Farnesylation of Ydj1 is required for in vivo interaction with Hsp90 client proteins.
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Optimal functional levels of activation-induced deaminase specifically require the Hsp40 DnaJa1Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins.Chemical inhibition of CaaX protease activity disrupts yeast Ras localization.Threonine 22 phosphorylation attenuates Hsp90 interaction with cochaperones and affects its chaperone activityGlobal proteomic analysis of prenylated proteins in Plasmodium falciparum using an alkyne-modified isoprenoid analogueThe HSP70 chaperone machinery: J proteins as drivers of functional specificitySpatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress.Hsp90 and co-chaperones twist the functions of diverse client proteins.An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humansHsp110 chaperones control client fate determination in the hsp70-Hsp90 chaperone systemHsp40s specify functions of Hsp104 and Hsp90 protein chaperone machines.The ribosomal biogenesis protein Utp21 interacts with Hsp90 and has differing requirements for Hsp90-associated proteins.Hsp70 clears misfolded kinases that partitioned into distinct quality-control compartments.Polypeptide transfer from Hsp40 to Hsp70 molecular chaperones.Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.A network of ubiquitin ligases is important for the dynamics of misfolded protein aggregates in yeast.c-Abl Mediated Tyrosine Phosphorylation of Aha1 Activates Its Co-chaperone Function in Cancer Cells.Mps1 Mediated Phosphorylation of Hsp90 Confers Renal Cell Carcinoma Sensitivity and Selectivity to Hsp90 Inhibitors.Identification of a consensus motif in substrates bound by a Type I Hsp40.Prion propagation by Hsp40 molecular chaperones.Influence of Hsp70s and their regulators on yeast prion propagationAsymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors.Mechanisms of the Hsp70 chaperone system.HSC90 is required for nascent hepatitis C virus core protein stability in yeast cells.A shunt pathway limits the CaaX processing of Hsp40 Ydj1p and regulates Ydj1p-dependent phenotypes.Hsp70/J-protein machinery from Glossina morsitans morsitans, vector of African trypanosomiasisThe DNAJA2 substrate release mechanism is essential for chaperone-mediated folding.The type I Hsp40 Ydj1 utilizes a farnesyl moiety and zinc finger-like region to suppress prion toxicity.Heat-shock protein 40 is the key farnesylation target in meristem size control, abscisic acid signaling, and drought resistance.Evidence for Hsp90 Co-chaperones in Regulating Hsp90 Function and Promoting Client Protein Folding.Functional and physical interaction between yeast Hsp90 and Hsp70.Farnesylated heat shock protein 40 is a component of membrane-bound RISC in
P2860
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P2860
Farnesylation of Ydj1 is required for in vivo interaction with Hsp90 client proteins.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Farnesylation of Ydj1 is required for in vivo interaction with Hsp90 client proteins.
@en
type
label
Farnesylation of Ydj1 is required for in vivo interaction with Hsp90 client proteins.
@en
prefLabel
Farnesylation of Ydj1 is required for in vivo interaction with Hsp90 client proteins.
@en
P2093
P2860
P356
P1476
Farnesylation of Ydj1 is required for in vivo interaction with Hsp90 client proteins
@en
P2093
Elizabeth A Fortunato
Gary A Flom
Jill L Johnson
P2860
P304
P356
10.1091/MBC.E08-04-0435
P577
2008-10-01T00:00:00Z