Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK - Wikidata - awgldk - TriplyDB

Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK

Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK

http://www.wikidata.org/entity/Q29618850

about

Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions.The early-onset torsion dystonia-associated protein, torsinA, displays molecular chaperone activity in vitro Human homologues of the bacterial heat-shock protein DnaJ are preferentially expressed in neurons RhoBTB3: a Rho GTPase-family ATPase required for endosome to Golgi transport.Regulated release of ERdj3 from unfolded proteins by BiP Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3 The DNAJB6 and DNAJB8 protein chaperones prevent intracellular aggregation of polyglutamine peptides Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70 Interaction between DNA-damage protein GADD34 and a new member of the Hsp40 family of heat shock proteins that is induced by a DNA-damaging reagent The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53.GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1 A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins.The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding Mechanisms for regulation of Hsp70 function by Hsp40 Eukaryotic homologues of Escherichia coli dnaJ: a diverse protein family that functions with hsp70 stress proteins Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions Hsp70 chaperones: cellular functions and molecular mechanism Interferon-induced human protein MxA is a GTPase which binds transiently to cellular proteins The T/t common exon of simian virus 40, JC, and BK polyomavirus T antigens can functionally replace the J-domain of the Escherichia coli DnaJ molecular chaperone Tim14, a novel key component of the import motor of the TIM23 protein translocase of mitochondria Interaction of murine BiP/GRP78 with the DnaJ homologue MTJ1 The nucleotide exchange factors of Hsp70 molecular chaperones Regulation of protein homeostasis in neurodegenerative diseases: the role of coding and non-coding genes The influence of C-terminal extension on the structure of the “J-domain” in E. coli DnaJ Crystal Structures of the 70-kDa Heat Shock Proteins in Domain Disjoining Conformation Atomic Structure of the KEOPS Complex: An Ancient Protein Kinase-Containing Molecular Machine Structural analysis of substrate binding by the molecular chaperone DnaK Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation.Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s.Nucleotide binding by Lhs1p is essential for its nucleotide exchange activity and for function in vivo.SSI1 encodes a novel Hsp70 of the Saccharomyces cerevisiae endoplasmic reticulum.A role for a eukaryotic GrpE-related protein, Mge1p, in protein translocation Zuotin, a ribosome-associated DnaJ molecular chaperone The Hsp70/90 cochaperone, Sti1, suppresses proteotoxicity by regulating spatial quality control of amyloid-like proteins.Prion-impairing mutations in Hsp70 chaperone Ssa1: effects on ATPase and chaperone activities.The nucleotide exchange factor MGE exerts a key function in the ATP-dependent cycle of mt-Hsp70-Tim44 interaction driving mitochondrial protein import.Characterization of Hsp70 binding and nucleotide exchange by the yeast Hsp110 chaperone Sse1.Role of the mitochondrial DnaJ homolog Mdj1p as a chaperone for mitochondrially synthesized and imported proteins.

P2860

Q22010047-1039C893-0F03-4D8E-BBCF-94DB1821F282 Q24300223-9E647D85-7823-4A28-B3E1-2CD49D8081B1 Q24306619-471B8A4C-1BBA-45BF-A86C-7D7F9D70E31E Q24316325-B125603A-5647-4642-B456-4A01DCC2022D Q24323860-33ADEFEB-40F5-4D4E-B841-933419D8ECDF Q24324029-E56645C9-2581-4634-93A6-A77447CD219E Q24338933-300322A9-4F59-4236-8223-C29C56467218 Q24520314-1C28D8A0-C183-4DC3-930A-B20A693C0FDA Q24532229-4A9F9572-12EE-4DD2-8A1D-E3D10073643C Q24533965-04B5EB31-92F4-4EEF-8E49-C1EC36E1BCC0 Q24535931-A98965FA-EDAE-402B-ABF6-50E5FE6449FB Q24536019-886ED054-9649-470C-8724-D643A3C8157A Q24541564-3B8BFE11-A7A6-4C3E-937C-9677374BA76B Q24562938-08BEEC88-F98D-4B3D-8AE7-F5FBC50EB2F3 Q24563232-E356104B-7CD6-42FC-A878-ED4C7BD54A1E Q24622449-62F1C879-B76C-4716-BE68-2FE65325AA8C Q24644464-51CDE30F-E93C-4D5C-9EF3-472DB940B52B Q24644472-7C282B8A-447D-4D74-808A-017B0153DF28 Q24644756-905C786D-7E84-4F9E-80FA-149D6FE73A0C Q24669835-10EDC541-8F05-4314-A3EB-1107F0CF5933 Q24672440-242AF3A2-3B93-48A1-8057-EEA3E05576B8 Q24681842-BBF344F1-2F68-49C2-9C06-BD68F3FA4691 Q26766367-2494A2F3-D384-4394-A9FF-322361161DB9 Q26799208-789D5770-0E95-470A-BE93-878C82742B47 Q27617982-DF54F57E-D500-4F87-AC2E-5A01AD663FEA Q27650298-0EEA82D5-A8B1-4435-AD96-04A359AEE0B8 Q27652648-4E22DD85-CB5B-4C4C-8D89-BCE615D9E060 Q27732810-E056741C-DD38-41BB-A390-0CD660718AAF Q27930004-6B24EB0A-6665-4952-8FF6-23630993489C Q27931293-3FFBEE1A-0319-4299-9FFF-94C62824BF74 Q27931808-7F977C5C-DE11-4E6F-88DB-D2C87C2D3E8F Q27932135-DE867A62-6A8A-4BA9-BE01-4DDD0A834EF2 Q27932136-46E6E61F-E9E2-4917-B8CB-29104D9D7DAF Q27932200-07EF5C04-D3CE-4031-B45A-D6CB9820D2FE Q27933106-E37B5C28-B57F-4D85-BA8A-B8C7578A8B40 Q27933148-322E7641-D7E0-476C-B913-84175254AAC4 Q27934126-156D3C7A-FCD2-4735-B026-4AD14147C786 Q27934584-AF97AD6C-E85C-406E-8D41-A6BD362B531B Q27934849-86C7B767-FB46-46DB-8EA2-46CB21D371A0 Q27935248-2E65E95E-01E2-42AD-92CE-2792E9CD142E

P2860

Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK

http://www.wikidata.org/entity/Q29618850

description

1991 nî lūn-bûn

@nan

1991 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

1991 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

1991年の論文

@ja

1991年論文

@yue

1991年論文

@zh-hant

1991年論文

@zh-hk

1991年論文

@zh-mo

1991年論文

@zh-tw

1991年论文

@wuu

name

Escherichia coli DnaJ and GrpE ...... mulate ATPase activity of DnaK

@ast

Escherichia coli DnaJ and GrpE ...... mulate ATPase activity of DnaK

@en

type

label

Escherichia coli DnaJ and GrpE ...... mulate ATPase activity of DnaK

@ast

Escherichia coli DnaJ and GrpE ...... mulate ATPase activity of DnaK

@en

prefLabel

Escherichia coli DnaJ and GrpE ...... mulate ATPase activity of DnaK

@ast

Escherichia coli DnaJ and GrpE ...... mulate ATPase activity of DnaK

@en

P1433

Q29618850-78D96AAD-4F23-44C3-980F-BA02CD2631A4

P1476

Q29618850-9A5AC7BD-7056-436A-92F6-9FE96D95ACCF

P2093

Q29618850-11777A6C-906B-404D-908D-9FC48AFE74B8

Q29618850-1A907FCC-5E08-46FB-80C3-D774C9F1CBD8

Q29618850-580542F3-493F-451A-8DD8-504A4B58E0C9

Q29618850-7D4204B9-A7F6-43C3-941A-F12B5EB685D1

Q29618850-A500FD33-9C73-486A-90BC-41CF33D0D24A

P2860

Q29618850-007E1329-307C-4923-9AEC-2F802926678C

Q29618850-082057C6-BA46-49A4-82BB-3E27991297E0

Q29618850-0E17E4FF-404A-4FB5-A659-B2238521326D

Q29618850-104F47B2-060D-4D58-9364-1C62596CE4F6

Q29618850-2EE8F2D0-55E5-4B33-A6B3-CDB22A4D9CD0

Q29618850-343B7521-B11B-40D0-9282-3A73E6E8489F

Q29618850-348D82CB-3E86-417B-902E-1B0A0F723E06

Q29618850-4D08105A-1513-4570-A5C4-F03E2467175F

Q29618850-4FF7B216-4785-4389-85D6-928B83480CA3

Q29618850-50AC9DAE-4868-4078-9428-4AB66F981F63

P304

Q29618850-45237AF7-0E27-4CAA-915D-B17FCEEEB630

P31

Q29618850-75140049-9294-4C69-82D5-3F8C2DF42D00

P356

Q29618850-EBE6699F-5C5D-4983-8F63-62417B799971

P407

Q29618850-944F72D6-7E2A-4E67-8BE0-2A66C3C0F602

P433

Q29618850-13586F61-4605-43CD-9663-4BBFCA6A73C9

P478

Q29618850-967C5EB7-D22C-4385-BBAE-D51BC244652B

P50

Q29618850-3DEF51DA-9D40-4415-8348-A85BF27B0886

Q29618850-B5CE3F64-458E-4CE8-A23C-B131676A006E

P577

Q29618850-7CE6392F-AF45-462B-AA44-E75EA03503D7

P698

Q29618850-69EFCD5B-0B0F-42E4-8D5A-C97189172545

P921

Q29618850-AA8A7510-286E-4B90-941B-F3F23A005A0C

P932

Q29618850-86DF7834-A515-40B2-A809-95459E0E9777

P356

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Escherichia coli DnaJ and GrpE ...... mulate ATPase activity of DnaK

@en

P2093

C Georgopoulos

http://www.w3.org/2001/XMLSchema#string

D Ang

http://www.w3.org/2001/XMLSchema#string

J Marszalek

http://www.w3.org/2001/XMLSchema#string

K Liberek

http://www.w3.org/2001/XMLSchema#string

M Zylicz

http://www.w3.org/2001/XMLSchema#string

P2860

An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein

Role of the Escherichia coli DnaK and DnaJ heat shock proteins in the initiation of bacteriophage lambda DNA replication

The 70-kd mammalian heat shock proteins are structurally and functionally related to the uncoating protein that releases clathrin triskelia from coated vesicles

Speculations on the functions of the major heat shock and glucose-regulated proteins.

Escherichia coli DnaK and GrpE heat shock proteins interact both in vivo and in vitro.

The heat-shock-regulated grpE gene of Escherichia coli is required for bacterial growth at all temperatures but is dispensable in certain mutant backgrounds.

Escherichia coli grpE gene codes for heat shock protein B25.3, essential for both lambda DNA replication at all temperatures and host growth at high temperature.

Escherichia coli DnaK protein possesses a 5'-nucleotidase activity that is inhibited by AppppA

Purification of complexes of nuclear oncogene p53 with rat and Escherichia coli heat shock proteins: in vitro dissociation of hsc70 and dnaK from murine p53 by ATP.

Rapid purification of mammalian 70,000-dalton stress proteins: affinity of the proteins for nucleotides

P304

2874-2878

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1073/PNAS.88.7.2874

http://www.w3.org/2001/XMLSchema#string

P407

P433

7

http://www.w3.org/2001/XMLSchema#string

P478

88

http://www.w3.org/2001/XMLSchema#string

P50

Krzysztof Liberek

P577

1991-04-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

1826368

http://www.w3.org/2001/XMLSchema#string

P921

Escherichia coli

P932

51342

http://www.w3.org/2001/XMLSchema#string