Salt sensitivity of minimal twin arginine translocases. - Wikidata - wikimedia - TriplyDB

Salt sensitivity of minimal twin arginine translocases.

Salt sensitivity of minimal twin arginine translocases.

http://www.wikidata.org/entity/Q39935919

about

Bacillus subtilis: from soil bacterium to super-secreting cell factory Escherichia coli genes and pathways involved in surviving extreme exposure to ionizing radiation.Diversity and evolution of bacterial twin arginine translocase protein, TatC, reveals a protein secretion system that is evolving to fit its environmental niche Ultrastructural characterisation of Bacillus subtilis TatA complexes suggests they are too small to form homooligomeric translocation pores.Twin-Arginine Protein Translocation.New dye-decolorizing peroxidases from Bacillus subtilis and Pseudomonas putida MET94: towards biotechnological applications.Co-factor insertion and disulfide bond requirements for twin-arginine translocase-dependent export of the Bacillus subtilis Rieske protein QcrA.Specific targeting of the metallophosphoesterase YkuE to the bacillus cell wall requires the twin-arginine translocation system.High-level secretion of a recombinant protein to the culture medium with a Bacillus subtilis twin-arginine translocation system in Escherichia coli.

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P2860

Salt sensitivity of minimal twin arginine translocases.

http://www.wikidata.org/entity/Q39935919

description

2011 nî lūn-bûn

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2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

2011年论文

@zh

2011年论文

@zh-cn

name

Salt sensitivity of minimal twin arginine translocases.

@en

Salt sensitivity of minimal twin arginine translocases.

@nl

type

label

Salt sensitivity of minimal twin arginine translocases.

@en

Salt sensitivity of minimal twin arginine translocases.

@nl

prefLabel

Salt sensitivity of minimal twin arginine translocases.

@en

Salt sensitivity of minimal twin arginine translocases.

@nl

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P356

JBC.M111.243824

P1433

Journal of Biological Chemistry

P1476

Salt sensitivity of minimal twin arginine translocases

@en

P2093

Colin Robinson

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

Jan Maarten van Dijl

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

Nishi Vasisht

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

P2860

The complete genome sequence of the gram-positive bacterium Bacillus subtilis

Overlapping functions of components of a bacterial Sec-independent protein export pathway

A new type of signal peptide: central role of a twin-arginine motif in transfer signals for the delta pH-dependent thylakoidal protein translocase

Solution NMR structure of the TatA component of the twin-arginine protein transport system from gram-positive bacterium Bacillus subtilis

A common export pathway for proteins binding complex redox cofactors?

A minimal Tat system from a gram-positive organism: a bifunctional TatA subunit participates in discrete TatAC and TatA complexes

Protein-specific energy requirements for protein transport across or into thylakoid membranes. Two lumenal proteins are transported in the absence of ATP

Genetic analysis of the twin arginine translocator secretion pathway in bacteria.

The Tat protein export pathway.

Environmental salinity determines the specificity and need for Tat-dependent secretion of the YwbN protein in Bacillus subtilis.

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43759-43770

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scholarly article

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10.1074/JBC.M111.243824

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286

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Dierk-Christoph Pöther

René van der Ploeg

James Paul Barnett

Vivianne J Goosens

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2011-10-31T00:00:00Z

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22041895

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3243503

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