Modeling the effects of prl mutations on the Escherichia coli SecY complex. - Wikidata - wikimedia - TriplyDB

Modeling the effects of prl mutations on the Escherichia coli SecY complex.

Modeling the effects of prl mutations on the Escherichia coli SecY complex.

http://www.wikidata.org/entity/Q34048338

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SecA, a remarkable nanomachine Structure of the Sec61 channel opened by a signal sequence Regulation of the Protein-Conducting Channel by a Bound Ribosome Conformation-specific labeling of BamA and suppressor analysis suggest a cyclic mechanism for β-barrel assembly in Escherichia coli Ser/Thr motifs in transmembrane proteins: conservation patterns and effects on local protein structure and dynamics Protein secretion and outer membrane assembly in Alphaproteobacteria How does Tremblaya princeps get essential proteins from its nested partner Moranella endobia in the Mealybug Planoccocus citri?Signal peptides are allosteric activators of the protein translocase.Hydrophobically stabilized open state for the lateral gate of the Sec translocon.The hydrophobic core of the Sec61 translocon defines the hydrophobicity threshold for membrane integration.Dynamics of SecY translocons with translocation-defective mutations Transport of preproteins by the accessory Sec system requires a specific domain adjacent to the signal peptide Structural and functional profiling of the lateral gate of the Sec61 translocon A simple and reproducible method for directed evolution: combination of random mutation with dITP and DNA fragmentation with endonuclease V.Effective use of a horizontally-transferred pathway for dichloromethane catabolism requires post-transfer refinement.Escherichia coli SecG is required for residual export mediated by mutant signal sequences and for SecY-SecE complex stability A prl mutation in SecY suppresses secretion and virulence defects of Listeria monocytogenes secA2 mutants Decatransin, a new natural product inhibiting protein translocation at the Sec61/SecYEG translocon.Translocation channel gating kinetics balances protein translocation efficiency with signal sequence recognition fidelity The bacterial Sec-translocase: structure and mechanism.Resistance to a novel antichlamydial compound is mediated through mutations in Chlamydia trachomatis secY.Direct simulation of early-stage Sec-facilitated protein translocation Emerging themes in SecA2-mediated protein export.Long-timescale dynamics and regulation of Sec-facilitated protein translocation.A gating motif in the translocation channel sets the hydrophobicity threshold for signal sequence function.Protein translocation across the rough endoplasmic reticulum.Protein export by the mycobacterial SecA2 system is determined by the preprotein mature domain.Interactions that drive Sec-dependent bacterial protein transport.The roles of pore ring and plug in the SecY protein-conducting channel.Assembly of the translocase motor onto the preprotein-conducting channel.Tail-anchored membrane protein insertion into the endoplasmic reticulum.Identification of a post-targeting step required for efficient cotranslational translocation of proteins across the Escherichia coli inner membrane.A signal sequence suppressor mutant that stabilizes an assembled state of the twin arginine translocase.Protein conducting channels-mechanisms, structures and applications.Selective transport by SecA2: an expanding family of customized motor proteins.The Sec translocon mediated protein transport in prokaryotes and eukaryotes.Unlocking the Bacterial SecY Translocon.Conformational dynamics of the plug domain of the SecYEG protein-conducting channel.Immobilization of the plug domain inside the SecY channel allows unrestricted protein translocation.Structure of the SecY complex unlocked by a preprotein mimic.

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P2860

Modeling the effects of prl mutations on the Escherichia coli SecY complex.

http://www.wikidata.org/entity/Q34048338

description

2005 nî lūn-bûn

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2005 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2005 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

Modeling the effects of prl mutations on the Escherichia coli SecY complex.

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Modeling the effects of prl mutations on the Escherichia coli SecY complex.

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Modeling the effects of prl mutations on the Escherichia coli SecY complex.

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type

label

Modeling the effects of prl mutations on the Escherichia coli SecY complex.

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Modeling the effects of prl mutations on the Escherichia coli SecY complex.

@en

Modeling the effects of prl mutations on the Escherichia coli SecY complex.

@nl

prefLabel

Modeling the effects of prl mutations on the Escherichia coli SecY complex.

@ast

Modeling the effects of prl mutations on the Escherichia coli SecY complex.

@en

Modeling the effects of prl mutations on the Escherichia coli SecY complex.

@nl

P1433

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P356

JB.187.18.6454-6465.2005

P1433

Journal of Bacteriology

P1476

Modeling the effects of prl mutations on the Escherichia coli SecY complex.

@en

P2093

Ann M Flower

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

Cathrine J DeMars

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Margaret A Smith

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P2860

Evolutionary conservation of components of the protein translocation complex

X-ray structure of a protein-conducting channel

Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter

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

Export of maltose-binding protein species with altered charge distribution surrounding the signal peptide hydrophobic core in Escherichia coli cells harboring prl suppressor mutations.

The Sec system.

Topology analysis of the SecY protein, an integral membrane protein involved in protein export in Escherichia coli.

A defined mutation in the protein export gene within the spc ribosomal protein operon of Escherichia coli: isolation and characterization of a new temperature-sensitive secY mutant.

A mutation affecting the regulation of a secA-lacZ fusion defines a new sec gene.

A signal sequence is not required for protein export in prlA mutants of Escherichia coli

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6454-6465

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scholarly article

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10.1128/JB.187.18.6454-6465.2005

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18

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187

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William M Clemons

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2005-09-01T00:00:00Z

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16159779

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Escherichia coli

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1236629

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