Mechanism of dimer formation of the 90-kDa heat-shock protein
about
In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysisHeat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetasesHsp90: a specialized but essential protein-folding toolA structure-based mutational analysis of cyclophilin 40 identifies key residues in the core tetratricopeptide repeat domain that mediate binding to Hsp90Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90p50(cdc37) acting in concert with Hsp90 is required for Raf-1 functionParalog Specific Hsp90 Inhibitors - A Brief History and a Bright FutureBinding of ATP to heat shock protein 90: evidence for an ATP-binding site in the C-terminal domainSubstrate-binding characteristics of proteins in the 90 kDa heat shock protein familyHigh-temperature protein G is an essential virulence factor of Leptospira interrogansComparative proteomics reveals novel components at the plasma membrane of differentiated HepaRG cells and different distribution in hepatocyte- and biliary-like cellsExploring the Functional Complementation between Grp94 and Hsp90Isolation and mapping of self-assembling protein domains encoded by the Saccharomyces cerevisiae genome using lambda repressor fusionsThe actin filament-associated protein AFAP-110 is an adaptor protein that modulates changes in actin filament integrity.A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering.Phosphorylation and oligomerization states of native pig brain HSP90 studied by mass spectrometry.Domain-domain interactions of HtpG, an Escherichia coli homologue of eukaryotic HSP90 molecular chaperone.The C-terminal domain of human grp94 protects the catalytic subunit of protein kinase CK2 (CK2alpha) against thermal aggregation. Role of disulfide bonds.The common tetratricopeptide repeat acceptor site for steroid receptor-associated immunophilins and hop is located in the dimerization domain of Hsp90.Identification of the pentapeptide constituting a dominant epitope common to all eukaryotic heat shock protein 90 molecular chaperones.To fold or not to fold: modulation and consequences of Hsp90 inhibition.Modular control of cross-oligomerization: analysis of superstabilized Hsp90 homodimers in vivo.HSP90 interacts with and regulates the activity of heat shock factor 1 in Xenopus oocytes.Molecular imaging of the efficacy of heat shock protein 90 inhibitors in living subjects.Characterizing heat shock protein 90 gene of Apolygus lucorum (Meyer-Dür) and its expression in response to different temperature and pesticide stressesA systematic survey of an intragenic epistatic landscape.Regulation of the Hsp90-binding immunophilin, cyclophilin 40, is mediated by multiple sites for GA-binding protein (GABP).Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90A systematic protocol for the characterization of Hsp90 modulators.Heat shock protein 90 is responsible for hyperdynamic circulation in portal hypertensive rats.Domain structures and immunogenic regions of the 90-kDa heat-shock protein (HSP90). Probing with a library of anti-HSP90 monoclonal antibodies and limited proteolysis.Novobiocin and additional inhibitors of the Hsp90 C-terminal nucleotide-binding pocket.A novel function for the 90 kDa heat-shock protein (Hsp90): facilitating nuclear export of 60 S ribosomal subunits.Hsp90 chaperone activity requires the full-length protein and interaction among its multiple domains.The biochemical role of the heat shock protein 90 chaperone complex in establishing human telomerase activity.Heat shock protein 90β in the Vero cell membrane binds Japanese encephalitis virus.Design and synthesis of Hsp90 inhibitors: exploring the SAR of Sansalvamide A derivatives.Macrocycles that inhibit the binding between heat shock protein 90 and TPR-containing proteins.Identification of Hsp90 as a stimulatory host factor involved in influenza virus RNA synthesis.Oligomeric forms of the 90-kDa heat shock protein.
P2860
Q22008008-D621FC54-508C-4FC6-A472-D1A8B62C21C5Q22254677-CB9C8DA5-4BFD-49A9-BFC2-AEEB28CDE9CCQ24291482-C1B6CC59-7375-4FB6-B97E-80F31131578AQ24302319-384D92BC-F0CA-4C17-BF76-47D9ECC4BA23Q24313523-3300D524-291E-48AD-9EB9-F3DF410DCB1FQ24554532-DDBDE1BA-4871-4AB3-9392-3467CCC8F6CCQ26748800-13C38977-DAC5-42AB-BC87-347D6D44074EQ28216259-11E23E5F-6E6F-4A48-827D-D401DD88D566Q28359659-AB43A820-1249-426C-8929-C2E8190F655BQ28485771-7149341A-D206-4087-9C9A-D25D761E33CEQ28535470-926C3082-6877-4DB1-8540-9478C064803CQ28553251-F2F8960E-443E-418C-9497-DDE44D6BBF11Q28757163-4BBD2C17-586C-48E6-8927-85C2EFE1BA41Q30167852-AF5AED69-46B8-43A5-9B6A-6218CDDF7671Q30402024-D4DD1E82-16B4-42FA-BA48-654777194159Q30664049-95D2EC2E-0D83-43BA-8F57-2194F3A6EF1FQ31018704-5B317DBD-5399-4014-B304-41D54332C580Q31896731-C55E9E9E-33EF-42E6-A355-1018F30A3FDAQ31920652-A3BE2CD9-5550-43D5-8B90-75BA61EA61E1Q33228775-7D719B2F-B03D-47EF-ADC2-C1FAB1312E83Q33531705-3B3BA9CD-882A-4229-8B91-F3388890DF04Q33581226-C234C6B9-344F-45A4-A131-F1337AB67C53Q33776598-40A4011C-BB35-4B1D-91D4-2BF58F6B1CC2Q34096497-8287ADF4-8876-4A6E-B388-7C4BF5400E66Q34099877-7E90DDF7-5509-458D-A37A-7475057AF865Q34740848-AB1F4098-F554-41C4-95BB-0B08343B1230Q35129802-7AE40919-B3A1-433F-891A-804602F266CFQ35816373-81EEDD9D-3F6B-4DC3-953C-2DBDB657DE07Q36201554-E1A74B44-3680-4E84-8B7B-390AD32A87E2Q36308872-EEF201F6-DE30-4805-944D-0C24913F3B8FQ36886428-42178F79-0799-4B2D-B159-0F1EC0FEEB1CQ37320252-F21BD964-3F82-4FDF-99DE-2D16CED62231Q38291469-39534FD8-7DF8-4D00-B525-044A485DB1E4Q38310098-F01468BB-F6AA-4A5A-85A4-630436DD0BD3Q38313087-FAFFD436-1354-434D-A2FE-5071F9745C92Q38705939-6E201692-626C-4911-B85D-AB4440E5CCD1Q39667620-DB9981D6-6CD9-4504-944D-67229A8B5420Q39894584-6C072A7C-9D45-4457-B155-7042759C55E6Q40704635-C992B631-5D88-4259-A67C-2B8BFBB7E7ADQ42120405-C7A770FF-8CBF-47D6-9435-21322B2B368A
P2860
Mechanism of dimer formation of the 90-kDa heat-shock protein
description
1995 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1995
@ast
im Oktober 1995 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1995/10/01)
@sk
vědecký článek publikovaný v roce 1995
@cs
wetenschappelijk artikel (gepubliceerd op 1995/10/01)
@nl
наукова стаття, опублікована в жовтні 1995
@uk
научни чланак (објављен 1995/10/01)
@sr
name
Mechanism of dimer formation of the 90-kDa heat-shock protein
@ast
Mechanism of dimer formation of the 90-kDa heat-shock protein
@en
Mechanism of dimer formation of the 90-kDa heat-shock protein
@nl
type
label
Mechanism of dimer formation of the 90-kDa heat-shock protein
@ast
Mechanism of dimer formation of the 90-kDa heat-shock protein
@en
Mechanism of dimer formation of the 90-kDa heat-shock protein
@nl
prefLabel
Mechanism of dimer formation of the 90-kDa heat-shock protein
@ast
Mechanism of dimer formation of the 90-kDa heat-shock protein
@en
Mechanism of dimer formation of the 90-kDa heat-shock protein
@nl
P2093
P2860
P921
P3181
P1433
P1476
Mechanism of dimer formation of the 90-kDa heat-shock protein
@en
P2093
K. Yokoyama
Y. Ohara-Nemoto
P2860
P3181
P356
10.1111/J.1432-1033.1995.001_1.X
P407
P577
1995-10-01T00:00:00Z