The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE - Wikidata - awgldk - TriplyDB

The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE

The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE

http://www.wikidata.org/entity/Q28239456

about

Regulated release of ERdj3 from unfolded proteins by BiP Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3 GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1 Mechanisms for regulation of Hsp70 function by Hsp40 Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells Tim14, a novel key component of the import motor of the TIM23 protein translocase of mitochondria Macromolecule-assisted de novo protein folding Protein homeostasis as a therapeutic target for diseases of protein conformation An essential nonredundant role for mycobacterial DnaK in native protein folding Structural Basis of J Cochaperone Binding and Regulation of Hsp70 Structure of the Hsp110:Hsc70 nucleotide exchange machine.Functional analysis of Hsp70 inhibitors Structural analysis of substrate binding by the molecular chaperone DnaK A role for the DnaJ homologue Scj1p in protein folding in the yeast endoplasmic reticulum.A lysine-rich region within fungal BAG domain-containing proteins mediates a novel association with ribosomes.Nucleotide binding by Lhs1p is essential for its nucleotide exchange activity and for function in vivo.PhLP3 modulates CCT-mediated actin and tubulin folding via ternary complexes with substrates.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.Role of the mitochondrial DnaJ homolog Mdj1p as a chaperone for mitochondrially synthesized and imported proteins.Domain structure of the HSC70 cochaperone, HIP Hop modulates Hsp70/Hsp90 interactions in protein folding Allostery in the Hsp70 chaperone proteins Evidence for the existence of distinct mammalian cytosolic, microsomal, and two mitochondrial GrpE-like proteins, the Co-chaperones of specific Hsp70 members Low resolution structural study of two human HSP40 chaperones in solution. DJA1 from subfamily A and DJB4 from subfamily B have different quaternary structures Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone.Characterization of functional domains of the eukaryotic co-chaperone Hip Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro The HSP70 chaperone machinery: J proteins as drivers of functional specificity A novel Hsp70 inhibitor prevents cell intoxication with the actin ADP-ribosylating Clostridium perfringens iota toxin Fatty acyl benzamido antibacterials based on inhibition of DnaK-catalyzed protein folding.Evaluation of similarities in the cis/trans isomerase function of trigger factor and DnaK.A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering.FoldEco: a model for proteostasis in E. coli.Protein folding rates and thermodynamic stability are key determinants for interaction with the Hsp70 chaperone system.BUNDLE SHEATH DEFECTIVE2, a novel protein required for post-translational regulation of the rbcL gene of maize.Substrate specificity of the SecB chaperone.Reversible thermal transition in GrpE, the nucleotide exchange factor of the DnaK heat-shock system.Biological heterogeneity of the peptide-binding motif of the 70-kDa heat shock protein by surface plasmon resonance analysis.

P2860

Q24323860-644059B0-757B-4AF6-A8FB-149FC55551A6 Q24324029-5E81415A-F314-4A44-85B3-FB59333D1127 Q24536019-1E672894-D533-45F4-872D-04B8FAE630A1 Q24563232-952D31AE-B011-4E57-943C-597D7123148D Q24644464-5375D0E2-A9BF-45D1-BA99-EB25920EFF23 Q24653464-A978DBC2-79ED-4270-B825-62DF440C8339 Q24672440-86EFB781-B39A-4C6F-B5C4-FA5DC323CAFE Q26852244-5162DEE9-F495-4AA3-8ABA-358EF58E47A0 Q27003283-E85BDF9F-4AA1-4855-B9A3-E4ED2B82A645 Q27314706-6FCCFC37-68B9-4FF8-A2B1-66828564B781 Q27649002-7FC3A180-32E9-41BC-806C-9D3685706CF9 Q27650814-0A1ECF87-F265-4C3F-9653-0DEA1A9C3F16 Q27680671-ED4A69FC-0EB2-4889-AFB5-B589D8C36D99 Q27732810-F7E0E971-EC16-4D2F-9EDD-31B3840EE751 Q27929932-026F1290-2E8E-4EED-8D82-D23BF9C88549 Q27931383-FCEF4859-B735-47D9-9314-ACE837AC7F87 Q27932135-34E10B13-9BA8-40EA-A61A-AFB4411E76B5 Q27934103-54F8DF72-35A6-4DA3-8C21-2925DCD8E473 Q27934126-0CC9E188-9D74-43EE-8FFC-9418DA497573 Q27934584-AC15AD8A-7CF4-4436-984A-43B9B3C542CF Q27935248-1DF22847-0393-4662-98EF-FE61B73EE516 Q28203002-7C0E1966-5607-4D29-A1A5-19748881590B Q28260829-26FE51C6-BEAD-40D0-8728-2A56CF00E99E Q28266387-27C7810D-73E1-468D-B49C-09DC75219296 Q28278845-FCD7B5E9-50E2-4580-B0D8-F504D9A4DEA3 Q28303408-69A8D5C7-8EC6-4EC8-A77B-AB9EF9DA6FAA Q28354756-96B5BC0F-1115-4FD3-860E-D2162F9FDBA3 Q28581007-F4E35E71-EA81-47D9-8DD5-938DA36E404E Q28771764-7637BF4C-A6B2-4097-B706-4CB289D4DA87 Q29616140-C0749CA4-E265-42B1-B5CF-E58F09BD4934 Q30315590-2F5B8AA4-FF6A-4FE8-B65B-2E4EB2DC46AA Q30319919-4135B3BF-EB1F-46F7-AD50-5DEB53B8B61C Q30320711-D35206DD-61C0-443B-B8F3-7C808C6A7B61 Q30402024-BC7D5130-9C7B-4310-8702-08EF9F2EC908 Q30512981-895C242E-BF8E-4785-961F-11BFA06BA18E Q30530315-F9B11902-DBF1-4735-A142-803559545815 Q30630049-EE4CC87F-2096-465D-A491-734B0FADB000 Q30815173-C1E48D60-7374-41BC-B032-464932A4A191 Q31578047-F73133DF-553C-4C62-B254-4F74A750754D Q33290603-3E62603B-2501-4039-830B-0F1664AA49EC

P2860

The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE

http://www.wikidata.org/entity/Q28239456

description

1994 nî lūn-bûn

@nan

1994 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

1994 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

1994年の論文

@ja

1994年論文

@yue

1994年論文

@zh-hant

1994年論文

@zh-hk

1994年論文

@zh-mo

1994年論文

@zh-tw

1994年论文

@wuu

name

The ATP hydrolysis-dependent r ...... 70 system DnaK, DnaJ, and GrpE

@ast

The ATP hydrolysis-dependent r ...... 70 system DnaK, DnaJ, and GrpE

@en

The ATP hydrolysis-dependent r ...... 70 system DnaK, DnaJ, and GrpE

@nl

type

label

The ATP hydrolysis-dependent r ...... 70 system DnaK, DnaJ, and GrpE

@ast

The ATP hydrolysis-dependent r ...... 70 system DnaK, DnaJ, and GrpE

@en

The ATP hydrolysis-dependent r ...... 70 system DnaK, DnaJ, and GrpE

@nl

prefLabel

The ATP hydrolysis-dependent r ...... 70 system DnaK, DnaJ, and GrpE

@ast

The ATP hydrolysis-dependent r ...... 70 system DnaK, DnaJ, and GrpE

@en

The ATP hydrolysis-dependent r ...... 70 system DnaK, DnaJ, and GrpE

@nl

P1433

Q28239456-68AD1806-9F41-4CF7-B7C0-8EA4CF826017

P1476

Q28239456-3EBCD796-12A0-449C-A474-BC63974217A6

P2093

Q28239456-10486D63-E814-48BF-9684-FCE7FFF383A6

Q28239456-39B2309F-4FE7-4BF9-A08C-1FB8C9AB726F

Q28239456-9095462E-1C34-48D2-9DA9-844F03D8E1CA

Q28239456-9EFC790E-46E3-4250-9D77-A0BEB49EA447

Q28239456-F9AF5E6F-08D2-4E3F-BA82-3A49DD0C4BE8

P2860

Q28239456-06368EDA-69D6-4F83-8DF9-F428A5B2878A

Q28239456-11D6AFEC-FAA3-4140-BE38-354AB547BC08

Q28239456-35162966-3000-47A7-8FB4-CB94CC76FB3C

Q28239456-495BFA7D-9F40-45FF-BC8A-7E493AD2E9DE

Q28239456-50D58458-44F7-43C5-8D78-8A7DF3777B84

Q28239456-520A2BBB-8451-4CCB-ADE6-20494192A6DD

Q28239456-54133564-2393-445C-A15E-F0A6C0E627DF

Q28239456-5963A155-9B2B-41E3-9D0A-3C6168ECEB60

Q28239456-6015D9B8-21A6-4E0E-91FC-4EB2D3229492

Q28239456-7AEA40C5-1651-4BC3-94E1-5A53FC485B6B

P304

Q28239456-5867A8D3-FC72-4571-A813-3D56474966F2

P31

Q28239456-D6F78EB8-3391-49CE-9CF2-03DFE38B4642

P3181

Q28239456-63D0810F-3180-4DCF-B697-DD5A53EB1728

P356

Q28239456-0E459FF1-04E1-4941-8CDD-88631EA5B810

P407

Q28239456-5F55FBC0-0FA0-4215-B86A-D58B33CAB686

P433

Q28239456-EE2035BB-C89E-4BC0-AC41-01415850C1CA

P478

Q28239456-14EF49E3-6BA6-4E17-8123-A05F10304E25

P50

Q28239456-B3AEF454-1F4B-4993-AC94-908B8AA3AFA2

P577

Q28239456-F1ABA2F5-95FE-49AA-AE11-D721B1F3F020

P5875

Q28239456-8956DC2F-8A23-4351-9749-0F64FF54EC3B

P698

Q28239456-82C014DF-FFD9-4491-8091-57B25D6392F7

P921

Q28239456-201792FB-779D-48BB-BC76-1F02A6615F74

P932

Q28239456-73E99750-FB22-4D4D-9FDC-3D3E0C6AF504

P3181

P356

PNAS.91.22.10345

P1433

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

P1476

The ATP hydrolysis-dependent r ...... 70 system DnaK, DnaJ, and GrpE

@en

P2093

A Szabo

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

B Bukau

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

H Schröder

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

J Flanagan

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

T Langer

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

P2860

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

A role for a eukaryotic GrpE-related protein, Mge1p, in protein translocation

Regulation of Hsp70 function by a eukaryotic DnaJ homolog.

Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange

Kinetics of molecular chaperone action

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

Protein folding in the cell

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

Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits

Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding.

P304

10345-9

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

P31

scholarly article

P3181

286940

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

P356

10.1073/PNAS.91.22.10345

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

P407

P433

22

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

P478

91

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

P50

Franz-Ulrich Hartl

P577

1994-10-25T00:00:00Z

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

P5875

15261190

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

P698

7937953

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

P921

Escherichia coli

P932

45016

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