Out with the old: Hsp90 finds amino acid residue more useful than co-chaperone protein
Redundant functions maintained from single to multi-cellular organisms have made Saccharomyces cere-visiae an important model for the analysis of con-served com-plex cellular processes. Yeast has been especially useful in understanding the regulation and function of the essential molecular chaperone...
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| Format: | Article |
| Language: | English |
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Shared Science Publishers OG
2017-08-01
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| Series: | Microbial Cell |
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| Online Access: | http://microbialcell.com/researcharticles/out-with-the-old-hsp90-finds-amino-acid-residue-more-useful-than-co-chaperone-protein/ |
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| _version_ | 1850050755384311808 |
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| author | Abbey D. Zuehlke Leonard Neckers |
| author_facet | Abbey D. Zuehlke Leonard Neckers |
| author_sort | Abbey D. Zuehlke |
| collection | DOAJ |
| description | Redundant functions maintained from single to multi-cellular organisms have made Saccharomyces cere-visiae an important model for the analysis of con-served com-plex cellular processes. Yeast has been especially useful in understanding the regulation and function of the essential molecular chaperone, Heat Shock Protein 90 (Hsp90). Research focused on Hsp90 has determined that it is highly regulated by both co-chaperones and posttranslational modifications. A recent study per-formed by (Zuehlke et al., 2017) demonstrates that the function of one co-chaperone in yeast is replaced by posttranslational modification (PTM) of a single amino acid within Hsp90 in higher eukaryotes. |
| format | Article |
| id | doaj-art-32dff5d1a80e483494e12ad0e5ecc411 |
| institution | DOAJ |
| issn | 2311-2638 |
| language | English |
| publishDate | 2017-08-01 |
| publisher | Shared Science Publishers OG |
| record_format | Article |
| series | Microbial Cell |
| spelling | doaj-art-32dff5d1a80e483494e12ad0e5ecc4112025-08-20T02:53:21ZengShared Science Publishers OGMicrobial Cell2311-26382017-08-014827327410.15698/mic2017.08.586Out with the old: Hsp90 finds amino acid residue more useful than co-chaperone proteinAbbey D. Zuehlke0Leonard Neckers1Urologic Oncology Branch, Center for Cancer Research, National Cancer Institute, 9000 Rockville Pike, Bethesda, MD 20892, USA.Urologic Oncology Branch, Center for Cancer Research, National Cancer Institute, 9000 Rockville Pike, Bethesda, MD 20892, USA.Redundant functions maintained from single to multi-cellular organisms have made Saccharomyces cere-visiae an important model for the analysis of con-served com-plex cellular processes. Yeast has been especially useful in understanding the regulation and function of the essential molecular chaperone, Heat Shock Protein 90 (Hsp90). Research focused on Hsp90 has determined that it is highly regulated by both co-chaperones and posttranslational modifications. A recent study per-formed by (Zuehlke et al., 2017) demonstrates that the function of one co-chaperone in yeast is replaced by posttranslational modification (PTM) of a single amino acid within Hsp90 in higher eukaryotes.http://microbialcell.com/researcharticles/out-with-the-old-hsp90-finds-amino-acid-residue-more-useful-than-co-chaperone-protein/co-chaperoneposttranslational modificationATPase cycleclient protein |
| spellingShingle | Abbey D. Zuehlke Leonard Neckers Out with the old: Hsp90 finds amino acid residue more useful than co-chaperone protein Microbial Cell co-chaperone posttranslational modification ATPase cycle client protein |
| title | Out with the old: Hsp90 finds amino acid residue more useful than co-chaperone protein |
| title_full | Out with the old: Hsp90 finds amino acid residue more useful than co-chaperone protein |
| title_fullStr | Out with the old: Hsp90 finds amino acid residue more useful than co-chaperone protein |
| title_full_unstemmed | Out with the old: Hsp90 finds amino acid residue more useful than co-chaperone protein |
| title_short | Out with the old: Hsp90 finds amino acid residue more useful than co-chaperone protein |
| title_sort | out with the old hsp90 finds amino acid residue more useful than co chaperone protein |
| topic | co-chaperone posttranslational modification ATPase cycle client protein |
| url | http://microbialcell.com/researcharticles/out-with-the-old-hsp90-finds-amino-acid-residue-more-useful-than-co-chaperone-protein/ |
| work_keys_str_mv | AT abbeydzuehlke outwiththeoldhsp90findsaminoacidresiduemoreusefulthancochaperoneprotein AT leonardneckers outwiththeoldhsp90findsaminoacidresiduemoreusefulthancochaperoneprotein |