about
S100A1 is a novel molecular chaperone and a member of the Hsp70/Hsp90 multichaperone complexCHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substratesInteraction of the Hsp90 cochaperone cyclophilin 40 with Hsc70Hsp70 chaperones: cellular functions and molecular mechanismThe cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome systemThe stress response against denatured proteins in the deletion of cytosolic chaperones SSA1/2 is different from heat-shock response in Saccharomyces cerevisiaeCrystal Structure of Get4-Get5 Complex and Its Interactions with Sgt2, Get3, and Ydj1The architecture of functional modules in the Hsp90 co-chaperone Sti1/HopChaperone ligand-discrimination by the TPR-domain protein Tah1.SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiaeThe Hsp70/90 cochaperone, Sti1, suppresses proteotoxicity by regulating spatial quality control of amyloid-like proteins.Analysis of quality control substrates in distinct cellular compartments reveals a unique role for Rpn4p in tolerating misfolded membrane proteins.The cytosolic cochaperone Sti1 is relevant for mitochondrial biogenesis and morphology.Cns1 is an activator of the Ssa1 ATPase activity.Dissection of Swa2p/auxilin domain requirements for cochaperoning Hsp70 clathrin-uncoating activity in vivo.CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abundance and cell-cycle progressionYeast prions are useful for studying protein chaperones and protein quality controlA proteomic snapshot of the human heat shock protein 90 interactomeSaccharomyces cerevisiae KNU5377 stress response during high-temperature ethanol fermentationATPase activity and ATP-dependent conformational change in the co-chaperone HSP70/HSP90-organizing protein (HOP)Hsp110 is required for spindle length control.The hop-like stress-induced protein 1 cochaperone is a novel cell-intrinsic restriction factor for mitochondrial tombusvirus replication.The lid domain of Caenorhabditis elegans Hsc70 influences ATP turnover, cofactor binding and protein folding activity.Regulation of vascular endothelial cell polarization and migration by Hsp70/Hsp90-organizing proteinIndependent regulation of Hsp70 and Hsp90 chaperones by Hsp70/Hsp90-organizing protein Sti1 (Hop1).Decarbonylated cyclophilin A Cpr1 protein protects Saccharomyces cerevisiae KNU5377Y when exposed to stress induced by menadione.Effect of mutation of the tetratricopeptide repeat and asparatate-proline 2 domains of Sti1 on Hsp90 signaling and interaction in Saccharomyces cerevisiaePrimate chaperones Hsc70 (constitutive) and Hsp70 (induced) differ functionally in supporting growth and prion propagation in Saccharomyces cerevisiae.Heterogeneity and dynamics in the assembly of the heat shock protein 90 chaperone complexes.Effects of chronic heat stress on the expressions of heat shock proteins 60, 70, 90, A2, and HSC70 in the rabbit testisImportance of the Hsp70 ATPase domain in yeast prion propagationHsp90-Associated Immunophilin Homolog Cpr7 Is Required for the Mitotic Stability of [URE3] Prion in Saccharomyces cerevisiae.Tetratricopeptide repeat cochaperones in steroid receptor complexesNovel interaction of the Hsp90 chaperone machine with Ssl2, an essential DNA helicase in Saccharomyces cerevisiae.HSP90/70 chaperones are required for rapid nucleosome removal upon induction of the GAL genes of yeastInfluence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2Influence of Hsp70s and their regulators on yeast prion propagationHsp70 structure, function, regulation and influence on yeast prions.Propagation of Saccharomyces cerevisiae [PSI+] prion is impaired by factors that regulate Hsp70 substrate bindingPharmacological targeting of the Hsp70 chaperone.
P2860
Q24300601-7191947A-FC11-4D59-A73D-796DD4CEA0E5Q24338386-98197EBF-18BA-4A0C-89E1-23A2CF2F7AE2Q24520314-A6CA7C14-EDD7-4A32-9756-48E656131692Q24644472-9ADD22DE-9983-43D4-AD94-3F6B4E4E839DQ24676115-484D779B-8F4E-45F8-900D-3E53965695BCQ24815041-E841D37D-B9E0-4226-BE2F-D076D0F850FBQ27659241-A9F66017-0A5A-4A49-9CDA-AF2237BD5BF4Q27676637-A6B4A0A9-CB64-4BD3-9324-EA105E95DF5EQ27929748-8DF9AD4C-0224-415D-B41D-DD7EBECDBA91Q27931740-8D8C92E9-18B3-4872-B50A-2CE4E0E44BD3Q27933148-BE26BD9D-165C-478B-AA51-D616B4D8F8FFQ27933335-224E5C32-693D-465D-A4F5-A1BA9D4F97EDQ27935948-7FC04BDC-C574-420C-9D19-EB6D4139AE7BQ27938204-5AC1CFD5-1BF9-409F-BBC5-5702D57A43A2Q27938386-ADB87DAE-16D0-4F80-ADAA-64A41B7105B8Q27938574-F21FD938-28BA-44F7-8C71-C8B76C5A1FC8Q28081556-4F1E3F1E-F6A3-4A98-A857-3997FB1D8068Q28279879-1FFEF361-9B97-4CCD-BB83-9C013DA3E5C7Q28660724-27E351D6-88A7-4ABE-A72E-BA4F95DC6EFBQ30359042-4175841D-C0B9-4126-8443-C468576EAFC7Q30528920-4402CCE2-3672-4AE3-BCB2-D9F5AB6EE954Q34059324-B3B59693-B2AD-4C67-A082-24A6ACB07052Q34221854-73BDCD36-FA1B-4FA4-92B1-B56C06002BF1Q34257507-497EC682-41CC-4E68-AF9E-EBDB0EF42D7BQ34293593-5BF46F15-91FF-4DA8-9A2D-46E006EEB60EQ34505918-34CF66C3-2233-42D0-8871-774E6D819F71Q34587324-96DF8EC6-30B4-44DB-BA43-202493D1C1F9Q34587831-C6F1162F-3EED-4CF8-B4AC-292798644712Q35517904-A607E343-DBEC-49A7-8869-B25A5343759BQ35583527-145A4479-CE7F-46DC-A7AC-81BEEE6D6C8CQ35641429-CE171AE2-508B-4CAC-BC60-9F3AD717AD47Q35810283-16BA7A4C-51AB-4BB5-A2B6-04AA61E68527Q35924587-59A4A3E9-A02A-4CFF-AADA-128980249D90Q36496582-7C4689E2-87BB-439C-BFD8-FFBE61DE22D2Q36498441-BC76C14B-73B0-4CF0-ADD0-82B58974BF1DQ36801199-5B25CAA5-DB08-4ED9-95D1-5E2F02EA17FFQ37266700-8540FC43-E27E-4A47-A180-3D509B7EB21DQ37353065-562ED828-CD81-4A04-B237-D44FFE65009EQ37423973-7A69A763-563A-40A1-8DBF-965F3E4736D4Q37622461-7B2A01BA-E60E-435E-946E-8DA559775CD2
P2860
description
2003 nî lūn-bûn
@nan
2003 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Sti1 is a novel activator of the Ssa proteins.
@ast
Sti1 is a novel activator of the Ssa proteins.
@en
Sti1 is a novel activator of the Ssa proteins.
@nl
type
label
Sti1 is a novel activator of the Ssa proteins.
@ast
Sti1 is a novel activator of the Ssa proteins.
@en
Sti1 is a novel activator of the Ssa proteins.
@nl
prefLabel
Sti1 is a novel activator of the Ssa proteins.
@ast
Sti1 is a novel activator of the Ssa proteins.
@en
Sti1 is a novel activator of the Ssa proteins.
@nl
P2093
P2860
P356
P1476
Sti1 is a novel activator of the Ssa proteins.
@en
P2093
Harald Wegele
Jochen Reinstein
Johannes Buchner
Martin Haslbeck
P2860
P304
P356
10.1074/JBC.M301548200
P407
P577
2003-07-11T00:00:00Z