The twin-arginine translocation (Tat) protein export pathway.
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The globally widespread genus Sulfurimonas: versatile energy metabolisms and adaptations to redox clinesTopological mapping methods for α-helical bacterial membrane proteins--an update and a guideOverview of organohalide-respiring bacteria and a proposal for a classification system for reductive dehalogenasesA microbial sensor for discovering structural probes of protein misfolding and aggregationYidC/Alb3/Oxa1 Family of InsertasesSubstrate-dependent assembly of the Tat translocase as observed in live Escherichia coli cellsStructure of the TatC core of the twin-arginine protein transport systemStructural model for the protein-translocating element of the twin-arginine transport systemThe Glove-like Structure of the Conserved Membrane Protein TatC Provides Insight into Signal Sequence Recognition in Twin-Arginine TranslocationStructural Basis for TatA Oligomerization: An NMR Study of Escherichia coli TatA Dimeric StructureSelective selC-independent selenocysteine incorporation into formate dehydrogenasesA Phytase-Based Reporter System for Identification of Functional Secretion Signals in BifidobacteriaThe neomuran revolution and phagotrophic origin of eukaryotes and cilia in the light of intracellular coevolution and a revised tree of lifeSurA is involved in the targeting to the outer membrane of a Tat signal sequence-anchored protein.Optimization of overexpression of a chaperone protein of steroid C25 dehydrogenase for biochemical and biophysical characterization.Coordination of Synthesis and Assembly of a Modular Membrane-Associated [NiFe]-Hydrogenase Is Determined by Cleavage of the C-Terminal Peptide.Dynamic localization of Tat protein transport machinery components in Streptomyces coelicolor.Live cell imaging shows reversible assembly of the TatA component of the twin-arginine protein transport system.A holin and an endopeptidase are essential for chitinolytic protein secretion in Serratia marcescens.Systematics and molecular phylogeny of the family oscarellidae (homoscleromorpha) with description of two new oscarella speciesThe PhoP-dependent ncRNA Mcr7 modulates the TAT secretion system in Mycobacterium tuberculosis.Tracking Proteins Secreted by Bacteria: What's in the Toolbox?The mononuclear molybdenum enzymes.Optimizing recombinant antibodies for intracellular function using hitchhiker-mediated survival selectionIdentification and evaluation of twin-arginine translocase inhibitorsOxidative protein biogenesis and redox regulation in the mitochondrial intermembrane space.The conserved GTPase LepA contributes mainly to translation initiation in Escherichia coli.Multitasking SecB chaperones in bacteriaMislocalization of Rieske protein PetA predominantly accounts for the aerobic growth defect of Tat mutants in Shewanella oneidensis.Moraxella catarrhalis uses a twin-arginine translocation system to secrete the β-lactamase BRO-2.Diversity and evolution of bacterial twin arginine translocase protein, TatC, reveals a protein secretion system that is evolving to fit its environmental nicheComparative genomics of transport proteins in developmental bacteria: Myxococcus xanthus and Streptomyces coelicolorFermentation stage-dependent adaptations of Bacillus licheniformis during enzyme production.Secretome of obligate intracellular Rickettsia.TatBC-independent TatA/Tat substrate interactions contribute to transport efficiency.A TatABC-type Tat translocase is required for unimpaired aerobic growth of Corynebacterium glutamicum ATCC13032.The J-domain of heat shock protein 40 can enhance the transduction efficiency of arginine-rich cell-penetrating peptides.Label-free Quantitative Proteomics Reveals a Role for the Mycobacterium tuberculosis SecA2 Pathway in Exporting Solute Binding Proteins and Mce Transporters to the Cell WallDead-end intermediates in the enterobacterial common antigen pathway induce morphological defects in Escherichia coli by competing for undecaprenyl phosphate.A novel method of consensus pan-chromosome assembly and large-scale comparative analysis reveal the highly flexible pan-genome of Acinetobacter baumannii
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The twin-arginine translocation (Tat) protein export pathway.
description
article científic
@ca
article scientifique
@fr
articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
@pt
artigo científico
@pt-br
artikel ilmiah
@id
artikull shkencor
@sq
artículo científico
@es
name
The twin-arginine translocation (Tat) protein export pathway.
@en
type
label
The twin-arginine translocation (Tat) protein export pathway.
@en
prefLabel
The twin-arginine translocation (Tat) protein export pathway.
@en
P2860
P356
P1476
The twin-arginine translocation (Tat) protein export pathway.
@en
P2860
P2888
P304
P356
10.1038/NRMICRO2814
P407
P577
2012-06-11T00:00:00Z
P6179
1038800956