Zobrazeno 1 - 10
of 57
pro vyhledávání: '"John R. Glover"'
Autor:
Chunzhong Yang, John R Glover
Publikováno v:
PLoS ONE, Vol 4, Iss 2, p e4459 (2009)
The ssrA gene encodes tmRNA that, together with a specialized tmRNA-binding protein, SmpB, forms part of a ribonucleoprotein complex, provides a template for the resumption of translation elongation, subsequent termination and recycling of stalled ri
Externí odkaz:
https://doaj.org/article/62fe22cd07bb432d93db45940f2ab6fd
Autor:
Ronnie Lum, John R. Glover
Publikováno v:
Protein & Peptide Letters. 16:587-597
Hsp104 is molecular chaperone in the AAA+ family of ATPases that specializes in the resolubilization and refolding of thermally denatured proteins in yeast. In addition to providing high levels of thermotolerance, Hsp104 plays a pivotal role in the p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67ca80a260461f30b1f1506ed174da7e
https://doi.org/10.2174/092986609788490087
https://doi.org/10.2174/092986609788490087
Publikováno v:
Journal of Biological Chemistry. 283:30139-30150
The AAA+ molecular chaperone Hsp104 mediates the extraction of proteins from aggregates by unfolding and threading them through its axial channel in an ATP-driven process. An Hsp104-binding peptide selected from solid phase arrays enhanced the refold
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a652fdc84e5c85098cd7ca72cf5f0b72
https://doi.org/10.1074/jbc.m804849200
https://doi.org/10.1074/jbc.m804849200
Autor:
Johnny M. Tkach, John R. Glover
Publikováno v:
Journal of Biological Chemistry. 279:35692-35701
Hsp104 is an important determinant of thermotolerance in yeast and is an unusual molecular chaperone that specializes in the remodeling of aggregated proteins. The structural requirements for Hsp104-substrate interactions remain unclear. Upon mild he
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e19e0ce495d71dc33b5dca11ff998214
https://doi.org/10.1074/jbc.m400782200
https://doi.org/10.1074/jbc.m400782200
Publikováno v:
Biochemistry. 43:8107-8115
Hsp104, the most potent thermotolerance factor in Saccharomyces cerevisiae, is an unusual molecular chaperone that is associated with the dispersal of aggregated, non-native proteins in vivo and in vitro. The close cooperation between Hsp100 oligomer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b31c177fee894fe651a6baea43e4d01d
https://doi.org/10.1021/bi0493766
https://doi.org/10.1021/bi0493766
Autor:
John R Glover, Susan Lindquist, Douglas A. Hattendorf, Danielle M. Ware, Eric C. Schirmer, Melarkode S Ramakrishnan, Anil G. Cashikar
Publikováno v:
Molecular Cell. 9:751-760
AAA proteins remodel other proteins to affect a multitude of biological processes. Their power to remodel substrates must lie in their capacity to couple substrate binding to conformational changes via cycles of nucleotide binding and hydrolysis, but
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9559cb242a5029ae77835944b7de826c
https://doi.org/10.1016/s1097-2765(02)00499-9
https://doi.org/10.1016/s1097-2765(02)00499-9
Autor:
John M Tkach, John R. Glover
Publikováno v:
Biochemistry and Cell Biology. 79:557-568
Molecular chaperones have the capacity to prevent inappropriate interactions between aggregation-prone folding or unfolding intermediates created in the cell during protein synthesis or in response to physical and chemical stress. What happens when s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::22cabcca689c7375517ea71da6e5eeee
https://doi.org/10.1139/o01-148
https://doi.org/10.1139/o01-148
Autor:
John R Glover, Susan Lindquist
Publikováno v:
Cell. 94:73-82
Hsp104 is a stress tolerance factor that promotes the reactivation of heat-damaged proteins in yeast by an unknown mechanism. Herein, we demonstrate that Hsp104 functions in this process directly. Unlike other chaperones, Hsp104 does not prevent the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8da1e1f8f902e7595210a19b1b157104
https://doi.org/10.1016/s0092-8674(00)81223-4
https://doi.org/10.1016/s0092-8674(00)81223-4
Autor:
Eric C. Schirmer, John R Glover, Maria M. Patino, Jia-Jia Liu, Susan Lindquist, Anthony S. Kowal
Publikováno v:
Cell. 89(5):811-819
The [PSI+] factor of S. cerevisiae represents a new form of inheritance: cytosolic transmission of an altered phenotype is apparently based upon inheritance of an altered protein structure rather than an altered nucleic acid. The molecular basis of i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::400cc33552c6abb260f2c961d9c3ea55
Publikováno v:
Science (New York, N.Y.). 339(6123)
Dissecting Disaggregation The excessive accumulation of misfolded protein aggregates can overwhelm the cell's "quality control" machinery, leading to cell death. The yeast Hsp104 protein and its bacterial homolog ClpB are molecular chaperones that ca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::185ec5492bba7cc2cf7608b047c57fcd
https://pubmed.ncbi.nlm.nih.gov/23449583
https://pubmed.ncbi.nlm.nih.gov/23449583