Domain structure and lipid interaction of recombinant yeast Tim44 - Test2 - elhamkhani - TriplyDB

Domain structure and lipid interaction of recombinant yeast Tim44

Domain structure and lipid interaction of recombinant yeast Tim44

http://www.wikidata.org/entity/Q35587615

about

The reducible complexity of a mitochondrial molecular machine The pro-apoptotic Bcl-2 family member tBid localizes to mitochondrial contact sites Architecture of the large subunit of the mammalian mitochondrial ribosome The essential function of Tim12 in vivo is ensured by the assembly interactions of its C-terminal domain.Residues of Tim44 involved in both association with the translocon of the inner mitochondrial membrane and regulation of mitochondrial Hsp70 tethering Domain structure of the HSC70 cochaperone, HIP Dual interaction of scaffold protein Tim44 of mitochondrial import motor with channel-forming translocase subunit Tim23 Mitochondrial protein import motor: the ATPase domain of matrix Hsp70 is crucial for binding to Tim44, while the peptide binding domain and the carboxy-terminal segment play a stimulatory role.Preliminary crystallographic studies of yeast mitochondrial peripheral membrane protein Tim44p Protein translocation channel of mitochondrial inner membrane and matrix-exposed import motor communicate via two-domain coupling protein.Patch clamp characterization of the effect of cardiolipin on MscS of E. coli.Cardiolipin mediates membrane and channel interactions of the mitochondrial TIM23 protein import complex receptor Tim50.The Pam18/Tim14-Pam16/Tim16 complex of the mitochondrial translocation motor: the formation of a stable complex from marginally stable proteins.Switching of the homooligomeric ATP-binding cassette transport complex MDL1 from post-translational mitochondrial import to endoplasmic reticulum insertion.The role and significance of potential lipid-binding regions in the mitochondrial protein import motor: an in-depth in silico study.

P2860

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P2860

Domain structure and lipid interaction of recombinant yeast Tim44

http://www.wikidata.org/entity/Q35587615

description

1999 nî lūn-bûn

@nan

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

1999年论文

@zh

1999年论文

@zh-cn

name

Domain structure and lipid interaction of recombinant yeast Tim44

@ast

Domain structure and lipid interaction of recombinant yeast Tim44

@en

type

label

Domain structure and lipid interaction of recombinant yeast Tim44

@ast

Domain structure and lipid interaction of recombinant yeast Tim44

@en

prefLabel

Domain structure and lipid interaction of recombinant yeast Tim44

@ast

Domain structure and lipid interaction of recombinant yeast Tim44

@en

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PNAS.96.16.8890

P1433

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

P1476

Domain structure and lipid interaction of recombinant yeast Tim44

@en

P2093

Azem A

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

Demel R

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

Horst M

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

Jenö P

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

Oppliger W

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

Schatz G

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

Vergères G

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

Weiss C

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

de Kruijff B

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

P2860

The Tim core complex defines the number of mitochondrial translocation contact sites and can hold arrested preproteins in the absence of matrix Hsp70-Tim44.

Tom5 functionally links mitochondrial preprotein receptors to the general import pore.

Mitochondrial Hsp70/MIM44 complex facilitates protein import.

The MIM complex mediates preprotein translocation across the mitochondrial inner membrane and couples it to the mt-Hsp70/ATP driving system

Dynamic interaction between Isp45 and mitochondrial hsp70 in the protein import system of the yeast mitochondrial inner membrane

MPI1, an essential gene encoding a mitochondrial membrane protein, is possibly involved in protein import into yeast mitochondria

Common principles of protein translocation across membranes

Protein import into mitochondria

Sequential action of two hsp70 complexes during protein import into mitochondria

Interaction of mitochondrial targeting signals with acidic receptor domains along the protein import pathway: evidence for the 'acid chain' hypothesis.

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8890-8894

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scholarly article

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10.1073/PNAS.96.16.8890

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16

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96

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1999-08-01T00:00:00Z

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12868620

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10430866

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17703

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