Maintenance of structure and function of mitochondrial Hsp70 chaperones requires the chaperone Hep1.
about
Chaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/alpha-synuclein complex by HipStructural basis of functional cooperation of Tim15/Zim17 with yeast mitochondrial Hsp70Pam17 is required for architecture and translocation activity of the mitochondrial protein import motorStructure and function of Tim14 and Tim16, the J and J-like components of the mitochondrial protein import motor.Plasmodium falciparum Hep1 Is Required to Prevent the Self Aggregation of PfHsp70-3Human mitochondrial Hsp70 (mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organizationThe Tom40 assembly process probed using the attachment of different intramitochondrial sorting signalsA review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering.Methylation-controlled J-protein MCJ acts in the import of proteins into human mitochondria.Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.A dynamic machinery for import of mitochondrial precursor proteins.Multiple pathways for mitochondrial protein traffic.Thermo and pH stable ATP-independent chaperone activity of heat-inducible Hsp70 from Pennisetum glaucum.Reactivation of protein aggregates by mortalin and Tid1--the human mitochondrial Hsp70 chaperone system.ATPase domain and interdomain linker play a key role in aggregation of mitochondrial Hsp70 chaperone Ssc1.Monitoring conformational heterogeneity of the lid of DnaK substrate-binding domain during its chaperone cycle.Mitochondrial heat shock protein (Hsp) 70 and Hsp10 cooperate in the formation of Hsp60 complexes.The human escort protein Hep binds to the ATPase domain of mitochondrial hsp70 and regulates ATP hydrolysis.Understanding the functional interplay between mammalian mitochondrial Hsp70 chaperone machine componentsReal-time observation of the conformational dynamics of mitochondrial Hsp70 by spFRET.The functional interaction of mitochondrial Hsp70s with the escort protein Zim17 is critical for Fe/S biogenesis and substrate interaction at the inner membrane preprotein translocase.Biogenesis of the mitochondrial Hsp70 chaperoneThe DNLZ/HEP zinc-binding subdomain is critical for regulation of the mitochondrial chaperone HSPA9.Primary sequence that determines the functional overlap between mitochondrial heat shock protein 70 Ssc1 and Ssc3 of Saccharomyces cerevisiae.Zim17/Tim15 links mitochondrial iron-sulfur cluster biosynthesis to nuclear genome stability.The chloroplast DnaJ homolog CDJ1 of Chlamydomonas reinhardtii is part of a multichaperone complex containing HSP70B, CGE1, and HSP90C.Arabidopsis Zinc Ribbon 3 is the ortholog of yeast mitochondrial HSP70 escort protein HEP1 and belongs to an ancient protein family in mitochondria and plastids.A folding nucleus and minimal ATP binding domain of Hsp70 identified by single-molecule force spectroscopy.Assistance for a chaperone: Chlamydomonas HEP2 activates plastidic HSP70B for cochaperone binding.
P2860
Q24312452-88E9EC8A-239E-43A2-922F-B752975BEE9EQ27645926-B1D43E32-7D8C-4C7E-9543-0AC1763AF04FQ27935671-0DEACE97-F2E6-44AE-908E-B6154A8E59C9Q27937176-640B546E-1742-4C5C-875B-480E5E1123A5Q27976466-5A2055C6-B85E-4AE5-A0FE-1E43521A4AC4Q28543073-E856BCF2-229F-462B-A5D2-A5833190EB85Q30155245-73B80616-B8B2-46B7-A17C-A352E00BC83FQ30402024-287326D5-9DFC-47F7-85F9-536E1F2A453EQ30668565-5B0D6028-1C9C-4594-AAB3-C565E06729E7Q36023274-0559403E-F969-4967-AF33-AA92B8AA05DBQ36766006-5F93CF6A-52E8-44F9-BFB1-050782EF46ECQ37488251-DB3198E3-6B86-49D8-9420-68B97F7FCDB8Q39383804-A36C60EA-2BD7-4625-B018-15EE6B338FF6Q39502948-971F7BC6-E008-4397-B28A-F749D87AF943Q39538987-E9C652DE-8A4A-4A4F-BBEB-7642F95A5A11Q39719019-8EAB94BB-8BE1-4951-8A02-42A8B9F761B6Q40166169-DD7F17D3-D341-4204-9BBC-418FEFB30D62Q40419483-6828BF27-383F-4412-80D6-98F53CDBECDEQ41048955-2F584BFA-9488-4985-954E-B83C68AA554EQ41460745-3BE86E4B-EC67-4149-AE88-287EFF135558Q41895199-C550AC54-7EB2-4FF1-994B-F94902B458B7Q42545832-DFE4FA5B-1AAF-441B-84BA-58127F33DDBCQ42549105-3A4203E9-CE8C-42CA-AE9C-F60E903C3E1DQ42737641-C778491C-D647-4B16-B568-27B46D52B88EQ42859219-63C565E2-5FF4-40BE-A866-E779BFB3C0EEQ46521725-322F4BA0-5E48-47C0-B2FF-DDA3B9277DE4Q47186927-99BC79BC-3E77-4D50-91A4-D52DACF7720AQ52316799-35337D24-8ACA-47EA-BD8D-D6823D708D65Q53482974-515BCE20-8607-450E-94E0-2A6B4884B373
P2860
Maintenance of structure and function of mitochondrial Hsp70 chaperones requires the chaperone Hep1.
description
2005 nî lūn-bûn
@nan
2005 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի մարտին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Maintenance of structure and f ...... s requires the chaperone Hep1.
@ast
Maintenance of structure and f ...... s requires the chaperone Hep1.
@en
Maintenance of structure and f ...... s requires the chaperone Hep1.
@nl
type
label
Maintenance of structure and f ...... s requires the chaperone Hep1.
@ast
Maintenance of structure and f ...... s requires the chaperone Hep1.
@en
Maintenance of structure and f ...... s requires the chaperone Hep1.
@nl
prefLabel
Maintenance of structure and f ...... s requires the chaperone Hep1.
@ast
Maintenance of structure and f ...... s requires the chaperone Hep1.
@en
Maintenance of structure and f ...... s requires the chaperone Hep1.
@nl
P2093
P2860
P3181
P356
P1433
P1476
Maintenance of structure and f ...... s requires the chaperone Hep1.
@en
P2093
Abdussalam Azem
Martin Sichting
P2860
P304
P3181
P356
10.1038/SJ.EMBOJ.7600580
P407
P577
2005-03-09T00:00:00Z