The Hsp organizer protein hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone system
about
Glucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cyclesCo-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53.Hsp70-RAP46 interaction in downregulation of DNA binding by glucocorticoid receptorHsp70 chaperones: cellular functions and molecular mechanismThe architecture of functional modules in the Hsp90 co-chaperone Sti1/HopMechanistic Asymmetry in Hsp90 DimersNucleotide binding states of hsp70 and hsp90 during sequential steps in the process of glucocorticoid receptor.hsp90 heterocomplex assemblyHSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptorMaternal Plane of Nutrition during Late Gestation and Weaning Age Alter Angus × Simmental Offspring Longissimus Muscle Transcriptome and Intramuscular Fat.Ligand discrimination by TPR domains. Relevance and selectivity of EEVD-recognition in Hsp70 x Hop x Hsp90 complexes.Inhibition of hsp70 by methylene blue affects signaling protein function and ubiquitination and modulates polyglutamine protein degradationThe cochaperone SGTA (small glutamine-rich tetratricopeptide repeat-containing protein alpha) demonstrates regulatory specificity for the androgen, glucocorticoid, and progesterone receptors.A Nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90. N-terminal nucleotide binding unmasks a C-terminal binding pocket.Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37.Efficient Hsp90-independent in vitro activation by Hsc70 and Hsp40 of duck hepatitis B virus reverse transcriptase, an assumed Hsp90 client protein.3D structure of human FK506-binding protein 52: implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex.Heterogeneity and dynamics in the assembly of the heat shock protein 90 chaperone complexes.Biochemical reconstitution of steroid receptor•Hsp90 protein complexes and reactivation of ligand bindingThe Cdc37 protein kinase-binding domain is sufficient for protein kinase activity and cell viability.Molecular chaperones and photoreceptor function.Interaction of heat shock protein 90 and the co-chaperone Cpr6 with Ura2, a bifunctional enzyme required for pyrimidine biosynthesisThe hsp90 cochaperone p23 is the limiting component of the multiprotein hsp90/hsp70-based chaperone system in vivo where it acts to stabilize the client protein: hsp90 complex.Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase.hsp90 is required for heme binding and activation of apo-neuronal nitric-oxide synthase: geldanamycin-mediated oxidant generation is unrelated to any action of hsp90.Stoichiometry, abundance, and functional significance of the hsp90/hsp70-based multiprotein chaperone machinery in reticulocyte lysate.Stepwise assembly of a glucocorticoid receptor.hsp90 heterocomplex resolves two sequential ATP-dependent events involving first hsp70 and then hsp90 in opening of the steroid binding pocket.HEAT SHOCK PROTEIN 90C is a bona fide Hsp90 that interacts with plastidic HSP70B in Chlamydomonas reinhardtii.Designed hybrid TPR peptide targeting Hsp90 as a novel anticancer agent.Hop/Sti1 - A Two-Faced Cochaperone Involved in Pattern Recognition Receptor Maturation and Viral Infection.Autoregulation of glucocorticoid receptor by cortisol in rainbow trout hepatocytes.Characterization of a plant homolog of hop, a cochaperone of hsp90.A small-molecule screen reveals that HSP90β promotes the conversion of induced pluripotent stem cell-derived endoderm to a hepatic fate and regulates HNF4A turnover.Regulation of mRNA expression encoding chaperone and co-chaperone proteins of the glucocorticoid receptor in peripheral blood: association with depressive symptoms during pregnancy.
P2860
Q24299657-4171A304-ED0F-486F-98BB-9F551EEF6326Q24535931-25435D9E-6281-4D72-B75F-9D2CDE7372D0Q24596488-20A47398-9E59-489E-8075-DAE56C770235Q24644472-708F3542-798E-44D1-8284-08BC5A46D607Q27676637-AB886DDA-DBC9-4E90-BDC0-676ADCC122C5Q28080783-274F8083-E360-4C53-8BA7-D117161E4BF2Q28208249-CFE0B9D4-FFAD-4830-9600-868A64EB8975Q28216531-9CC59523-C31D-4444-AD1C-943180D3E96BQ30406845-ADD23F45-8E27-4700-8ECA-DFC3E4D7E80DQ30823415-6DA4729C-D2F4-477A-B5BF-75F60795B7C4Q33855062-9238F3D1-3140-46F1-9A32-350C34B1F1EDQ34075879-9593B809-7EC9-4DCC-80B1-FEBB62B806AFQ34105936-05530112-6793-40F2-A8BE-DCD378678A5FQ34120745-5402A99A-776B-4E9A-B7FB-6D2A1625E64FQ34212832-1CF2D739-0300-4CB1-8691-3E411F135667Q34375305-EEC696D6-0242-4D5F-9545-09BD7558024BQ35517904-59FE2B0E-0B61-406B-97C1-5063C7F9276EQ35591253-F221AF35-C3FB-43DB-BD9A-655BBA602002Q36325580-9377DECD-A147-4A7D-B5F1-A28DA6FBB5FEQ37167901-3F64A3AF-A64C-4345-A353-0CAEB21CE437Q37189539-927BEEE6-D15C-47B5-BEE5-17A8248AC687Q40631693-DF94D89E-198A-4C81-948A-BADF41BDC5ACQ40725739-DA578FFB-2F4F-4148-903D-28A1590914B2Q40741495-83A88473-B698-4DED-B5E7-7779ECDDF916Q40798891-757C2FEE-3C2C-4F17-B01D-DDFB000FD89CQ42056801-110ECED2-BE1D-4968-AECA-C03B9DC1F4B7Q42480755-198F1EE0-7E49-4D26-A8FE-3AFE34CE7618Q42588374-E127DD6C-BFAC-45A7-8DF7-6151CADAA29FQ42700262-046818D4-AE19-4D83-9574-ADB44AEEEDC9Q44313240-9A29151D-227A-4C5C-A22F-C478C83E3704Q44315461-83778C6F-D123-4326-88F6-C299407C9C25Q48343445-7A0E8141-1B3C-4477-A5D0-96B1A1E299F2Q54344099-2D43125D-C5B3-4E53-B1FF-E4E998C1FC21
P2860
The Hsp organizer protein hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone system
description
2000 nî lūn-bûn
@nan
2000 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի մարտին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
The Hsp organizer protein hop ...... n Hsp90-based chaperone system
@ast
The Hsp organizer protein hop ...... n Hsp90-based chaperone system
@en
The Hsp organizer protein hop ...... n Hsp90-based chaperone system
@nl
type
label
The Hsp organizer protein hop ...... n Hsp90-based chaperone system
@ast
The Hsp organizer protein hop ...... n Hsp90-based chaperone system
@en
The Hsp organizer protein hop ...... n Hsp90-based chaperone system
@nl
prefLabel
The Hsp organizer protein hop ...... n Hsp90-based chaperone system
@ast
The Hsp organizer protein hop ...... n Hsp90-based chaperone system
@en
The Hsp organizer protein hop ...... n Hsp90-based chaperone system
@nl
P2093
P2860
P921
P356
P1476
The Hsp organizer protein hop ...... n Hsp90-based chaperone system
@en
P2093
A M Silverstein
K C Kanelakis
K D Dittmar
Y Morishima
P2860
P304
P356
10.1074/JBC.275.10.6894
P407
P577
2000-03-10T00:00:00Z