Translocation of proteins through the Sec61 and SecYEG channels - Wikidata - awgldk - TriplyDB

Translocation of proteins through the Sec61 and SecYEG channels

Translocation of proteins through the Sec61 and SecYEG channels

http://www.wikidata.org/entity/Q34046866

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Regulation of the Protein-Conducting Channel by a Bound Ribosome Structure of Monomeric Yeast and Mammalian Sec61 Complexes Interacting with the Translating Ribosome The mitochondrial oxidase assembly protein1 (Oxa1) insertase forms a membrane pore in lipid bilayers.Ancestral and derived protein import pathways in the mitochondrion of Reclinomonas americana On the energetics of translocon-assisted insertion of charged transmembrane helices into membranes Free-energy cost for translocon-assisted insertion of membrane proteins.Free energy of nascent-chain folding in the translocon.Cotranslational folding inhibits translocation from within the ribosome-Sec61 translocon complex.Translocation channel gating kinetics balances protein translocation efficiency with signal sequence recognition fidelity Functional implementation of the posttranslational SecB-SecA protein-targeting pathway in Bacillus subtilis.Glycolipozyme MPIase is essential for topology inversion of SecG during preprotein translocation Secretory protein profiling reveals TNF-α inactivation by selective and promiscuous Sec61 modulators.Small single transmembrane domain (STMD) proteins organize the hydrophobic subunits of large membrane protein complexes.Protein secretion and the endoplasmic reticulum.Co-translational protein targeting to the bacterial membrane.Breaking the bacterial protein targeting and translocation model: oral organisms as a case in point.Illumination of growth, division and secretion by metabolic labeling of the bacterial cell surface.Transcriptional regulation of secretory capacity by bZip transcription factors.Plastids contain a second sec translocase system with essential functions.Partial suppression of Oxa1 mutants by mitochondria-targeted signal recognition particle provides insights into the evolution of the cotranslational insertion systems.Anionic Phospholipids and the Albino3 Translocase Activate Signal Recognition Particle-Receptor Interaction during Light-harvesting Chlorophyll a/b-binding Protein Targeting.The Sec61/SecY complex is inherently deficient in translocating intrinsically disordered proteins.Novel translocation intermediate allows re-evaluation of roles of ATP, proton motive force and SecG at the late stage of preprotein translocation.

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P2860

Translocation of proteins through the Sec61 and SecYEG channels

http://www.wikidata.org/entity/Q34046866

description

2009 nî lūn-bûn

@nan

2009 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Translocation of proteins through the Sec61 and SecYEG channels

@ast

Translocation of proteins through the Sec61 and SecYEG channels

@en

Translocation of proteins through the Sec61 and SecYEG channels

@nl

type

label

Translocation of proteins through the Sec61 and SecYEG channels

@ast

Translocation of proteins through the Sec61 and SecYEG channels

@en

Translocation of proteins through the Sec61 and SecYEG channels

@nl

prefLabel

Translocation of proteins through the Sec61 and SecYEG channels

@ast

Translocation of proteins through the Sec61 and SecYEG channels

@en

Translocation of proteins through the Sec61 and SecYEG channels

@nl

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P356

J.CEB.2009.04.010

P1433

Current Opinion in Cell Biology

P1476

Translocation of proteins through the Sec61 and SecYEG channels

@en

P2093

Elisabet C Mandon

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

Reid Gilmore

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

Steven F Trueman

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

P2860

X-ray structure of a protein-conducting channel

Structural Basis for Signal-Sequence Recognition by the Translocase Motor SecA as Determined by NMR

Ribosome binding of a single copy of the SecY complex: implications for protein translocation

Structure of a complex of the ATPase SecA and the protein-translocation channel

Conformational transition of Sec machinery inferred from bacterial SecYE structures

An interaction between the SRP receptor and the translocon is critical during cotranslational protein translocation.

A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae

SSS1 encodes a stabilizing component of the Sec61 subcomplex of the yeast protein translocation apparatus.

Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p.

SecA, the motor of the secretion machine, binds diverse partners on one interactive surface.

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501-507

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scholarly article

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10.1016/J.CEB.2009.04.010

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4

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21

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2009-05-18T00:00:00Z

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24435790

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19450960

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2916700

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