A J-protein is an essential subunit of the presequence translocase-associated protein import motor of mitochondria.
about
Role of Magmas in protein transport and human mitochondria biogenesisThe mitochondrial protein translocation motor: structural conservation between the human and yeast Tim14/Pam18-Tim16/Pam16 co-chaperonesMutation of DNAJC19, a human homologue of yeast inner mitochondrial membrane co-chaperones, causes DCMA syndrome, a novel autosomal recessive Barth syndrome-like conditionThe fast-mobility isoform of mouse Mcl-1 is a mitochondrial matrix-localized protein with attenuated anti-apoptotic activityGiardia mitosomes and trichomonad hydrogenosomes share a common mode of protein targetingRole of Pam16's degenerate J domain in protein import across the mitochondrial inner membrane.Ups1p and Ups2p antagonistically regulate cardiolipin metabolism in mitochondria.The J domain-related cochaperone Tim16 is a constituent of the mitochondrial TIM23 preprotein translocase.Yeast Miro GTPase, Gem1p, regulates mitochondrial morphology via a novel pathway.Active remodelling of the TIM23 complex during translocation of preproteins into mitochondria.Essential role of Isd11 in mitochondrial iron-sulfur cluster synthesis on Isu scaffold proteins.Ribosome-binding proteins Mdm38 and Mba1 display overlapping functions for regulation of mitochondrial translation.Characterization of Mmp37p, a Saccharomyces cerevisiae mitochondrial matrix protein with a role in mitochondrial protein import.Pam17 is required for architecture and translocation activity of the mitochondrial protein import motorZim17, a novel zinc finger protein essential for protein import into mitochondria.Structural properties of substrate proteins determine their proteolysis by the mitochondrial AAA+ protease Pim1.Taz1, an outer mitochondrial membrane protein, affects stability and assembly of inner membrane protein complexes: implications for Barth SyndromeMitochondrial protein import motor: differential role of Tim44 in the recruitment of Pam17 and J-complex to the presequence translocase.Structure and function of Tim14 and Tim16, the J and J-like components of the mitochondrial protein import motor.The channel-forming Sym1 protein is transported by the TIM23 complex in a presequence-independent mannerThe import motor of the yeast mitochondrial TIM23 preprotein translocase contains two different J proteins, Tim14 and Mdj2.Conserved N-terminal negative charges in the Tim17 subunit of the TIM23 translocase play a critical role in the import of preproteins into mitochondria.The Import of Proteins into the Mitochondrion of Toxoplasma gondiiResidues of Tim44 involved in both association with the translocon of the inner mitochondrial membrane and regulation of mitochondrial Hsp70 tetheringDisorders of phospholipid metabolism: an emerging class of mitochondrial disease due to defects in nuclear genesMCJ/DnaJC15, an endogenous mitochondrial repressor of the respiratory chain that controls metabolic alterationsA respiratory chain controlled signal transduction cascade in the mitochondrial intermembrane space mediates hydrogen peroxide signalingMethylation-controlled J-protein MCJ acts in the import of proteins into human mitochondria.Dual interaction of scaffold protein Tim44 of mitochondrial import motor with channel-forming translocase subunit Tim23Role of the loop L4,5 in allosteric regulation in mtHsp70s: in vivo significance of domain communication and its implications in protein translocationMolecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.Architecture of the TIM23 inner mitochondrial translocon and interactions with the matrix import motorMolecular insights revealing interaction of Tim23 and channel subunits of presequence translocaseHsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling.Ancient gene duplication provided a key molecular step for anaerobic growth of Baker's yeastReevaluation of the role of the Pam18:Pam16 interaction in translocation of proteins by the mitochondrial Hsp70-based import motorMitochondrial import and the twin-pore translocase.Genetic analysis of complex interactions among components of the mitochondrial import motor and translocon in Saccharomyces cerevisiaeBiology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Enhanced J-protein interaction and compromised protein stability of mtHsp70 variants lead to mitochondrial dysfunction in Parkinson's disease
P2860
6876334ab75818b581b79977ec8b46d3881a5a5475e47674e6001376c0a104874d47602f214263427778a51916972e90a9f8ca4b0508c7aa83b7beb981a786453f402e4a1044c3f4189b6d4431fb2cd788668dd9756c75ca7633e307b2e5ac918cb75f3e9448b625c0f248530e213167dc582b558a6a21629cb8893ee33d0201ff684bffe2973902d81e35c4c208d5fcef3bd6c4535d6bf60a3df17d70e5ed0be9da9514685f5111b80b0f44c4874e7a9f5e82f5
P248
Q24294308-FE2FE788-B2D1-4A58-80F5-EDF6D533EA11Q24309210-20FED5D5-E039-4685-9440-C0105C4C824CQ24311734-09D1189F-733D-48C1-9F1B-1B8267C01CCAQ24338742-ED86E08E-E600-42CE-86B0-2AA771A066DCQ24534322-C7F5A6EF-8BA9-44A6-96F4-61F1F3371F94Q27930421-5DB40B33-F951-424A-9DE6-E145F8CCDA88Q27930903-8284D508-6CDE-453B-ADB9-1E4BC578FACBQ27931269-390C96F3-9C79-49E3-BABC-2C697FDAC944Q27932069-17D59169-3C4D-4D26-B086-60EBA323BDCFQ27932754-841CC376-FE18-4125-AAC3-DB95E2080295Q27934369-B98FB1EF-86F6-4178-8958-723C703FFB55Q27934411-5CD652F9-3BD1-4BA7-BB1A-DD10F2E964B7Q27934449-C02D6CEC-7E84-4D3A-AB3E-5C197BEABD5AQ27935671-F44B0152-033D-44F6-9694-32CDA0687A23Q27935898-03BF9592-D493-4E29-BD08-05A56228AC1DQ27936117-04228FB1-2076-483A-B2BF-3F74908EBDE0Q27936928-B81A34E7-ADFB-45FA-8EBC-0F36007E25B4Q27936963-31402EBD-48C0-40AA-868A-2B7C02E7470BQ27937176-2029466E-F190-4EFE-933C-2F1EFEAAAA5AQ27938469-AF062B35-D3A7-4335-A5B3-5C9A0F7B89E6Q27938719-B1151682-263F-46E8-9C64-13645E2A4812Q27940344-10640A79-B3B5-44A0-8A0F-A0FB19A56528Q27972732-DC353F6D-EF89-45A6-99E1-7B9153411D6AQ28114318-2695927D-9721-4F42-BA0F-46F3988C03E3Q28387241-93E70BA4-6BB1-4192-A135-AEBF4BA5A06AQ28513253-089987D8-71FE-4335-9856-FCA28A904A3FQ28608443-5C097080-1DA5-4916-A441-9AF937F80852Q30668565-F3636A35-B25E-4891-9D62-04B558AF27B3Q33649453-237C8526-FF9A-4957-A746-EF3BA5F85673Q33881367-D2F8645D-C1B2-40BF-B59C-2E45EBFE9596Q34038270-4AED6B79-2139-4620-9F43-8CAD1EDD8E6CQ34317502-FAD809D0-5D4A-45D2-87C4-1D13E299519BQ34372928-38E77A29-AD00-4AE2-974F-E17D42C5B638Q34597309-DEF2A810-98C6-44AF-9D17-171825436E0BQ35129297-DF96C2CB-B470-48CD-88B8-D9A3D9450201Q35612234-CBA10EE2-791A-425F-82F9-B037F8BBAD0EQ35825850-531A62F1-EA20-4FF4-8886-85F4EB308D3BQ35863069-BCE30072-2447-4981-8B60-417C4523514FQ36023274-110F1C11-FE27-4887-87D7-2110ACD57964Q36083113-49C2FBB9-1FEE-4FF2-B569-9299EF342E92
P2860
A J-protein is an essential subunit of the presequence translocase-associated protein import motor of mitochondria.
description
2003 nî lūn-bûn
@nan
2003 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
A J-protein is an essential su ...... import motor of mitochondria.
@ast
A J-protein is an essential su ...... import motor of mitochondria.
@en
A J-protein is an essential su ...... import motor of mitochondria.
@nl
type
label
A J-protein is an essential su ...... import motor of mitochondria.
@ast
A J-protein is an essential su ...... import motor of mitochondria.
@en
A J-protein is an essential su ...... import motor of mitochondria.
@nl
prefLabel
A J-protein is an essential su ...... import motor of mitochondria.
@ast
A J-protein is an essential su ...... import motor of mitochondria.
@en
A J-protein is an essential su ...... import motor of mitochondria.
@nl
P2093
P2860
P50
P921
P356
P1476
A J-protein is an essential su ...... import motor of mitochondria.
@en
P2093
Andreas Geissler
Ann E Frazier
Hanne Müller
Helmut E Meyer
Maria Lind
Wolfgang Voos
Yanfeng Li
P2860
P304
P356
10.1083/JCB.200308004
P407
P577
2003-11-24T00:00:00Z