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Metallochaperones Regulate Intracellular Copper Levels

W. Lee Pang, Amardeep Kaur, Alexander V. Ratushny, Aleksandar Cvetkovic, Sunil Kumar, Min Pan, Adam P. Arkin, John D. Aitchison, Michael W. W. Adams, Nitin S. Baliga, Jennifer L. Reed
<span title="2013-01-17">2013</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;
Here, we have investigated the mechanistic role of metallochaperones in regulating Cu efflux.  ...  This buffering function of metallochaperones ultimately sets the upper limit for intracellular Cu levels and provides a mechanistic explanation for previously observed Cu metallochaperone mutation phenotypes  ...  the role of metallochaperones in regulation of transcriptional dynamics of Cu-responsive efflux as well setting the homeostatic limits for intracellular Cu levels.  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1371/journal.pcbi.1002880">doi:10.1371/journal.pcbi.1002880</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/23349626">pmid:23349626</a> <a target="_blank" rel="external noopener" href="https://pubmed.ncbi.nlm.nih.gov/PMC3551603/">pmcid:PMC3551603</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/s4wc3tik6zhvhfve5vfqqrjuii">fatcat:s4wc3tik6zhvhfve5vfqqrjuii</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20171015140311/http://journals.plos.org/ploscompbiol/article/file?id=10.1371/journal.pcbi.1002880&amp;type=printable" 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/d4/2e/d42e75b11c1304ea47df8bec8b13ed165716485b.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1371/journal.pcbi.1002880"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="unlock alternate icon" style="background-color: #fb971f;"></i> plos.org </button> </a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3551603" 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 Janus face of copper: its expanding roles in biology and the pathophysiology of disease. Meeting on Copper and Related Metals in Biology

Scot C. Leary, Dennis R. Winge
<span title="2007-02-16">2007</span> <i title="Wiley"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/ad4yn77omvbz5mxraouyuuhroq" style="color: black;">EMBO Reports</a> </i> &nbsp;
Regulation of cellular copper levels Cellular copper levels are controlled by the interplay between the ATPase exporters and the Ctr family of copper permeases. J.  ...  Cu(I) is trafficked in the cytoplasm of eukaryotic cells by metallochaperone proteins to various intracellular sites of utilization.  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1038/sj.embor.7400915">doi:10.1038/sj.embor.7400915</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/17304237">pmid:17304237</a> <a target="_blank" rel="external noopener" href="https://pubmed.ncbi.nlm.nih.gov/PMC1808038/">pmcid:PMC1808038</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/h4plswgmwndj5ig6tgcvvmfqpm">fatcat:h4plswgmwndj5ig6tgcvvmfqpm</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20170809031826/http://embor.embopress.org/content/embor/8/3/224.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/c7/f6/c7f69de42d8c1392047a39a7f8e376411c59fec3.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1038/sj.embor.7400915"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="external alternate icon"></i> Publisher / doi.org </button> </a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1808038" 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 SLC31 (Ctr) copper transporter family

Michael J. Petris
<span title="2004-02-01">2004</span> <i title="Springer Nature"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/vzoeefih5ne67lh2qmgxzke42m" style="color: black;">Pflügers Archiv: European Journal of Physiology</a> </i> &nbsp;
These high-affinity copper transporters exist in all eukaryotes and their discovery has provided new insights into how cells acquire and regulate this essential nutrient.  ...  The identification of proteins for high affinity copper uptake and export has greatly expanded our understanding of cellular copper homeostasis.  ...  copper to each metallochaperone.  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1007/s00424-003-1092-1">doi:10.1007/s00424-003-1092-1</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/12827356">pmid:12827356</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/m77e27tllrdupbcq4wx4voqgmq">fatcat:m77e27tllrdupbcq4wx4voqgmq</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20040510232651/http://129.22.192.74:80/Papers/SLC-Reviews/SLC31-Ctr-PfArch2004.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/f6/0e/f60e56356364714b3999b5da92f312b6df2cef9f.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1007/s00424-003-1092-1"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="external alternate icon"></i> springer.com </button> </a>

Recent developments in copper and zinc homeostasis in bacterial pathogens

Joseph J Braymer, David P Giedroc
<span title="2014-01-22">2014</span> <i title="Elsevier BV"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/o5uh5dlljbbfjm7vgxk2jibrwu" style="color: black;">Current Opinion in Chemical Biology</a> </i> &nbsp;
Cu-specific and Zn-specific metalloregulatory proteins regulate the transcription of metal-responsive genes while metallochaperones and related proteins ensure that these metals are appropriately buffered  ...  by the intracellular milieu and delivered to correct intracellular targets.  ...  Metallochaperones buffer highly competitive Cu(I) to low levels in the cytoplasm [31] and shuttle Cu(I) to intracellular targets including cytoplasmic Cu(I) sensors and to Cu(I)-specific P-type ATPase  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1016/j.cbpa.2013.12.021">doi:10.1016/j.cbpa.2013.12.021</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/24463765">pmid:24463765</a> <a target="_blank" rel="external noopener" href="https://pubmed.ncbi.nlm.nih.gov/PMC4008645/">pmcid:PMC4008645</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/yae7xprdqfdktozumxdu2svtnu">fatcat:yae7xprdqfdktozumxdu2svtnu</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20200207211857/http://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC4008645&amp;blobtype=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/d9/59/d959574ce08ed92490b5f8e86ca06756cc9198b3.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1016/j.cbpa.2013.12.021"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="external alternate icon"></i> elsevier.com </button> </a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4008645" title="pubmed link"> <button class="ui compact blue labeled icon button serp-button"> <i class="file alternate outline icon"></i> pubmed.gov </button> </a>

Metal Ion availability in mitochondria

Fabien Pierrel, Paul A. Cobine, Dennis R. Winge
<span title="2007-01-16">2007</span> <i title="Springer Nature"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/2yxcbkleljg7vhw4ll45joo3zy" style="color: black;">Biometals</a> </i> &nbsp;
Thus, regulation of metal ion accessibility and bioavailability must exist.  ...  Copper, iron, manganese and zinc are cofactors in metalloenzymes and metalloproteins within the organelle.  ...  The set of genes regulated by Aft1 and Aft2 includes a series of genes whose products function in iron acquisition and intracellular iron distribution.  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1007/s10534-006-9052-9">doi:10.1007/s10534-006-9052-9</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/17225062">pmid:17225062</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/5cx23ivijzdi3ouzdy3w2sznze">fatcat:5cx23ivijzdi3ouzdy3w2sznze</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20180724001626/https://hal.archives-ouvertes.fr/hal-00375433/file/Biometals.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/a9/02/a902dc8aad82edfa0f1c0b281284625b72c80a99.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1007/s10534-006-9052-9"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="external alternate icon"></i> springer.com </button> </a>

Copper Metallochaperones are Required for the Assembly of Bacteroid Cytochrome c Oxidase Which is Functioning for Nitrogen Fixation in Soybean Nodules

Hatthaya Arunothayanan, Mika Nomura, Rie Hamaguchi, Manabu Itakura, Kiwamu Minamisawa, Shigeyuki Tajima
<span title="2010-06-14">2010</span> <i title="Oxford University Press (OUP)"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/qyzgzqbtjbd3xewtgies5bhl2e" style="color: black;">Plant and Cell Physiology</a> </i> &nbsp;
Bll4880 contained a copper-binding motif for metallochaperone, H(M)X 10 MX 21 HXM. A mutant strain, Bj4880, induced nodules with lower acetylene reduction activity.  ...  Our data suggest that bll4880 protein is involved in copper ion delivery to Cco through blr1131 protein, and the expression of both proteins was induced under microaerobic conditions.  ...  In contrast, an aa3 -type heme copper Cco (CoxA, CoxB; Bott et al. 1990 ) and an alternative heme -copper Cco (CoxN, CoxM; Bott et al. 1990 ) showed expression at a higher level with aerobically grown  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1093/pcp/pcq079">doi:10.1093/pcp/pcq079</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/20519277">pmid:20519277</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/n4f5zrkgvzb6nord3bt2unpxau">fatcat:n4f5zrkgvzb6nord3bt2unpxau</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20190221231942/http://pdfs.semanticscholar.org/3057/1f3fe72fc1401f2ad16a8cc3c677be0d43a8.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/30/57/30571f3fe72fc1401f2ad16a8cc3c677be0d43a8.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1093/pcp/pcq079"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="external alternate icon"></i> oup.com </button> </a>

Metalloproteins and metal sensing

Kevin J. Waldron, Julian C. Rutherford, Dianne Ford, Nigel J. Robinson
<span title="">2009</span> <i title="Springer Nature"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/drfdii35rzaibj3aml5uhvr5xm" style="color: black;">Nature</a> </i> &nbsp;
Cells are not ideal solutions and kinetic factors can dominate the distribution of metals, for example where metals are delivered by metallochaperones.  ...  The natural order of stability for divalent metals, often called the Irving-Williams series 4 , sets out a resulting trend with copper and zinc forming the tightest complexes, then nickel and cobalt, followed  ...  ZIP4 has three levels of post-translational regulation in response to zinc.  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1038/nature08300">doi:10.1038/nature08300</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/19675642">pmid:19675642</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/3jwxzj2jlzfozbt33lhrnhgq3y">fatcat:3jwxzj2jlzfozbt33lhrnhgq3y</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20170809110751/http://bohr.winthrop.edu/faculty/grossoehme/link_to_webpages/personal/articles/Reviews/Nijel%20Robinson%20Nature%202009%20Review.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/2f/dc/2fdca495a006aed4cb7d7eb822ce97186102e4b5.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1038/nature08300"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="external alternate icon"></i> nature.com </button> </a>

Higher plants possess two different types of ATX1-like copper chaperones

Sergi Puig, Helena Mira, Eavan Dorcey, Vicente Sancenón, Nuria Andrés-Colás, Antoni Garcia-Molina, Jason L. Burkhead, Kathryn A. Gogolin, Salah E. Abdel-Ghany, Dennis J. Thiele, Joseph R. Ecker, Marinus Pilon (+1 others)
<span title="">2007</span> <i title="Elsevier BV"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/ypsixbtbfrezvpluf74fdc2aeq" style="color: black;">Biochemical and Biophysical Research Communications - BBRC</a> </i> &nbsp;
Copper (Cu) chaperones constitute a family of small Cu + -binding proteins required for Cu homeostasis in eukaryotes.  ...  Eukaryotic organisms deal with copper (Cu) through complex homeostatic networks that tightly regulate intracellular Cu levels to ensure its availability, while avoiding its potential toxicity (reviewed  ...  Second, only CCH but not AtATX1 mRNA levels are down-regulated upon Cu treatment ( [13] , and Fig. S2 ).  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1016/j.bbrc.2006.12.215">doi:10.1016/j.bbrc.2006.12.215</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/17223078">pmid:17223078</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/6jjgozbetjbefnpcii6tej6mjq">fatcat:6jjgozbetjbefnpcii6tej6mjq</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20100527234859/http://www.hiram.edu/biology/faculty/documents/Puigetal2007_000.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/eb/e9/ebe96588ca409b4a34e47434f328c7ff15295b97.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1016/j.bbrc.2006.12.215"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="external alternate icon"></i> elsevier.com </button> </a>

Metallochaperones and metalloregulation in bacteria

Daiana A. Capdevila, Katherine A. Edmonds, David P. Giedroc
<span title="2017-05-09">2017</span> <i title="Portland Press Ltd."> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/y5hbc7qpnjd73b3umji6wrwbce" style="color: black;">Essays in Biochemistry</a> </i> &nbsp;
in the metallocofactor active site assembly in metalloenzymes and metallosensors, which govern the systems-level response to metal limitation and intoxication.  ...  Bacterial transition metal homoeostasis or simply 'metallostasis' describes the process by which cells control the intracellular availability of functionally required metal cofactors, from manganese (Mn  ...  copper-responsive repressor CsoR copper-sensitive operon repressor CzrA chromosomal zinc-regulated repressor DtxR diphtheria toxin repressor Fur ferric uptake regulator GntR gluconate  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1042/ebc20160076">doi:10.1042/ebc20160076</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/28487396">pmid:28487396</a> <a target="_blank" rel="external noopener" href="https://pubmed.ncbi.nlm.nih.gov/PMC5858914/">pmcid:PMC5858914</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/huz2iw6jqjgjvp64ql7ryzqxmy">fatcat:huz2iw6jqjgjvp64ql7ryzqxmy</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20200210013403/http://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC5858914&amp;blobtype=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/1a/cc/1accc28452cea9266805356c39fc44d6abfe7ec6.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1042/ebc20160076"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="external alternate icon"></i> Publisher / doi.org </button> </a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5858914" title="pubmed link"> <button class="ui compact blue labeled icon button serp-button"> <i class="file alternate outline icon"></i> pubmed.gov </button> </a>

A Novel Role for the Immunophilin FKBP52 in Copper Transport

Reiko Sanokawa-Akakura, Huachang Dai, Shin Akakura, David Weinstein, J. Eduardo Fajardo, Steven E. Lang, Scott Wadsworth, John Siekierka, Raymond B. Birge
<span title="2004-05-07">2004</span> <i title="American Society for Biochemistry &amp; Molecular Biology (ASBMB)"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/mryncoafc5cxdicldzfm4vlsze" style="color: black;">Journal of Biological Chemistry</a> </i> &nbsp;
that the interaction is regulated in part by intracellular copper.  ...  We identified an interaction between FKBP52 domain I and Atox1, a copper-binding metallochaperone.  ...  Although FKBP52 could conceivably effect copper by regulating the transfer of copper from apo-Atox1 to Cu-Atox1, studies by Hamza and colleagues (28) showed that when intracellular copper levels are  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1074/jbc.c400118200">doi:10.1074/jbc.c400118200</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/15133031">pmid:15133031</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/zlziuxsmz5bzrodpbw426iepge">fatcat:zlziuxsmz5bzrodpbw426iepge</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20180723034437/http://www.jbc.org/content/279/27/27845.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/77/c8/77c8d2b8efc0f3ee3fe194094cb19d0a201a8119.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1074/jbc.c400118200"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="unlock alternate icon" style="background-color: #fb971f;"></i> Publisher / doi.org </button> </a>

An NMR Study of the Interaction of the N-terminal Cytoplasmic Tail of the Wilson Disease Protein with Copper(I)-HAH1

Lucia Banci, Ivano Bertini, Francesca Cantini, Chiara Massagni, Manuele Migliardi, Antonio Rosato
<span title="2009-01-30">2009</span> <i title="American Society for Biochemistry &amp; Molecular Biology (ASBMB)"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/mryncoafc5cxdicldzfm4vlsze" style="color: black;">Journal of Biological Chemistry</a> </i> &nbsp;
ATP7B is a human P 1B -type ATPase that has a crucial role in maintaining copper(I) homeostasis. Mutations in the corresponding gene are the cause of Wilson disease.  ...  We expressed the entire tail as a single construct in Escherichia coli and investigated its interaction with its copper chaperone (i.e. HAH1) by solution NMR spectroscopy.  ...  The presence of either the intact fifth or intact sixth metal-binding domain in the human proteins is sufficient to support both WLN/MNK activity and intracellular trafficking at essentially normal levels  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1074/jbc.m805981200">doi:10.1074/jbc.m805981200</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/19181666">pmid:19181666</a> <a target="_blank" rel="external noopener" href="https://pubmed.ncbi.nlm.nih.gov/PMC2666587/">pmcid:PMC2666587</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/au7nazmwxnd6rmpky6xqyh6xhm">fatcat:au7nazmwxnd6rmpky6xqyh6xhm</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20180725002524/http://www.jbc.org/content/284/14/9354.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/08/41/0841a5bb96491fe07e033cd3a0e9db867480dfea.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1074/jbc.m805981200"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="unlock alternate icon" style="background-color: #fb971f;"></i> Publisher / doi.org </button> </a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2666587" title="pubmed link"> <button class="ui compact blue labeled icon button serp-button"> <i class="file alternate outline icon"></i> pubmed.gov </button> </a>

Copper Metallochaperones

Nigel J. Robinson, Dennis R. Winge
<span title="2010-06-07">2010</span> <i title="Annual Reviews"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/k4xilfaaarb7ngi345nlojrsmq" style="color: black;">Annual Review of Biochemistry</a> </i> &nbsp;
The current state of knowledge on how copper metallochaperones support the maturation of cuproproteins is reviewed.  ...  Copper metallochaperones assist copper in reaching vital destinations without inflicting damage or becoming trapped in adventitious binding sites.  ...  If CopZ solely donated Cu(I) ions to a copper exporter, then intracellular copper levels would be elevated in copZ, and copper-responsive expression of the cop operon would be predicted to become higher  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1146/annurev-biochem-030409-143539">doi:10.1146/annurev-biochem-030409-143539</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/20205585">pmid:20205585</a> <a target="_blank" rel="external noopener" href="https://pubmed.ncbi.nlm.nih.gov/PMC3986808/">pmcid:PMC3986808</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/emzifidldvdqdl4ip4obomqhim">fatcat:emzifidldvdqdl4ip4obomqhim</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20190222235021/http://pdfs.semanticscholar.org/3c51/0c24e88ce9bdb411d2a81ef645809e57375a.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/3c/51/3c510c24e88ce9bdb411d2a81ef645809e57375a.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1146/annurev-biochem-030409-143539"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="external alternate icon"></i> Publisher / doi.org </button> </a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3986808" title="pubmed link"> <button class="ui compact blue labeled icon button serp-button"> <i class="file alternate outline icon"></i> pubmed.gov </button> </a>

Determinants of Copper Resistance in Acidithiobacillus Ferrivorans ACH Isolated from the Chilean Altiplano

Sergio Barahona, Juan Castro-Severyn, Cristina Dorador, Claudia Saavedra, Francisco Remonsellez
<span title="2020-07-24">2020</span> <i title="MDPI AG"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/githwx23ynaxdoftesby3jya3y" style="color: black;">Genes</a> </i> &nbsp;
Moreover, transcriptional expression showed an up-regulation response (acop, copZ, cusA, rusA, and rusB) to high copper concentrations.  ...  Therefore, we propose to elucidate the response mechanisms of A. ferrivorans ACH to high copper concentrations (0–800 mM), describing its genetic repertoire and transcriptional regulation.  ...  Then, when the cells were grown in 40 mM of CuSO 4 , the transcriptional level was up-regulated (threefold) at a lower magnitude [60] .  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.3390/genes11080844">doi:10.3390/genes11080844</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/32722087">pmid:32722087</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/36waqnphovds3i6slm46mli7c4">fatcat:36waqnphovds3i6slm46mli7c4</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20200725040648/https://res.mdpi.com/d_attachment/genes/genes-11-00844/article_deploy/genes-11-00844.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/32/18/32183fae464913dad56b328274eb3a7f727ba27a.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.3390/genes11080844"> <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>

Sensing Nickel

John D Helmann
<span title="">2002</span> <i title="Elsevier BV"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/v6fzdolajra2detrgb2pojrdpm" style="color: black;">Chemistry and Biology</a> </i> &nbsp;
that sense the intracellular levels of metal ions.  ...  Are there specific metallochaperones Ni(II) concentrations above 100 M [13] , suggesting that such levels may also be achieved in vivo. Clearly, this for all the essential trace metals?  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1016/s1074-5521(02)00251-x">doi:10.1016/s1074-5521(02)00251-x</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/12401490">pmid:12401490</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/mukoq4yxbva73j47hnbfz3enk4">fatcat:mukoq4yxbva73j47hnbfz3enk4</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20170927111433/http://publisher-connector.core.ac.uk/resourcesync/data/elsevier/pdf/518/aHR0cDovL2FwaS5lbHNldmllci5jb20vY29udGVudC9hcnRpY2xlL3BpaS9zMTA3NDU1MjEwMjAwMjUxeA%3D%3D.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/ce/ad/ceada99c7ff631cdc489eebde4da1c0f5705d830.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1016/s1074-5521(02)00251-x"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="external alternate icon"></i> elsevier.com </button> </a>

The structural flexibility of the human copper chaperone Atox1: Insights from combined pulsed EPR studies and computations

Ariel R. Levy, Meital Turgeman, Lada Gevorkyan-Aiapetov, Sharon Ruthstein
<span title="2017-05-31">2017</span> <i title="Wiley"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/6bubxfqklvdwthsc43yvjbtjae" style="color: black;">Protein Science</a> </i> &nbsp;
Here, we sought to shed light on the structure of Atox1, a metallochaperone involved in the human copper regulation system.  ...  Statement (50-75 Words) Using EPR spectroscopy and computations, we show that the human copper metallochaperone Atox1 can accommodate at least six different conformational states.  ...  adjusted in response to shifting levels of cellular Cu(I). 12, 14 The metallochaperone Atox1 is responsible for transferring copper from Ctr1 to the N-terminal domains of ATP7a and ATP7b in the Golgi  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1002/pro.3197">doi:10.1002/pro.3197</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/28543811">pmid:28543811</a> <a target="_blank" rel="external noopener" href="https://pubmed.ncbi.nlm.nih.gov/PMC5521546/">pmcid:PMC5521546</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/imez2ypom5cqrdikjdajdgpc7e">fatcat:imez2ypom5cqrdikjdajdgpc7e</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20200209000759/http://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC5521546&amp;blobtype=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/9c/b9/9cb985b8fc5e19ad64942ad08209496025e4f4c5.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1002/pro.3197"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="external alternate icon"></i> wiley.com </button> </a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5521546" title="pubmed link"> <button class="ui compact blue labeled icon button serp-button"> <i class="file alternate outline icon"></i> pubmed.gov </button> </a>
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