Role of a highly conserved bacterial protein in outer membrane protein assembly
about
The cyst-dividing bacterium Ramlibacter tataouinensis TTB310 genome reveals a well-stocked toolbox for adaptation to a desert environmentMycobacterial outer membranes: in search of proteinsMechanisms of protein export across the bacterial outer membraneMembrane protein insertion: mixing eukaryotic and prokaryotic concepts.Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporterIdentification of an outer membrane protein required for the transport of lipopolysaccharide to the bacterial cell surfaceThe translocation domain in trimeric autotransporter adhesins is necessary and sufficient for trimerization and autotransportationContribution of trimeric autotransporter C-terminal domains of oligomeric coiled-coil adhesin (Oca) family members YadA, UspA1, EibA, and Hia to translocation of the YadA passenger domain and virulence of Yersinia enterocoliticaA growing toolbox of techniques for studying β-barrel outer membrane protein folding and biogenesisFrom evolution to pathogenesis: the link between β-barrel assembly machineries in the outer membrane of mitochondria and gram-negative bacteriaExceptionally widespread nanomachines composed of type IV pilins: the prokaryotic Swiss Army knivesBacterial contact-dependent growth inhibitionVirB8-like protein TraH is crucial for DNA transfer in Enterococcus faecalisStructure and function of an essential component of the outer membrane protein assembly machineAutotransporter structure reveals intra-barrel cleavage followed by conformational changesFold and function of polypeptide transport-associated domains responsible for delivering unfolded proteins to membranesCrystal Structure of YaeT: Conformational Flexibility and Substrate RecognitionOmp85 from the Thermophilic Cyanobacterium Thermosynechococcus elongatus Differs from Proteobacterial Omp85 in Structure and Domain CompositionFunctional importance of a conserved sequence motif in FhaC, a prototypic member of the TpsB/Omp85 superfamilyStructure and Flexibility of the Complete Periplasmic Domain of BamA: The Protein Insertion Machine of the Outer MembraneStructure and function of BamE within the outer membrane and the β-barrel assembly machineCrystal Structure of BamD: An Essential Component of the β-Barrel Assembly Machinery of Gram-Negative BacteriaHigh-resolution structure of a new crystal form of BamA POTRA4–5 fromEscherichia coliStructure and Assembly of a Trans-Periplasmic Channel for Type IV Pili in Neisseria meningitidisCrystal Structure of -Barrel Assembly Machinery BamCD Protein ComplexCrystal Structure of BamB from Pseudomonas aeruginosa and Functional Evaluation of Its Conserved Structural FeaturesCrystallographic analysis of the C-terminal domain of theEscherichia colilipoprotein BamCStructure of Escherichia coli BamB and its interaction with POTRA domains of BamAStructure of BamA, an essential factor in outer membrane protein biogenesisStructural basis for the interaction of BamB with the POTRA3-4 domains of BamAStructure of the BAM complex and its implications for biogenesis of outer-membrane proteinsAn essential role of Sam50 in the protein sorting and assembly machinery of the mitochondrial outer membrane.The morphology proteins Mdm12/Mmm1 function in the major beta-barrel assembly pathway of mitochondria.The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria.Alternative function for the mitochondrial SAM complex in biogenesis of alpha-helical TOM proteinsTob38, a novel essential component in the biogenesis of beta-barrel proteins of mitochondria.Contact-Dependent Growth Inhibition (CDI) and CdiB/CdiA Two-Partner Secretion ProteinsExpression, folding, and proton transport activity of human uncoupling protein-1 (UCP1) in lipid membranes: evidence for associated functional formsIdentification of two inner-membrane proteins required for the transport of lipopolysaccharide to the outer membrane of Escherichia coliHxcQ liposecretin is self-piloted to the outer membrane by its N-terminal lipid anchor
P2860
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P2860
Role of a highly conserved bacterial protein in outer membrane protein assembly
description
2003 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունվարին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Science
@fr
artículu científicu espublizáu en 2003
@ast
im Januar 2003 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2003/01/10)
@sk
vědecký článek publikovaný v roce 2003
@cs
wetenschappelijk artikel (gepubliceerd op 2003/01/10)
@nl
наукова стаття, опублікована в січні 2003
@uk
name
Role of a highly conserved bacterial protein in outer membrane protein assembly
@ast
Role of a highly conserved bacterial protein in outer membrane protein assembly
@en
Role of a highly conserved bacterial protein in outer membrane protein assembly
@nl
type
label
Role of a highly conserved bacterial protein in outer membrane protein assembly
@ast
Role of a highly conserved bacterial protein in outer membrane protein assembly
@en
Role of a highly conserved bacterial protein in outer membrane protein assembly
@nl
prefLabel
Role of a highly conserved bacterial protein in outer membrane protein assembly
@ast
Role of a highly conserved bacterial protein in outer membrane protein assembly
@en
Role of a highly conserved bacterial protein in outer membrane protein assembly
@nl
P2093
P3181
P356
P1433
P1476
Role of a highly conserved bacterial protein in outer membrane protein assembly
@en
P2093
Jan Tommassen
Jeroen Geurtsen
Maarten Mols
Martine P. Bos
Romé Voulhoux
P304
P3181
P356
10.1126/SCIENCE.1078973
P407
P577
2003-01-10T00:00:00Z