\\n\\n
More than half of the publishers listed alongside IntechOpen (18 out of 30) are Social Science and Humanities publishers. IntechOpen is an exception to this as a leader in not only Open Access content but Open Access content across all scientific disciplines, including Physical Sciences, Engineering and Technology, Health Sciences, Life Science, and Social Sciences and Humanities.
\\n\\nOur breakdown of titles published demonstrates this with 47% PET, 31% HS, 18% LS, and 4% SSH books published.
\\n\\n“Even though ItechOpen has shown the potential of sci-tech books using an OA approach,” other publishers “have shown little interest in OA books.”
\\n\\nAdditionally, each book published by IntechOpen contains original content and research findings.
\\n\\nWe are honored to be among such prestigious publishers and we hope to continue to spearhead that growth in our quest to promote Open Access as a true pioneer in OA book publishing.
\\n\\n\\n\\n
\\n"}]',published:!0,mainMedia:{caption:"IntechOpen Maintains",originalUrl:"/media/original/113"}},components:[{type:"htmlEditorComponent",content:'
Simba Information has released its Open Access Book Publishing 2020 - 2024 report and has again identified IntechOpen as the world’s largest Open Access book publisher by title count.
\n\nSimba Information is a leading provider for market intelligence and forecasts in the media and publishing industry. The report, published every year, provides an overview and financial outlook for the global professional e-book publishing market.
\n\nIntechOpen, De Gruyter, and Frontiers are the largest OA book publishers by title count, with IntechOpen coming in at first place with 5,101 OA books published, a good 1,782 titles ahead of the nearest competitor.
\n\nSince the first Open Access Book Publishing report published in 2016, IntechOpen has held the top stop each year.
\n\n\n\nMore than half of the publishers listed alongside IntechOpen (18 out of 30) are Social Science and Humanities publishers. IntechOpen is an exception to this as a leader in not only Open Access content but Open Access content across all scientific disciplines, including Physical Sciences, Engineering and Technology, Health Sciences, Life Science, and Social Sciences and Humanities.
\n\nOur breakdown of titles published demonstrates this with 47% PET, 31% HS, 18% LS, and 4% SSH books published.
\n\n“Even though ItechOpen has shown the potential of sci-tech books using an OA approach,” other publishers “have shown little interest in OA books.”
\n\nAdditionally, each book published by IntechOpen contains original content and research findings.
\n\nWe are honored to be among such prestigious publishers and we hope to continue to spearhead that growth in our quest to promote Open Access as a true pioneer in OA book publishing.
\n\n\n\n
\n'}],latestNews:[{slug:"intechopen-supports-asapbio-s-new-initiative-publish-your-reviews-20220729",title:"IntechOpen Supports ASAPbio’s New Initiative Publish Your Reviews"},{slug:"webinar-introduction-to-open-science-wednesday-18-may-1-pm-cest-20220518",title:"Webinar: Introduction to Open Science | Wednesday 18 May, 1 PM CEST"},{slug:"step-in-the-right-direction-intechopen-launches-a-portfolio-of-open-science-journals-20220414",title:"Step in the Right Direction: IntechOpen Launches a Portfolio of Open Science Journals"},{slug:"let-s-meet-at-london-book-fair-5-7-april-2022-olympia-london-20220321",title:"Let’s meet at London Book Fair, 5-7 April 2022, Olympia London"},{slug:"50-books-published-as-part-of-intechopen-and-knowledge-unlatched-ku-collaboration-20220316",title:"50 Books published as part of IntechOpen and Knowledge Unlatched (KU) Collaboration"},{slug:"intechopen-joins-the-united-nations-sustainable-development-goals-publishers-compact-20221702",title:"IntechOpen joins the United Nations Sustainable Development Goals Publishers Compact"},{slug:"intechopen-signs-exclusive-representation-agreement-with-lsr-libros-servicios-y-representaciones-s-a-de-c-v-20211123",title:"IntechOpen Signs Exclusive Representation Agreement with LSR Libros Servicios y Representaciones S.A. de C.V"},{slug:"intechopen-expands-partnership-with-research4life-20211110",title:"IntechOpen Expands Partnership with Research4Life"}]},book:{item:{type:"book",id:"3139",leadTitle:null,fullTitle:"Wireless Ad-Hoc Networks",title:"Wireless Ad-Hoc Networks",subtitle:null,reviewType:"peer-reviewed",abstract:"A wireless ad-hoc network is a wireless network deployed without any infrastructure. 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\r\n\tThe goal of the book is to give the reader an overview of a field related to click chemistry. This book aims to provide information about click chemistry to the synthesis nano/microstructures, click chemistry for drug delivery nanosystems, and applications of click reactions in environmental technologies. The book welcomes submissions written by authors in the field of experimental methods and critical reviews from multi-disciplines such as chemistry, environmental chemistry, pharmacy and materials science.
\r\n\r\n\tAmong others, welcome topics are in situ click chemistry, classification of click chemistry, click chemistry in polymer science, click chemistry in materials science, click chemistry reactions in medicinal chemistry and pharmaceutical applications, click chemistry in environmental chemistry applications and pollutants, chemical sensors sensor based on click chemistry, photoelectrochemical sensor based on click chemistry, wastewater treatment, nanoadsorbent, hydrogel networks.
\r\n\r\n\tAll interested authors are welcome to focus on recent studies, industrial applications, and new technological developments on click chemistry in nanotechnology.
\r\n\t
The textile dyeing industry is constantly increasing because of the growing consumption of fabrics and garments; moreover, till the next decade, a billion consumers will be added to the global market [1]. The processing of such a large volume of fabrics and garments is conducted through dyes and chemicals. A variety of factors can influence the quality of dyeing and its complex mechanisms in batch reproduction. The degree of levelness and reproducibility of dyeing depends on not only the dyes and chemicals used but also the control of temperatures and pH conditions in the dye bath [2]. To achieve any progress in such studies, it is necessary to control the parameters in order to determine their effect on the dyeing system. To study the performance of dyeing in an aqueous dye bath system, it is essential to alter the dye concentration while maintaining, and all other conditions constant so that the changes in the chemical structure of the solvent and the nature of the dye species can be analyzed [3].
Natural and synthetic dyes play an important role in the process of dyeing textile fabrics and garments. Different classes of dyes are used for coloring different textile materials with the aid of auxiliaries, which facilitate the homogenization of the mixtures [4]. The method of determining the equilibrium constant of the dye–auxiliary complex can be constructed.
The association between the dye and the auxiliary agent may proceed as far as the colloidal particles are dispersed in dyes. Apart from this, there exists an equilibrium between the dyes and the textile auxiliaries, which have been added to the dye bath [5]. The auxiliaries exist in a state of association equilibrium [6]. A new era of dyeing chemical research began in 1930 when soap was replaced by synthetic surfactants [7]. Since many researchers have described the use of various textile auxiliaries in dyeing [8]. Thermodynamic studies of dyeing make useful contributions to the general theories of intermolecular forces while diffusion processes are also influenced by the dye concentration, temperature, nature of dyeing auxiliaries, and polymer structure [9]. A major challenge for textile wet processors is addressing the increasing cost and demand associated with the use of different auxiliaries in industrialized countries. However, in recent years, there has been significant demonstration of a lack of knowledge about the usage of dyeing chemicals. In this study, the potential for dyeing auxiliaries was explained.
This chapter demonstrates the characteristics of different auxiliary agents, which tend to form colloidal flocculation and dye–auxiliary complexes with dyes. A chelating agent is used to remove the hardness of water by bonding with calcium and magnesium ions and other heavy metal ions in hard water, by forming a stable complex compound that does not decompose over a prolonged processing period [10]. Dispersing agents, pH, and temperatures affect the changes in shade and fastness of disperse dyes [2, 11]. A greater degree of levelness is linked with greater retarding effect, which means a longer dyeing time [4]. In the presence of electrolytes, dyeing of cotton fabric with anionic dyes is to suppress negative charge at the fiber surface and to promote increased dye exhaustion [12]. If the dye bath pH is adjusted prior to the dyeing process, it may affect the absorption of dye on the fiber [13]. Synthetic surfactants have been extensively studied by many researchers [14]. After World War II, fabric softeners emerged through the introduction of the synthetic surfactant [15].
The word “chelate” is obtained from the Greek word “chel,” which means crab’s claw. Chemically, a chelate is an organic compound that can form a ring structure by bonding with metal ions. Chelating agents are mostly used in dye baths, as they remove the hardness of water by bonding with heavy metal ion. Chelating agents form a stable complex compound that does not decompose over a prolonged processing period [10]. The coordination of water with metal ions enhances the acidity of the dye solution, which is dependent on the physical and chemical characteristics of the metal ions [16]. Inorganic chelating agents are also used as detergent by suspending and dispersing agents. They require less than the stoichiometric quantity predicted to keep ions in solution (threshold effect). They will dissociate to sodium phosphate in water over time losing their ability to chelate, especially in hot water. Polyphosphates are derivatives of phosphoric acid and are made by reacting phosphorous pentoxide with phosphoric acid. Important polyphosphates are tetra sodium pyrophosphate (Na4P2O7), sodium phosphate (Na5P3O10), and sodium hexametaphosphate (Na6P6O18) [17] (Figure 1).
Formation of sodium polyphosphates.
Organophosphonic acids also act as chelating agents and aid detergency by dispersing and suspending soil. They are more stable than inorganic polyphosphates in hot water and exhibit threshold effect (Figure 2).
Organophosphonic acids.
Amino carboxylic acids form very stable complexes, when reacting with metal ions. They react stoichiometrically and can be formed quantitatively to determine calcium and magnesium by titration. Disodium-ethylenediaminetetraacetic acid (EDTA) and nitrilotriacetic acid (NTA) are categorized in these groups [17] (Figure 3).
Disodium-ethylenediaminetetraacetic acids and nitrilotriacetic acid.
Several hydroxyl groups containing organic compounds precipitate bi- and trivalent metal cations in alkaline medium and also acts as effective sequestering agents; however, they are not effective for calcium and magnesium. Some of the well-known products in this category are glycolic acid, gluconic acid, and citric acid (Figure 4).
Hydroxy acids sequestering agents.
Ethylenediaminetetraacetic acid also prevents or removes scales by forming water-soluble complex compounds, which vigorously react with metal ions [18]. Gluconic acid is obtained from fruit, honey, and wine. In an aqueous solution at neutral pH, gluconic acid forms gluconate ion, which is used in cleaning products in which it dissolves mineral deposits through the formation of ligand with metal compounds [19]. Citric acid also strongly interacts with active metal components. This interaction helps metal dispersion and decreases the specific surface area and pore volume of the metal components. The addition of citric acid increases the amount of metal ion adsorption. Increasing the adsorption depends on the formation of more complex structures (Figure 5).
Coordination of metal ions with different chelating agents.
Glycolic acid exhibits better chelation power in all metal ions because of the lower molecular weight, which helps to remove all metal ions. Glycolic acid, which is a naturally occurring organic agent, exhibits more penetration of metal ions. Natural chelates are biodegradable and non-toxic to the environment. Under natural conditions, EDTA is converted into ethylenediaminetriacetic acid, and then forms a ring structure with other metals, creating persistent organic pollutants [20]. Kabir and Koh [21] have demonstrated that glycolic acid provides effective chelation efficiency for a moderate acid donor. Consequently, glycolic acid exhibited a higher percentage of dyebath exhaustions and better dye ability than other organic chelating agents.
Disperse dyes are nonionic chemicals that are barely soluble in water and often crystallize with varying particle size [22]. These characteristics are inadequate for dispersing dyes of water and cause unleveled dyeing. To achieve the required particle size and distribution, the disperse dye is milled, usually in the presence of a dispersing agent [23]. Generally, the dispersing agents are anionic, e.g., ligninsulfonates, or polycondensates of arylsulfonic acids with formaldehyde, which facilitate milling. Dispersing agents have shown a dual function role: breaking down aggregated dye particles and dispersing dyes in the dye liquor. Dispersing agents consists of high-molecular weight or polymeric compounds in which polar or ionizing groups alternate with nonpolar groups along the chain. The backbone of a dispersing agent is nonpolar, while the polar or ionizing groups are located in the side chains. Johnson [24] demonstrated that the adsorption of dispersing agent is oriented parallel to the surface, so that the nonpolar groups adjoin to the surface and the polar groups turn outward.
The application of disperse dyes on polyester fabric mainly occurs via the inclusion of dispersing agents. The hydrophobic tails of the dispersing-agent molecules are oriented toward the center of the dye micelle, which facilitates micellar solubilization of the disperse dye molecules, thereby conferring higher dye solubility. The disperse dyeing mechanism has been categorized in four stages: (i) dissolution of dye in water by the formation of the dye micelle with dispersing agents; (ii) transference of dye molecules from the solution to the surface of the fiber; (iii) replenishment of dyebath by the dissolution of solid material from the dispersion; and (iv) diffusion of dye into the fiber (Figure 6).
Sodium dinaphthylmethane sulfonate and sodium lignosulfonate.
Murray and Mortimer [25] mentioned sodium dinaphthylmethane sulfonate and lignosulfonates as agents used for disperse dyes. A combination of dispersing agents and water-soluble polymers, for example, poly (vinyl alcohol), sodium polyacrylate, and the maleic anhydride-styrene copolymer, in admixture with anionic surfactants, would be useful in processing the pigments. Wolf and Bauer [26] suggested the use of dissolved disperse dyes in dimethylformamide and formed dispersions by pouring these solutions into aqueous solutions of the dispersing agents. Dispersing agents formed the dispersion by varying particle size of disperse dyes (Figure 7).
Mechanism for dyeing of polyester with disperse dye and dispersing agents.
Heimanns [27] explained that a high-concentration of dispersing agent acts as a barrier to diffusion and reduces the dye yield in thermo-fixation. For better color yield, liquid brands of disperse dyes contain a smaller amount of dispersing agent. To ensure stability, the amount of dispersing agents must be maintained in the dye bath [8].
To achieve uniform dyeing on fabric, it is essential to add a suitable leveling agent in the dye baths. However, it is quite difficult to explain the functions and actions of leveling agents. Werner [4] explained that the effects of textile auxiliaries, such as leveling agents, would appear at first sight to contradict the very nature of physical methods.
Figure 8 shows that equilibrium in dyebath-fiber systems is caused by a large number of processes that play an important part in producing good dyeing. Leveling agents enhance the force in a state of association equilibrium in the dye bath. Werner [4] investigated that the formation of dyes and leveling agents represents bonding similar to what occurs in the dyeing of fibers. The effects of leveling agents are: (i) leveling agents tend to decrease the absorption of dyes by forming a dye-auxiliary complex with free dyes maintaining equilibrium; (ii) leveling agents act as retarding agents; and (iii) dye migration proceeds slowly, leads better leading to improved leveling of dye on the fiber. A cationic polyethoxylated amine can perform strong leveling action. The greater cationic character a strong complex formation, pronounced retardation of dyeing, and higher risk of precipitation (Figure 9).
Equilibrium in dyebath-fiber systems containing leveling agents.
Different leveling agents.
The polyethoxylated chain is longer (n > 50), and the dye auxiliary complex is dispersed by the cationic leveling agents. Amphoteric leveling agents have both anionic and cationic groups, so its activation depends on the dye bath pH [20].
During dyeing in the dyebath, electrolyte serves as three important roles—driving dye into textiles causing, maximum exhaustion of dye molecules through the presence of salt, and fixing dyestuff to the cellulose material [28]. The dyeing mechanism of reactive dye can be classified into two phases, exhaustion and fixation. The process is lengthy because considerable time is spent on the controlled heating of the dyebath and the portion-wise addition of salt and alkali to avoid unleveled dyeing and maximize the exhaustion and fixation [20]. A colorless crystalline solid NaCl composed of inorganic compound of sodium and chloride, a salt in which ionic bonds hold the two components together in the familiar water-soluble white crystals, has a key role in the textile dyeing process in maintaining the electrolytic balance in the textile dyeing process. Glauber’s salt is the common name for sodium sulfate dehydrates Na2SO4. 10H2O; it occurs as white or colorless monoclinic crystals, which are most commonly used in the dyeing industry [29]. Vacuum salt is manufactured by recrystallization of purified brine solution. In the vacuum crystallization process, raw salt is dissolved in water to make a saturated solution and clarify the impurities from the bottom. A vacuum is generated by using a suitable vacuum pump [30]. When cotton/bast fibers are immersed in water, its surface due to the hydroxyl ions also becomes anionic; hence, the dye particles and the cellulosic fiber tend to repel each other. So, the level of substantivity is reduced. The addition of salt creates an electrical positive double layer, which hides the negative electrostatic charge (Donnan Potential) of the cellulose surface. This allows the dye to approach the fiber, allowing better interaction of Van der Waals forces as well; this improves the substantivity. Neale et al. [31] proposed the existence of the Donnan equilibrium. The idea of the Donnan equilibrium was employed for the modern electrochemical theories of the dyeing of cellulose from aqueous solutions of direct dyes [32].
NaCl enhances the diffusion of dye and its adsorption onto fiber. Bicarbonate and carbonate increase the dye bath pH and perform dye fixation through the formation of covalent bonds. “Bolaform” electrolytes contain anionic and cationic organic groups, which are separated by large distances. The word ‘bola’ means a long cord with heavy balls. The alkyl chains whose lengths are sufficiently long act as electrolyte to become surface-active compounds. Hamada et al. [33] extensively studied various physical properties of bolaform electrolytes or amphiphilies. The bolaform electrolytes or amphiphilies contain a single positive or negative site (Figure 10).
Bolaform electrolyte.
Dyebath pH is adjusted prior to the dyeing process; otherwise, it may affect various factors, such as the absorption of dye into the fiber, by increasing or reducing alkalinity [34]. The pH controlling agents play three important roles: (a) maintain a high degree of acidity; (b) control the pH within narrow tolerances; and (c) slide the pH in acidic conditions [35]. The pH controlling agents are usually based on two chemicals, a weak acid and its salt, with a stronger base such as acetic acid, sodium acetate, or phosphoric acid-sodium phosphate. When the dyeing temperature increases, pH control agents release more acidic compounds. Ammonium sulfate decomposes gradually, proucing ammonia and sulfuric acid, which is a strong acid that subsequently lowers the pH when ammonia escapes, at boiling temperatures. However, enclosed or partially enclosed machine, such as a winch, it is not very efficient because ammonia is prevented from escaping into the dye bath (Figure 11).
Dissociation of ammonium salt.
Organic esters are also used as an alternative method for obtaining a pH that slides in the direction of acidity under the conditions of processing. In 1953, Brotherton Co. Ltd. introduced the Estrocon process, which is based on the addition of diethyl tartrate or ethyl lactate for dyeing wool with acid milling dyes and chrome dyes by the single-bath method [36] (Figure 12).
Action of ethyl lactate as pH sliding agents.
Almost 35 years ago, Sandoz introduced the Sandacid V process, in which γ-butyrolactone undergoes hydrolysis to produce butyric acid [37] (Figure 13).
Dissociation of γ-butyrolactone.
Koh et al. [37] found that hydrolysable organic esters achieved a relatively wider range of pH sliding than ammonium sulfate or sodium di hydrogen phosphate, which can produce good exhaustion with satisfactory dyeing in the closed dyeing process.
Surfactant molecules should have surface active properties with the chemical structure of a hydrophilic (water loving) and hydrophobic (having little attraction for organic molecules) balance [38] (Figure 14).
Schematic of a surfactant molecule.
These molecules get preferentially oriented at the interface between air and water, which lowers the surface tension of water substantially when dissolved in the concentration range of 0.1–10 g/l. The driving force for the activation of surface active agents is the formation of micelles, in which the lyophobic tails are associated with themselves, and the hydrophilic heads are surrounded by water molecules. Surfactants are classified into different ways such as use, ionic charge, and chemical structure. According to the ionic structure, surfactants can be classified into four categories: anionic, cationic, amphoteric, and nonionic [39]. Anionic surfactants are surfactants that are ionized into anions and cations but the anion is the dominating ion in the solution. Examples are alkyl benzene sulfonate and sodium lauryl sulfate (Figure 15).
Structure of anionic surfactants.
An ionic surface active agent that produces cation as the dominating ion when dissolved in water is called a cationic surfactant. For example, dodecyl dimethyl ammonium chloride and distearyl dimethyl ammonium chloride (Figure 16).
Structure of cationic surfactants.
Nonionic surfactants that does not show any ionic behavior when dissolved in water are called nonionic surfactants. Examples are Lanolin ethoxylate and glycerol monostearate (Figure 17).
Structure of nonionic surfactants.
Surfactants that ionize and produce large segments (these segments are called Zwitter ions) carrying both anionic and cationic ions when dissolved in water are called amphoteric surfactants. Lauryl dimethyl betaine and cocamidopropyl betaine are the most commonly used (Figure 18).
Structure of amphoteric surfactants.
Surfactants are widely used as wetting agents, emulsifiers, detergent, lubricants, or dispersing agents [40].
The dyeing process can lead to the formation of macro and micro foams during circulation of dyes and auxiliaries in the dye bath. A macro foam is displayed with large bubbles, which are visible on the surface of the system and produce cosmetic imperfections [41]. A typical list of anti-foaming agents is as follows: 2-ethyl hexanol (EH), tributyl phosphate (TBP), poly (dimethyl siloxane) (PDMS) amides, mineral oil, fatty acids, and their derivatives [42] (Figure 19).
Anti-foaming agents.
Silicone-based anti-foaming agents consist of small polar groups and hydrophobic polymer chain. The hydrophobic polymer chain is typically a permethylated siloxane. The PDMS chain gains its hydrophilic character by modification with poly (ethylene glycol) (PEG) and poly (propylene glycol) (PPG). PEG and PPG are water-soluble polymers that allow materials to retain good water swellability [43]. A decrease in foaming occurs with an increase in the hydrophilicity of the co-polymers. When the hydrophilicity of the copolymers increased, the micro foams were removed more effectively. Kekevi et al. [43] demonstrate that the uniqueness of these anti-foaming agents is caused by two properties—flexibility, which enhances the acquired conformations that result in efficient packing at various interfaces and lower cohesive energy, which is derived from the cross-sectional area of the siloxane at the interface (Figure 20).
Silicone-based anti-foaming agents.
Beginning of the nineteenth century, sodium dithionate (Na2S2O4) was introduced as a reducing agent for the vat dyeing process [8]. Effective sodium dithionate, also called hydrose, provides an effective reduction in indigo dyes [44]. The amount of Na2S2O4 used in the reduction of indigo dyeing, formed a large amount of by products and sulfite (SO32−) and sulfate (SO42−) ions- (Figure 21).
Oxidation-reduction of indigo.
Stripping methods, mostly used in textile finishing, can remove dye from colored fabric. The process is named as ‘back stripping’ or ‘destructive stripping’. The depth of shade is changed by back stripping; on the other hand, dyes are chemically altered by destructive stripping. Fono and Montclair [45] showed that dyes containing azo groups that can be chemically reduced to an almost colorless amine by using chemical reducing agents. The mechanism of reductive stripping depends on the structure of dyes and fibers and the chemical nature of reducing agents. Chavan [46] explained that different chemical combinations of reducing agents and stripping assistants, which are being used to strip the dye from fabric (Figure 22).
Stripping process of azo dyes.
Sodium formaldehyde sulfoxylate (CH3NaO3S) (Rongalite C) and Rongalite FD are also used as reducing agents in the dyeing industry (Figure 23).
Rongalite FD salts.
As sodium dithionate is highly toxic, many researchers [47] have investigated to replacing it with ecological reducing agents such as glucose, fructose, inverted sugar, and molasses (Figure 24).
Ecological reducing agents.
Many studies have been devoted to catalysts that accelerate the reduction of vat dyes when added to certain reducing agents. BASF-marketed a catalyst, bis-(dimethylglyoximato-diamminocobaltinitrite) for use as a reducing agent.
A softener is a chemical used to make the touch of fabric more pleasing. Softened fabrics are fluffier and have better drape ability. In addition to esthetics, softeners improve abrasion resistance, improve tearing strength, and reduce needle cutting when the garments are sewn. Softeners are divided into three major chemical categories: anionic, cationic, and nonionic. Anionic softeners have a negative charge on the molecule, which comes from the carboxylate group (▬COO▬), sulfate group (▬OSO3▬), or phosphate group (▬PO4−). Fatty alcohol sulfates are made by the reaction of a hydrophobe with sulfuric acid [17] (Figure 25).
Fatty alcohol sulfates formation.
Fewer sulfate groups result in better softeners. Lightly sulfonated oils are sometimes called self-emulsifying because they form turbid water solutions (Figure 26).
Formation of sulfated triglycerides.
Cationic softeners have a positive charge on the large part of the molecule. The amine becomes functionalized under a pH of 7. Quaternary ammonium salts are activated at all pH levels. The ionic interaction causes complete exhaustion from baths and orientation on the fiber surfaces, which cause good slipperiness and reduction in the static charge on the fabric surface. There are several cationic softeners that are usually used in the textile industry, such as fatty amines, fatty amino esters, fatty amino amides, and quaternary ammonium salts (Figure 27).
Synthesis of quaternary ammonium salts.
The nonionic softener has three subcategories: ethylene oxide derivatives, silicones, and hydrocarbon waxes based on paraffin or polyethylene. Polyethylene emulsions are hard, waxy films, which serve to reduce the coefficient of friction. Silicones are polysiloxane polymers. Silicon resembles carbon in which it is tetravalent and forms a covalent bond with other elements (Figure 28).
Reaction of dimethylpolysiloxane.
Crease is formed in cotton fiber because of the intermolecular hydrogen bonding of primary and secondary hydroxyl groups of the polymer chains. The amorphous regions of the hydrogen bonds can easily break down by folding. In the folding state, the broken hydrogen bonds stabilize. Different durable press finishes have been used for many years for use in cotton fabric. N-methylol compounds such as dihydroxyethylene urea react readily with the hydroxyl groups of cellulose chains [48] (Figure 29).
Cross-linking agents based on N-hydroxyethyl and N-alkoxymethyl compounds.
N-Hydroxyethyl acrylamide is also used as a cross-linking agent for cellulosic fibers (Figure 30).
Cross-linking agents based on reactive monomers.
Activated vinyl groups or divinyl sulfone and N, N-methylene-bis-acrylamide are also used cross-linking agents. Divinyl sulfone precursors are used for the cross-linking reaction with cellulose. Cross-linking reactions with epoxides such as epichlorohydrin are mostly used on cellulosic fibers. In addition, aziridine derivatives such as tetramethylene-bis-(N, N-ethylene urea) and trisaziridinyltriazine are effective cross-linking agents [49] (Figure 31).
Cross-linking agents based on aziridine derivatives.
Although considerable research has been conducted regarding dyeing auxiliaries, chemical and other related industries have faced many problems with respect to environmental issues and cost effectiveness for consumers. Although thermodynamic studies of dyeing can make useful contributions to the general theories of intermolecular forces, diffusion processes, and the influence of different parameters such as dye concentration, temperature, dyeing time, and polymer structure remain largely unexplained. When equilibrium studies are carried out and assessed in conjunction with the growing amount of information on the structure of dyeing chemicals and aqueous solutions, their relevance to the dyeing theory should not be underestimated. Due to the lack of chemical knowledge of dyers, quality dyeing is deteriorating with a significant effluent load. This study clearly shows that the different dyeing chemicals used in the dye houses also need investigation to determine the procedures in which the chemicals are used to dye natural and synthetic textiles. This may be a good first step in presenting different chemicals used in the coloration industry.
Cellular senescence is best described as an inevitable irreversible proliferation arrest the phase of primary human fibroblasts in culture [1, 2]. The senescent phenotype is characterized by distinctive changes in morphology to become enlarged, flattened, and granular [2]. Multiple factors that activate senescence include various types of stress-related stimuli such as aberrant oncogenic signaling, oxidative stress, and DNA damage [2]. Moreover, the onset of senescence can be regulated by events such as epigenetic regulation, chromosome dynamics, protein degradation, mitochondrial mechanisms, and metabolic pathways. The molecular pathways of senescence differ considerably among cell types as well as different species [3].
Alternative splicing of pre-mRNAs is a process in which varied mRNA transcripts are generated to provide a major source of protein diversity in higher eukaryotes. Pre-mRNA splicing is a nuclear process that can be constitutive or alternative [4, 5]. Constitutive splicing involves the removal of introns and the joining of adjacent exons in the order of their arrangement. One of the core proteins involved in splicing is hnRNPA1 [5, 6]. Consequently, a single protein may be produced from a single pre-mRNA in constitutive splicing [7]. In contrast, in alternative splicing, the variable use of splice sites permits two or more mature mRNAs to be generated from the same pre-mRNA. Among the nuclear complexes primarily responsible for alternative splicing are heterogeneous nuclear ribonucleoproteins, small nuclear ribonucleoproteins snRNPs, and SR proteins [8, 9]. Splicing factors that play a crucial role through concentration changes or alterations of their expression patterns have significant impacts on mRNA alternative splicing [9, 10].
We have previously found that hnRNP A1 is significantly downregulated in cellular senescence [10] and can regulate the levels of the alternatively spliced
We initiated this study to identify novel targets of hnRNP A1 and to further explore the role of hnRNP A1 in the modulation of gene expression during cellular senescence. The experimental approach used in this study was to identify the
We sought to identify putative mRNA substrates for hnRNP A1 by identifying mRNA sequences that directly bind to the hnRNP A1 protein. We employed a modification of a procedure that had been used for the characterization of RNP complexes by Mili et al. [12]. We isolated hnRNP A1 protein complexes bound to their RNA targets from total young and senescent fibroblast cell lysates. To demonstrate that the complexes represented the majority of hnRNP A1-mRNP complexes found in cellular pools, we measured the mRNA levels of hnRNP A1 and actin in the isolated complexes by RT-PCR. Actin has been previously reported to be in hnRNP A1 RNP complexes; thus, we used actin as a positive control. The results in Figure 1A, show that actin and hnRNP A1 protein were present in lysates isolated from young and senescent IMR-90 fibroblasts. We assessed the protein level of hnRNP A1 in 4B10 RNP complexes isolated from young and senescent protein lysates. 4B10 RNP complexes reflect the results in panel A (Figure 1B) as hnRNP A1 was lower in senescent IMR-90 protein lysates following immunoprecipitation when compared with young cell lysates. These observations indicate that hnRNP A1 was present in the isolated RNP complexes. One known mRNA target of hnRNP A1 is its own RNA; therefore, we measured the level of hnRNP A1 mRNA by RT-PCR (Figure 1
A. Expression of hnRNPA1 in young and old IMR90 fibroblasts. The endogenous level of hnRNP A1 protein is significantly lower in old IMR90 fibroblasts (major band at ~34 kDa is hnRNPA1). Equivalent amounts of protein (20 μg) were loaded. B. Post-immunoprecipitation levels of hnRNPA1 were also low in old cells, see the band at ~34 kDa. C. RT-PCR on cDNA transcribed from RNA isolated complexes, using hnRNPA1 and β-actin primer sets. In both young and old lysates, there appear to be comparable amounts of hnRNPA1 mRNA species in the isolated hnRNPA1-containing complexes.
RNA that was isolated from the hnRNP A1-complexes was reverse transcribed and then amplified by PCR using random decamers to amplify all cDNA sequences. We used two different concentrations of cDNA template for PCR as it was not always possible to visualize PCR products in the senescent samples because the cDNA abundance is typically lower in these cells. There was a correlative increase in PCR products as shown in Figure 2 with an increase in cDNA template. PCR products were then immediately ligated into a pCR2.1cloning vector.
Analysis of hnRNP A1 RNP complexes. A. RNA isolated from hnRNPA1 complexes was reverse transcribed to cDNA and amplified using random decamers as primers for the reaction. No amplification was observed in the absence of cDNA as indicated in the (−) lane.
There may also be a differential availability of hnRNP A1 protein in old cells as hnRNPA1 is modified by post-translational events, such as phosphorylation and methylation [13, 14]. There is an additional possibility that rearrangements of individual components in hnRNPA1-mRNA ribonucleoparticles may change during senescence, which could alter specific and non-specific mRNA sequences bound in the complex.
We then determined the identity of the cloned inserts by sequencing. We found that there were partial mRNA sequences for four human genes bound in young and senescent RNP complexes. The identity of genes was identical for both young and old cells. Scores were considered to be positive if the similarity score was more than 200 [15]. The genes identified were Homo sapiens
PESX analysis. PESX (putative exon spliyancer/silencers) is a utility that can predict regions of an mRNA that may be involved in exon splicing to enhance the inclusion or exclusion of an exon. In addition to the identification of the putative splicing regulatory sequences, the sequences were also scanned for putative hnRNPA1-binding sites [UAG (G/a)] based on known binding sites.
The identification of the human double minute 2 gene (
The human murine double minute 2 (
To determine whether the full-length
HDM2 mRNA variant expression levels. RNA was isolated from co- immunoprecipitated hnRNPA1 protein complexes from young IMR90 fibroblasts and reverse transcribed. Three independent replicates of cDNA were used as templates for detecting
We have previously shown that changes in the expression of hnRNP A1 regulate the alternative splicing and mRNA levels of two mRNA isoforms of the INK4a locus known as p14Arf and p16(INK4a) [10]. Both protein isoforms are growth suppressors and knockout of the INK4a gene allows cells to escape cellular senescence [11]. Our previous studies have shown [9] that overexpression of hnRNA1 results in a preferential expression of the p14Arf mRNA isoform, and an increase in the mRNA levels of both isoforms, thus suggesting a role for hnRNP A1 in control of cell proliferation and senescence [10]. In this study, we assessed the ability of hnRNP A1 to directly bind to INK4a transcripts in hnRNPA1 complexes. For this, we used AR5 cells and PRNS-1 (SV40-transformed clones of HS74 primary human bone marrow fibroblasts) since these cells express high levels of INK4a transcripts as compared with normal IMR-90 fibroblasts [26].
Figure 5 shows that the p16 transcript was amplified from hnRNPA1RNP complexes indicating that hnRNP A1 directly binds to p16 mRNA. We also measured the ability of hnRNP A1 to bind to actin mRNA as a positive control for our co-immunoprecipitation studies. Actin mRNA has been previously identified in hnRNPA1-RNP complexes [12]. Figure 5 shows that in addition to p16, we were also able to detect actin mRNA in the RNP complexes.
Immunoprecipitation of specific
We next sought to determine whether hnRNPA1 modulated the expression of
Expression of
We also investigated whether the protein level of HDM2 was modulated by the level of hnRNP A1 protein expression. To determine whether endogenous hnRNP A1 has an effect on HDM2 protein expression, scrambled siRNA or siA1 was transfected into IMR-90 fibroblast cells. We found that upon siRNA knockdown of hnRNP A1, the protein level of HDM2 was not altered as shown in Figure 7A. hnRNP A2, which has overlapping biochemical activity with hnRNP A1, when inhibited by siRNA interference, did not affect HDM2 expression. On the other hand, overexpression of hnRNP A1 in young cells transfected with GFP-A1 resulted in a slight decrease of HDM2 protein levels and an increase in p53 levels when compared with cells transfected with the GFP-Empty vector (Figure 7B). The increase in p53 protein levels may be a result of the decreased HDM2 expression. A direct correlation between protein and mRNA levels for any given gene is complicated by varying processes. For instance, studies conducted by various groups such as Vogel et al. [28] pointed out that transcription, mRNA export, decay, translation, and protein degradation are key processes in determining steady-state protein concentration [28].
Effect of varying hnRNP A1 expression on HDM2 protein levels a. scrambled siRNA (control), siA1, siA2, or both oligonucleotides were transfected into IMR-90 fibroblast cells. About 30 μg of protein lysates were subjected to 12% SDS-PAGE and immunoblotted for hnRNPA1 and actin. The membranes were stripped and reprobed for total actin levels. B. IMR-90 cells were transiently transfected with GFP-hnRNP A1 and empty vector for 48 hours. Whole-cell lysates were prepared using RIPA lysis buffer. 30 μg of protein lysates were simultaneously subjected to 12% SDS-PAGE and immunoblotted for hnRNP A1, HDM2, p53 and actin. The membranes were stripped and reprobed for total actin levels. C. the relative protein levels was quantified by image density analysis software (image J), and the data were represented as mean value ± SEM (n = 3, and * p < 0.05 value).
Our PESX analysis revealed that hnRNP A1 has a putative binding site within the intronic region between intron 9 and exon 10 of HDM2 (Figure 4). We obtained HDM2 constructs from Dr. Meek (University of Dundee). We performed biotin pull-down assay using MP4 construct that is similar to the MDM2-B isoform lacking p53-binding region followed by Western immunoblotting. We performed the biotin pull-down assay by first incubating the hnRNP A1 antibody (4B10) with Dynabeads Myone streptavidin. We also incubated the Biotinlabeled
The role of hnRNP A1 during cellular senescence is unclear. Significant alterations in its levels, localization, and activity in senescent cells suggest that hnRNP A1 may contribute to the senescent phenotype [27]. However, only a few gene targets are known for hnRNP A1 [12]. This prompted us to search for additional mRNA targets for hnRNP A1 in young and senescent IMR-90 cells. We used an RNA co-immunoprecipitation protocol [12] to identify mRNA new targets for the hnRNP A1 protein. We found that hnRNP A1 is bound to several mRNAs not previously identified. Of particular interest to us was the observation that hnRNP A1 bound to
Posttranscriptional regulation of gene expression is important for the control of cellular processes such as cell proliferation, differentiation, development, and apoptosis [33]. RNA-binding proteins are the main regulators of post-transcriptional regulation [33]. hnRNP A1 is a multifunctional RNA-binding protein implicated in the regulation of major steps in posttranscriptional regulation of gene expression [14]. Upon observation that hnRNP A1 binds to
In this study, our findings suggest that hnRNP A1 binds to the Biotinlabeled
The human lung fibroblast cell strain IMR90 from Coriell, NJ, was subcultured from early passage to terminal passage as previously described by Hubbard and Ozer [43] in Dulbecco’s modified Eagle’s medium and Ham’s F10 medium in a 1:1 mixture supplemented with 10% fetal bovine serum. IMR90 fibroblasts at population doubling <35 were used in all experiments and are considered comparable to young fibroblasts as determined by gene expression profiles previously performed [43]. Senescent IMR90 in all experiments was at a population doubling of 62. For transfection experiments, once cells had reached 90% confluence, either the expression plasmid pEFGP (Control) or pEFGP-A1 was transfected into IMR-90 cells in DMEM/F10 media without FBS/penicillin using Lipofectamine 2000 (Invitrogen) and incubate at 37°C in a CO2 incubator for 6 h.
After RNA was isolated as detailed above, to ensure that there was no genomic contamination, an RNA–PCR procedure was performed. 2 μL of template RNA was added to a PCR mixture using β-actin primers, which would detect genomic sequences if present. The total PCR reaction was composed of 2 μl of template RNA, 5 μl of 10× RT-PCR Buffer (100 mM Tris–HCl, pH 8.3, 500 mM KCl, 15 mM MgCl2), 2.5 μl of dNTP mix (2.5 mM each dNTP), 0.25 μM each PCR primer, 0.5 unit of Thermostable DNA Polymerase (Novagen).
The primers for actin were: actin forward (5′CGCCGCCCTAGGCACCA3′) and actin reverse (5′TTGGCCTTAGGGTTCAGGGGGG 3′). For hnRNPA1, primer set were: hnRNP A1 forward (5′CTAAAGAGCCCGAACAGCTGAG 3′) and hnRNP A1 reverse (5′TCAGTGTCTTCTTTAATGCCACCA 3′). SYBR™ green stain. SYBR™ green can be visualized by blue fluorescence (Molecular Dynamics, Amersham) and quantified with ImageQuant software (Amersham).
Standard Western blotting protocols (Harlow et al. 1999) were to analyze specific proteins [44]. Protein extracts isolated from young and senescent fibroblasts were generated by washing cells were washed 3 times with 1X cold PBS and then, cultures were placed on ice. Cold RIPA (radioimmunoassay buffer containing NP-40 at 1%, sodium deoxycholate at 1%, sodium dodecyl sulfate at 0.1%, NaCl at 150 mM and Tris-HCl at 10 mM with protease inhibitors leupeptin at 0.1 μg/ml, pepstatin at 0.1 μg/ml, and phenylmethylsulfonyl fluoride at 1 mM) was added to culture dishes followed by scraping cells into cold microfuge tubes. The lysate was passed through a 21-gauge syringe needle to ensure complete lysis. Lysates were centrifuged at 10,000×g for 10 minutes at 4°C. The cleared lysate was collected and aliquots were prepared to estimate the amount of protein by the Bradford protein assay (Bio-Rad). Lysates were run on 8–12% acrylamide gels and then transferred in an electroblotting apparatus. Membranes (PVDF, Osmonics) were blocked with 5% non-fat milk in PBS. Monoclonal antibody 4B10 (1:10,000) was used to detect hnRNPA1/A1. An anti-actin monoclonal antibody (1:5000) was obtained from Chemicon. Antibodies specific for HDM2 were graciously provided by Dr. Jill Bargonetti. Secondary antibody, goat IgG, or mouse IgG conjugated with HRP were used for visualization of bands using the ECL kit (Amersham).
Young IMR-90 cells were cultured in 10-cm plates. After approximately 24 h of incubation when the cells reached 90% confluence, the expression plasmid pEFGP (control) or pEFGP-A1 was transfected into IMR-90 cells in DMEM/F10 media without FBS/penicillin using Lipofectamine 2000 (Invitrogen) and incubated at 37°C in CO2 incubator for 6 h. We changed the media to DMEM with FBS and without penicillin and incubated for 48 h at 37°C.
The RNA co-immunoprecipitation protocol was a modified version published by Mili et al. [12] that included a short immunoprecipitation step that minimized degradation of protein-associated RNA.
Real-time PCR experiments on selected genes were performed using an Applied Biosystems 7500 real-time PCR system that utilizes TaqMan gene expression assays for the following genes: mdm2; Human GAPD (GAPDH) Endogenous Control FAM/MGB (4333764F). Reactions were performed according to standard methods using the universal 10X PCR TaqMan mix, at a final reaction volume of 25 μL (Applied Biosystems).
PCR products were ligated into the pCR 2.1 (Invitrogen, TA cloning kit) cloning vector that utilizes the single dT overhangs that are a by-product of PCR reactions catalyzed by Taq polymerase. The ligation reaction was performed at 14°C overnight using T4 DNA ligase and 3 μL of fresh PCR product (Invitrogen protocols).
Vector sequences were subtracted from the sequences obtained. The rest of the sequence was compared against known sequences using the BLAST tool (www.ncbi.nlm.nih.gov). Sequences were chosen based on being previously identified as human genes and either in the coding regions or in the flanking regions of the mRNA sequences of known genes.
Biotinylated transcripts were obtained by reverse transcription with the Maxiscript Kit (Invitrogen) according to manufacturer instructions and as previously described above in Section 3.2. The biotin pull-down assay was performed by first incubating hnRNP A1 antibody (4B10) with Dynabeads Myone streptavidin (Invitrogen) for 1 hour at 4 C. Also, incubated Biotinlabeled
We are grateful to Alisa Chalmers for technical assistance. This research was supported by NIH/NCI U54CA137788/U54CA132378 to KH and to NIH/NIMHD 3G12MD007603-30S2 and NIH RISE R25GM056833 to HM. We also thank Dr. Serafin Pinol-Roma for hnRNP specific antibodies and consultation on the RNA co-immunoprecipitation assays. We also thank Dr. Bargonetti for the HDM2 antibody and Dr. Meek for providing HDM2 plasmid constructs. Heriberto Moran and Shanaz A. Ghandhi contributed equally to this work.
There are no conflicts of interest nor financial interest or benefits.
HDM2 | Human Double Minute 2 |
UTR | Untranslated region |
hnRNPA1 | Heterogeneous nuclear ribonucleoprotein A1 |
RNP | Ribonucleoprotein |
MP4 | Biotin-labeled HDM2 RNA probe |
mRNP | Messenger ribonucleoprotein |
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This chapter explains briefly the fire retardation of wood by using fire retardant coatings.",book:{id:"5827",slug:"new-technologies-in-protective-coatings",title:"New Technologies in Protective Coatings",fullTitle:"New Technologies in Protective Coatings"},signatures:"Thirumal Mariappan",authors:[{id:"198114",title:"Dr.",name:"Thirumal",middleName:null,surname:"Mariappan",slug:"thirumal-mariappan",fullName:"Thirumal Mariappan"}]},{id:"75967",title:"Recent Advances in Ceramic Materials for Dentistry",slug:"recent-advances-in-ceramic-materials-for-dentistry",totalDownloads:811,totalCrossrefCites:0,totalDimensionsCites:0,abstract:"Dental ceramics constitute a heterogeneous group of materials with desirable optical and mechanical proprieties combined with chemical stability. They are inorganic non-metallic materials used in several applications. These materials are biocompatible to tissue, highly esthetic, with satisfying resistance to tensile and shear stress. Over the past years, several developments in new ceramic materials in dental restoration were achieved, including processing techniques and high mechanical properties. Thus, concepts on the structure and strengthening mechanisms of dental ceramic materials are also discussed. The dental practitioner requires best knowledge concerning indications, limitations, and correct use of started materials. The purpose of this book chapter is to overview advances in new ceramic materials and processes, which are used in dentistry. The properties of these materials are also discussed.",book:{id:"9894",slug:"advanced-ceramic-materials",title:"Advanced Ceramic Materials",fullTitle:"Advanced Ceramic Materials"},signatures:"Mohsen Mhadhbi, Faïçal Khlissa and Chaker Bouzidi",authors:[{id:"228366",title:"Dr.",name:"Mohsen",middleName:null,surname:"Mhadhbi",slug:"mohsen-mhadhbi",fullName:"Mohsen Mhadhbi"},{id:"324375",title:"Dr.",name:"Faïçal",middleName:null,surname:"Khlissa",slug:"faical-khlissa",fullName:"Faïçal Khlissa"},{id:"324535",title:"Dr.",name:"Chaker",middleName:null,surname:"Bouzidi",slug:"chaker-bouzidi",fullName:"Chaker Bouzidi"}]},{id:"66615",title:"Survey of Bauxite Resources, Alumina Industry and the Prospects of the Production of Geopolymer Composites from the Resulting by-product",slug:"survey-of-bauxite-resources-alumina-industry-and-the-prospects-of-the-production-of-geopolymer-compo",totalDownloads:1231,totalCrossrefCites:2,totalDimensionsCites:2,abstract:"Guinea is endowed with huge mineral resources. Several geological surveys have identified bauxite, iron, gold, diamond, and several metal ores. Because of the diversity and the magnitude of its resources, the country is referred to as a geological scandal. Nowadays the aluminum industry is still at the quarrying stage of bauxite, the main raw material that is converted into alumina and further to aluminum. Approximately 35–40% of the processed bauxite ore goes into the waste as alkaline red mud RM slurry which consists of 15–40% solids. RM and other industrial wastes material such as fly ash FA, rice husk ash RHA, that poses environmental hazards can be mixed to make them apt for usage in engineering applications. Geopolymers GP represent a new class of materials consisting of Al2O3▬SiO2-based material suitable for several engineering application. The present chapter presents the bauxitic potential of Guinea, the subsequent developing alumina industry. 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She is also the Global Harmonization Initiative (GHI)",institutionString:"Australian College of Business & Technology",institution:{name:"Kobe College",institutionURL:null,country:{name:"Japan"}}}]},{type:"book",id:"6820",title:"Keratin",subtitle:null,coverURL:"https://cdn.intechopen.com/books/images_new/6820.jpg",slug:"keratin",publishedDate:"December 19th 2018",editedByType:"Edited by",bookSignature:"Miroslav Blumenberg",hash:"6def75cd4b6b5324a02b6dc0359896d0",volumeInSeries:2,fullTitle:"Keratin",editors:[{id:"31610",title:"Dr.",name:"Miroslav",middleName:null,surname:"Blumenberg",slug:"miroslav-blumenberg",fullName:"Miroslav Blumenberg",profilePictureURL:"https://mts.intechopen.com/storage/users/31610/images/system/31610.jpg",biography:"Miroslav Blumenberg, Ph.D., was born in Subotica and received his BSc in Belgrade, Yugoslavia. He completed his Ph.D. at MIT in Organic Chemistry; he followed up his Ph.D. with two postdoctoral study periods at Stanford University. Since 1983, he has been a faculty member of the RO Perelman Department of Dermatology, NYU School of Medicine, where he is codirector of a training grant in cutaneous biology. 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"}}}]},{type:"book",id:"7978",title:"Vitamin A",subtitle:null,coverURL:"https://cdn.intechopen.com/books/images_new/7978.jpg",slug:"vitamin-a",publishedDate:"May 15th 2019",editedByType:"Edited by",bookSignature:"Leila Queiroz Zepka, Veridiana Vera de Rosso and Eduardo Jacob-Lopes",hash:"dad04a658ab9e3d851d23705980a688b",volumeInSeries:3,fullTitle:"Vitamin A",editors:[{id:"261969",title:"Dr.",name:"Leila",middleName:null,surname:"Queiroz Zepka",slug:"leila-queiroz-zepka",fullName:"Leila Queiroz Zepka",profilePictureURL:"https://mts.intechopen.com/storage/users/261969/images/system/261969.png",biography:"Prof. Dr. Leila Queiroz Zepka is currently an associate professor in the Department of Food Technology and Science, Federal University of Santa Maria, Brazil. She has more than fifteen years of teaching and research experience. She has published more than 550 scientific publications/communications, including 15 books, 50 book chapters, 100 original research papers, 380 research communications in national and international conferences, and 12 patents. She is a member of the editorial board of five journals and acts as a reviewer for several national and international journals. 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He received his post-doctoral training in oncology and cancer proteomics for two years at the Cancer Research Institute of Human Medical University in China. In 2001, he went to the University of Tennessee Health Science Center (UTHSC) in USA, where he was a post-doctoral researcher and focused on mass spectrometry and cancer proteomics. Then, he was appointed as an Assistant Professor of Neurology, UTHSC in 2005. He moved to the Cleveland Clinic in USA as a Project Scientist/Staff in 2006 where he focused on the studies of eye disease proteomics and biomarkers. He returned to UTHSC as an Assistant Professor of Neurology in the end of 2007, engaging in proteomics and biomarker studies of lung diseases and brain tumors, and initiating the studies of predictive, preventive, and personalized medicine (PPPM) in cancer. In 2010, he was promoted to Associate Professor of Neurology, UTHSC. Currently, he is a Professor at Xiangya Hospital of Central South University in China, Fellow of Royal Society of Medicine (FRSM), the European EPMA National Representative in China, Regular Member of American Association for the Advancement of Science (AAAS), European Cooperation of Science and Technology (e-COST) grant evaluator, Associate Editors of BMC Genomics, BMC Medical Genomics, EPMA Journal, and Frontiers in Endocrinology, Executive Editor-in-Chief of Med One. He has\npublished 116 peer-reviewed research articles, 16 book chapters, 2 books, and 2 US patents. His current main research interest focuses on the studies of cancer proteomics and biomarkers, and the use of modern omics techniques and systems biology for PPPM in cancer, and on the development and use of 2DE-LC/MS for the large-scale study of human proteoforms.",institutionString:null,institution:{name:"Xiangya Hospital Central South University",country:{name:"China"}}},{id:"40482",title:null,name:"Rizwan",middleName:null,surname:"Ahmad",slug:"rizwan-ahmad",fullName:"Rizwan Ahmad",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/40482/images/system/40482.jpeg",biography:"Dr. Rizwan Ahmad is a University Professor and Coordinator, Quality and Development, College of Medicine, Imam Abdulrahman bin Faisal University, Saudi Arabia. Previously, he was Associate Professor of Human Function, Oman Medical College, Oman, and SBS University, Dehradun. Dr. Ahmad completed his education at Aligarh Muslim University, Aligarh. He has published several articles in peer-reviewed journals, chapters, and edited books. His area of specialization is free radical biochemistry and autoimmune diseases.",institutionString:"Imam Abdulrahman Bin Faisal University",institution:{name:"Imam Abdulrahman Bin Faisal University",country:{name:"Saudi Arabia"}}},{id:"41865",title:"Prof.",name:"Farid A.",middleName:null,surname:"Badria",slug:"farid-a.-badria",fullName:"Farid A. Badria",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/41865/images/system/41865.jpg",biography:"Farid A. Badria, Ph.D., is the recipient of several awards, including The World Academy of Sciences (TWAS) Prize for Public Understanding of Science; the World Intellectual Property Organization (WIPO) Gold Medal for best invention; Outstanding Arab Scholar, Kuwait; and the Khwarizmi International Award, Iran. He has 250 publications, 12 books, 20 patents, and several marketed pharmaceutical products to his credit. He continues to lead research projects on developing new therapies for liver, skin disorders, and cancer. Dr. Badria was listed among the world’s top 2% of scientists in medicinal and biomolecular chemistry in 2019 and 2020. He is a member of the Arab Development Fund, Kuwait; International Cell Research Organization–United Nations Educational, Scientific and Cultural Organization (ICRO–UNESCO), Chile; and UNESCO Biotechnology France",institutionString:"Mansoura University",institution:{name:"Mansoura University",country:{name:"Egypt"}}},{id:"329385",title:"Dr.",name:"Rajesh K.",middleName:"Kumar",surname:"Singh",slug:"rajesh-k.-singh",fullName:"Rajesh K. Singh",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/329385/images/system/329385.png",biography:"Dr. Singh received a BPharm (2003) and MPharm (2005) from Panjab University, Chandigarh, India, and a Ph.D. (2013) from Punjab Technical University (PTU), Jalandhar, India. He has more than sixteen years of teaching experience and has supervised numerous postgraduate and Ph.D. students. He has to his credit more than seventy papers in SCI- and SCOPUS-indexed journals, fifty-five conference proceedings, four books, six Best Paper Awards, and five projects from different government agencies. He is currently an editorial board member of eight international journals and a reviewer for more than fifty scientific journals. He received Top Reviewer and Excellent Peer Reviewer Awards from Publons in 2016 and 2017, respectively. He is also on the panel of The International Reviewer for reviewing research proposals for grants from the Royal Society. He also serves as a Publons Academy mentor and Bentham brand ambassador.",institutionString:"Punjab Technical University",institution:{name:"Punjab Technical University",country:{name:"India"}}},{id:"142388",title:"Dr.",name:"Thiago",middleName:"Gomes",surname:"Gomes Heck",slug:"thiago-gomes-heck",fullName:"Thiago Gomes Heck",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/142388/images/7259_n.jpg",biography:null,institutionString:null,institution:{name:"Universidade Regional do Noroeste do Estado do Rio Grande do Sul",country:{name:"Brazil"}}},{id:"336273",title:"Assistant Prof.",name:"Janja",middleName:null,surname:"Zupan",slug:"janja-zupan",fullName:"Janja Zupan",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/336273/images/14853_n.jpeg",biography:"Janja Zupan graduated in 2005 at the Department of Clinical Biochemistry (superviser prof. dr. Janja Marc) in the field of genetics of osteoporosis. Since November 2009 she is working as a Teaching Assistant at the Faculty of Pharmacy, Department of Clinical Biochemistry. In 2011 she completed part of her research and PhD work at Institute of Genetics and Molecular Medicine, University of Edinburgh. She finished her PhD entitled The influence of the proinflammatory cytokines on the RANK/RANKL/OPG in bone tissue of osteoporotic and osteoarthritic patients in 2012. From 2014-2016 she worked at the Institute of Biomedical Sciences, University of Aberdeen as a postdoctoral research fellow on UK Arthritis research project where she gained knowledge in mesenchymal stem cells and regenerative medicine. She returned back to University of Ljubljana, Faculty of Pharmacy in 2016. She is currently leading project entitled Mesenchymal stem cells-the keepers of tissue endogenous regenerative capacity facing up to aging of the musculoskeletal system funded by Slovenian Research Agency.",institutionString:null,institution:{name:"University of Ljubljana",country:{name:"Slovenia"}}},{id:"357453",title:"Dr.",name:"Radheshyam",middleName:null,surname:"Maurya",slug:"radheshyam-maurya",fullName:"Radheshyam Maurya",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/357453/images/16535_n.jpg",biography:null,institutionString:null,institution:{name:"University of Hyderabad",country:{name:"India"}}},{id:"418340",title:"Dr.",name:"Jyotirmoi",middleName:null,surname:"Aich",slug:"jyotirmoi-aich",fullName:"Jyotirmoi Aich",position:null,profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0033Y000038Ugi5QAC/Profile_Picture_2022-04-15T07:48:28.png",biography:"Biotechnologist with 15 years of research including 6 years of teaching experience. Demonstrated record of scientific achievements through consistent publication record (H index = 13, with 874 citations) in high impact journals such as Nature Communications, Oncotarget, Annals of Oncology, PNAS, and AJRCCM, etc. Strong research professional with a post-doctorate from ACTREC where I gained experimental oncology experience in clinical settings and a doctorate from IGIB where I gained expertise in asthma pathophysiology. A well-trained biotechnologist with diverse experience on the bench across different research themes ranging from asthma to cancer and other infectious diseases. An individual with a strong commitment and innovative mindset. Have the ability to work on diverse projects such as regenerative and molecular medicine with an overall mindset of improving healthcare.",institutionString:"DY Patil Deemed to Be University",institution:null},{id:"349288",title:"Prof.",name:"Soumya",middleName:null,surname:"Basu",slug:"soumya-basu",fullName:"Soumya Basu",position:null,profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0033Y000035QxIDQA0/Profile_Picture_2022-04-15T07:47:01.jpg",biography:"Soumya Basu, Ph.D., is currently working as an Associate Professor at Dr. D. Y. Patil Biotechnology and Bioinformatics Institute, Dr. D. Y. Patil Vidyapeeth, Pune, Maharashtra, India. With 16+ years of trans-disciplinary research experience in Drug Design, development, and pre-clinical validation; 20+ research article publications in journals of repute, 9+ years of teaching experience, trained with cross-disciplinary education, Dr. Basu is a life-long learner and always thrives for new challenges.\r\nHer research area is the design and synthesis of small molecule partial agonists of PPAR-γ in lung cancer. She is also using artificial intelligence and deep learning methods to understand the exosomal miRNA’s role in cancer metastasis. Dr. Basu is the recipient of many awards including the Early Career Research Award from the Department of Science and Technology, Govt. of India. She is a reviewer of many journals like Molecular Biology Reports, Frontiers in Oncology, RSC Advances, PLOS ONE, Journal of Biomolecular Structure & Dynamics, Journal of Molecular Graphics and Modelling, etc. She has edited and authored/co-authored 21 journal papers, 3 book chapters, and 15 abstracts. She is a Board of Studies member at her university. She is a life member of 'The Cytometry Society”-in India and 'All India Cell Biology Society”- in India.",institutionString:"Dr. D.Y. Patil Vidyapeeth, Pune",institution:{name:"Dr. D.Y. Patil Vidyapeeth, Pune",country:{name:"India"}}},{id:"354817",title:"Dr.",name:"Anubhab",middleName:null,surname:"Mukherjee",slug:"anubhab-mukherjee",fullName:"Anubhab Mukherjee",position:null,profilePictureURL:"https://intech-files.s3.amazonaws.com/0033Y0000365PbRQAU/ProfilePicture%202022-04-15%2005%3A11%3A18.480",biography:"A former member of Laboratory of Nanomedicine, Brigham and Women’s Hospital, Harvard University, Boston, USA, Dr. Anubhab Mukherjee is an ardent votary of science who strives to make an impact in the lives of those afflicted with cancer and other chronic/acute ailments. He completed his Ph.D. from CSIR-Indian Institute of Chemical Technology, Hyderabad, India, having been skilled with RNAi, liposomal drug delivery, preclinical cell and animal studies. He pursued post-doctoral research at College of Pharmacy, Health Science Center, Texas A & M University and was involved in another postdoctoral research at Department of Translational Neurosciences and Neurotherapeutics, John Wayne Cancer Institute, Santa Monica, California. In 2015, he worked in Harvard-MIT Health Sciences & Technology as a visiting scientist. He has substantial experience in nanotechnology-based formulation development and successfully served various Indian organizations to develop pharmaceuticals and nutraceutical products. He is an inventor in many US patents and an author in many peer-reviewed articles, book chapters and books published in various media of international repute. Dr. Mukherjee is currently serving as Principal Scientist, R&D at Esperer Onco Nutrition (EON) Pvt. Ltd. and heads the Hyderabad R&D center of the organization.",institutionString:"Esperer Onco Nutrition Pvt Ltd.",institution:null},{id:"319365",title:"Assistant Prof.",name:"Manash K.",middleName:null,surname:"Paul",slug:"manash-k.-paul",fullName:"Manash K. Paul",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/319365/images/system/319365.png",biography:"Manash K. Paul is a Principal Investigator and Scientist at the University of California Los Angeles. He has contributed significantly to the fields of stem cell biology, regenerative medicine, and lung cancer. His research focuses on various signaling processes involved in maintaining stem cell homeostasis during the injury-repair process, deciphering lung stem cell niche, pulmonary disease modeling, immuno-oncology, and drug discovery. He is currently investigating the role of extracellular vesicles in premalignant lung cell migration and detecting the metastatic phenotype of lung cancer via machine-learning-based analyses of exosomal signatures. Dr. Paul has published in more than fifty peer-reviewed international journals and is highly cited. He is the recipient of many awards, including the UCLA Vice Chancellor’s award, a senior member of the Institute of Electrical and Electronics Engineers (IEEE), and an editorial board member for several international journals.",institutionString:"University of California Los Angeles",institution:{name:"University of California Los Angeles",country:{name:"United States of America"}}},{id:"311457",title:"Dr.",name:"Júlia",middleName:null,surname:"Scherer Santos",slug:"julia-scherer-santos",fullName:"Júlia Scherer Santos",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/311457/images/system/311457.jpg",biography:"Dr. Júlia Scherer Santos works in the areas of cosmetology, nanotechnology, pharmaceutical technology, beauty, and aesthetics. Dr. Santos also has experience as a professor of graduate courses. Graduated in Pharmacy, specialization in Cosmetology and Cosmeceuticals applied to aesthetics, specialization in Aesthetic and Cosmetic Health, and a doctorate in Pharmaceutical Nanotechnology. Teaching experience in Pharmacy and Aesthetics and Cosmetics courses. She works mainly on the following subjects: nanotechnology, cosmetology, pharmaceutical technology, aesthetics.",institutionString:"Universidade Federal de Juiz de Fora",institution:{name:"Universidade Federal de Juiz de Fora",country:{name:"Brazil"}}},{id:"219081",title:"Dr.",name:"Abdulsamed",middleName:null,surname:"Kükürt",slug:"abdulsamed-kukurt",fullName:"Abdulsamed Kükürt",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/219081/images/system/219081.png",biography:"Dr. Kükürt graduated from Uludağ University in Turkey. He started his academic career as a Research Assistant in the Department of Biochemistry at Kafkas University. In 2019, he completed his Ph.D. program in the Department of Biochemistry at the Institute of Health Sciences. He is currently working at the Department of Biochemistry, Kafkas University. He has 27 published research articles in academic journals, 11 book chapters, and 37 papers. He took part in 10 academic projects. He served as a reviewer for many articles. He still serves as a member of the review board in many academic journals. He is currently working on the protective activity of phenolic compounds in disorders associated with oxidative stress and inflammation.",institutionString:null,institution:{name:"Kafkas University",country:{name:"Turkey"}}},{id:"178366",title:"Dr.",name:"Volkan",middleName:null,surname:"Gelen",slug:"volkan-gelen",fullName:"Volkan Gelen",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/178366/images/system/178366.jpg",biography:"Volkan Gelen is a Physiology specialist who received his veterinary degree from Kafkas University in 2011. Between 2011-2015, he worked as an assistant at Atatürk University, Faculty of Veterinary Medicine, Department of Physiology. In 2016, he joined Kafkas University, Faculty of Veterinary Medicine, Department of Physiology as an assistant professor. Dr. Gelen has been engaged in various academic activities at Kafkas University since 2016. There he completed 5 projects and has 3 ongoing projects. He has 60 articles published in scientific journals and 20 poster presentations in scientific congresses. His research interests include physiology, endocrine system, cancer, diabetes, cardiovascular system diseases, and isolated organ bath system studies.",institutionString:"Kafkas University",institution:{name:"Kafkas University",country:{name:"Turkey"}}},{id:"418963",title:"Dr.",name:"Augustine Ododo",middleName:"Augustine",surname:"Osagie",slug:"augustine-ododo-osagie",fullName:"Augustine Ododo Osagie",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/418963/images/16900_n.jpg",biography:"Born into the family of Osagie, a prince of the Benin Kingdom. I am currently an academic in the Department of Medical Biochemistry, University of Benin. Part of the duties are to teach undergraduate students and conduct academic research.",institutionString:null,institution:{name:"University of Benin",country:{name:"Nigeria"}}},{id:"192992",title:"Prof.",name:"Shagufta",middleName:null,surname:"Perveen",slug:"shagufta-perveen",fullName:"Shagufta Perveen",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/192992/images/system/192992.png",biography:"Prof. Shagufta Perveen is a Distinguish Professor in the Department of Pharmacognosy, College of Pharmacy, King Saud University, Riyadh, Saudi Arabia. Dr. Perveen has acted as the principal investigator of major research projects funded by the research unit of King Saud University. She has more than ninety original research papers in peer-reviewed journals of international repute to her credit. She is a fellow member of the Royal Society of Chemistry UK and the American Chemical Society of the United States.",institutionString:"King Saud University",institution:{name:"King Saud University",country:{name:"Saudi Arabia"}}},{id:"49848",title:"Dr.",name:"Wen-Long",middleName:null,surname:"Hu",slug:"wen-long-hu",fullName:"Wen-Long Hu",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/49848/images/system/49848.jpg",biography:"Wen-Long Hu is Chief of the Division of Acupuncture, Department of Chinese Medicine at Kaohsiung Chang Gung Memorial Hospital, as well as an adjunct associate professor at Fooyin University and Kaohsiung Medical University. Wen-Long is President of Taiwan Traditional Chinese Medicine Medical Association. He has 28 years of experience in clinical practice in laser acupuncture therapy and 34 years in acupuncture. He is an invited speaker for lectures and workshops in laser acupuncture at many symposiums held by medical associations. He owns the patent for herbal preparation and producing, and for the supercritical fluid-treated needle. Dr. Hu has published three books, 12 book chapters, and more than 30 papers in reputed journals, besides serving as an editorial board member of repute.",institutionString:"Kaohsiung Chang Gung Memorial Hospital",institution:{name:"Kaohsiung Chang Gung Memorial Hospital",country:{name:"Taiwan"}}},{id:"298472",title:"Prof.",name:"Andrey V.",middleName:null,surname:"Grechko",slug:"andrey-v.-grechko",fullName:"Andrey V. Grechko",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/298472/images/system/298472.png",biography:"Andrey Vyacheslavovich Grechko, Ph.D., Professor, is a Corresponding Member of the Russian Academy of Sciences. He graduated from the Semashko Moscow Medical Institute (Semashko National Research Institute of Public Health) with a degree in Medicine (1998), the Clinical Department of Dermatovenerology (2000), and received a second higher education in Psychology (2009). Professor A.V. Grechko held the position of Сhief Physician of the Central Clinical Hospital in Moscow. He worked as a professor at the faculty and was engaged in scientific research at the Medical University. Starting in 2013, he has been the initiator of the creation of the Federal Scientific and Clinical Center for Intensive Care and Rehabilitology, Moscow, Russian Federation, where he also serves as Director since 2015. He has many years of experience in research and teaching in various fields of medicine, is an author/co-author of more than 200 scientific publications, 13 patents, 15 medical books/chapters, including Chapter in Book «Metabolomics», IntechOpen, 2020 «Metabolomic Discovery of Microbiota Dysfunction as the Cause of Pathology».",institutionString:"Federal Research and Clinical Center of Intensive Care Medicine and Rehabilitology",institution:null},{id:"199461",title:"Prof.",name:"Natalia V.",middleName:null,surname:"Beloborodova",slug:"natalia-v.-beloborodova",fullName:"Natalia V. Beloborodova",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/199461/images/system/199461.jpg",biography:'Natalia Vladimirovna Beloborodova was educated at the Pirogov Russian National Research Medical University, with a degree in pediatrics in 1980, a Ph.D. in 1987, and a specialization in Clinical Microbiology from First Moscow State Medical University in 2004. She has been a Professor since 1996. Currently, she is the Head of the Laboratory of Metabolism, a division of the Federal Research and Clinical Center of Intensive Care Medicine and Rehabilitology, Moscow, Russian Federation. N.V. Beloborodova has many years of clinical experience in the field of intensive care and surgery. She studies infectious complications and sepsis. She initiated a series of interdisciplinary clinical and experimental studies based on the concept of integrating human metabolism and its microbiota. Her scientific achievements are widely known: she is the recipient of the Marie E. Coates Award \\"Best lecturer-scientist\\" Gustafsson Fund, Karolinska Institutes, Stockholm, Sweden, and the International Sepsis Forum Award, Pasteur Institute, Paris, France (2014), etc. Professor N.V. Beloborodova wrote 210 papers, five books, 10 chapters and has edited four books.',institutionString:"Federal Research and Clinical Center of Intensive Care Medicine and Rehabilitology",institution:null},{id:"354260",title:"Ph.D.",name:"Tércio Elyan",middleName:"Azevedo",surname:"Azevedo Martins",slug:"tercio-elyan-azevedo-martins",fullName:"Tércio Elyan Azevedo Martins",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/354260/images/16241_n.jpg",biography:"Graduated in Pharmacy from the Federal University of Ceará with the modality in Industrial Pharmacy, Specialist in Production and Control of Medicines from the University of São Paulo (USP), Master in Pharmaceuticals and Medicines from the University of São Paulo (USP) and Doctor of Science in the program of Pharmaceuticals and Medicines by the University of São Paulo. Professor at Universidade Paulista (UNIP) in the areas of chemistry, cosmetology and trichology. Assistant Coordinator of the Higher Course in Aesthetic and Cosmetic Technology at Universidade Paulista Campus Chácara Santo Antônio. Experience in the Pharmacy area, with emphasis on Pharmacotechnics, Pharmaceutical Technology, Research and Development of Cosmetics, acting mainly on topics such as cosmetology, antioxidant activity, aesthetics, photoprotection, cyclodextrin and thermal analysis.",institutionString:null,institution:{name:"University of Sao Paulo",country:{name:"Brazil"}}},{id:"334285",title:"Ph.D. Student",name:"Sameer",middleName:"Kumar",surname:"Jagirdar",slug:"sameer-jagirdar",fullName:"Sameer Jagirdar",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/334285/images/14691_n.jpg",biography:"I\\'m a graduate student at the center for biosystems science and engineering at the Indian Institute of Science, Bangalore, India. I am interested in studying host-pathogen interactions at the biomaterial interface.",institutionString:null,institution:{name:"Indian Institute of Science Bangalore",country:{name:"India"}}},{id:"329248",title:"Dr.",name:"Md. Faheem",middleName:null,surname:"Haider",slug:"md.-faheem-haider",fullName:"Md. Faheem Haider",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/329248/images/system/329248.jpg",biography:"Dr. Md. Faheem Haider completed his BPharm in 2012 at Integral University, Lucknow, India. In 2014, he completed his MPharm with specialization in Pharmaceutics at Babasaheb Bhimrao Ambedkar University, Lucknow, India. He received his Ph.D. degree from Jamia Hamdard University, New Delhi, India, in 2018. He was selected for the GPAT six times and his best All India Rank was 34. Currently, he is an assistant professor at Integral University. Previously he was an assistant professor at IIMT University, Meerut, India. He has experience teaching DPharm, Pharm.D, BPharm, and MPharm students. He has more than five publications in reputed journals to his credit. Dr. Faheem’s research area is the development and characterization of nanoformulation for the delivery of drugs to various organs.",institutionString:"Integral University",institution:{name:"Integral University",country:{name:"India"}}},{id:"329795",title:"Dr.",name:"Mohd Aftab",middleName:"Aftab",surname:"Siddiqui",slug:"mohd-aftab-siddiqui",fullName:"Mohd Aftab Siddiqui",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/329795/images/system/329795.png",biography:"Dr. Mohd Aftab Siddiqui is an assistant professor in the Faculty of Pharmacy, Integral University, Lucknow, India, where he obtained a Ph.D. in Pharmacology in 2020. He also obtained a BPharm and MPharm from the same university in 2013 and 2015, respectively. His area of research is the pharmacological screening of herbal drugs/natural products in liver cancer and cardiac diseases. He is a member of many professional bodies and has guided many MPharm and PharmD research projects. Dr. Siddiqui has many national and international publications and one German patent to his credit.",institutionString:"Integral University",institution:null}]}},subseries:{item:{id:"2",type:"subseries",title:"Prosthodontics and Implant Dentistry",keywords:"Osseointegration, Hard Tissue, Peri-implant Soft Tissue, Restorative Materials, Prosthesis Design, Prosthesis, Patient Satisfaction, Rehabilitation",scope:"