High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70
about
Does Japanese encephalitis virus share the same cellular receptor with other mosquito-borne flaviviruses on the C6/36 mosquito cells?Crystal structure of the C-terminal 10-kDa subdomain of Hsc70NMR structure of the forkhead-associated domain from the Arabidopsis receptor kinase-associated protein phosphataseThe solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide NRLLLTGDomain structure of the HSC70 cochaperone, HIPhsp70 genes in the human genome: Conservation and differentiation patterns predict a wide array of overlapping and specialized functionsAllostery in the Hsp70 chaperone proteinsMicroautophagy of cytosolic proteins by late endosomesAllostery in Hsp70 chaperones is transduced by subdomain rotationsHSPA8/HSC70 chaperone protein: structure, function, and chemical targeting.ATPase activity and ATP-dependent conformational change in the co-chaperone HSP70/HSP90-organizing protein (HOP)A large conformational change of the translocation ATPase SecACrystallization and X-ray data analysis of the 10 kDa C-terminal lid subdomain from Caenorhabditis elegans Hsp70Ionic contacts at DnaK substrate binding domain involved in the allosteric regulation of lid dynamics.Hsp70 mutant proteins modulate additional apoptotic pathways and improve cell survival.Heat stress cognate 70 host protein as a potential drug target against drug resistance in hepatitis B virus.Maturation of steroid receptors: an example of functional cooperation among molecular chaperones and their associated proteinsRecognition between flexible protein molecules: induced and assisted folding.Molecular structures of proteins involved in vesicle coat formation.The lid domain of Caenorhabditis elegans Hsc70 influences ATP turnover, cofactor binding and protein folding activity.Expression of selected Ginkgo biloba heat shock protein genes after cold treatment could be induced by other abiotic stress.T antigens of simian virus 40: molecular chaperones for viral replication and tumorigenesisHsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain.Critical role of extracellular heat shock cognate protein 70 in the myocardial inflammatory response and cardiac dysfunction after global ischemia-reperfusion.The Hsp70 and Hsp40 chaperones influence microtubule stability in ChlamydomonasKeep the traffic moving: mechanism of the Hsp70 motor.Dancing through Life: Molecular Dynamics Simulations and Network-Centric Modeling of Allosteric Mechanisms in Hsp70 and Hsp110 Chaperone Proteins.Computational Analysis of Residue Interaction Networks and Coevolutionary Relationships in the Hsp70 Chaperones: A Community-Hopping Model of Allosteric Regulation and CommunicationHsc70 is required for endocytosis and clathrin function in Drosophila.Experimentally biased model structure of the Hsc70/auxilin complex: substrate transfer and interdomain structural changeThe 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains.Myocardial TLR4 is a determinant of neutrophil infiltration after global myocardial ischemia: mediating KC and MCP-1 expression induced by extracellular HSC70.Predisposition to abacavir hypersensitivity conferred by HLA-B*5701 and a haplotypic Hsp70-Hom variant.DYNLL/LC8: a light chain subunit of the dynein motor complex and beyond.Role of the C-terminal region of mouse inducible Hsp72 in the recognition of peptide substrate for chaperone activity.Resonance assignments for the substrate binding domain of Hsp70 chaperone Ssa1 from Saccharomyces cerevisiae.Structural and Biological Interaction of hsc-70 Protein with Phosphatidylserine in Endosomal Microautophagy.The chaperone toolbox at the single-molecule level: From clamping to confining.Backbone and methyl resonance assignments of the 42 kDa human Hsc70 nucleotide binding domain in the ADP state.Hsp72 chaperone function is dispensable for protection against stress-induced apoptosis
P2860
Q27481648-E86136C1-C196-4F46-A379-980141AC2099Q27641340-7E077F0E-3DF8-4736-8FC3-4B915AE52ECEQ27642196-121A2F16-C62F-46BE-89AA-981DC0D35CC3Q27642406-F0BBC4AE-3BC8-451D-87BE-323B0765138BQ28203002-1D8F4AEF-1946-4191-B38A-AB9298653ADFQ28265695-2D009B6F-3D0B-416D-A70D-40EBE08DC4AEQ28266387-B4C78399-6394-4762-98AA-4CCD27953575Q28509224-5A0299F0-C569-48DE-9199-C3F16AF10F55Q28752577-CD158F6B-4B05-43A2-97AF-A6E0E3C40300Q30354473-8A15F2FF-CDEF-4175-ABF6-9D24698B5987Q30359042-6546DD06-92F5-4E12-A830-87B632E049C2Q30776655-145E4D83-EDDA-4EC7-BC5D-C4D730D5DABEQ31058410-E4C5456B-52AC-4DA5-BE69-E73E50F1B470Q33231727-534500CA-AC0F-40E3-8103-770AE22A9C92Q33716832-484056B0-56F4-4498-8C14-73986694B833Q33826248-DD14242D-15E0-46DD-B628-C41F163CFE3EQ34124519-8A04FA33-98F0-4CCE-9073-8FC313B28210Q34141716-B8EA8DFD-1BF0-48E9-B408-71FD9F731E4CQ34156663-5B58D761-FF0F-437C-9A7B-103A911B5496Q34221854-9FA72179-B68B-404D-9C02-DE8E8434A676Q34324008-2BB64D27-135C-4C81-9565-740636BF11BFQ34662543-78282D6A-DEF9-4E21-96A1-FFEE47D2DF56Q34808252-88DCD978-47CA-4F8B-8FCB-AA68B3F965AAQ35109063-58FE3D79-F56B-4445-8958-DE817DCDDF77Q35620413-12730C30-E484-4D27-8DD5-399B507D93DBQ35653384-477EEF98-910F-4BE3-B71F-27BD7C14ED3FQ35855961-7CFDCA33-7D7D-4FA0-BAB5-3E3023EFBD4EQ36251118-338F7D06-0D94-4896-918C-23E3ECFADB0CQ36323720-364E16A7-49E1-43A8-9875-FB6331CA7F76Q36519208-D0469A88-EEB1-47CD-BC1B-ADEB4904F6F0Q36671475-4BA2A3F7-71A2-4D65-83F9-6D895F47EF36Q37264415-DF29B82B-7EE6-432B-B963-8C71B0617B1BQ37356747-DC3B18E8-712C-4A2A-BBE2-3DF3BD8A8E25Q37903411-0C421520-2D65-46D7-9E1A-2E23E04884CCQ38335127-B6431EF3-F49C-4576-86BA-27B4E8F6D674Q38428604-B3C1B1F5-C7F4-4DEB-A200-25E55F76336BQ38758528-DF0F9BAF-51D4-48AD-B930-59A64732E9B1Q39200186-23500712-49E8-4490-B2E4-D5120E016999Q39325573-63839514-4641-4D58-BE81-7EA9AA4ECC2AQ39935467-8FFBA813-D287-43D7-961B-350B0B13CBAE
P2860
High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
High-resolution solution struc ...... malian chaperone protein Hsc70
@ast
High-resolution solution struc ...... malian chaperone protein Hsc70
@en
High-resolution solution struc ...... malian chaperone protein Hsc70
@nl
type
label
High-resolution solution struc ...... malian chaperone protein Hsc70
@ast
High-resolution solution struc ...... malian chaperone protein Hsc70
@en
High-resolution solution struc ...... malian chaperone protein Hsc70
@nl
prefLabel
High-resolution solution struc ...... malian chaperone protein Hsc70
@ast
High-resolution solution struc ...... malian chaperone protein Hsc70
@en
High-resolution solution struc ...... malian chaperone protein Hsc70
@nl
P2093
P921
P356
P1476
High-resolution solution struc ...... malian chaperone protein Hsc70
@en
P2093
P304
P356
10.1006/JMBI.1999.2776
P407
P577
1999-06-25T00:00:00Z