We are analyzing https://link.springer.com/article/10.1186/s12575-021-00145-9.

Title:
Effects of Cell Proteostasis Network on the Survival of SARS-CoV-2 | Biological Procedures Online
Description:
The proteostasis network includes all the factors that control the function of proteins in their native state and minimize their non-functional or harmful reactions. The molecular chaperones, the important mediator in the proteostasis network can be considered as any protein that contributes to proper folding and assembly of other macromolecules, through maturating of unfolded or partially folded macromolecules, refolding of stress-denatured proteins, and modifying oligomeric assembly, otherwise it leads to their proteolytic degradation. Viruses that use the hosts’ gene expression tools and protein synthesis apparatus to survive and replicate, are obviously protected by such a host chaperone system. This means that many viruses use members of the hosts’ chaperoning system to infect the target cells, replicate, and spread. During viral infection, increase in endoplasmic reticulum (ER) stress due to high expression of viral proteins enhances the level of heat shock proteins (HSPs) and induces cell apoptosis or necrosis. Indeed, evidence suggests that ER stress and the induction of unfolded protein response (UPR) may be a major aspect of the corona-host virus interaction. In addition, several clinical reports have confirmed the autoimmune phenomena in COVID-19-patients, and a strong association between this autoimmunity and severe SARS-CoV-2 infection. Part of such autoimmunity is due to shared epitopes among the virus and host. This article reviews the proteostasis network and its relationship to the immune system in SARS-CoV-2 infection.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

Science
Health & Fitness
Video & Online Content

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're unsure how the site profits.

While many websites aim to make money, others are created to share knowledge or showcase creativity. People build websites for various reasons. This could be one of them. Link.springer.com could be secretly minting cash, but we can't detect the process.

Keywords {🔍}

pubmed, article, google, scholar, cas, sarscov, central, proteins, protein, covid, cell, chaperones, viral, virus, stress, infection, host, molecular, hsp, coronavirus, cells, disease, patients, due, proteostasis, ace, folding, viruses, severe, role, function, network, system, high, respiratory, chaperone, apoptosis, response, immune, spike, synthesis, rna, expression, syndrome, factor, membrane, heat, autoimmune, acute, receptor,

Topics {✒️}

anti–sjögren’s-syndrome-related antigen c-jun n-terminal kinase article download pdf xbp1s-dependent transcriptional reprogramming local renin-angiotensin system ace-2/angiotensin 1-7/mas axis ace2-mediated signaling reduces nf-kb mediated control explain multi-organ damage bat-borne virus diversity single-stranded rna virus viral-encoded proteinases encoded anti-ssa/ro antibodies small heat-shock proteins amino-terminal functional domains cell-protecting process managed undergo cap-dependent translation reduced atf4-chop increases cellular heat/oxidative stress severe sars-cov-2 infection sahar yarahmadi angiotensin-converting enzyme 2 angiotensin converting enzyme negative-sense genomic rnas shows autoimmune disease/syndromes sars-cov-2-ace2 complex found anti-mda5 antibody sars-cov-2-infected patients [70] biol proced online privacy choices/manage cookies er related kinase intracellular ca2+ homeostasis puerta-puerta jm nf-κb pathway er-mitochondria ca2+ transfer anti-mda5 syndrome prevent sars-cov-2 infection corona-host virus interaction common fatal complication public health policies severe respiratory failure ace2-receptor complex recognized ubiquitin-proteasome system article khomari related subjects /ebp homologous protein biological networks introduction heat-shock cognates heat shock response rough endoplasmic reticulum

Questions {❓}

COVID-19 and hypertension: is the HSP60 culprit for the severe course and worse outcome?
SARS-CoV-2 and DPP4 inhibition: Is it time to pray for Janus Bifrons?
Similarities between COVID-19 and anti-MDA5 syndrome: what can we learn for better care?
What can we learn from rapidly progressive interstitial lung disease related to anti-MDA5 dermatomyositis in the management of COVID-19?

Schema {🗺️}

WebPage:
      mainEntity:
         headline:Effects of Cell Proteostasis Network on the Survival of SARS-CoV-2
         description:The proteostasis network includes all the factors that control the function of proteins in their native state and minimize their non-functional or harmful reactions. The molecular chaperones, the important mediator in the proteostasis network can be considered as any protein that contributes to proper folding and assembly of other macromolecules, through maturating of unfolded or partially folded macromolecules, refolding of stress-denatured proteins, and modifying oligomeric assembly, otherwise it leads to their proteolytic degradation. Viruses that use the hosts’ gene expression tools and protein synthesis apparatus to survive and replicate, are obviously protected by such a host chaperone system. This means that many viruses use members of the hosts’ chaperoning system to infect the target cells, replicate, and spread. During viral infection, increase in endoplasmic reticulum (ER) stress due to high expression of viral proteins enhances the level of heat shock proteins (HSPs) and induces cell apoptosis or necrosis. Indeed, evidence suggests that ER stress and the induction of unfolded protein response (UPR) may be a major aspect of the corona-host virus interaction. In addition, several clinical reports have confirmed the autoimmune phenomena in COVID-19-patients, and a strong association between this autoimmunity and severe SARS-CoV-2 infection. Part of such autoimmunity is due to shared epitopes among the virus and host. This article reviews the proteostasis network and its relationship to the immune system in SARS-CoV-2 infection.
         datePublished:2021-02-22T00:00:00Z
         dateModified:2021-02-22T00:00:00Z
         pageStart:1
         pageEnd:10
         license:http://creativecommons.org/publicdomain/zero/1.0/
         sameAs:https://doi.org/10.1186/s12575-021-00145-9
         keywords:
            Coronavirus
            COVID-19
            SARS-CoV-2
            Chaperone
            Proteostasis
            Biomedicine
            general
            Biological Techniques
         image:
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2Fs12575-021-00145-9/MediaObjects/12575_2021_145_Fig1_HTML.png
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2Fs12575-021-00145-9/MediaObjects/12575_2021_145_Fig2_HTML.png
         isPartOf:
            name:Biological Procedures Online
            issn:
               1480-9222
            volumeNumber:23
            type:
               Periodical
               PublicationVolume
         publisher:
            name:BioMed Central
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:Fateme Khomari
               affiliation:
                     name:Iran University of Medical Sciences
                     address:
                        name:Department of Biochemistry, Faculty of Medicine, Iran University of Medical Sciences, Tehran, Iran
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Mohsen Nabi-Afjadi
               affiliation:
                     name:Tarbiat Modares University
                     address:
                        name:Department of Biochemistry, Faculty of Biological Science, Tarbiat Modares University, Tehran, Iran
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Sahar Yarahmadi
               affiliation:
                     name:Iran University of Medical Sciences
                     address:
                        name:Department of Biochemistry, Faculty of Medicine, Iran University of Medical Sciences, Tehran, Iran
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Hanie Eskandari
               affiliation:
                     name:Islamic Azad University of Tehran
                     address:
                        name:Department of Biology, Science and Research Branch, Islamic Azad University of Tehran, Tehran, Iran
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Elham Bahreini
               url:https://orcid.org/0000-0001-6823-8638
               affiliation:
                     name:Iran University of Medical Sciences
                     address:
                        name:Department of Biochemistry, Faculty of Medicine, Iran University of Medical Sciences, Tehran, Iran
                        type:PostalAddress
                     type:Organization
               email:[email protected]
               type:Person
         isAccessibleForFree:1
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:Effects of Cell Proteostasis Network on the Survival of SARS-CoV-2
      description:The proteostasis network includes all the factors that control the function of proteins in their native state and minimize their non-functional or harmful reactions. The molecular chaperones, the important mediator in the proteostasis network can be considered as any protein that contributes to proper folding and assembly of other macromolecules, through maturating of unfolded or partially folded macromolecules, refolding of stress-denatured proteins, and modifying oligomeric assembly, otherwise it leads to their proteolytic degradation. Viruses that use the hosts’ gene expression tools and protein synthesis apparatus to survive and replicate, are obviously protected by such a host chaperone system. This means that many viruses use members of the hosts’ chaperoning system to infect the target cells, replicate, and spread. During viral infection, increase in endoplasmic reticulum (ER) stress due to high expression of viral proteins enhances the level of heat shock proteins (HSPs) and induces cell apoptosis or necrosis. Indeed, evidence suggests that ER stress and the induction of unfolded protein response (UPR) may be a major aspect of the corona-host virus interaction. In addition, several clinical reports have confirmed the autoimmune phenomena in COVID-19-patients, and a strong association between this autoimmunity and severe SARS-CoV-2 infection. Part of such autoimmunity is due to shared epitopes among the virus and host. This article reviews the proteostasis network and its relationship to the immune system in SARS-CoV-2 infection.
      datePublished:2021-02-22T00:00:00Z
      dateModified:2021-02-22T00:00:00Z
      pageStart:1
      pageEnd:10
      license:http://creativecommons.org/publicdomain/zero/1.0/
      sameAs:https://doi.org/10.1186/s12575-021-00145-9
      keywords:
         Coronavirus
         COVID-19
         SARS-CoV-2
         Chaperone
         Proteostasis
         Biomedicine
         general
         Biological Techniques
      image:
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2Fs12575-021-00145-9/MediaObjects/12575_2021_145_Fig1_HTML.png
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2Fs12575-021-00145-9/MediaObjects/12575_2021_145_Fig2_HTML.png
      isPartOf:
         name:Biological Procedures Online
         issn:
            1480-9222
         volumeNumber:23
         type:
            Periodical
            PublicationVolume
      publisher:
         name:BioMed Central
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Fateme Khomari
            affiliation:
                  name:Iran University of Medical Sciences
                  address:
                     name:Department of Biochemistry, Faculty of Medicine, Iran University of Medical Sciences, Tehran, Iran
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Mohsen Nabi-Afjadi
            affiliation:
                  name:Tarbiat Modares University
                  address:
                     name:Department of Biochemistry, Faculty of Biological Science, Tarbiat Modares University, Tehran, Iran
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Sahar Yarahmadi
            affiliation:
                  name:Iran University of Medical Sciences
                  address:
                     name:Department of Biochemistry, Faculty of Medicine, Iran University of Medical Sciences, Tehran, Iran
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Hanie Eskandari
            affiliation:
                  name:Islamic Azad University of Tehran
                  address:
                     name:Department of Biology, Science and Research Branch, Islamic Azad University of Tehran, Tehran, Iran
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Elham Bahreini
            url:https://orcid.org/0000-0001-6823-8638
            affiliation:
                  name:Iran University of Medical Sciences
                  address:
                     name:Department of Biochemistry, Faculty of Medicine, Iran University of Medical Sciences, Tehran, Iran
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      isAccessibleForFree:1
["Periodical","PublicationVolume"]:
      name:Biological Procedures Online
      issn:
         1480-9222
      volumeNumber:23
Organization:
      name:BioMed Central
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Iran University of Medical Sciences
      address:
         name:Department of Biochemistry, Faculty of Medicine, Iran University of Medical Sciences, Tehran, Iran
         type:PostalAddress
      name:Tarbiat Modares University
      address:
         name:Department of Biochemistry, Faculty of Biological Science, Tarbiat Modares University, Tehran, Iran
         type:PostalAddress
      name:Iran University of Medical Sciences
      address:
         name:Department of Biochemistry, Faculty of Medicine, Iran University of Medical Sciences, Tehran, Iran
         type:PostalAddress
      name:Islamic Azad University of Tehran
      address:
         name:Department of Biology, Science and Research Branch, Islamic Azad University of Tehran, Tehran, Iran
         type:PostalAddress
      name:Iran University of Medical Sciences
      address:
         name:Department of Biochemistry, Faculty of Medicine, Iran University of Medical Sciences, Tehran, Iran
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Fateme Khomari
      affiliation:
            name:Iran University of Medical Sciences
            address:
               name:Department of Biochemistry, Faculty of Medicine, Iran University of Medical Sciences, Tehran, Iran
               type:PostalAddress
            type:Organization
      name:Mohsen Nabi-Afjadi
      affiliation:
            name:Tarbiat Modares University
            address:
               name:Department of Biochemistry, Faculty of Biological Science, Tarbiat Modares University, Tehran, Iran
               type:PostalAddress
            type:Organization
      name:Sahar Yarahmadi
      affiliation:
            name:Iran University of Medical Sciences
            address:
               name:Department of Biochemistry, Faculty of Medicine, Iran University of Medical Sciences, Tehran, Iran
               type:PostalAddress
            type:Organization
      name:Hanie Eskandari
      affiliation:
            name:Islamic Azad University of Tehran
            address:
               name:Department of Biology, Science and Research Branch, Islamic Azad University of Tehran, Tehran, Iran
               type:PostalAddress
            type:Organization
      name:Elham Bahreini
      url:https://orcid.org/0000-0001-6823-8638
      affiliation:
            name:Iran University of Medical Sciences
            address:
               name:Department of Biochemistry, Faculty of Medicine, Iran University of Medical Sciences, Tehran, Iran
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Department of Biochemistry, Faculty of Medicine, Iran University of Medical Sciences, Tehran, Iran
      name:Department of Biochemistry, Faculty of Biological Science, Tarbiat Modares University, Tehran, Iran
      name:Department of Biochemistry, Faculty of Medicine, Iran University of Medical Sciences, Tehran, Iran
      name:Department of Biology, Science and Research Branch, Islamic Azad University of Tehran, Tehran, Iran
      name:Department of Biochemistry, Faculty of Medicine, Iran University of Medical Sciences, Tehran, Iran

External Links {🔗}(292)

Analytics and Tracking {📊}

Google Tag Manager

Libraries {📚}

Clipboard.js
Particles.js
Prism.js

CDN Services {📦}

Crossref

5.79s.

LINK . SPRINGER . COM {}