Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Micheal E. Barnett"'
Autor:
Micheal E. Barnett, Maria I. Zavodszky, Sabina Kędzierska-Mieszkowska, Michal Zolkiewski, Izabela Guenther, Vladimir Akoyev, Maria Nagy
Publikováno v:
Journal of Molecular Biology. 396:697-707
Bacterial AAA+ ATPase ClpB cooperates with DnaK during reactivation of aggregated proteins. The ClpB-mediated disaggregation is linked to translocation of polypeptides through the channel in the oligomeric ClpB. Two isoforms of ClpB are produced in v
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ea550cc57d252a702dbccf257f43955
https://doi.org/10.1016/j.jmb.2009.11.059
https://doi.org/10.1016/j.jmb.2009.11.059
Autor:
Samuel Lobell, Guido A. Zampighi, D. Madgwick, Micheal E. Barnett, Dingbo Lin, Dolores J. Takemoto, Lloyd Willard, Denton Shanks
Publikováno v:
Journal of Experimental Biology. 209:4371-4378
Cataracts, or lens opacities, are the leading cause of blindness worldwide. Cataracts increase with age and environmental insults, e.g. oxidative stress. Lens homeostasis depends on functional gap junctions. Knockout or missense mutations of lens gap
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5de35f2c62c39836a2cc36267d66d09
https://doi.org/10.1242/jeb.02524
https://doi.org/10.1242/jeb.02524
Publikováno v:
Journal of Biological Chemistry. 280:34940-34945
Bacterial heat-shock proteins, ClpB and DnaK form a bichaperone system that efficiently reactivates aggregated proteins. ClpB undergoes nucleotide-dependent self-association and forms ring-shaped oligomers. The ClpB-assisted dissociation of protein a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8425defda7fb5fd90bc52dec9609614d
https://doi.org/10.1074/jbc.m505653200
https://doi.org/10.1074/jbc.m505653200
Publikováno v:
Biochemistry. 42:14242-14248
ClpB belongs to the Hsp100/Clp ATPase family. Whereas a homologue of ClpB, ClpA, interacts with and stimulates the peptidase ClpP, ClpB does not associate with peptidases and instead cooperates with DnaK/DnaJ/GrpE in an efficient reactivation of seve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::145ae767ba58a336577980a0bffe933d
https://doi.org/10.1021/bi035573d
https://doi.org/10.1021/bi035573d
Autor:
Michal Zolkiewski, Micheal E. Barnett
Publikováno v:
Biochemistry. 41:11277-11283
ClpB is a member of a multichaperone system in Escherichia coli (with DnaK, DnaJ, and GrpE) that reactivates strongly aggregated proteins. The sequence of ClpB contains two ATP-binding domains, each containing Walker consensus motifs. The N- and C-te
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::18f7aee7c559830c3e876919a0ac5fb2
https://doi.org/10.1021/bi026161s
https://doi.org/10.1021/bi026161s
While there are many reviews which examine the group of proteins known as protein kinase C (PKC), the focus of this article is to examine the cellular roles of two PKCs that are important for stress responses in neurological tissues (PKC gamma and ep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::741426e3a0fa7f3de0c6c97f275d44ba
https://europepmc.org/articles/PMC1986756/
https://europepmc.org/articles/PMC1986756/
Publikováno v:
FEBS letters. 579(20)
ClpB/Hsp104 collaborates with the Hsp70 system to promote the solubilization and reactivation of proteins that misfold and aggregate following heat shock. In Escherichia coli and other eubacteria, two ClpB isoforms (ClpB95 and ClpB80) that differ by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::338c54d345d5dcfb6c76db40191db3ed
https://pubmed.ncbi.nlm.nih.gov/16051221
https://pubmed.ncbi.nlm.nih.gov/16051221
ClpB is a member of the bacterial protein-disaggregating chaperone machinery and belongs to the AAA(+) superfamily of ATPases associated with various cellular activities. The mechanism of ClpB-assisted reactivation of strongly aggregated proteins is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c79d746e89879b6b4161094ee9a5f43d
https://europepmc.org/articles/PMC1828688/
https://europepmc.org/articles/PMC1828688/