Structural analysis of substrate binding by the molecular chaperone DnaK - Wikidata - wikimedia - TriplyDB

Structural analysis of substrate binding by the molecular chaperone DnaK

Structural analysis of substrate binding by the molecular chaperone DnaK

http://www.wikidata.org/entity/Q27732810

about

Crystal structure of the stress-inducible human heat shock protein 70 substrate-binding domain in complex with peptide substrate Structure and intermolecular interactions of the luminal dimerization domain of human IRE1alpha Glucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cycles Identification and characterization of a novel human methyltransferase modulating Hsp70 protein function through lysine methylation Regulated release of ERdj3 from unfolded proteins by BiP Stress-induced localization of HSPA6 (HSP70B') and HSPA1A (HSP70-1) proteins to centrioles in human neuronal cells Mechanisms for regulation of Hsp70 function by Hsp40 Characterization and regulation of the major histocompatibility complex-encoded proteins Hsp70-Hom and Hsp70-1/2 Hsp70 chaperones: cellular functions and molecular mechanism Interaction of murine BiP/GRP78 with the DnaJ homologue MTJ1 Peptide substrate identification for yeast Hsp40 Ydj1 by screening the phage display library Various hypotheses on MHC evolution suggested by the concerted evolution of CD94L and MHC class Ia molecules RNA-Binding Proteins in Trichomonas vaginalis: Atypical Multifunctional Proteins Insights into the molecular mechanism of allostery in Hsp70s.Fine-tuning multiprotein complexes using small molecules Heat shock proteins: stimulators of innate and acquired immunity Functions of heat shock proteins in pathways of the innate and adaptive immune system High molecular weight stress proteins: Identification, cloning and utilisation in cancer immunotherapy Protein homeostasis at the plasma membrane Chaperone machines for protein folding, unfolding and disaggregation The crystal structure of the fab fragment of the monoclonal antibody MAK33. Implications for folding and interaction with the chaperone bip Solution structure and stability of the anti-sigma factor AsiA: implications for novel functions.Crystal structure of the C-terminal 10-kDa subdomain of Hsc70 The crystal structure of Escherichia coli heat shock protein YedU reveals three potential catalytic active sites The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide NRLLLTG A new native EcHsp31 structure suggests a key role of structural flexibility for chaperone function Insights into Hsp70 Chaperone Activity from a Crystal Structure of the Yeast Hsp110 Sse1 Structural Basis of J Cochaperone Binding and Regulation of Hsp70 Crystal Structures of the 70-kDa Heat Shock Proteins in Domain Disjoining Conformation Structure of the Hsp110:Hsc70 nucleotide exchange machine.Allosteric Coupling between the Lid and Interdomain Linker in DnaK Revealed by Inhibitor Binding Studies Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate Crystal Structures of the ATPase Domains of Four Human Hsp70 Isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78 Structural Analysis of Protein Folding by the Long-Chain Archaeal Chaperone FKBP26 Rational design of oncocin derivatives with superior protease stabilities and antibacterial activities based on the high-resolution structure of the oncocin-DnaK complex Structural analysis of the Sil1-Bip complex reveals the mechanism for Sil1 to function as a nucleotide-exchange factor Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP Crystal Structure of DnaK Protein Complexed with Nucleotide Exchange Factor GrpE in DnaK Chaperone System: INSIGHT INTO INTERMOLECULAR COMMUNICATION Functional analysis of Hsp70 inhibitors Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle

P2860

Q21090602-235384DA-ADF6-43E5-B96E-5C14056E6D85 Q24297815-F16CDD5E-6511-4FA6-A4D9-0E552E01619F Q24299657-B7F39773-0971-4FEB-807F-4E54CAFF07E9 Q24315705-5293A034-BC2B-4FFD-8DF6-FB2610769FFA Q24323860-9F37DB4F-848E-46C4-945C-52B2C978864F Q24337158-43322CC8-98B3-4D28-8012-A1F7981F3EB9 Q24563232-2E5CF440-8C84-48C9-B63D-864DA58F0283 Q24563881-125646BD-2186-4FCA-B74B-F7BB97FA87A3 Q24644472-1D9EC3B2-778E-45E9-AC08-C09250650571 Q24681842-0E9AA775-BBA9-4DDD-AD0D-20AE6AD3CF64 Q24798059-13F168CE-A3A0-4FDA-8FC8-C164CCFCF564 Q25256392-DAAC84A4-D8D7-47B4-9845-ADF3BE21172D Q26771978-D312E4A4-64BB-4A8E-AA6E-F5C0DB0B8C76 Q26779247-A2972152-1014-462C-880A-0D4E82FBF7A4 Q26822675-41DDA963-6BA5-4863-9677-B1F7DD88209B Q26829100-93F72128-A96E-4509-B677-A5132028E209 Q26830705-E8DFAEED-56F6-4248-8886-61C06FDEF8FE Q26853566-753504C3-E324-40FC-8C71-A916F3C1571C Q27009009-F1B9B5CC-6674-489E-890B-A6629E2C543E Q27026110-F2370AE7-8899-424F-93B0-4DECCC51667E Q27627511-E2989539-A3DC-4D5B-BF4F-2C9F6D9BF585 Q27637678-CC93A83C-E451-414F-B2DE-49528464BC7A Q27641340-81562C0F-7C03-4643-AD81-AD454F139078 Q27642199-B6977733-C779-4984-9104-17C281B3036B Q27642406-40BD486E-F631-4D70-9769-B7506DAD9253 Q27642847-E783FAC7-1E5C-4E08-8A33-756AFA64735A Q27648730-1A2C61E6-83D4-4878-8625-0D07116B206F Q27649002-E39D575D-C771-4228-BFF4-51138643EDBE Q27650298-1F2E89AE-5A42-4D03-9173-6C2649149465 Q27650814-7C9D428D-F8ED-43D7-B0F8-BAC525B67F7C Q27653249-A503FF56-38DA-4B0D-B49D-E360E28A7394 Q27655465-2ABD9DF9-86EC-4E33-B768-361F5A62B1D6 Q27658953-757DEE17-5BD8-4CC1-B1BC-C9FEC56CD6D3 Q27666696-DEDFE7EE-0A8C-427F-86E1-17F136424C6D Q27666903-AFDD2C12-405E-4BA1-A374-7C611CEB79F7 Q27670444-AE8CDC74-6A58-4F56-AE90-D6C22ADBB365 Q27678317-E70E8268-69C6-4FB8-B48E-D64197DEAEDF Q27678812-3702383D-F19A-4AB2-BD05-BDC614F6218E Q27680671-DB59A7E8-8FB0-4E54-9C99-8D108BE05CE2 Q27685147-98E02930-D07F-4CDC-8449-4D497590B073

P2860

Structural analysis of substrate binding by the molecular chaperone DnaK

http://www.wikidata.org/entity/Q27732810

description

1996 nî lūn-bûn

@nan

1996 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

1996 թվականի հունիսին հրատարակված գիտական հոդված

@hy

1996年の論文

@ja

1996年論文

@yue

1996年論文

@zh-hant

1996年論文

@zh-hk

1996年論文

@zh-mo

1996年論文

@zh-tw

1996年论文

@wuu

name

Structural analysis of substrate binding by the molecular chaperone DnaK

@ast

Structural analysis of substrate binding by the molecular chaperone DnaK

@en

Structural analysis of substrate binding by the molecular chaperone DnaK

@nl

type

label

Structural analysis of substrate binding by the molecular chaperone DnaK

@ast

Structural analysis of substrate binding by the molecular chaperone DnaK

@en

Structural analysis of substrate binding by the molecular chaperone DnaK

@nl

prefLabel

Structural analysis of substrate binding by the molecular chaperone DnaK

@ast

Structural analysis of substrate binding by the molecular chaperone DnaK

@en

Structural analysis of substrate binding by the molecular chaperone DnaK

@nl

P1433

Q27732810-145C6C2C-F8BF-418F-9BE8-FB71369ADB34

P1476

Q27732810-C2C4FA17-AE96-4036-9B0C-2C8335329E0B

P2093

Q27732810-56991952-A2FF-4ABF-8D11-6B5DE2439CE3

Q27732810-69322D34-BBF7-4B9C-A3E5-0EE45A4C13C3

Q27732810-78B5E4A8-69D1-4682-93BB-EA802E26073F

Q27732810-806EE6E1-9822-49A3-8CE9-A20638732C73

Q27732810-9245434B-6A80-42E8-AD5A-D82E682ADA53

Q27732810-DF5477FF-A1B3-4BAA-96CE-612404E95A78

Q27732810-F90AE4BB-4F5A-4665-98EB-507D91CB230F

P2860

Q27732810-04913B60-DE4E-4037-AC3B-4430CFFA7E6D

Q27732810-061A1745-6ADB-4BB0-BD6B-CF3AE4D7B530

Q27732810-0693A380-CDD8-4F28-AAD7-D203C3F41423

Q27732810-08AEAE22-6ECC-4EBF-9498-C5CF0370AB4B

Q27732810-0C7A0AF3-643D-46E9-9974-FE108E35EE39

Q27732810-0E128F06-8D40-4099-9514-8C6704405384

Q27732810-1253381E-E75E-4F3E-87CD-75B1B9C9A7B1

Q27732810-13FDF8E9-AB32-42A3-A15B-9DF91C14C99F

Q27732810-14B50531-E0AC-4ACD-8290-8666DA9C958E

Q27732810-23BC46E8-3866-4DA7-95D6-E89755ADC969

P304

Q27732810-6766DE0C-4D4E-4EC7-8AB3-7B12C2F6A63B

P31

Q27732810-8D85ABA6-6333-46EC-BCCF-EFCDF1D193F0

P3181

Q27732810-8B4B35CF-6C54-4737-95AB-5DB02C5A53B3

P356

Q27732810-38E05DAA-9663-4F9E-B703-2BB595951A16

P407

Q27732810-2069012D-40B4-479B-B75B-F748AFBA59D7

P433

Q27732810-DC82A484-6B87-435E-AABA-8D742C69FF9C

P478

Q27732810-AD970088-4E66-4CEC-9B56-56E047AD607C

P577

Q27732810-CCA0678F-2B9E-4FAE-865F-DBD47B5AAB7D

P5875

Q27732810-4562258B-536E-48FD-A19E-C49239067FFC

P698

Q27732810-3C7ADE2B-B288-4E43-8E84-1BE3902FFD91

P921

Q27732810-12130AC3-1D1B-426B-A082-6C6D6302DBE2

P932

Q27732810-AEDC0786-E3E6-4F90-8A25-03ECBB6FBB76

P3181

P356

SCIENCE.272.5268.1606

P1433

P1476

Structural analysis of substrate binding by the molecular chaperone DnaK

@en

P2093

A Gragerov

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

C M Ogata

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

M E Gottesman

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

W A Hendrickson

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

W F Burkholder

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

X Zhao

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

X Zhu

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

P2860

Improved methods for building protein models in electron density maps and the location of errors in these models

Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein

Structure of myohemerythrin in the azidomet state at 1.7/1.3 A resolution

Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains

Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis

The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma S

Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures

Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing

Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure

Determination of macromolecular structures from anomalous diffraction of synchrotron radiation

P304

1606-1614

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

P31

scholarly article

P3181

635292

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

P356

10.1126/SCIENCE.272.5268.1606

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

P407

P433

5268

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

P478

272

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

P577

1996-06-01T00:00:00Z

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

P5875

14542699

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

P698

8658133

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

P921

molecular chaperones

P932

5629921

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