We are analyzing https://link.springer.com/article/10.1007/s12192-017-0762-4.

Title:
Role of sHsps in organizing cytosolic protein aggregation and disaggregation | Cell Stress and Chaperones
Description:
Small heat shock proteins (sHsps) exhibit an ATP-independent chaperone activity to prevent the aggregation of misfolded proteins in vitro. The seemingly conflicting presence of sHsps in insoluble protein aggregates in cells obstructs a precise definition of sHsp function in proteostasis networks. Recent findings specify sHsp activities in protein quality control systems. The sHsps of yeast, Hsp42 and Hsp26, interact with early unfolding intermediates of substrates, keeping them in a ready-to-refold conformation close to the native state. This activity facilitates substrate refolding by ATP-dependent Hsp70-Hsp100 disaggregating chaperones. Hsp42 can actively sequester misfolded proteins and promote their deposition at specific cellular sites. This aggregase activity represents a cytoprotective protein quality control strategy. The aggregase function of Hsp42 controls the formation of cytosolic aggregates (CytoQs) under diverse stress regimes and can be reconstituted in vitro, demonstrating that Hsp42 is necessary and sufficient to promote protein aggregation. Substrates sequestered at CytoQs can be dissociated by Hsp70-Hsp100 disaggregases for subsequent triage between refolding and degradation pathways or are targeted for destruction by selective autophagy termed proteophagy.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

Science
Health & Fitness
Education

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.

Earning money isn't the goal of every website; some are designed to offer support or promote social causes. People have different reasons for creating websites. This might be one such reason. Link.springer.com has a revenue plan, but it's either invisible or we haven't found it.

Keywords {🔍}

pubmed, article, google, scholar, protein, cas, heat, proteins, central, shock, small, biol, cell, hsp, chaperone, aggregation, bukau, mogk, aggregates, mol, vierling, stress, chem, chaperones, misfolded, quality, control, disaggregation, cellular, nature, coli, buchner, function, refolding, access, escherichia, molecular, privacy, cookies, content, shsps, yeast, substrate, asymmetric, inheritance, doijcell, doijjmb, plos, embo, lee,

Topics {✒️}

month download article/chapter multi-type substrate-binding residues small heat-shock proteins heat-denatured protein vac17-dependent vacuolar functions atp-independent chaperone activity heat-shock proteins protein quality control heat shock creates full article pdf quality-control foci hsp70 chaperone levels article cell stress accumulated protein damage hspb8/hspb6-bag3 interaction power protein disaggregation promote protein aggregation reversing protein aggregation controlling protein aggregation friedrich kl miller sb misfolded protein stress small hsps relies opposing activities protect privacy choices/manage cookies heterologous protein expression insoluble protein deposit article mogk giese kc dnak system form nillegoda nb kampinga hh misfolded proteins partition heat shock metazoan hsp70 machines insoluble protein aggregates disassembling protein aggregates polyq proteins mediated chaperone action derived hsp70-hsp100 disaggregases axel mogk oxidatively damaged proteins disaggregation reaction mediated related subjects ubiquitin-atg8 adaptors ubiquitin receptor cue5 spatially organized aggregation misassembled proteasome subunits aggregase activity represents specific cellular sites

Schema {🗺️}

WebPage:
      mainEntity:
         headline:Role of sHsps in organizing cytosolic protein aggregation and disaggregation
         description:Small heat shock proteins (sHsps) exhibit an ATP-independent chaperone activity to prevent the aggregation of misfolded proteins in vitro. The seemingly conflicting presence of sHsps in insoluble protein aggregates in cells obstructs a precise definition of sHsp function in proteostasis networks. Recent findings specify sHsp activities in protein quality control systems. The sHsps of yeast, Hsp42 and Hsp26, interact with early unfolding intermediates of substrates, keeping them in a ready-to-refold conformation close to the native state. This activity facilitates substrate refolding by ATP-dependent Hsp70-Hsp100 disaggregating chaperones. Hsp42 can actively sequester misfolded proteins and promote their deposition at specific cellular sites. This aggregase activity represents a cytoprotective protein quality control strategy. The aggregase function of Hsp42 controls the formation of cytosolic aggregates (CytoQs) under diverse stress regimes and can be reconstituted in vitro, demonstrating that Hsp42 is necessary and sufficient to promote protein aggregation. Substrates sequestered at CytoQs can be dissociated by Hsp70-Hsp100 disaggregases for subsequent triage between refolding and degradation pathways or are targeted for destruction by selective autophagy termed proteophagy.
         datePublished:2017-01-24T00:00:00Z
         dateModified:2017-01-24T00:00:00Z
         pageStart:493
         pageEnd:502
         sameAs:https://doi.org/10.1007/s12192-017-0762-4
         keywords:
            Chaperone
            Small heat shock protein
            Holdase, aggregase
            Protein aggregation
            Protein disaggregation
            Biomedicine
            general
            Cell Biology
            Biochemistry
            Immunology
            Cancer Research
            Neurosciences
         image:
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs12192-017-0762-4/MediaObjects/12192_2017_762_Fig1_HTML.gif
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs12192-017-0762-4/MediaObjects/12192_2017_762_Fig2_HTML.gif
         isPartOf:
            name:Cell Stress and Chaperones
            issn:
               1466-1268
               1355-8145
            volumeNumber:22
            type:
               Periodical
               PublicationVolume
         publisher:
            name:Springer Netherlands
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:Axel Mogk
               affiliation:
                     name:DKFZ-ZMBH Alliance
                     address:
                        name:Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Heidelberg, Germany
                        type:PostalAddress
                     type:Organization
                     name:German Cancer Research Center (DKFZ)
                     address:
                        name:German Cancer Research Center (DKFZ), Heidelberg, Germany
                        type:PostalAddress
                     type:Organization
               email:[email protected]
               type:Person
               name:Bernd Bukau
               affiliation:
                     name:DKFZ-ZMBH Alliance
                     address:
                        name:Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Heidelberg, Germany
                        type:PostalAddress
                     type:Organization
                     name:German Cancer Research Center (DKFZ)
                     address:
                        name:German Cancer Research Center (DKFZ), Heidelberg, Germany
                        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:Role of sHsps in organizing cytosolic protein aggregation and disaggregation
      description:Small heat shock proteins (sHsps) exhibit an ATP-independent chaperone activity to prevent the aggregation of misfolded proteins in vitro. The seemingly conflicting presence of sHsps in insoluble protein aggregates in cells obstructs a precise definition of sHsp function in proteostasis networks. Recent findings specify sHsp activities in protein quality control systems. The sHsps of yeast, Hsp42 and Hsp26, interact with early unfolding intermediates of substrates, keeping them in a ready-to-refold conformation close to the native state. This activity facilitates substrate refolding by ATP-dependent Hsp70-Hsp100 disaggregating chaperones. Hsp42 can actively sequester misfolded proteins and promote their deposition at specific cellular sites. This aggregase activity represents a cytoprotective protein quality control strategy. The aggregase function of Hsp42 controls the formation of cytosolic aggregates (CytoQs) under diverse stress regimes and can be reconstituted in vitro, demonstrating that Hsp42 is necessary and sufficient to promote protein aggregation. Substrates sequestered at CytoQs can be dissociated by Hsp70-Hsp100 disaggregases for subsequent triage between refolding and degradation pathways or are targeted for destruction by selective autophagy termed proteophagy.
      datePublished:2017-01-24T00:00:00Z
      dateModified:2017-01-24T00:00:00Z
      pageStart:493
      pageEnd:502
      sameAs:https://doi.org/10.1007/s12192-017-0762-4
      keywords:
         Chaperone
         Small heat shock protein
         Holdase, aggregase
         Protein aggregation
         Protein disaggregation
         Biomedicine
         general
         Cell Biology
         Biochemistry
         Immunology
         Cancer Research
         Neurosciences
      image:
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs12192-017-0762-4/MediaObjects/12192_2017_762_Fig1_HTML.gif
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs12192-017-0762-4/MediaObjects/12192_2017_762_Fig2_HTML.gif
      isPartOf:
         name:Cell Stress and Chaperones
         issn:
            1466-1268
            1355-8145
         volumeNumber:22
         type:
            Periodical
            PublicationVolume
      publisher:
         name:Springer Netherlands
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Axel Mogk
            affiliation:
                  name:DKFZ-ZMBH Alliance
                  address:
                     name:Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Heidelberg, Germany
                     type:PostalAddress
                  type:Organization
                  name:German Cancer Research Center (DKFZ)
                  address:
                     name:German Cancer Research Center (DKFZ), Heidelberg, Germany
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
            name:Bernd Bukau
            affiliation:
                  name:DKFZ-ZMBH Alliance
                  address:
                     name:Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Heidelberg, Germany
                     type:PostalAddress
                  type:Organization
                  name:German Cancer Research Center (DKFZ)
                  address:
                     name:German Cancer Research Center (DKFZ), Heidelberg, Germany
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
["Periodical","PublicationVolume"]:
      name:Cell Stress and Chaperones
      issn:
         1466-1268
         1355-8145
      volumeNumber:22
Organization:
      name:Springer Netherlands
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:DKFZ-ZMBH Alliance
      address:
         name:Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Heidelberg, Germany
         type:PostalAddress
      name:German Cancer Research Center (DKFZ)
      address:
         name:German Cancer Research Center (DKFZ), Heidelberg, Germany
         type:PostalAddress
      name:DKFZ-ZMBH Alliance
      address:
         name:Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Heidelberg, Germany
         type:PostalAddress
      name:German Cancer Research Center (DKFZ)
      address:
         name:German Cancer Research Center (DKFZ), Heidelberg, Germany
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Axel Mogk
      affiliation:
            name:DKFZ-ZMBH Alliance
            address:
               name:Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Heidelberg, Germany
               type:PostalAddress
            type:Organization
            name:German Cancer Research Center (DKFZ)
            address:
               name:German Cancer Research Center (DKFZ), Heidelberg, Germany
               type:PostalAddress
            type:Organization
      email:[email protected]
      name:Bernd Bukau
      affiliation:
            name:DKFZ-ZMBH Alliance
            address:
               name:Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Heidelberg, Germany
               type:PostalAddress
            type:Organization
            name:German Cancer Research Center (DKFZ)
            address:
               name:German Cancer Research Center (DKFZ), Heidelberg, Germany
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Heidelberg, Germany
      name:German Cancer Research Center (DKFZ), Heidelberg, Germany
      name:Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Heidelberg, Germany
      name:German Cancer Research Center (DKFZ), Heidelberg, Germany
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(334)

Analytics and Tracking {📊}

Google Tag Manager

Libraries {📚}

Clipboard.js
Prism.js

CDN Services {📦}

Crossref

4.57s.

LINK . SPRINGER . COM {}