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Promiscuity and preferences of metallothioneins: the cell rules
Metalloproteins are essential for many cellular functions, but it has not been clear how they distinguish between the different metals to bind the correct ones. A report in BMC Biology finds that preferences of two metallothionein isoforms for two different cations are due to inherent properties of...
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2011
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3084178/ https://www.ncbi.nlm.nih.gov/pubmed/21527046 http://dx.doi.org/10.1186/1741-7007-9-25 |
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author | Foster, Andrew W Robinson, Nigel J |
author_facet | Foster, Andrew W Robinson, Nigel J |
author_sort | Foster, Andrew W |
collection | PubMed |
description | Metalloproteins are essential for many cellular functions, but it has not been clear how they distinguish between the different metals to bind the correct ones. A report in BMC Biology finds that preferences of two metallothionein isoforms for two different cations are due to inherent properties of these usually less discriminating proteins. Here these observations are discussed in the context of the cellular mechanisms that regulate metal binding to proteins. See research article: http://www.biomedcentral.com/1741-7007/9/4 |
format | Text |
id | pubmed-3084178 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-30841782011-04-29 Promiscuity and preferences of metallothioneins: the cell rules Foster, Andrew W Robinson, Nigel J BMC Biol Commentary Metalloproteins are essential for many cellular functions, but it has not been clear how they distinguish between the different metals to bind the correct ones. A report in BMC Biology finds that preferences of two metallothionein isoforms for two different cations are due to inherent properties of these usually less discriminating proteins. Here these observations are discussed in the context of the cellular mechanisms that regulate metal binding to proteins. See research article: http://www.biomedcentral.com/1741-7007/9/4 BioMed Central 2011-04-28 /pmc/articles/PMC3084178/ /pubmed/21527046 http://dx.doi.org/10.1186/1741-7007-9-25 Text en Copyright ©2011 Foster and Robinson; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Commentary Foster, Andrew W Robinson, Nigel J Promiscuity and preferences of metallothioneins: the cell rules |
title | Promiscuity and preferences of metallothioneins: the cell rules |
title_full | Promiscuity and preferences of metallothioneins: the cell rules |
title_fullStr | Promiscuity and preferences of metallothioneins: the cell rules |
title_full_unstemmed | Promiscuity and preferences of metallothioneins: the cell rules |
title_short | Promiscuity and preferences of metallothioneins: the cell rules |
title_sort | promiscuity and preferences of metallothioneins: the cell rules |
topic | Commentary |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3084178/ https://www.ncbi.nlm.nih.gov/pubmed/21527046 http://dx.doi.org/10.1186/1741-7007-9-25 |
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