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Two-step mechanism of J-domain action in driving Hsp70 function [article]

Bartlomiej Tomiczek, Wojciech Delewski, Lukasz Nierzwicki, Milena Stolarska, Igor Grochowina, Brenda Schilke, Rafal Dutkiewicz, Marta A. Uzarska, Szymon J. Ciesielski, Jacek Czub, Elizabeth A. Craig, Jaroslaw Marszalek
<span title="2020-01-13">2020</span> <i title="Cold Spring Harbor Laboratory"> bioRxiv </i> &nbsp; <span class="release-stage" >pre-print</span>
Together, our data points to a two-step mode of J-domain action, a recognition stage followed by a mechanistic stage.  ...  J-domain proteins (JDPs), obligatory Hsp70 cochaperones, play critical roles in protein homeostasis.  ...  This research was supported in part by PL-Grid Infrastructure (http://www.plgrid.pl/en).  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1101/2020.01.13.901538">doi:10.1101/2020.01.13.901538</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/w3au6tlfh5h6zpcnvwnagchani">fatcat:w3au6tlfh5h6zpcnvwnagchani</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20200325154558/https://www.biorxiv.org/content/biorxiv/early/2020/01/13/2020.01.13.901538.full.pdf" title="fulltext PDF download" data-goatcounter-click="serp-fulltext" data-goatcounter-title="serp-fulltext"> <button class="ui simple right pointing dropdown compact black labeled icon button serp-button"> <i class="icon ia-icon"></i> Web Archive [PDF] <div class="menu fulltext-thumbnail"> <img src="https://blobs.fatcat.wiki/thumbnail/pdf/69/1a/691a05d453bda4754a3f2452896a0cfe6d403d40.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1101/2020.01.13.901538"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="external alternate icon"></i> biorxiv.org </button> </a>

Two-step mechanism of J-domain action in driving Hsp70 function

Bartlomiej Tomiczek, Wojciech Delewski, Lukasz Nierzwicki, Milena Stolarska, Igor Grochowina, Brenda Schilke, Rafal Dutkiewicz, Marta A. Uzarska, Szymon J. Ciesielski, Jacek Czub, Elizabeth A. Craig, Jaroslaw Marszalek (+1 others)
<span title="2020-06-01">2020</span> <i title="Public Library of Science (PLoS)"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/ch57atmlprauhhbqdf7x4ytejm" style="color: black;">PLoS Computational Biology</a> </i> &nbsp;
Together, our data points to a two-step mode of J-domain action, a recognition stage followed by a mechanistic stage.  ...  J-domain proteins (JDPs), obligatory Hsp70 cochaperones, play critical roles in protein homeostasis.  ...  Acknowledgments We thank Xavier Meyer and Daniele Silvestro, University of Lausanne, for discussions about  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1371/journal.pcbi.1007913">doi:10.1371/journal.pcbi.1007913</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/32479549">pmid:32479549</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/7fp7qog4qbdfbpv3avwqe54p2m">fatcat:7fp7qog4qbdfbpv3avwqe54p2m</a> </span>
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Page 674 of Cellular and Molecular Life Sciences Vol. 62, Issue 6 [page]

<span title="">2005</span> <i title="Springer Science &amp; Business Media"> <a target="_blank" rel="noopener" href="https://archive.org/details/pub_cellular-and-molecular-life-sciences" style="color: black;">Cellular and Molecular Life Sciences </a> </i> &nbsp;
This stimulation by substrates is too low to drive the functional cycle of Hsp70 chaperones.  ...  The substrate can then be transferred onto DnaK in a two-step process involving the transient interaction of the J-domain with DnaK:ATP and the association of the substrate with the open substrate binding  ... 
<span class="external-identifiers"> </span>
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Prion propagation by Hsp40 molecular chaperones

Daniel W. Summers, Peter M. Douglas, Douglas M. Cyr
<span title="">2009</span> <i title="Informa UK Limited"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/auhjmzxuvfcn3kwip3acbiejx4" style="color: black;">Prion</a> </i> &nbsp;
Yeast prions possess domains enriched in glutamines and asparagines that act as templates to drive the assembly of native proteins into beta-sheet-rich, amyloid-like fibrils.  ...  Several recent studies highlight a significant and complex function for Hsp40 co-chaperones in propagation of prion elements in yeast.  ...  Protein Quality Control by Hsp40 Molecular Chaperones Hsp40 co-chaperones are essential partners in Hsp70 function. 32 Hsp40s share a highly conserved region called a J-domain that stimulates the intrinsic  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.4161/pri.3.2.9062">doi:10.4161/pri.3.2.9062</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/19535913">pmid:19535913</a> <a target="_blank" rel="external noopener" href="https://pubmed.ncbi.nlm.nih.gov/PMC2712600/">pmcid:PMC2712600</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/5cpa325dprgftf35fur5envts4">fatcat:5cpa325dprgftf35fur5envts4</a> </span>
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Hsp70 at the membrane: driving protein translocation

Elizabeth A. Craig
<span title="2018-01-17">2018</span> <i title="Springer Nature"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/sim25qtjzrbhfpgmid2b4zhpd4" style="color: black;">BMC Biology</a> </i> &nbsp;
function.  ...  The "import motor" in the mitochondrial matrix, which is essential for driving the movement of proteins across the mitochondrial inner membrane, is arguably the most complex Hsp70based system in the cell  ...  This work was supported by National Institutes of Health Grant GM27870.  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1186/s12915-017-0474-3">doi:10.1186/s12915-017-0474-3</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/29343244">pmid:29343244</a> <a target="_blank" rel="external noopener" href="https://pubmed.ncbi.nlm.nih.gov/PMC5773037/">pmcid:PMC5773037</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/wnvkttlaf5d4bjhihhsb3wzhuq">fatcat:wnvkttlaf5d4bjhihhsb3wzhuq</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20190428053453/https://bmcbiol.biomedcentral.com/track/pdf/10.1186/s12915-017-0474-3" title="fulltext PDF download" data-goatcounter-click="serp-fulltext" data-goatcounter-title="serp-fulltext"> <button class="ui simple right pointing dropdown compact black labeled icon button serp-button"> <i class="icon ia-icon"></i> Web Archive [PDF] <div class="menu fulltext-thumbnail"> <img src="https://blobs.fatcat.wiki/thumbnail/pdf/ae/4e/ae4e55fedc4bdbec0cc51b3cc3227e1b4a00cbc5.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1186/s12915-017-0474-3"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="unlock alternate icon" style="background-color: #fb971f;"></i> springer.com </button> </a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5773037" title="pubmed link"> <button class="ui compact blue labeled icon button serp-button"> <i class="file alternate outline icon"></i> pubmed.gov </button> </a>

The HSP70 chaperone machinery: J proteins as drivers of functional specificity

Harm H. Kampinga, Elizabeth A. Craig
<span title="">2010</span> <i title="Springer Nature"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/3azejq3banhutbh2ddqiyhaiyu" style="color: black;">Nature reviews. Molecular cell biology</a> </i> &nbsp;
linker Peptide-binding cleft Lid ATPase domain Peptide-binding domain b J domain J proteins drive the multifunctionality of HSP70s.  ...  Much of the functional diversity of the HSP70s is driven by a diverse class of cofactors: J proteins. Often, multiple J proteins function with a single HSP70.  ...  Hageman for his detailed work on the human J proteins and help with the bioinformatics and M. Cheetham (UK) for valuable discussions on the functionality and nomenclature of the human J proteins.  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1038/nrm2941">doi:10.1038/nrm2941</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/20651708">pmid:20651708</a> <a target="_blank" rel="external noopener" href="https://pubmed.ncbi.nlm.nih.gov/PMC3003299/">pmcid:PMC3003299</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/ikxm4ciox5ehvfis2ldrtbffsm">fatcat:ikxm4ciox5ehvfis2ldrtbffsm</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20200320181613/https://biochem.wisc.edu/sites/default/files/labs/craig/Publications/56.pdf" title="fulltext PDF download" data-goatcounter-click="serp-fulltext" data-goatcounter-title="serp-fulltext"> <button class="ui simple right pointing dropdown compact black labeled icon button serp-button"> <i class="icon ia-icon"></i> Web Archive [PDF] <div class="menu fulltext-thumbnail"> <img src="https://blobs.fatcat.wiki/thumbnail/pdf/b5/1d/b51d4dae03c2626f3496f8a1c64245ca6f1dbecd.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1038/nrm2941"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="external alternate icon"></i> nature.com </button> </a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3003299" title="pubmed link"> <button class="ui compact blue labeled icon button serp-button"> <i class="file alternate outline icon"></i> pubmed.gov </button> </a>

What is the driving force for protein import into mitochondria?

Martin Horst, Abdussalam Azem, Gottfried Schatz, Benjamin S Glick
<span title="">1997</span> <i title="Elsevier BV"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/s7j4gsfdrzgo3mspdvmzrosp74" style="color: black;">Biochimica et Biophysica Acta - Bioenergetics</a> </i> &nbsp;
It is known that hsp70 proteins bind to unfolded segments of polypeptide chains w x 17-20 , but the mechanism of hsp70 action is still incompletely understood.  ...  This protein contains a domain that is weakly homologous to the J domain of Sec63p w x 13 .  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1016/s0005-2728(96)00131-4">doi:10.1016/s0005-2728(96)00131-4</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/9030256">pmid:9030256</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/hwvbj6ma25dapkekamenzpuwdi">fatcat:hwvbj6ma25dapkekamenzpuwdi</a> </span>
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The Physics of Entropic Pulling: A Novel Model for the Hsp70 Motor Mechanism

Rui Sousa, Eileen M. Lafer
<span title="2019-05-11">2019</span> <i title="MDPI AG"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/3loumxx7kzamnlu4h6x3xoz6ay" style="color: black;">International Journal of Molecular Sciences</a> </i> &nbsp;
We hope that increased understanding of the entropic pulling mechanism will inform future efforts to characterize how Hsp70s function as motors, and how they coordinate with their regulatory cochaperones  ...  In this review we address persistent misconceptions regarding the dynamics of proteins in solution that contribute to this lack of understanding, and we clarify the basic physics of entropic pulling with  ...  Conflicts of Interest: The authors declare no conflict of interest. Abbreviations  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.3390/ijms20092334">doi:10.3390/ijms20092334</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/vt7lsywa6vfetcj7p5npwapoie">fatcat:vt7lsywa6vfetcj7p5npwapoie</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20200208200349/https://res.mdpi.com/d_attachment/ijms/ijms-20-02334/article_deploy/ijms-20-02334.pdf" title="fulltext PDF download" data-goatcounter-click="serp-fulltext" data-goatcounter-title="serp-fulltext"> <button class="ui simple right pointing dropdown compact black labeled icon button serp-button"> <i class="icon ia-icon"></i> Web Archive [PDF] <div class="menu fulltext-thumbnail"> <img src="https://blobs.fatcat.wiki/thumbnail/pdf/e3/53/e353d749d36f200c9070ee8e131c697a0070b0e2.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.3390/ijms20092334"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="unlock alternate icon" style="background-color: #fb971f;"></i> mdpi.com </button> </a>

Swapping Nucleotides, Tuning Hsp70

Douglas M. Cyr
<span title="">2008</span> <i title="Elsevier BV"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/iwommhyo5bdk7c3u37mhjzexfe" style="color: black;">Cell</a> </i> &nbsp;
The elegant structures of Polier et al. (2008) and Schuermann et al. (2008) not only shed light on the mechanism of Hsp110 action but also may provide fresh leads in understanding the actions of other  ...  These new structures shed light on the mechanism by which NEF action regulates Hsp70 activity.  ...  This work expands the synthetic biology toolbox and represents a significant step forward in the engineering of protein-based synthetic pathways.  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1016/j.cell.2008.05.036">doi:10.1016/j.cell.2008.05.036</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/18555768">pmid:18555768</a> <a target="_blank" rel="external noopener" href="https://pubmed.ncbi.nlm.nih.gov/PMC4445657/">pmcid:PMC4445657</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/z43mvx6yjbeihoa2zmilt6ecvq">fatcat:z43mvx6yjbeihoa2zmilt6ecvq</a> </span>
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Energy use by biological protein transport pathways

Nathan N. Alder, Steven M. Theg
<span title="">2003</span> <i title="Elsevier BV"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/rg373qd4c5a2npre7o4rshhyyi" style="color: black;">TIBS -Trends in Biochemical Sciences. Regular ed</a> </i> &nbsp;
Several recent advances in our knowledge of the structure and function of these transport systems have provided insights into the mechanisms of energy transduction, force generation and energy use by different  ...  Force: an action that causes an object with mass to accelerate, typically expressed in units of Newtons (N).  ...  (b) Models of Hsp70 action.  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1016/s0968-0004(03)00167-1">doi:10.1016/s0968-0004(03)00167-1</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/12932733">pmid:12932733</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/fgre3d7jbffbjooa7dtby2vwde">fatcat:fgre3d7jbffbjooa7dtby2vwde</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20170811210200/http://ecoserver.imbb.forth.gr/documents/Alder03.pdf" title="fulltext PDF download" data-goatcounter-click="serp-fulltext" data-goatcounter-title="serp-fulltext"> <button class="ui simple right pointing dropdown compact black labeled icon button serp-button"> <i class="icon ia-icon"></i> Web Archive [PDF] <div class="menu fulltext-thumbnail"> <img src="https://blobs.fatcat.wiki/thumbnail/pdf/13/b7/13b785b867ddfe6b28890ae761678a4846e727fe.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1016/s0968-0004(03)00167-1"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="external alternate icon"></i> elsevier.com </button> </a>

Multi-layered molecular mechanisms of polypeptide holding, unfolding and disaggregation by HSP70/HSP110 chaperones

Andrija Finka, Sandeep K. Sharma, Pierre Goloubinoff
<span title="2015-06-05">2015</span> <i title="Frontiers Media SA"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/zqzewb742bdglfxhkef3ke6cla" style="color: black;">Frontiers in Molecular Biosciences</a> </i> &nbsp;
Members of the HSP70/HSP110 family (HSP70s) form a central hub of the chaperone network controlling all aspects of proteostasis in bacteria and the ATP-containing compartments of eukaryotic cells.  ...  The HSP70s carry out a plethora of housekeeping cellular functions, such as assisting proper de novo folding, assembly and disassembly of protein complexes, pulling polypeptides out of the ribosome and  ...  The multilayer mechanisms of HSP70 as holding and unfolding chaperones can be summarized in four steps (Figure 2A) .  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.3389/fmolb.2015.00029">doi:10.3389/fmolb.2015.00029</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/26097841">pmid:26097841</a> <a target="_blank" rel="external noopener" href="https://pubmed.ncbi.nlm.nih.gov/PMC4456865/">pmcid:PMC4456865</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/2nwromptfnb6hple23evz4s2w4">fatcat:2nwromptfnb6hple23evz4s2w4</a> </span>
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Pushing, pulling and trapping - Modes of motor protein supported protein translocation

Danuta Tomkiewicz, Nico Nouwen, Arnold J.M. Driessen
<span title="2007-04-18">2007</span> <i title="Wiley"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/kn6dhptylrb77b5atyiom5ysjm" style="color: black;">FEBS Letters</a> </i> &nbsp;
Recent insights in the structure and function of the molecular motors suggest that different mechanisms can be employed simultaneously.  ...  Since motor proteins are found either at the cis-or trans-side of the membrane, different mechanisms for translocation have been proposed.  ...  Acknowledgements: This work was supported by the Foundation for Fundamental Research on Matter (FOM), Earth and Life Sciences (ALW), the Royal Academy of Sciences of the Netherlands (KNAW), and NanoNed  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1016/j.febslet.2007.04.015">doi:10.1016/j.febslet.2007.04.015</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/17466297">pmid:17466297</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/sbg2yoct4zbhvdx3e4twftz7ae">fatcat:sbg2yoct4zbhvdx3e4twftz7ae</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20190315080405/https://core.ac.uk/download/pdf/82465693.pdf" title="fulltext PDF download" data-goatcounter-click="serp-fulltext" data-goatcounter-title="serp-fulltext"> <button class="ui simple right pointing dropdown compact black labeled icon button serp-button"> <i class="icon ia-icon"></i> Web Archive [PDF] <div class="menu fulltext-thumbnail"> <img src="https://blobs.fatcat.wiki/thumbnail/pdf/4e/82/4e8244faa0fae667051c8f9f358a1aff96a092ec.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1016/j.febslet.2007.04.015"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="external alternate icon"></i> Publisher / doi.org </button> </a>

Mitochondrial molecular chaperones: their role in protein translocation

Rosemary A. Stuart, Douglas M. Cyr, Elizabeth A. Craig, Walter Neupert
<span title="">1994</span> <i title="Elsevier BV"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/rg373qd4c5a2npre7o4rshhyyi" style="color: black;">TIBS -Trends in Biochemical Sciences. Regular ed</a> </i> &nbsp;
Manipulation of mt-Hsp70 action Two important tools exist for studying the actions of mitochondrial chaperones, in particular mt-Hsp70; these are (I) modulation r'f matrix ATP concentrations to levels  ...  that adversely affect the ATP<lependent action of mt-Hsp70, and (2) mutations in the SSCI gene resuiting in altered mt-HspT0 proteins that are temperature sensitive for function. in addition to A~, hydrolysis  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1016/0968-0004(94)90041-8">doi:10.1016/0968-0004(94)90041-8</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/8160272">pmid:8160272</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/pnluj6oaw5emrltghybow6tooe">fatcat:pnluj6oaw5emrltghybow6tooe</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20170813044645/https://epub.ub.uni-muenchen.de/7688/1/Neupert_Walter_7688.pdf" title="fulltext PDF download" data-goatcounter-click="serp-fulltext" data-goatcounter-title="serp-fulltext"> <button class="ui simple right pointing dropdown compact black labeled icon button serp-button"> <i class="icon ia-icon"></i> Web Archive [PDF] <div class="menu fulltext-thumbnail"> <img src="https://blobs.fatcat.wiki/thumbnail/pdf/83/72/83728a719456b2e4cbe717746517b93b9d36ad0e.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1016/0968-0004(94)90041-8"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="external alternate icon"></i> elsevier.com </button> </a>

Hsp70 chaperones: Cellular functions and molecular mechanism

M. P. Mayer, B. Bukau
<span title="">2005</span> <i title="Springer Nature"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/a5zaemqj4za4nekjggicuat22q" style="color: black;">Cellular and Molecular Life Sciences (CMLS)</a> </i> &nbsp;
This ATPase cycle is controlled by co-chaperones of the family of J-domain proteins, which target Hsp70s to their substrates, and by nucleotide exchange factors, which determine the lifetime of the Hsp70  ...  For specific tasks the Hsp70 cycle is coupled to the action of other chaperones, such as Hsp90 and Hsp100.  ...  The substrate can then be transferred onto DnaK in a two-step process involving the transient interaction of the J-domain with DnaK·ATP and the association of the substrate with the open substrate binding  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1007/s00018-004-4464-6">doi:10.1007/s00018-004-4464-6</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/15770419">pmid:15770419</a> <a target="_blank" rel="external noopener" href="https://pubmed.ncbi.nlm.nih.gov/PMC2773841/">pmcid:PMC2773841</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/qgns4pknznbably27hjqatzicq">fatcat:qgns4pknznbably27hjqatzicq</a> </span>
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Chaperoned Protein Disaggregation—The ClpB Ring Uses Its Central Channel

Arthur L. Horwich
<span title="">2004</span> <i title="Elsevier BV"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/iwommhyo5bdk7c3u37mhjzexfe" style="color: black;">Cell</a> </i> &nbsp;
ClpB, to gain some mechanistic and physiologic un-Remarkably, the functions of protein disaggregation and derstanding of the action of this chaperone in mediatrefolding as mediated by ClpB and the Hsp70  ...  in vivo and in vitro, cooperation of ClpB. of these components with the Hsp70 system can bring But could passage into ClpP in these experiments aggregated proteins back to a functional fold (e.g., somehow  ...  One, a La Jolla, California, 92037 two-step type of mechanism, would have the Hsp70 system acting in an initial step together with the propel- t-SNARE Vam3p, including the fact that the two purified  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1016/j.cell.2004.11.018">doi:10.1016/j.cell.2004.11.018</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/15550237">pmid:15550237</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/yrsjyo6uv5ar3jciwoo5cngxda">fatcat:yrsjyo6uv5ar3jciwoo5cngxda</a> </span>
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