species [47, 48]. Sequence comparisons between the lizard (Anolis carolinensis) ADAM 28 gene and viper (Echis ocellatus) SVMP gene suggested that SVMPs originated from a nonsense mutation following ADAM gene duplication. This nucleotide substitution resulted in a chain-termination codon (STOP codon) at the end of exon 12, following the CRD. The modified gene precursor produced proteins that were devoid of the C-terminal membrane anchor and cytoplasmic region present in ADAMs [49]. As more snake genome sequences have become available, it has been hypothesized that the ancestral SVMP coded for the P-III class of SVMPs. Gene duplications of P-III SVMPs resulted in P-II and P-I SVMP genes, each generated by domain loss from splicing site mutations. These last two classes, P-II and P-I, are only found in Viperidae. The reason why a large number of different SVMPs are expressed in viper venoms is still unclear, even though some of these SVMPs are not primary lethal toxins.
SVMPs constitute more than 30% of the total venom proteins present in many Viperidae species. While these proteins are less abundant in the venoms of Elapidae, Atractaspididae, and Colubridae, they appear to be ubiquitously occurring [50, 51]. These observations suggest that P-III SVMP in Elapidae, Atractaspididae, and Colubridae venoms may have a conserve ancestral function and serve a common biological role in snake envenomation. Therefore, the functional roles of the diversified SVMPs are important for the clinical symptomology associated with Viperidae envenoming in humans. Domain structure, at least the topological shape, and sequence, especially the catalytic motif on the MD, are very similar among SVMPs, but SVMP activities vary, including their target substrates. Elucidating the structure-function relationships within this protein superfamily has applications for both protein evolution and snakebite treatment.
2.2 SVMP structure-function relationships and mechanism of action
Viperid snakebites are characterized by severe hemorrhagic, microvessel damage and inflammation, both local and systemic [52]. There is strong evidence from in vivo and in vitro studies of isolated SVMPs that these proteins are responsible for snakebite hemorrhage. Mitigating hemorrhage is critical in snakebite treatment; therefore studying the SVMP molecular mechanism of inducing hemorrhage is of critical importance. Hemorrhage results from SVMP proteolysis, targeted cleavage of extracellular matrix components, transmembrane receptors, and fibrinogen, mostly around microvessels. Interestingly, despite sharing similar catalytic activity, not all SVMPs induce hemorrhage in vivo. SVMP effects also include blood coagulation irregularities, platelet aggregation, cell infiltration, apoptosis-induced activity, and alternations in vascular permeability, even if these SVMPs do not show hemorrhagic activity [52]. These additional functionalities and targets likely result from C-terminal P-III SVMP binding, not only the catalytic activity of the N-terminally located MP domain [53]. To design inhibitors to neutralized hemorrhagic effects of SVMPs, we must first understand SVMP targets, as well as the tissue distribution and localization of SVMPs upon envenomation.
Both of P-III and P-I SVMPs have hemorrhagic activities, but P-III SVMPs tend to show greater hemorrhagic activity than P-I SVMPs [54, 55]. It has been proposed that the occurrence of hemorrhage results from the degradation of the vascular basement membrane of capillaries. Immunofluorescence confocal microscopy, immunochemical and proteomic analyses of tissue, and exudate in vivo have revealed a distinct pattern of P-I and P-III SVMP distribution in tissue. Observations from SVMPs labeled with Alexa Fluor 647 have found that P-III SVMP co-localized with capillary collagen IV, especially in those of microvesicles. P-I SVMPs applied to whole tissues appear to function primarily in the degradation of basement membrane components [56]. Hemorrhagic P-I and P-III SVMPs show a preference for type IV collagen in targeted degradation. J.M. Gutiérrez et al. provided a two-step hypothesis for SVMP mechanism of hemorrhage [56]. First, SVMPs hydrolyze type IV collagen and perlecan at the basement membrane components of capillaries and surrounding endothelial cells, resulting in a weakening of the mechanical stability of the basement membrane and microvessel wall. The second step occurs when the biophysical hemodynamic forces operating in microcirculation induce a distention in the wall, causing capillaries to disrupt, followed by consequent extravasation.
SVMP hemorrhage disrupts capillary networks, facilitating toxin dispersion. In 2016, reviews by Sanhajariya and colleagues investigated snake venom pharmacokinetics using an ELISA time course, varying venom concentrations mixed with the plasma of laboratory animals (rat, rabbit, and sheep) and humans [57]. In laboratory animals, two phases were observed in the metabolism of snake venom by intravenous injection of the venoms or toxins: the first phase consisting of rapid distribution with half-lives of 5–48 min and a second a slow elimination phase with half-lives of 0.8–28 h. Half-lives of the second phase did not show a significant difference among the species (Bothrops alternatus, Vipera aspis, and Naja sp.) explored under intravenous injection, but Naja sp. did show a twofold shorter phase time than Vipera aspis 32 hours after intermuscular injection. For humans, venom concentrations in plasma were examined from 24 pharmacokinetic studies in humans that used similar ELISA criteria. Venom concentrations of the patients bitten by vipers were typically higher than those of by elapids. Eventually, total 218 timed concentration data of 145 patients bitten by snakes of Viperidae and Elapid were used for the computational analysis within a nonlinear mixed-effects modeling framework with NONMEM. The result provided an estimated venom elimination half-life of 9.71 ± 1.29 h. Interestingly, these data also show that there is no big difference between Viperid and Elapid. It is very important to understand the certain pharmacokinetic of venom for post-treatment of inhibitor to neutralize toxicity of venoms.
3. Toxin resistance in venomous snakes
Given the toxic and proteolytic nature of venom, it is of the utmost importance that venomous snakes are protected against the activity of their own venom. This is an interesting area of research because venoms, especially viper venoms, have high concentrations of proteases that must be stored in an inactive state in the venom gland to prevent degradation of both the snake’s own tissue and other proteins present in the venom. These proteases must then be readily activated when delivered into prey, requiring a finely tuned on/off switch. Here, we briefly summarize how these toxins are regulated in snake venom glands, with a focus on endogenous inhibitors, especially SVMP inhibitors, as SVMPs are one of the major venom compounds in Viperid snake venoms.
3.1 Mechanisms of toxin resistance
Three toxin resistance mechanisms have been proposed for venomous snakes: (1) target receptor mutations, (2) venom gland physiological conditions, and (3) inhibitors present in the venom gland or blood circulation. For the first mechanism, limited mutations on target receptors in snakes prevent the binding of their own toxins [58, 59, 60]. An example of this has been described by Takacs et al., where resistance against conspecific α-neurotoxins, major lethal components of Elapidae venoms, has been shown to be mediated by a unique N-glycosylation of the nicotinic acetylcholine receptor ligand binding domain of Elapidae snakes [58]. This observation has only been made for a few Elapidae species, but there is currently a limited amount of research in this area. The second mechanism involves the physiological conditions within the venom gland and those required for enzymatic toxins to be active. A high concentration of citrate is present in venom, and this results in a low pH environment. It is estimated that 25% of dried crude venom (30–150 mM) from Crotalus sp., Agkistrodon sp., Bothrops sp. Dendroaspis sp., Sistrurus miliarius barbouri, Bitis gabonica gabonica, Vipera russellii russellii, and Lachesis muta is citrate. Citrate concentrations of 18 or 27 mM exogenously added to whole venom have been shown to inhibit protease activity in vitro [61]. Secreted whole venom of Crotalus sp. has been observed to be acidic (pH 5.25–5.75), suggestive of an acidic storage condition for venom enzymes, which then when delivered into prey or human tissue at a pH of 7.2–7.4, these enzymes become activated [62]. In addition to the acidic storage conditions of the venom gland, four tripeptide inhibitors of venom metalloproteinases, pEKW, pENW, pEQW, and pERW, have been documented in the venoms of Protobothrops mucrosquamatus [63, 64], Bothrops asper [65], Echis ocellatus, Cerastes cerastes cerastes [66], and some rattlesnakes [67] and are likely present in the venom gland lumen. These inhibitors have been found in relatively large amounts (approximate concentrations in P. mucrosquamatus venom were reported greater than 5.0 mM), but their inhibitory activity is not strong, with IC50 values between 0.15 and 0.95 mM for different SVMPs in vitro [63, 67]. The X-ray crystal structure of a SVMP complexed with a pExW inhibitor revealed the indole ring of Trp in the pExW inhibitor stacked against the imidazole in the first histidine residue of the SVMP Zn2+ binding site [64]. In 2007, Philippe and colleagues discovered the 2–3 kDa polyHis-polyGly peptides in venom of Atheris squamigera by mass spectrometry-based strategies, and it was identified as a new class of peptides with clusters of histidine and glycine residues [68]. Similar peptides were found coded in C-type natriuretic peptide (CNP) and bradykinin-potentiating peptide (BPP)–CNP transcript precursors and were isolated from E. ocellatus and Atheris sp. venoms. Interestingly, these pHpGs have shown stronger inhibitory effect against SVMP in vivo than tripeptides [66].
In addition to inhibitors present in the venom and venom gland, serum proteins in some venomous snakes have also been found to bind toxins with high affinity and neutralize toxin pathophysiological effects [69]. These serum proteins and those found in the venom/venom gland are referred to as “endogenous inhibitors,” but kinds of their inhibitor are different. Serum inhibitors circulate in the blood to effectively bind and neutralize host toxins, but they are different than immune antibodies. The roles of these endogenous inhibitors and their classifications will be discussed in the next sections.
3.2 Endogenous inhibitor protein families
There are three main endogenous inhibitor classes; these are phospholipase A2 inhibitors (PLI) [70, 71], anti-hemorrhagic factors [72], and small serum proteins [73, 74, 75, 76], which have predominately been found in the blood of vipers. All endogenous inhibitors are stable at high temperatures and in acidic conditions and have been purified by reverse-phase high-performance liquid chromatography (RP-HPLC).
3.2.1 Phospholipase A2 inhibitors (PLIs)
Snake venom PLA2s are ubiquitous to Viperidae and Elapidae venoms and one of the primary components in viper venoms. These toxins are versatile and can induced a variety of effects, including neurotoxicity, myotoxicity, cardiotoxicity, hemolysis, and anticoagulation [77]. Inhibitors of PLA2s, PLIs, have been identified and characterized from the blood sera of both venomous and nonvenomous snakes. PLI genes have been found uniquely expressed in snake liver tissues [78]. This suggests that the secretion of PLIs into blood circulation could be to provide protection against accidental self-envenomation in venomous snakes.
PLIs are divided into three groups (PLIα, PLIβ, and PLIγ) based on structural characteristics. PLIαs are glycoproteins with molecular masses ranging from 75 to 120 kDa and more than three non-covalently associated subunits. Their structural features demonstrate sequence homology to the carbohydrate-recognition domain of Ca2+-dependent lectins (C-type lectin-like domain), but they lack the carbohydrate-binding ability. A highly conserved region (residues 49–143) shares 80–90% sequence identity between PLIαs and appears to be responsible for PLA2 binding [79]. PLIβs are 150–160 kDa glycoproteins composed of three non-covalently bonded subunits and have nine tandem leucine-rich repeats. A homology analysis by BLAST shows similarity to human leucine-rich α2-glycoproteins, which structurally forms horseshoe-shaped molecules, as observed in Toll-like receptors [80]. PLIβs have been purified and characterized from only one venomous snake, Gloydius brevicaudus [81], whereas there are a couple examples of these proteins that have been found in nonvenomous colubrids (Elaphe quadrivirgata and Elaphe climacophora) [82, 83]. The presence of a PLIβ gene in Lachesis muta was discovered by Lima et al., but the exact function of this inhibitor has not been identified [84]. PLIβs from G. brevicaudus specifically inhibited only group-II basic PLA2s, forming stable toxin-inhibitor complexes at a 1:1 molar ratio [80]. PLIγs are acidic glycoproteins consisting of oligomers with 20–30 kDa subunits, the primary structure of which consists of conserved patterns of cysteine residues to form two units of repeats known as three-finger motifs. Structurally related proteins belong to the urokinase activating plasminogen receptor (u-PAR)/ly-6 superfamily [85]. This gamma class inhibitor comprises the greatest number of endogenous PLIs and has been isolated from the sera of many snake species, including those from Elapidae, Viperidae, Hydrophidae, Boidae, and Colubridae families [70].
Numerous studies have described highly effective inhibition of PLA2 toxicity in vitro and in vivo by PLIs purified as a highly soluble protein from snake serum. However, binding sites, as well as inhibitory mechanism, have not been fully elucidated for these proteins because each PLIs’ group targets different PLA2s. Currently, there are two review articles that have attempted to determine the PLA2 targets of PLI classes based on structural predictions [70, 71]. In 2015, Zhen and colleagues successfully established recombinant expression of PLIγ in Escherichia coli. After expression optimization, the amount of recombinant PLIγ achieved was 23 mg/l of culture, and the recombinant PLIγ demonstrated inhibitory activity against Deinagkistrodon acutus venom purified PLA2s, and D. acutus, Naja atra, and Agkistrodon halys crude venoms in vitro and in vivo. This type of experimental work will make it possible in the future to determine the inhibitory mechanism by inhibitor mutant analysis and/or obtaining the three-dimensional structure of the inhibitor and PLA2 complexes.
3.2.2 Anti-hemorrhagic factors
As previously detailed, hemorrhage, one of the main symptoms of viper envenomation, is induced by snake venom metalloproteinases (SVMPs). The first anti-hemorrhagic factor, habu serum factor (HSF), was identified from the serum of Protobothrops flavoviridis by Omori-Satoh et al. in 1972 [86]; in 1992, the complete amino acid sequence was determined for this protein [87]. To date, anti-hemorrhagic factors habu serum factor (HSF), BJ46a [88], and mamushi serum factor (MSF) [89] have been purified and characterized from the venomous snakes P. flavoviridis (habu), Bothrops jararaca, and Gloydius blomhoffii, respectively (Table 3). These anti-hemorrhagic factors belong to the fetuin family, part of the cystatin superfamily, consisting of two cystatin-like domains and a His-rich domain. These anti-hemorrhagic factors show high sequence identity and are all single-chain, acidic glycoproteins. They also all demonstrate strong anti-hemorrhagic activity in vivo against the crude venom of the snake species they are isolated from. HSF and MSF showed relatively broad range inhibitory activity against both nonhemorrhagic and hemorrhagic SVMPs, as well as both P-I and P-III SVMP classes, but preferentially inhibited P-III SVMPs. These observations were also exhibited in the differences in the degree and specificity of inhibition against individual SVMP [89, 90]. HSF strongly inhibited the proteolytic and hemorrhagic activities in vivo and in vitro of HR1 and HR2 (P-III SVMPs), the main toxins in P. flavoviridis venom. Similarly, BJ46a is a potent inhibitor of atrolysin C (P-I SVMP) and jararhagin (P-III SVMP) proteolytic activities and the overall hemorrhagic activity of B. jararaca venom [88]. HSF and MSF did appear to be specific to SVMPs and were found to not inhibit cysteine proteases, such as papain and cathepsin B, serine proteases trypsin and chymotrypsin, or thermolysin, a bacterial MP. Binding studies of these factors suggest that they are forming noncovalent complexes with the MD of SVMPs; this has been hypothesized because they interacted with P-I SVMPs, but did not bind to the C-terminal region of SVMP jararhagin-C. Interestingly, the molar ratios for complex formation vary between inhibitors; for HSF and brevilysin H6 (P-III SVMP), a 1:1 ratio is required, but complex formation between BJ46a and jararhagin (or atrolysin C) was found in a 1:2 ratio. The N-terminal region of HSF (residues 5–89) has been found to be responsible for anti-hemorrhagic activity [91], and sequence comparisons between HSF and a HSF-like protein (HLP), which does not show SVMP inhibition, identified a substitution difference in the first cystatin-like domain [92]. These results suggested that N-terminal region of HSF is potentially responsible for SVMP binding.
sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) under reducing condition
N.D; not determined, XX; not named or not determined,
Recently, BaltMPI [93] was found as a hemorrhagic inhibitor in Bothrops alternatus serum. BaltMPI should also be of the fetuin family as the N-terminal region consists of 60 amino acid residues (determined by Edman degradation) that showed high homology (97%) with BJ46a. BaltMPI has potent anti-hemorrhagic activity and inhibited the proteolytic activity of Batroxase and BjussuMP-I but has yet to be investigated against the crude venom Bothrops alternatus, the snake species it originates from.
3.2.3 Small serum proteins (SSPs)
Since 2007, a new class of endogenous inhibitors, named small serum proteins (SSP-1 to SSP-5), has been characterized from Japanese vipers, P. flavoviridis (habu) and G. b. blomhoffii, that have been found to effectively neutralize various snake toxins [73, 75]. SSP-1, SSP-2, and SSP-5 consist of two domains of approximately 90 amino acid residues, while SSP-3 and SSP-4 have only a 60 residue N-terminal domain. All serum proteins have conserved cysteine residues and belong to the prostatic secretory protein of 94 amino acid (PSP94) family, despite only limited sequence identity to any mammalian PSP94 [94]. These inhibitors target different toxins; SSP-2 and SSP-5 have high affinity for CRISP family toxins [73, 95], while SSP-1, SSP-4, and SSP-3 inhibit distinct SVMPs. These results suggested SSP-1 to SSP-5 contributes to a snake’s natural resistance against toxins. SSP-1 and SSP-4 complex with HSF, inhibiting apoptosis induced by HV1, a P-III SVMP from P. flavoviridis venom [74]. Each SSP alone could bind to target SVMPs, but SSP-1 and SSP-4 inhibit HV1 through a ternary complex involving HSF, SSPs, and HV1 (SSP-4, data has not published). In contrast, SSP-3 alone inhibits flavorase, a P-III SVMP from P. flavoviridis [76], and is not dependent on other proteins. These results suggested that the inhibition mechanisms of the SSP group are different, but they are noncompetitive. Recently, the crystal structure of complex SSP-2 and triflin, an ion channel-blocking CRISP toxin, was determined [96]. The interface between these two proteins consists of the two short β-strands of SSP-2 binding to the concave region centrally located in the N-terminal domain of triflin. Interestingly, the key β-strand on the N-terminal of SSPs is a hypervariable region, which might correspond to the ability to bind and target different venom toxins. This is in agreement with the molecular evolution of SSP genes, where the number of non-synonymous nucleotide substitutions is significantly greater than those of synonymous substitutions in N-terminal regions. Additionally, these mutational hotspots are found on the molecular surface, specifically located on the toxin interaction interface, while the protein scaffold structure is highly conserved [97].
4. Undetermined proteinous inhibitors
Isolated proteins from the serum of Bothrops asper [98], Agkistrodon contortrix [99], Crotalus atrox [100], and Vipera palaestinae [101] have shown effective neutralization of hemorrhagic activity in vivo from crude venom corresponding to each species or species-specific toxins (Table 3). The SVMP inhibitor isolated from Protobothrops mucrosquamatus serum, named TMI, demonstrated a 1000-fold stronger in vitro inhibitory activity than endogenous tripeptides (IC50 = 0.2–1.0 μM) and additionally inhibited venom proteolytic activity from other species [102]. Despite in vivo and in vitro experimental evidence, the sequence of these inhibitors has not yet been determined. A novel group of endogenous inhibitors may be responsible for this activity, as the molecule sizes of these proteins are different than what has been previously reported for other characterized inhibitors.
Venom resistant has been discovered in some species in mammals, birds, and reptiles, which are either predators or prey of venomous snakes. Natural inhibitors isolated from resistant animals are detailed in reviews by Domont et al. [69, 103] and Bastos et al. [72], which summarized toxin resistance corresponding to several snake species from the plasma, serum, and muscle of mammals. There are a few reports of natural inhibitors isolated from nonvenomous snakes, such as NtAH from Natrix tessellate [104] and a 59 kDa protein from Dinodon semicarinatus [105]. Recently, the whole serum of Drymarchon couperi [106] has also shown anti-hemorrhagic activity to venom, but the protein responsible for this activity has yet to be determined. These natural inhibitors in nonvenomous snakes are potentially protective for a diet that consists of venomous snakes, while resistance to SVMPs may be relatively widespread among snake species.
Endogenous inhibitor genes are expressed in the liver of venomous snakes, and these genes appear to be evolving by gene duplication and rapid diversification. This facilitates the neutralization of various toxins within venoms, which also are evolving under similar mechanism [97, 107]. Thus, a detailed characterization of inhibitors against species-specific toxins may help to decipher the evolution of endogenous natural resistance in venomous snakes. Unfortunately, the structural features that govern the inhibitor interaction are still unknown. Recently, there are reports that making a computational analysis predicted three-dimensional structure available [81], and one paper demonstrated that recombinantly expressed BJ46 was able to produce using the expression system of the methylotrophic yeast Pichia pastoris [108]. The ability to recombinantly produce these inhibitors will provide material for future work deciphering complex formations between inhibitors and toxins from mutation and structural analyses, providing insight into the molecular mechanisms behind toxin activity inhibition. With current technologies, it is not difficult to comprehensively evaluate venomous snake sera components or the sera from resistant animals. However, we have to be informed from structure-function studies to correlate amino acid sequence to the physiological activity of an inhibitor. It is possible that different inhibitors are operating under different mechanisms, even if they show high similarity, as has been the case for various venomous snake toxins. Thus, understanding in depth how toxin inhibitors function may aid in identifying novel inhibitors and new strategies for snakebite treatment.
5. Conclusions and remaining challenges
There are still many current challenges in the field of toxin inhibitors. Systemic effects of envenomation in humans by snakebite are often mitigated by antivenom therapy, the medically accepted treatment to date. Inhibitors have yet to gain acceptance in clinical use. However, local tissue damage is not neutralized by antivenom and results in permanent morbidity and disability in patients [109]. Local tissue damage is incurred by enzymatic toxins and thus is one of the reasons that Viperidae species occupy just over 60% of venomous snakes listed as Category 1 of highest importance to human health (Tables 1 and 2). Endogenous inhibitors isolated from almost all Viperidae show potent inhibition against their own venom and have also demonstrated to be selective toward highly lethal enzymes within these venoms. The serum inhibitor genes of venomous snakes might have evolved by gene duplication and rapid diversification to facilitate the neutralization of various venom toxins. These serum inhibitors are very stable (resistant to acidic, alkaline, and high temperature environments), selective in inhibitory activity against snake toxins, and are nontoxic, given they exist in blood serum and consist of amino acids (Table 3). However, the molecule mechanism of toxin neutralization involving endogenous inhibitors remains unclear due to a lack of three-dimensional structures detailing toxin and inhibitor complexes. By exploring molecular mechanisms responsible for natural toxin resistance in snakes, we may begin to understand the specificity and selectivity of endogenous inhibitors and use these insights in the design of better therapeutic agents for the treatment of snakebite victims.
Conflict of interest
The authors declare no conflict of interest.
\n',keywords:"venomous snake, snake venom metalloprotease, hemorrhagic, nonhemorrhagic, toxin resistance, natural inhibitor, endogenous inhibitor",chapterPDFUrl:"https://cdn.intechopen.com/pdfs/70678.pdf",chapterXML:"https://mts.intechopen.com/source/xml/70678.xml",downloadPdfUrl:"/chapter/pdf-download/70678",previewPdfUrl:"/chapter/pdf-preview/70678",totalDownloads:700,totalViews:0,totalCrossrefCites:0,dateSubmitted:"May 27th 2019",dateReviewed:"November 24th 2019",datePrePublished:"December 30th 2019",datePublished:"February 3rd 2021",dateFinished:"December 30th 2019",readingETA:"0",abstract:"Venomous snakebite is a major human health issue in many countries and has been categorized as a neglected tropical disease by the World Health Organization. Venomous snakes have evolved to produce venom, which is a complex mixture of toxic proteins and peptides, both enzymatic and nonenzymatic in nature. In this current era of high-throughput technologies, venomics projects, which include genome, transcriptome, and proteome analyses of various venomous species, have been conducted to characterize divergent venom phenotypes and the evolution of venom-related genes. Additionally, venomics can also inform about mechanisms of toxin production, storage, and delivery. Venomics can guide antivenom and therapeutic strategies against envenomations and identify new toxin-derived drugs/tools. One potentially promising drug development direction is the use of endogenous inhibitors present in snake venom glands and serum that could be useful for snakebite therapeutics. These inhibitors suppress the activity of venom proteases, enzymatic proteins responsible for the irreversible damage from snakebite. This book chapter will focus on insights from venomous snake adaptations, such as the evolution of venom proteases to generate diverse activities and snake natural resistance to inhibit activity, and how this information can inform and have applications in the treatment of venomous snakebite.",reviewType:"peer-reviewed",bibtexUrl:"/chapter/bibtex/70678",risUrl:"/chapter/ris/70678",signatures:"Narumi Aoki-Shioi and Cassandra M. Modahl",book:{id:"7847",type:"book",title:"Medical Toxicology",subtitle:null,fullTitle:"Medical Toxicology",slug:"medical-toxicology",publishedDate:"February 3rd 2021",bookSignature:"Pınar Erkekoglu and Tomohisa Ogawa",coverURL:"https://cdn.intechopen.com/books/images_new/7847.jpg",licenceType:"CC BY 3.0",editedByType:"Edited by",isbn:"978-1-83880-278-3",printIsbn:"978-1-83880-277-6",pdfIsbn:"978-1-83969-155-3",isAvailableForWebshopOrdering:!0,editors:[{id:"109978",title:"Prof.",name:"Pınar",middleName:null,surname:"Erkekoglu",slug:"pinar-erkekoglu",fullName:"Pınar Erkekoglu"}],productType:{id:"1",title:"Edited Volume",chapterContentType:"chapter",authoredCaption:"Edited by"}},authors:[{id:"306349",title:"Ph.D.",name:"Narumi",middleName:null,surname:"Aoki-Shioi",fullName:"Narumi Aoki-Shioi",slug:"narumi-aoki-shioi",email:"anarumi@fukuoka-u.ac.jp",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",institution:{name:"Fukuoka University",institutionURL:null,country:{name:"Japan"}}},{id:"311863",title:"Dr.",name:"Cassandra",middleName:null,surname:"M. Modahl",fullName:"Cassandra M. Modahl",slug:"cassandra-m.-modahl",email:"dbscmm@nus.edu.sg",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",institution:{name:"National University of Singapore",institutionURL:null,country:{name:"Singapore"}}}],sections:[{id:"sec_1",title:"1. Introduction",level:"1"},{id:"sec_2",title:"2. Metalloproteinases",level:"1"},{id:"sec_2_2",title:"2.1 Structural classification of snake venom metalloproteinases (SVMPs)",level:"2"},{id:"sec_3_2",title:"2.2 SVMP structure-function relationships and mechanism of action",level:"2"},{id:"sec_5",title:"3. Toxin resistance in venomous snakes",level:"1"},{id:"sec_5_2",title:"3.1 Mechanisms of toxin resistance",level:"2"},{id:"sec_6_2",title:"3.2 Endogenous inhibitor protein families",level:"2"},{id:"sec_6_3",title:"3.2.1 Phospholipase A2 inhibitors (PLIs)",level:"3"},{id:"sec_7_3",title:"Table 3.",level:"3"},{id:"sec_8_3",title:"3.2.3 Small serum proteins (SSPs)",level:"3"},{id:"sec_11",title:"4. Undetermined proteinous inhibitors",level:"1"},{id:"sec_12",title:"5. Conclusions and remaining challenges",level:"1"},{id:"sec_16",title:"Conflict of interest",level:"1"}],chapterReferences:[{id:"B1",body:'Fifty-ninth report/WHO Expert Committee on Biological Standardization. WHO Technical Report Series; No. 964. ISSN: 0512-3054, ISBN: 978 92 4 120964 6'},{id:"B2",body:'Hargreaves AD, Mulley JF. Assessing the utility of the Oxford Nanopore MinION for snake venom gland cDNA sequencing. PeerJ. 2015;3:e1441'},{id:"B3",body:'Calvete JJ. 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Primary structure of the Antihemorrhagic factor in serum of the Japanese Habu: A snake venom metalloproteinase inhibitor with a double-headed cystatin domain. The Journal of Biochemistry. 1992;112:583-589'},{id:"B88",body:'Valente RH, Dragulev B, Perales J, et al. BJ46a, a snake venom metalloproteinase inhibitor: Isolation, characterization, cloning and insights into its mechanism of action. European Journal of Biochemistry. 2001;268:3042-3052'},{id:"B89",body:'Aoki N, Tsutsumi K, Deshimaru M, et al. Properties and cDNA cloning of antihemorrhagic factors in sera of Chinese and Japanese mamushi (Gloydius blomhoffi). Toxicon. 2008;51:251-261'},{id:"B90",body:'Deshimaru M, Tanaka C, Fujino K, et al. Properties and cDNA cloning of an antihemorrhagic factor (HSF) purified from the serum of Trimeresurus flavoviridis. Toxicon. 2005;46:937-945'},{id:"B91",body:'Aoki N, Deshimaru M, Terada S. Active fragments of the antihemorrhagic protein HSF from serum of habu (Trimeresurus flavoviridis). Toxicon. 2007;49:653-662'},{id:"B92",body:'Aoki N, Deshimaru M, Kihara K, et al. Snake fetuin: Isolation and structural analysis of new fetuin family proteins from the sera of venomous snakes. Toxicon. 2009;54:481-490'},{id:"B93",body:'Palacio TZ, Santos-Filho NA, Rosa JC, et al. Isolation and characterization of a novel metalloprotease inhibitor from Bothrops alternatus snake serum. International Journal of Biological Macromolecules. 2017;98:436-446'},{id:"B94",body:'Aoki N, Matsuo H, Deshimaru M, et al. Accelerated evolution of small serum proteins (SSPs)—The PSP94 family proteins in a Japanese viper. Gene. 2008;426:7-14'},{id:"B95",body:'Aoki N, Sakiyama A, Kuroki K, et al. Serotriflin, a CRISP family protein with binding affinity for small serum protein-2 in snake serum. Biochimica et Biophysica Acta (BBA)—Proteins and Proteomics. 2008;1784:621-628'},{id:"B96",body:'Shioi N, Tadokoro T, Shioi S, et al. Crystal structure of the complex between venom toxin and serum inhibitor from Viperidae snake. The Journal of Biological Chemistry. 2019;294:1250-1256'},{id:"B97",body:'Tanaka Y, Oyama S, Hori S, et al. Accelerated evolution of Fetuin family proteins in Protobothrops flavoviridis (Habu Snake) serum and the discovery of an L1-like genomic element in the Intronic sequence of a Fetuin-encoding gene. Bioscience, Biotechnology, and Biochemistry. 2013;77:582-590'},{id:"B98",body:'Borkow G, Gutierrez JM, Ovadia M. Isolation, characterization and mode of neutralization of a potent antihemorrhagic factor from the serum of the snake Bothrops asper. Biochimica et Biophysica Acta (BBA)—General Subjects. 1995;1245:232-238'},{id:"B99",body:'Weinstein SA, Lafaye PJ, Smith LA. Observations on a venom neutralizing fraction isolated from serum of the northern copperhead. Agkistrodon contortrix mokasen. Copeia. 1991;1991:777'},{id:"B100",body:'Weissenberg S, Ovadia M, Kochva E. Inhibition of the proteolytic activity of hemorrhagin-e from Crotalus atrox venom by antihemorrhagins from homologous serum. Toxicon. 1992;30:591-597'},{id:"B101",body:'Ovadia M. Purification and characterization of an antihemorrhagic factor from the serum of the snake Vipera palaestinae. Toxicon. 1978;16:661-672'},{id:"B102",body:'Huang K-F, Chow L-P, Chiou S-H. Isolation and characterization of a novel proteinase inhibitor from the Snake serum of Taiwan Habu (Trimeresurus mucrosquamatus). Biochemical and Biophysical Research Communications. 1999;263:610-616'},{id:"B103",body:'Domont GB, Perales J, Moussatché H. Natural anti-snake venom proteins. Toxicon. 1991;29:1183-1194'},{id:"B104",body:'Borkow G, Gutierrez JM, Ovadia M. A potent antihemorrhagin in the serum of the non-poisonous water snake Natrix tessellata: Isolation, characterization and mechanism of neutralization. Biochimica et Biophysica Acta (BBA)—General Subjects. 1994;1201:482-490'},{id:"B105",body:'Goetz SM, Piccolomini S, Hoffman M, et al. Serum-based inhibition of pit viper venom by eastern indigo snakes (Drymarchon couperi). Biology Open. 2019;8:bio040964'},{id:"B106",body:'Tomihara Y, Yonaha K, Nozaki M, et al. Purification of an antihemorrhagic factor from the serum of the non-venomous snake Dinodon semicarinatus. Toxicon. 1988;26:420-423'},{id:"B107",body:'Chijiwa T, Inamaru K, Takeuchi A, et al. Unique structure (construction and configuration) and evolution of the array of small serum protein genes of Protobothrops flavoviridis snake. Bioscience Reports. 2019;39:BSR20190560'},{id:"B108",body:'Shi Y, Ji M-K, Xu J-W, et al. High-level expression, purification, characterization and structural prediction of a snake venom metalloproteinase inhibitor in Pichia pastoris. The Protein Journal. 2012;31:212-221'},{id:"B109",body:'Gutiérrez JM, Calvete JJ, Habib AG, et al. Snakebite envenoming. Nature Reviews. Disease Primers. 2017;3:17063'}],footnotes:[],contributors:[{corresp:"yes",contributorFullName:"Narumi Aoki-Shioi",address:"anarumi@fukuoka-u.ac.jp",affiliation:'
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Dr. Gaiceanu is a member of the National Council for Attesting Titles, Diplomas and Certificates, an expert of the Executive Agency for Higher Education, Research Funding, and a member of the Senate of the Dunarea de Jos University of Galati. He has been the head of the Integrated Energy Conversion Systems and Advanced Control of Complex Processes Research Center, Romania, since 2016. He has conducted several projects in power converter systems for electrical drives, power quality, PEM and SOFC fuel cell power converters for utilities, electric vehicles, and marine applications with the Department of Regulation and Control, SIEI S.pA. (2002–2004) and the Polytechnic University of Turin, Italy (2002–2004, 2006–2007). He is a member of the Institute of Electrical and Electronics Engineers (IEEE) and cofounder-member of the IEEE Power Electronics Romanian Chapter. He is a guest editor at Energies and an academic book editor for IntechOpen. 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He has been listed among the top 2% of scientists in the world for the last three consecutive years, 2019 to 2021 as per studies conducted by the Stanford University, USA.",institutionString:"Praxis Business School",institution:null},{id:"320071",title:"Dr.",name:"Sidra",middleName:null,surname:"Mehtab",slug:"sidra-mehtab",fullName:"Sidra Mehtab",position:null,profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0033Y00002v6KHoQAM/Profile_Picture_1584512086360",biography:"Sidra Mehtab has completed her BS with honors in Physics from Calcutta University, India in 2018. She has done MS in Data Science and Analytics from Maulana Abul Kalam Azad University of Technology (MAKAUT), Kolkata, India in 2020. Her research areas include Econometrics, Time Series Analysis, Machine Learning, Deep Learning, Artificial Intelligence, and Computer and Network Security with a particular focus on Cyber Security Analytics. Ms. Mehtab has published seven papers in international conferences and one of her papers has been accepted for publication in a reputable international journal. She has won the best paper awards in two prestigious international conferences – BAICONF 2019, and ICADCML 2021, organized in the Indian Institute of Management, Bangalore, India in December 2019, and SOA University, Bhubaneswar, India in January 2021. Besides, Ms. Mehtab has also published two book chapters in two books. Seven of her book chapters will be published in a volume shortly in 2021 by Cambridge Scholars’ Press, UK. Currently, she is working as the joint editor of two edited volumes on Time Series Analysis and Forecasting to be published in the first half of 2021 by an international house. Currently, she is working as a Data Scientist with an MNC in Delhi, India.",institutionString:"NSHM College of Management and Technology",institution:{name:"Association for Computing Machinery",country:{name:"United States of America"}}},{id:"226240",title:"Dr.",name:"Andri Irfan",middleName:null,surname:"Rifai",slug:"andri-irfan-rifai",fullName:"Andri Irfan Rifai",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/226240/images/7412_n.jpg",biography:"Andri IRFAN is a Senior Lecturer of Civil Engineering and Planning. He completed the PhD at the Universitas Indonesia & Universidade do Minho with Sandwich Program Scholarship from the Directorate General of Higher Education and LPDP scholarship. He has been teaching for more than 19 years and much active to applied his knowledge in the project construction in Indonesia. His research interest ranges from pavement management system to advanced data mining techniques for transportation engineering. He has published more than 50 papers in journals and 2 books.",institutionString:null,institution:{name:"Universitas Internasional Batam",country:{name:"Indonesia"}}},{id:"314576",title:"Dr.",name:"Ibai",middleName:null,surname:"Laña",slug:"ibai-lana",fullName:"Ibai Laña",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/314576/images/system/314576.jpg",biography:"Dr. Ibai Laña works at TECNALIA as a data analyst. He received his Ph.D. in Artificial Intelligence from the University of the Basque Country (UPV/EHU), Spain, in 2018. He is currently a senior researcher at TECNALIA. His research interests fall within the intersection of intelligent transportation systems, machine learning, traffic data analysis, and data science. He has dealt with urban traffic forecasting problems, applying machine learning models and evolutionary algorithms. He has experience in origin-destination matrix estimation or point of interest and trajectory detection. Working with large volumes of data has given him a good command of big data processing tools and NoSQL databases. He has also been a visiting scholar at the Knowledge Engineering and Discovery Research Institute, Auckland University of Technology.",institutionString:"TECNALIA Research & Innovation",institution:{name:"Tecnalia",country:{name:"Spain"}}},{id:"314575",title:"Dr.",name:"Jesus",middleName:null,surname:"L. Lobo",slug:"jesus-l.-lobo",fullName:"Jesus L. Lobo",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/314575/images/system/314575.png",biography:"Dr. Jesús López is currently based in Bilbao (Spain) working at TECNALIA as Artificial Intelligence Research Scientist. In most cases, a project idea or a new research line needs to be investigated to see if it is good enough to take into production or to focus on it. That is exactly what he does, diving into Machine Learning algorithms and technologies to help TECNALIA to decide whether something is great in theory or will actually impact on the product or processes of its projects. So, he is expert at framing experiments, developing hypotheses, and proving whether they’re true or not, in order to investigate fundamental problems with a longer time horizon. He is also able to design and develop PoCs and system prototypes in simulation. He has participated in several national and internacional R&D projects.\n\nAs another relevant part of his everyday research work, he usually publishes his findings in reputed scientific refereed journals and international conferences, occasionally acting as reviewer and Programme Commitee member. Concretely, since 2018 he has published 9 JCR (8 Q1) journal papers, 9 conference papers (e.g. ECML PKDD 2021), and he has co-edited a book. He is also active in popular science writing data science stories for reputed blogs (KDNuggets, TowardsDataScience, Naukas). Besides, he has recently embarked on mentoring programmes as mentor, and has also worked as data science trainer.",institutionString:"TECNALIA Research & Innovation",institution:{name:"Tecnalia",country:{name:"Spain"}}},{id:"103779",title:"Prof.",name:"Yalcin",middleName:null,surname:"Isler",slug:"yalcin-isler",fullName:"Yalcin Isler",position:null,profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRyQ8QAK/Profile_Picture_1628834958734",biography:"Yalcin Isler (1971 - Burdur / Turkey) received the B.Sc. degree in the Department of Electrical and Electronics Engineering from Anadolu University, Eskisehir, Turkey, in 1993, the M.Sc. degree from the Department of Electronics and Communication Engineering, Suleyman Demirel University, Isparta, Turkey, in 1996, the Ph.D. degree from the Department of Electrical and Electronics Engineering, Dokuz Eylul University, Izmir, Turkey, in 2009, and the Competence of Associate Professorship from the Turkish Interuniversity Council in 2019.\n\nHe was Lecturer at Burdur Vocational School in Suleyman Demirel University (1993-2000, Burdur / Turkey), Software Engineer (2000-2002, Izmir / Turkey), Research Assistant in Bulent Ecevit University (2002-2003, Zonguldak / Turkey), Research Assistant in Dokuz Eylul University (2003-2010, Izmir / Turkey), Assistant Professor at the Department of Electrical and Electronics Engineering in Bulent Ecevit University (2010-2012, Zonguldak / Turkey), Assistant Professor at the Department of Biomedical Engineering in Izmir Katip Celebi University (2012-2019, Izmir / Turkey). He is an Associate Professor at the Department of Biomedical Engineering at Izmir Katip Celebi University, Izmir / Turkey, since 2019. In addition to academics, he has also founded Islerya Medical and Information Technologies Company, Izmir / Turkey, since 2017.\n\nHis main research interests cover biomedical signal processing, pattern recognition, medical device design, programming, and embedded systems. He has many scientific papers and participated in several projects in these study fields. He was an IEEE Student Member (2009-2011) and IEEE Member (2011-2014) and has been IEEE Senior Member since 2014.",institutionString:null,institution:{name:"Izmir Kâtip Çelebi University",country:{name:"Turkey"}}},{id:"339677",title:"Dr.",name:"Mrinmoy",middleName:null,surname:"Roy",slug:"mrinmoy-roy",fullName:"Mrinmoy Roy",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/339677/images/16768_n.jpg",biography:"An accomplished Sales & Marketing professional with 12 years of cross-functional experience in well-known organisations such as CIPLA, LUPIN, GLENMARK, ASTRAZENECA across different segment of Sales & Marketing, International Business, Institutional Business, Product Management, Strategic Marketing of HIV, Oncology, Derma, Respiratory, Anti-Diabetic, Nutraceutical & Stomatological Product Portfolio and Generic as well as Chronic Critical Care Portfolio. A First Class MBA in International Business & Strategic Marketing, B.Pharm, D.Pharm, Google Certified Digital Marketing Professional. Qualified PhD Candidate in Operations and Management with special focus on Artificial Intelligence and Machine Learning adoption, analysis and use in Healthcare, Hospital & Pharma Domain. Seasoned with diverse therapy area of Pharmaceutical Sales & Marketing ranging from generating revenue through generating prescriptions, launching new products, and making them big brands with continuous strategy execution at the Physician and Patients level. Moved from Sales to Marketing and Business Development for 3.5 years in South East Asian Market operating from Manila, Philippines. Came back to India and handled and developed Brands such as Gluconorm, Lupisulin, Supracal, Absolut Woman, Hemozink, Fabiflu (For COVID 19), and many more. In my previous assignment I used to develop and execute strategies on Sales & Marketing, Commercialization & Business Development for Institution and Corporate Hospital Business portfolio of Oncology Therapy Area for AstraZeneca Pharma India Ltd. Being a Research Scholar and Student of ‘Operations Research & Management: Artificial Intelligence’ I published several pioneer research papers and book chapters on the same in Internationally reputed journals and Books indexed in Scopus, Springer and Ei Compendex, Google Scholar etc. Currently, I am launching PGDM Pharmaceutical Management Program in IIHMR Bangalore and spearheading the course curriculum and structure of the same. I am interested in Collaboration for Healthcare Innovation, Pharma AI Innovation, Future trend in Marketing and Management with incubation on Healthcare, Healthcare IT startups, AI-ML Modelling and Healthcare Algorithm based training module development. I am also an affiliated member of the Institute of Management Consultant of India, looking forward to Healthcare, Healthcare IT and Innovation, Pharma and Hospital Management Consulting works.",institutionString:null,institution:{name:"Lovely Professional University",country:{name:"India"}}},{id:"1063",title:"Prof.",name:"Constantin",middleName:null,surname:"Volosencu",slug:"constantin-volosencu",fullName:"Constantin Volosencu",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/1063/images/system/1063.png",biography:"Prof. Dr. Constantin Voloşencu graduated as an engineer from\nPolitehnica University of Timișoara, Romania, where he also\nobtained a doctorate degree. He is currently a full professor in\nthe Department of Automation and Applied Informatics at the\nsame university. Dr. Voloşencu is the author of ten books, seven\nbook chapters, and more than 160 papers published in journals\nand conference proceedings. He has also edited twelve books and\nhas twenty-seven patents to his name. He is a manager of research grants, editor in\nchief and member of international journal editorial boards, a former plenary speaker, a member of scientific committees, and chair at international conferences. His\nresearch is in the fields of control systems, control of electric drives, fuzzy control\nsystems, neural network applications, fault detection and diagnosis, sensor network\napplications, monitoring of distributed parameter systems, and power ultrasound\napplications. He has developed automation equipment for machine tools, spooling\nmachines, high-power ultrasound processes, and more.",institutionString:'"Politechnica" University Timişoara',institution:null},{id:"221364",title:"Dr.",name:"Eneko",middleName:null,surname:"Osaba",slug:"eneko-osaba",fullName:"Eneko Osaba",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/221364/images/system/221364.jpg",biography:"Dr. Eneko Osaba works at TECNALIA as a senior researcher. He obtained his Ph.D. in Artificial Intelligence in 2015. He has participated in more than twenty-five local and European research projects, and in the publication of more than 130 papers. He has performed several stays at universities in the United Kingdom, Italy, and Malta. Dr. Osaba has served as a program committee member in more than forty international conferences and participated in organizing activities in more than ten international conferences. He is a member of the editorial board of the International Journal of Artificial Intelligence, Data in Brief, and Journal of Advanced Transportation. He is also a guest editor for the Journal of Computational Science, Neurocomputing, Swarm, and Evolutionary Computation and IEEE ITS Magazine.",institutionString:"TECNALIA Research & Innovation",institution:{name:"Tecnalia",country:{name:"Spain"}}},{id:"275829",title:"Dr.",name:"Esther",middleName:null,surname:"Villar-Rodriguez",slug:"esther-villar-rodriguez",fullName:"Esther Villar-Rodriguez",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/275829/images/system/275829.jpg",biography:"Dr. Esther Villar obtained a Ph.D. in Information and Communication Technologies from the University of Alcalá, Spain, in 2015. She obtained a degree in Computer Science from the University of Deusto, Spain, in 2010, and an MSc in Computer Languages and Systems from the National University of Distance Education, Spain, in 2012. Her areas of interest and knowledge include natural language processing (NLP), detection of impersonation in social networks, semantic web, and machine learning. Dr. Esther Villar made several contributions at conferences and publishing in various journals in those fields. Currently, she is working within the OPTIMA (Optimization Modeling & Analytics) business of TECNALIA’s ICT Division as a data scientist in projects related to the prediction and optimization of management and industrial processes (resource planning, energy efficiency, etc).",institutionString:"TECNALIA Research & Innovation",institution:{name:"Tecnalia",country:{name:"Spain"}}},{id:"49813",title:"Dr.",name:"Javier",middleName:null,surname:"Del Ser",slug:"javier-del-ser",fullName:"Javier Del Ser",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/49813/images/system/49813.png",biography:"Prof. Dr. Javier Del Ser received his first PhD in Telecommunication Engineering (Cum Laude) from the University of Navarra, Spain, in 2006, and a second PhD in Computational Intelligence (Summa Cum Laude) from the University of Alcala, Spain, in 2013. He is currently a principal researcher in data analytics and optimisation at TECNALIA (Spain), a visiting fellow at the Basque Center for Applied Mathematics (BCAM) and a part-time lecturer at the University of the Basque Country (UPV/EHU). His research interests gravitate on the use of descriptive, prescriptive and predictive algorithms for data mining and optimization in a diverse range of application fields such as Energy, Transport, Telecommunications, Health and Industry, among others. In these fields he has published more than 240 articles, co-supervised 8 Ph.D. theses, edited 6 books, coauthored 7 patents and participated/led more than 40 research projects. He is a Senior Member of the IEEE, and a recipient of the Biscay Talent prize for his academic career.",institutionString:"Tecnalia Research & Innovation",institution:{name:"Tecnalia",country:{name:"Spain"}}},{id:"278948",title:"Dr.",name:"Carlos Pedro",middleName:null,surname:"Gonçalves",slug:"carlos-pedro-goncalves",fullName:"Carlos Pedro Gonçalves",position:null,profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRcmyQAC/Profile_Picture_1564224512145",biography:'Carlos Pedro Gonçalves (PhD) is an Associate Professor at Lusophone University of Humanities and Technologies and a researcher on Complexity Sciences, Quantum Technologies, Artificial Intelligence, Strategic Studies, Studies in Intelligence and Security, FinTech and Financial Risk Modeling. He is also a progammer with programming experience in:\n\nA) Quantum Computing using Qiskit Python module and IBM Quantum Experience Platform, with software developed on the simulation of Quantum Artificial Neural Networks and Quantum Cybersecurity;\n\nB) Artificial Intelligence and Machine learning programming in Python;\n\nC) Artificial Intelligence, Multiagent Systems Modeling and System Dynamics Modeling in Netlogo, with models developed in the areas of Chaos Theory, Econophysics, Artificial Intelligence, Classical and Quantum Complex Systems Science, with the Econophysics models having been cited worldwide and incorporated in PhD programs by different Universities.\n\nReceived an Arctic Code Vault Contributor status by GitHub, due to having developed open source software preserved in the \\"Arctic Code Vault\\" for future generations (https://archiveprogram.github.com/arctic-vault/), with the Strategy Analyzer A.I. module for decision making support (based on his PhD thesis, used in his Classes on Decision Making and in Strategic Intelligence Consulting Activities) and QNeural Python Quantum Neural Network simulator also preserved in the \\"Arctic Code Vault\\", for access to these software modules see: https://github.com/cpgoncalves. He is also a peer reviewer with outsanding review status from Elsevier journals, including Physica A, Neurocomputing and Engineering Applications of Artificial Intelligence. Science CV available at: https://www.cienciavitae.pt//pt/8E1C-A8B3-78C5 and ORCID: https://orcid.org/0000-0002-0298-3974',institutionString:"University of Lisbon",institution:{name:"Universidade Lusófona",country:{name:"Portugal"}}},{id:"310576",title:"Prof.",name:"Erick Giovani",middleName:null,surname:"Sperandio Nascimento",slug:"erick-giovani-sperandio-nascimento",fullName:"Erick Giovani Sperandio Nascimento",position:null,profilePictureURL:"https://intech-files.s3.amazonaws.com/0033Y00002pDKxDQAW/ProfilePicture%202022-06-20%2019%3A57%3A24.788",biography:"Prof. Erick Sperandio is the Lead Researcher and professor of Artificial Intelligence (AI) at SENAI CIMATEC, Bahia, Brazil, also working with Computational Modeling (CM) and HPC. He holds a PhD in Environmental Engineering in the area of Atmospheric Computational Modeling, a Master in Informatics in the field of Computational Intelligence and Graduated in Computer Science from UFES. He currently coordinates, leads and participates in R&D projects in the areas of AI, computational modeling and supercomputing applied to different areas such as Oil and Gas, Health, Advanced Manufacturing, Renewable Energies and Atmospheric Sciences, advising undergraduate, master's and doctoral students. He is the Lead Researcher at SENAI CIMATEC's Reference Center on Artificial Intelligence. In addition, he is a Certified Instructor and University Ambassador of the NVIDIA Deep Learning Institute (DLI) in the areas of Deep Learning, Computer Vision, Natural Language Processing and Recommender Systems, and Principal Investigator of the NVIDIA/CIMATEC AI Joint Lab, the first in Latin America within the NVIDIA AI Technology Center (NVAITC) worldwide program. He also works as a researcher at the Supercomputing Center for Industrial Innovation (CS2i) and at the SENAI Institute of Innovation for Automation (ISI Automação), both from SENAI CIMATEC. He is a member and vice-coordinator of the Basic Board of Scientific-Technological Advice and Evaluation, in the area of Innovation, of the Foundation for Research Support of the State of Bahia (FAPESB). He serves as Technology Transfer Coordinator and one of the Principal Investigators at the National Applied Research Center in Artificial Intelligence (CPA-IA) of SENAI CIMATEC, focusing on Industry, being one of the six CPA-IA in Brazil approved by MCTI / FAPESP / CGI.br. He also participates as one of the representatives of Brazil in the BRICS Innovation Collaboration Working Group on HPC, ICT and AI. He is the coordinator of the Work Group of the Axis 5 - Workforce and Training - of the Brazilian Strategy for Artificial Intelligence (EBIA), and member of the MCTI/EMBRAPII AI Innovation Network Training Committee. He is the coordinator, by SENAI CIMATEC, of the Artificial Intelligence Reference Network of the State of Bahia (REDE BAH.IA). He leads the working group of experts representing Brazil in the Global Partnership on Artificial Intelligence (GPAI), on the theme \"AI and the Pandemic Response\".",institutionString:null,institution:null},{id:"241400",title:"Prof.",name:"Mohammed",middleName:null,surname:"Bsiss",slug:"mohammed-bsiss",fullName:"Mohammed Bsiss",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/241400/images/8062_n.jpg",biography:null,institutionString:null,institution:null},{id:"276128",title:"Dr.",name:"Hira",middleName:null,surname:"Fatima",slug:"hira-fatima",fullName:"Hira Fatima",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/276128/images/14420_n.jpg",biography:"Dr. Hira Fatima\nAssistant Professor\nDepartment of Mathematics\nInstitute of Applied Science\nMangalayatan University, Aligarh\nMobile: no : 8532041179\nhirafatima2014@gmal.com\n\nDr. Hira Fatima has received his Ph.D. degree in pure Mathematics from Aligarh Muslim University, Aligarh India. Currently working as an Assistant Professor in the Department of Mathematics, Institute of Applied Science, Mangalayatan University, Aligarh. She taught so many courses of Mathematics of UG and PG level. Her research Area of Expertise is Functional Analysis & Sequence Spaces. She has been working on Ideal Convergence of double sequence. She has published 17 research papers in National and International Journals including Cogent Mathematics, Filomat, Journal of Intelligent and Fuzzy Systems, Advances in Difference Equations, Journal of Mathematical Analysis, Journal of Mathematical & Computer Science etc. She has also reviewed few research papers for the and international journals. She is a member of Indian Mathematical Society.",institutionString:null,institution:null},{id:"417317",title:"Mrs.",name:"Chiedza",middleName:null,surname:"Elvina Mashiri",slug:"chiedza-elvina-mashiri",fullName:"Chiedza Elvina Mashiri",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Midlands State University",country:{name:"Zimbabwe"}}},{id:"352140",title:"Dr.",name:"Edina",middleName:null,surname:"Chandiwana",slug:"edina-chandiwana",fullName:"Edina Chandiwana",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Midlands State University",country:{name:"Zimbabwe"}}},{id:"342259",title:"B.Sc.",name:"Leonard",middleName:null,surname:"Mushunje",slug:"leonard-mushunje",fullName:"Leonard Mushunje",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Midlands State University",country:{name:"Zimbabwe"}}},{id:"347042",title:"Mr.",name:"Maxwell",middleName:null,surname:"Mashasha",slug:"maxwell-mashasha",fullName:"Maxwell Mashasha",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Midlands State University",country:{name:"Zimbabwe"}}},{id:"2941",title:"Dr.",name:"Alberto J.",middleName:"Jorge",surname:"Rosales-Silva",slug:"alberto-j.-rosales-silva",fullName:"Alberto J. Rosales-Silva",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Instituto Politécnico Nacional",country:{name:"Mexico"}}},{id:"437913",title:"Dr.",name:"Guillermo",middleName:null,surname:"Urriolagoitia-Sosa",slug:"guillermo-urriolagoitia-sosa",fullName:"Guillermo Urriolagoitia-Sosa",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Instituto Politécnico Nacional",country:{name:"Mexico"}}},{id:"435126",title:"Prof.",name:"Joaquim",middleName:null,surname:"José de Castro Ferreira",slug:"joaquim-jose-de-castro-ferreira",fullName:"Joaquim José de Castro Ferreira",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of Aveiro",country:{name:"Portugal"}}},{id:"437899",title:"MSc.",name:"Miguel Angel",middleName:null,surname:"Ángel Castillo-Martínez",slug:"miguel-angel-angel-castillo-martinez",fullName:"Miguel Angel Ángel Castillo-Martínez",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Instituto Politécnico Nacional",country:{name:"Mexico"}}},{id:"289955",title:"Dr.",name:"Raja",middleName:null,surname:"Kishor Duggirala",slug:"raja-kishor-duggirala",fullName:"Raja Kishor Duggirala",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Jawaharlal Nehru Technological University, Hyderabad",country:{name:"India"}}}]}},subseries:{item:{id:"12",type:"subseries",title:"Human Physiology",keywords:"Anatomy, Cells, Organs, Systems, Homeostasis, Functions",scope:"Human physiology is the scientific exploration of the various functions (physical, biochemical, and mechanical properties) of humans, their organs, and their constituent cells. The endocrine and nervous systems play important roles in maintaining homeostasis in the human body. Integration, which is the biological basis of physiology, is achieved through communication between the many overlapping functions of the human body's systems, which takes place through electrical and chemical means. Much of the basis of our knowledge of human physiology has been provided by animal experiments. Because of the close relationship between structure and function, studies in human physiology and anatomy seek to understand the mechanisms that help the human body function. The series on human physiology deals with the various mechanisms of interaction between the various organs, nerves, and cells in the human body.",coverUrl:"https://cdn.intechopen.com/series_topics/covers/12.jpg",hasOnlineFirst:!1,hasPublishedBooks:!0,annualVolume:11408,editor:{id:"195829",title:"Prof.",name:"Kunihiro",middleName:null,surname:"Sakuma",slug:"kunihiro-sakuma",fullName:"Kunihiro Sakuma",profilePictureURL:"https://mts.intechopen.com/storage/users/195829/images/system/195829.jpg",biography:"Professor Kunihiro Sakuma, Ph.D., currently works in the Institute for Liberal Arts at the Tokyo Institute of Technology. He is a physiologist working in the field of skeletal muscle. He was awarded his sports science diploma in 1995 by the University of Tsukuba and began his scientific work at the Department of Physiology, Aichi Human Service Center, focusing on the molecular mechanism of congenital muscular dystrophy and normal muscle regeneration. His interest later turned to the molecular mechanism and attenuating strategy of sarcopenia (age-related muscle atrophy). His opinion is to attenuate sarcopenia by improving autophagic defects using nutrient- and pharmaceutical-based treatments.",institutionString:null,institution:{name:"Tokyo Institute of Technology",institutionURL:null,country:{name:"Japan"}}},editorTwo:{id:"331519",title:"Dr.",name:"Kotomi",middleName:null,surname:"Sakai",slug:"kotomi-sakai",fullName:"Kotomi Sakai",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0033Y000031QtFXQA0/Profile_Picture_1637053227318",biography:"Senior researcher Kotomi Sakai, Ph.D., MPH, works at the Research Organization of Science and Technology in Ritsumeikan University. She is a researcher in the geriatric rehabilitation and public health field. She received Ph.D. from Nihon University and MPH from St.Luke’s International University. 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Dr. Blumenberg’s research is focused on the epidermis, expression of keratin genes, transcription profiling, keratinocyte differentiation, inflammatory diseases and cancers, and most recently the effects of the microbiome on the skin. He has published more than 100 peer-reviewed research articles and graduated numerous Ph.D. and postdoctoral students.",institutionString:null,institution:{name:"New York University Langone Medical Center",institutionURL:null,country:{name:"United States of America"}}},subseries:[{id:"14",title:"Cell and Molecular Biology",keywords:"Omics (Transcriptomics; Proteomics; Metabolomics), Molecular Biology, Cell Biology, Signal Transduction and Regulation, Cell Growth and Differentiation, Apoptosis, Necroptosis, Ferroptosis, Autophagy, Cell Cycle, Macromolecules and Complexes, Gene Expression",scope:"The Cell and Molecular Biology topic within the IntechOpen Biochemistry Series aims to rapidly publish contributions on all aspects of cell and molecular biology, including aspects related to biochemical and genetic research (not only in humans but all living beings). We encourage the submission of manuscripts that provide novel and mechanistic insights that report significant advances in the fields. Topics include, but are not limited to: Advanced techniques of cellular and molecular biology (Molecular methodologies, imaging techniques, and bioinformatics); Biological activities at the molecular level; Biological processes of cell functions, cell division, senescence, maintenance, and cell death; Biomolecules interactions; Cancer; Cell biology; Chemical biology; Computational biology; Cytochemistry; Developmental biology; Disease mechanisms and therapeutics; DNA, and RNA metabolism; Gene functions, genetics, and genomics; Genetics; Immunology; Medical microbiology; Molecular biology; Molecular genetics; Molecular processes of cell and organelle dynamics; Neuroscience; Protein biosynthesis, degradation, and functions; Regulation of molecular interactions in a cell; Signalling networks and system biology; Structural biology; Virology and microbiology.",annualVolume:11410,isOpenForSubmission:!0,coverUrl:"https://cdn.intechopen.com/series_topics/covers/14.jpg",editor:{id:"165627",title:"Dr.",name:"Rosa María",middleName:null,surname:"Martínez-Espinosa",fullName:"Rosa María Martínez-Espinosa",profilePictureURL:"https://mts.intechopen.com/storage/users/165627/images/system/165627.jpeg",institutionString:"University of Alicante",institution:{name:"University of Alicante",institutionURL:null,country:{name:"Spain"}}},editorTwo:null,editorThree:null,editorialBoard:[{id:"79367",title:"Dr.",name:"Ana Isabel",middleName:null,surname:"Flores",fullName:"Ana Isabel Flores",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRpIOQA0/Profile_Picture_1632418099564",institutionString:null,institution:{name:"Hospital Universitario 12 De Octubre",institutionURL:null,country:{name:"Spain"}}},{id:"328234",title:"Ph.D.",name:"Christian",middleName:null,surname:"Palavecino",fullName:"Christian Palavecino",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0033Y000030DhEhQAK/Profile_Picture_1628835318625",institutionString:null,institution:{name:"Central University of Chile",institutionURL:null,country:{name:"Chile"}}},{id:"186585",title:"Dr.",name:"Francisco Javier",middleName:null,surname:"Martin-Romero",fullName:"Francisco Javier Martin-Romero",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bSB3HQAW/Profile_Picture_1631258137641",institutionString:null,institution:{name:"University of Extremadura",institutionURL:null,country:{name:"Spain"}}}]},{id:"15",title:"Chemical Biology",keywords:"Phenolic Compounds, Essential Oils, Modification of Biomolecules, Glycobiology, Combinatorial Chemistry, Therapeutic peptides, Enzyme Inhibitors",scope:"Chemical biology spans the fields of chemistry and biology involving the application of biological and chemical molecules and techniques. In recent years, the application of chemistry to biological molecules has gained significant interest in medicinal and pharmacological studies. This topic will be devoted to understanding the interplay between biomolecules and chemical compounds, their structure and function, and their potential applications in related fields. Being a part of the biochemistry discipline, the ideas and concepts that have emerged from Chemical Biology have affected other related areas. This topic will closely deal with all emerging trends in this discipline.",annualVolume:11411,isOpenForSubmission:!0,coverUrl:"https://cdn.intechopen.com/series_topics/covers/15.jpg",editor:{id:"441442",title:"Dr.",name:"Şükrü",middleName:null,surname:"Beydemir",fullName:"Şükrü Beydemir",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0033Y00003GsUoIQAV/Profile_Picture_1634557147521",institutionString:null,institution:{name:"Anadolu University",institutionURL:null,country:{name:"Turkey"}}},editorTwo:{id:"13652",title:"Prof.",name:"Deniz",middleName:null,surname:"Ekinci",fullName:"Deniz Ekinci",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002aYLT1QAO/Profile_Picture_1634557223079",institutionString:null,institution:{name:"Ondokuz Mayıs University",institutionURL:null,country:{name:"Turkey"}}},editorThree:null,editorialBoard:[{id:"219081",title:"Dr.",name:"Abdulsamed",middleName:null,surname:"Kükürt",fullName:"Abdulsamed Kükürt",profilePictureURL:"https://mts.intechopen.com/storage/users/219081/images/system/219081.png",institutionString:null,institution:{name:"Kafkas University",institutionURL:null,country:{name:"Turkey"}}},{id:"241413",title:"Dr.",name:"Azhar",middleName:null,surname:"Rasul",fullName:"Azhar Rasul",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRT1oQAG/Profile_Picture_1635251978933",institutionString:null,institution:{name:"Government College University, Faisalabad",institutionURL:null,country:{name:"Pakistan"}}},{id:"178316",title:"Ph.D.",name:"Sergey",middleName:null,surname:"Sedykh",fullName:"Sergey Sedykh",profilePictureURL:"https://mts.intechopen.com/storage/users/178316/images/system/178316.jfif",institutionString:null,institution:{name:"Novosibirsk State University",institutionURL:null,country:{name:"Russia"}}}]},{id:"17",title:"Metabolism",keywords:"Biomolecules Metabolism, Energy Metabolism, Metabolic Pathways, Key Metabolic Enzymes, Metabolic Adaptation",scope:"Metabolism is frequently defined in biochemistry textbooks as the overall process that allows living systems to acquire and use the free energy they need for their vital functions or the chemical processes that occur within a living organism to maintain life. Behind these definitions are hidden all the aspects of normal and pathological functioning of all processes that the topic ‘Metabolism’ will cover within the Biochemistry Series. Thus all studies on metabolism will be considered for publication.",annualVolume:11413,isOpenForSubmission:!0,coverUrl:"https://cdn.intechopen.com/series_topics/covers/17.jpg",editor:{id:"138626",title:"Dr.",name:"Yannis",middleName:null,surname:"Karamanos",fullName:"Yannis Karamanos",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002g6Jv2QAE/Profile_Picture_1629356660984",institutionString:null,institution:{name:"Artois University",institutionURL:null,country:{name:"France"}}},editorTwo:null,editorThree:null,editorialBoard:[{id:"243049",title:"Dr.",name:"Anca",middleName:null,surname:"Pantea Stoian",fullName:"Anca Pantea Stoian",profilePictureURL:"https://mts.intechopen.com/storage/users/243049/images/system/243049.jpg",institutionString:null,institution:{name:"Carol Davila University of Medicine and Pharmacy",institutionURL:null,country:{name:"Romania"}}},{id:"203824",title:"Dr.",name:"Attilio",middleName:null,surname:"Rigotti",fullName:"Attilio Rigotti",profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",institutionString:null,institution:{name:"Pontifical Catholic University of Chile",institutionURL:null,country:{name:"Chile"}}},{id:"300470",title:"Dr.",name:"Yanfei (Jacob)",middleName:null,surname:"Qi",fullName:"Yanfei (Jacob) Qi",profilePictureURL:"https://mts.intechopen.com/storage/users/300470/images/system/300470.jpg",institutionString:null,institution:{name:"Centenary Institute of Cancer Medicine and Cell Biology",institutionURL:null,country:{name:"Australia"}}}]},{id:"18",title:"Proteomics",keywords:"Mono- and Two-Dimensional Gel Electrophoresis (1-and 2-DE), Liquid Chromatography (LC), Mass Spectrometry/Tandem Mass Spectrometry (MS; MS/MS), Proteins",scope:"With the recognition that the human genome cannot provide answers to the etiology of a disorder, changes in the proteins expressed by a genome became a focus in research. Thus proteomics, an area of research that detects all protein forms expressed in an organism, including splice isoforms and post-translational modifications, is more suitable than genomics for a comprehensive understanding of the biochemical processes that govern life. The most common proteomics applications are currently in the clinical field for the identification, in a variety of biological matrices, of biomarkers for diagnosis and therapeutic intervention of disorders. From the comparison of proteomic profiles of control and disease or different physiological states, which may emerge, changes in protein expression can provide new insights into the roles played by some proteins in human pathologies. Understanding how proteins function and interact with each other is another goal of proteomics that makes this approach even more intriguing. Specialized technology and expertise are required to assess the proteome of any biological sample. Currently, proteomics relies mainly on mass spectrometry (MS) combined with electrophoretic (1 or 2-DE-MS) and/or chromatographic techniques (LC-MS/MS). MS is an excellent tool that has gained popularity in proteomics because of its ability to gather a complex body of information such as cataloging protein expression, identifying protein modification sites, and defining protein interactions. The Proteomics topic aims to attract contributions on all aspects of MS-based proteomics that, by pushing the boundaries of MS capabilities, may address biological problems that have not been resolved yet.",annualVolume:11414,isOpenForSubmission:!0,coverUrl:"https://cdn.intechopen.com/series_topics/covers/18.jpg",editor:{id:"200689",title:"Prof.",name:"Paolo",middleName:null,surname:"Iadarola",fullName:"Paolo Iadarola",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bSCl8QAG/Profile_Picture_1623568118342",institutionString:null,institution:{name:"University of Pavia",institutionURL:null,country:{name:"Italy"}}},editorTwo:{id:"201414",title:"Dr.",name:"Simona",middleName:null,surname:"Viglio",fullName:"Simona Viglio",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRKDHQA4/Profile_Picture_1630402531487",institutionString:null,institution:{name:"University of Pavia",institutionURL:null,country:{name:"Italy"}}},editorThree:null,editorialBoard:[{id:"72288",title:"Dr.",name:"Arli Aditya",middleName:null,surname:"Parikesit",fullName:"Arli Aditya Parikesit",profilePictureURL:"https://mts.intechopen.com/storage/users/72288/images/system/72288.jpg",institutionString:null,institution:{name:"Indonesia International Institute for Life Sciences",institutionURL:null,country:{name:"Indonesia"}}},{id:"40928",title:"Dr.",name:"Cesar",middleName:null,surname:"Lopez-Camarillo",fullName:"Cesar Lopez-Camarillo",profilePictureURL:"https://mts.intechopen.com/storage/users/40928/images/3884_n.png",institutionString:null,institution:{name:"Universidad Autónoma de la Ciudad de México",institutionURL:null,country:{name:"Mexico"}}},{id:"81926",title:"Dr.",name:"Shymaa",middleName:null,surname:"Enany",fullName:"Shymaa Enany",profilePictureURL:"https://mts.intechopen.com/storage/users/81926/images/system/81926.png",institutionString:"Suez Canal University",institution:{name:"Suez Canal University",institutionURL:null,country:{name:"Egypt"}}}]}]}},libraryRecommendation:{success:null,errors:{},institutions:[]},route:{name:"profile.detail",path:"/profiles/308435",hash:"",query:{},params:{id:"308435"},fullPath:"/profiles/308435",meta:{},from:{name:null,path:"/",hash:"",query:{},params:{},fullPath:"/",meta:{}}}},function(){var e;(e=document.currentScript||document.scripts[document.scripts.length-1]).parentNode.removeChild(e)}()