We are analyzing https://link.springer.com/article/10.1007/s00018-019-03237-8.

Title:
An interplay of structure and intrinsic disorder in the functionality of peptidylarginine deiminases, a family of key autoimmunity-related enzymes | Cellular and Molecular Life Sciences
Description:
Citrullination is a post-translation modification of proteins, where the proteinaceous arginine residues are converted to non-coded citrulline residues. The immune tolerance to such citrullinated protein can be lost, leading to inflammatory and autoimmune diseases. Citrullination is a chemical reaction mediated by peptidylarginine deiminase enzymes (PADs), which are a family of calcium-dependent cysteine hydrolase enzymes that includes five isotypes: PAD1, PAD2, PAD3, PAD4, and PAD6. Each PAD has specific substrates and tissue distribution, where it modifies the arginine to produce a citrullinated protein with altered structure and function. All mammalian PADs have a sequence similarity of about 70–95%, whereas in humans, they are 50–55% homologous in their structure and amino acid sequences. Being calcium-dependent hydrolases, PADs are inactive under the physiological level of calcium, but could be activated due to distortions in calcium homeostasis, or when the cellular calcium levels are increased. In this article, we analyze some of the currently available data on the structural properties of human PADs, the mechanisms of their calcium-induced activation, and show that these proteins contain functionally important regions of intrinsic disorder. Citrullination represents an important trigger of multiple physiological and pathological processes, and as a result, PADs are recognized to play a number of important roles in autoimmune diseases, cancer, and neurodegeneration. Therefore, we also review the current state of the art in the development of PAD inhibitors with good potency and selectivity.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

Education
Science
Health & Fitness

Content Management System {📝}

What CMS is link.springer.com built with?

Custom-built

No common CMS systems were detected on Link.springer.com, and no known web development framework was identified.

Traffic Estimate {📈}

What is the average monthly size of link.springer.com audience?

🌠 Phenomenal Traffic: 5M - 10M visitors per month

Based on our best estimate, this website will receive around 5,000,019 visitors per month in the current month.
However, some sources were not loaded, we suggest to reload the page to get complete results.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

How Does Link.springer.com Make Money? {💸}

We can't see how the site brings in money.

Not all websites are made for profit; some exist to inform or educate users. Or any other reason why people make websites. And this might be the case. Link.springer.com might be plotting its profit, but the way they're doing it isn't detectable yet.

Keywords {🔍}

pubmed, google, scholar, cas, central, protein, deiminase, biol, peptidylarginine, pad, proteins, thompson, cell, arginine, chem, human, arthritis, rheumatoid, citrullination, van, res, uversky, calcium, disease, sci, article, mol, deimination, immunol, thioredoxin, deiminases, knuckley, role, extracellular, molecular, structure, disorder, coonrod, health, biochem, database, research, enzymes, citrullinated, physiological, structural, inhibitors, biophys, jones, rev,

Topics {✒️}

post-translational modification detect post-translational modifications sequential post-translational modifications phosphorylation-dependent interaction dna-encoded small-molecule libraries /books/psoriasis-a-systemic-disease/peptidylarginine-deiminases histidine-rich ca2+-binding protein small-angle x-ray scattering thioredoxin-target recognition post-translation modification universal entropy-driven mechanism month download article/chapter fluopol-abpp hts assay molecular diagnostics-e-book calcium-dependent hydrolases key autoimmunity-related enzymes fluoroacetamidine-based inactivator calcium-dependent properties carbon dioxide/bicarbonate/ph reverse protonation mechanism calcium ionophore-induced apoptosis haloacetamidine-based inactivators substrate-assisted mechanism apoptosis signal-regulating kinase peptidy l-arginine deiminase ros-generating nadph oxidases mrna-msy2 complex murine collagen-induced arthritis check access instant access protein binding regions proteins based interaction aggregatibacter actinomycetemcomitans leukotoxin posttranslational modification visual molecular dynamics usage analysis sequence analysis functionality calcium binding properties identify pad substrates functional analysis protein research department calcium-binding sites structural properties privacy choices/manage cookies cellular calcium levels identify pad inhibitors calcium binding proteins protein arginine deiminase

Questions {❓}

Bellingan GJ, Laurent GJ (2008) Fate of macrophages once having ingested apoptotic cells: lymphatic clearance or in situ apoptosis?
Gazitt T, Lood C, Elkon KB (2016) Citrullination in rheumatoid arthritis—a process promoted by neutrophil lysis?
How neutrophils die or survive along NET release and is “NETosis” = necroptosis?
Lange S, Gallagher M, Kholia S, Kosgodage US, Hristova M, Hardy J, Inal JM (2017) Peptidylarginine deiminases-roles in cancer and neurodegeneration and possible avenues for therapeutic intervention via modulation of exosome and microvesicle (EMV) release?
Proskuryakov SY, Konoplyannikov AG, Gabai VL (2003) Necrosis: a specific form of programmed cell death?
Selective inhibition of peptidyl-arginine deiminase (PAD): can it control multiple inflammatory disorders as a promising therapeutic strategy?

Schema {🗺️}

WebPage:
      mainEntity:
         headline:An interplay of structure and intrinsic disorder in the functionality of peptidylarginine deiminases, a family of key autoimmunity-related enzymes
         description:Citrullination is a post-translation modification of proteins, where the proteinaceous arginine residues are converted to non-coded citrulline residues. The immune tolerance to such citrullinated protein can be lost, leading to inflammatory and autoimmune diseases. Citrullination is a chemical reaction mediated by peptidylarginine deiminase enzymes (PADs), which are a family of calcium-dependent cysteine hydrolase enzymes that includes five isotypes: PAD1, PAD2, PAD3, PAD4, and PAD6. Each PAD has specific substrates and tissue distribution, where it modifies the arginine to produce a citrullinated protein with altered structure and function. All mammalian PADs have a sequence similarity of about 70–95%, whereas in humans, they are 50–55% homologous in their structure and amino acid sequences. Being calcium-dependent hydrolases, PADs are inactive under the physiological level of calcium, but could be activated due to distortions in calcium homeostasis, or when the cellular calcium levels are increased. In this article, we analyze some of the currently available data on the structural properties of human PADs, the mechanisms of their calcium-induced activation, and show that these proteins contain functionally important regions of intrinsic disorder. Citrullination represents an important trigger of multiple physiological and pathological processes, and as a result, PADs are recognized to play a number of important roles in autoimmune diseases, cancer, and neurodegeneration. Therefore, we also review the current state of the art in the development of PAD inhibitors with good potency and selectivity.
         datePublished:2019-07-24T00:00:00Z
         dateModified:2019-07-24T00:00:00Z
         pageStart:4635
         pageEnd:4662
         sameAs:https://doi.org/10.1007/s00018-019-03237-8
         keywords:
            Calcium-dependent protein
            Disorder-based functionality
            Eukaryotic linear motif
            Inactivation mechanism
            Molecular recognition feature
            MoRF
            PAD activity
            PAD inhibitor
            Post-translational modification
            Protein–protein interaction
            PTM
            Structural analysis
            Structural disorder
            Cell Biology
            Biomedicine
            general
            Life Sciences
            Biochemistry
         image:
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig1_HTML.png
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig2_HTML.png
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig3_HTML.png
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig4_HTML.png
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig5_HTML.png
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig6_HTML.png
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig7_HTML.png
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig8_HTML.png
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig9_HTML.png
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig10_HTML.png
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig11_HTML.png
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig12_HTML.png
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig13_HTML.png
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig14_HTML.png
         isPartOf:
            name:Cellular and Molecular Life Sciences
            issn:
               1420-9071
               1420-682X
            volumeNumber:76
            type:
               Periodical
               PublicationVolume
         publisher:
            name:Springer International Publishing
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:Mohammed Alghamdi
               affiliation:
                     name:King Abdulaziz University
                     address:
                        name:Biological Sciences Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia
                        type:PostalAddress
                     type:Organization
                     name:King Abdulaziz University
                     address:
                        name:Laboratory Department, University Medical Services Center, King Abdulaziz University, Jeddah, Saudi Arabia
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Khaled A. Al Ghamdi
               affiliation:
                     name:King Abdulaziz University
                     address:
                        name:Biological Sciences Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Rizwan H. Khan
               affiliation:
                     name:Aligarh Muslim University
                     address:
                        name:Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, India
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Vladimir N. Uversky
               affiliation:
                     name:King Abdulaziz University
                     address:
                        name:Biological Sciences Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia
                        type:PostalAddress
                     type:Organization
                     name:Institute for Biological Instrumentation of the Russian Academy of Sciences
                     address:
                        name:Protein Research Group, Institute for Biological Instrumentation of the Russian Academy of Sciences, Pushchino, Russia
                        type:PostalAddress
                     type:Organization
                     name:University of South Florida
                     address:
                        name:Department of Molecular Medicine and USF Health Byrd Alzheimer’s Research Institute, Morsani College of Medicine, University of South Florida, Tampa, USA
                        type:PostalAddress
                     type:Organization
               email:[email protected]
               type:Person
               name:Elrashdy M. Redwan
               url:http://orcid.org/0000-0001-8246-0075
               affiliation:
                     name:King Abdulaziz University
                     address:
                        name:Biological Sciences Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia
                        type:PostalAddress
                     type:Organization
                     name:City for Scientific Research and Technology Applications
                     address:
                        name:Therapeutic and Protective Proteins Laboratory, Protein Research Department, Genetic Engineering and Biotechnology Research Institute, City for Scientific Research and Technology Applications, Alexandria, Egypt
                        type:PostalAddress
                     type:Organization
               email:[email protected]
               type:Person
         isAccessibleForFree:
         hasPart:
            isAccessibleForFree:
            cssSelector:.main-content
            type:WebPageElement
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:An interplay of structure and intrinsic disorder in the functionality of peptidylarginine deiminases, a family of key autoimmunity-related enzymes
      description:Citrullination is a post-translation modification of proteins, where the proteinaceous arginine residues are converted to non-coded citrulline residues. The immune tolerance to such citrullinated protein can be lost, leading to inflammatory and autoimmune diseases. Citrullination is a chemical reaction mediated by peptidylarginine deiminase enzymes (PADs), which are a family of calcium-dependent cysteine hydrolase enzymes that includes five isotypes: PAD1, PAD2, PAD3, PAD4, and PAD6. Each PAD has specific substrates and tissue distribution, where it modifies the arginine to produce a citrullinated protein with altered structure and function. All mammalian PADs have a sequence similarity of about 70–95%, whereas in humans, they are 50–55% homologous in their structure and amino acid sequences. Being calcium-dependent hydrolases, PADs are inactive under the physiological level of calcium, but could be activated due to distortions in calcium homeostasis, or when the cellular calcium levels are increased. In this article, we analyze some of the currently available data on the structural properties of human PADs, the mechanisms of their calcium-induced activation, and show that these proteins contain functionally important regions of intrinsic disorder. Citrullination represents an important trigger of multiple physiological and pathological processes, and as a result, PADs are recognized to play a number of important roles in autoimmune diseases, cancer, and neurodegeneration. Therefore, we also review the current state of the art in the development of PAD inhibitors with good potency and selectivity.
      datePublished:2019-07-24T00:00:00Z
      dateModified:2019-07-24T00:00:00Z
      pageStart:4635
      pageEnd:4662
      sameAs:https://doi.org/10.1007/s00018-019-03237-8
      keywords:
         Calcium-dependent protein
         Disorder-based functionality
         Eukaryotic linear motif
         Inactivation mechanism
         Molecular recognition feature
         MoRF
         PAD activity
         PAD inhibitor
         Post-translational modification
         Protein–protein interaction
         PTM
         Structural analysis
         Structural disorder
         Cell Biology
         Biomedicine
         general
         Life Sciences
         Biochemistry
      image:
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig1_HTML.png
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig2_HTML.png
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig3_HTML.png
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig4_HTML.png
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig5_HTML.png
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig6_HTML.png
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig7_HTML.png
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig8_HTML.png
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig9_HTML.png
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig10_HTML.png
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig11_HTML.png
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig12_HTML.png
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig13_HTML.png
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-019-03237-8/MediaObjects/18_2019_3237_Fig14_HTML.png
      isPartOf:
         name:Cellular and Molecular Life Sciences
         issn:
            1420-9071
            1420-682X
         volumeNumber:76
         type:
            Periodical
            PublicationVolume
      publisher:
         name:Springer International Publishing
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Mohammed Alghamdi
            affiliation:
                  name:King Abdulaziz University
                  address:
                     name:Biological Sciences Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia
                     type:PostalAddress
                  type:Organization
                  name:King Abdulaziz University
                  address:
                     name:Laboratory Department, University Medical Services Center, King Abdulaziz University, Jeddah, Saudi Arabia
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Khaled A. Al Ghamdi
            affiliation:
                  name:King Abdulaziz University
                  address:
                     name:Biological Sciences Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Rizwan H. Khan
            affiliation:
                  name:Aligarh Muslim University
                  address:
                     name:Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, India
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Vladimir N. Uversky
            affiliation:
                  name:King Abdulaziz University
                  address:
                     name:Biological Sciences Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia
                     type:PostalAddress
                  type:Organization
                  name:Institute for Biological Instrumentation of the Russian Academy of Sciences
                  address:
                     name:Protein Research Group, Institute for Biological Instrumentation of the Russian Academy of Sciences, Pushchino, Russia
                     type:PostalAddress
                  type:Organization
                  name:University of South Florida
                  address:
                     name:Department of Molecular Medicine and USF Health Byrd Alzheimer’s Research Institute, Morsani College of Medicine, University of South Florida, Tampa, USA
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
            name:Elrashdy M. Redwan
            url:http://orcid.org/0000-0001-8246-0075
            affiliation:
                  name:King Abdulaziz University
                  address:
                     name:Biological Sciences Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia
                     type:PostalAddress
                  type:Organization
                  name:City for Scientific Research and Technology Applications
                  address:
                     name:Therapeutic and Protective Proteins Laboratory, Protein Research Department, Genetic Engineering and Biotechnology Research Institute, City for Scientific Research and Technology Applications, Alexandria, Egypt
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
["Periodical","PublicationVolume"]:
      name:Cellular and Molecular Life Sciences
      issn:
         1420-9071
         1420-682X
      volumeNumber:76
Organization:
      name:Springer International Publishing
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:King Abdulaziz University
      address:
         name:Biological Sciences Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia
         type:PostalAddress
      name:King Abdulaziz University
      address:
         name:Laboratory Department, University Medical Services Center, King Abdulaziz University, Jeddah, Saudi Arabia
         type:PostalAddress
      name:King Abdulaziz University
      address:
         name:Biological Sciences Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia
         type:PostalAddress
      name:Aligarh Muslim University
      address:
         name:Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, India
         type:PostalAddress
      name:King Abdulaziz University
      address:
         name:Biological Sciences Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia
         type:PostalAddress
      name:Institute for Biological Instrumentation of the Russian Academy of Sciences
      address:
         name:Protein Research Group, Institute for Biological Instrumentation of the Russian Academy of Sciences, Pushchino, Russia
         type:PostalAddress
      name:University of South Florida
      address:
         name:Department of Molecular Medicine and USF Health Byrd Alzheimer’s Research Institute, Morsani College of Medicine, University of South Florida, Tampa, USA
         type:PostalAddress
      name:King Abdulaziz University
      address:
         name:Biological Sciences Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia
         type:PostalAddress
      name:City for Scientific Research and Technology Applications
      address:
         name:Therapeutic and Protective Proteins Laboratory, Protein Research Department, Genetic Engineering and Biotechnology Research Institute, City for Scientific Research and Technology Applications, Alexandria, Egypt
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Mohammed Alghamdi
      affiliation:
            name:King Abdulaziz University
            address:
               name:Biological Sciences Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia
               type:PostalAddress
            type:Organization
            name:King Abdulaziz University
            address:
               name:Laboratory Department, University Medical Services Center, King Abdulaziz University, Jeddah, Saudi Arabia
               type:PostalAddress
            type:Organization
      name:Khaled A. Al Ghamdi
      affiliation:
            name:King Abdulaziz University
            address:
               name:Biological Sciences Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia
               type:PostalAddress
            type:Organization
      name:Rizwan H. Khan
      affiliation:
            name:Aligarh Muslim University
            address:
               name:Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, India
               type:PostalAddress
            type:Organization
      name:Vladimir N. Uversky
      affiliation:
            name:King Abdulaziz University
            address:
               name:Biological Sciences Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia
               type:PostalAddress
            type:Organization
            name:Institute for Biological Instrumentation of the Russian Academy of Sciences
            address:
               name:Protein Research Group, Institute for Biological Instrumentation of the Russian Academy of Sciences, Pushchino, Russia
               type:PostalAddress
            type:Organization
            name:University of South Florida
            address:
               name:Department of Molecular Medicine and USF Health Byrd Alzheimer’s Research Institute, Morsani College of Medicine, University of South Florida, Tampa, USA
               type:PostalAddress
            type:Organization
      email:[email protected]
      name:Elrashdy M. Redwan
      url:http://orcid.org/0000-0001-8246-0075
      affiliation:
            name:King Abdulaziz University
            address:
               name:Biological Sciences Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia
               type:PostalAddress
            type:Organization
            name:City for Scientific Research and Technology Applications
            address:
               name:Therapeutic and Protective Proteins Laboratory, Protein Research Department, Genetic Engineering and Biotechnology Research Institute, City for Scientific Research and Technology Applications, Alexandria, Egypt
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Biological Sciences Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia
      name:Laboratory Department, University Medical Services Center, King Abdulaziz University, Jeddah, Saudi Arabia
      name:Biological Sciences Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia
      name:Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, India
      name:Biological Sciences Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia
      name:Protein Research Group, Institute for Biological Instrumentation of the Russian Academy of Sciences, Pushchino, Russia
      name:Department of Molecular Medicine and USF Health Byrd Alzheimer’s Research Institute, Morsani College of Medicine, University of South Florida, Tampa, USA
      name:Biological Sciences Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia
      name:Therapeutic and Protective Proteins Laboratory, Protein Research Department, Genetic Engineering and Biotechnology Research Institute, City for Scientific Research and Technology Applications, Alexandria, Egypt
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(453)

Analytics and Tracking {📊}

Google Tag Manager

Libraries {📚}

Clipboard.js
Prism.js

CDN Services {📦}

Crossref
Pbgrd

4.52s.

LINK . SPRINGER . COM {}