Folding and biogenesis of mitochondrial small Tim proteins. - Wikidata - thesis-toulmin - TriplyDB

Folding and biogenesis of mitochondrial small Tim proteins.

Folding and biogenesis of mitochondrial small Tim proteins.

http://www.wikidata.org/entity/Q37139210

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Dimeric Structure of the Bacterial Extracellular Foldase PrsA.Labile Low-Molecular-Mass Metal Complexes in Mitochondria: Trials and Tribulations of a Burgeoning Field Mitochondrial thiol oxidase Erv1: both shuttle cysteine residues are required for its function with distinct roles.Mitochondrial Tim9 protects Tim10 from degradation by the protease Yme1.The disease-associated mutation of the mitochondrial thiol oxidase Erv1 impairs cofactor binding during its catalytic reaction.Oxeiptosis, a ROS-induced caspase-independent apoptosis-like cell-death pathway.The divergent N-terminal domain of Tim17 is critical for its assembly in the TIM complex in Trypanosoma brucei.Identification of a Degradation Signal Sequence within Substrates of the Mitochondrial i-AAA Protease.

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Folding and biogenesis of mitochondrial small Tim proteins.

http://www.wikidata.org/entity/Q37139210

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 13 August 2013

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vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

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name

Folding and biogenesis of mitochondrial small Tim proteins.

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Folding and biogenesis of mitochondrial small Tim proteins.

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type

label

Folding and biogenesis of mitochondrial small Tim proteins.

@en

Folding and biogenesis of mitochondrial small Tim proteins.

@nl

prefLabel

Folding and biogenesis of mitochondrial small Tim proteins.

@en

Folding and biogenesis of mitochondrial small Tim proteins.

@nl

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International Journal of Molecular Sciences

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Folding and biogenesis of mitochondrial small Tim proteins

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Efrain Ceh-Pavia

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

Michael P Spiller

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Creative Commons Attribution 3.0 Unported

P2860

Crystal structure of the mitochondrial chaperone TIM9.10 reveals a six-bladed alpha-propeller

Molecular chaperone function of Mia40 triggers consecutive induced folding steps of the substrate in mitochondrial protein import

MIA40 is an oxidoreductase that catalyzes oxidative protein folding in mitochondria

Functional and mutational characterization of human MIA40 acting during import into the mitochondrial intermembrane space

Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70

Transport of the ADP/ATP carrier of mitochondria from the TOM complex to the TIM22.54 complex

Assembly of the three small Tim proteins precedes docking to the mitochondrial carrier translocase

Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins

The Tim8–Tim13 Complex Has Multiple Substrate Binding Sites and Binds Cooperatively to Tim23

Structural and Functional Requirements for Activity of the Tim9-Tim10 Complex in Mitochondrial Protein Import

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16685-16705

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scholarly article

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10.3390/IJMS140816685

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8

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14

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2013-08-13T00:00:00Z

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255954931

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23945562

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membrane proteins

mitochondrial proteins

protein folding

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3759932

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