Pertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins.
about
The translocation domain in trimeric autotransporter adhesins is necessary and sufficient for trimerization and autotransportationType V secretion: mechanism(s) of autotransport through the bacterial outer membraneAn Overview of Helicobacter pylori VacA Toxin BiologyBacterial serine proteases secreted by the autotransporter pathway: classification, specificity, and role in virulenceOf linkers and autochaperones: an unambiguous nomenclature to identify common and uncommon themes for autotransporter secretion.Crystal structure of the Helicobacter pylori vacuolating toxin p55 domainStructure of the Receptor-Binding Protein of Bacteriophage Det7: a Podoviral Tail Spike in a MyovirusStructural and Functional Studies of Truncated Hemolysin A from Proteus mirabilisAutotransporter passenger domain secretion requires a hydrophobic cavity at the extracellular entrance of the β-domain poreCrystal Structure of the Autochaperone Region from the Shigella flexneri Autotransporter IcsACrystal Structure of the Passenger Domain of the Escherichia coli Autotransporter EspPRickettsia Sca2 has evolved formin-like activity through a different molecular mechanismCrystal Structures of the Outer Membrane Domain of Intimin and Invasin from Enterohemorrhagic E. coli and Enteropathogenic Y. pseudotuberculosisSecretion of the Intimin Passenger Domain Is Driven by Protein Folding.Sequential unfolding of the hemolysin two-partner secretion domain from Proteus mirabilis.Looks can be deceiving: recent insights into the mechanism of protein secretion by the autotransporter pathway.The passenger-associated transport repeat promotes virulence factor secretion efficiency and delineates a distinct autotransporter subtype.Reconstitution of bacterial autotransporter assembly using purified components.A mortise-tenon joint in the transmembrane domain modulates autotransporter assembly into bacterial outer membranes.Analysis of surface-exposed outer membrane proteins in Helicobacter pylori.Stepwise folding of an autotransporter passenger domain is not essential for its secretionCharge-dependent secretion of an intrinsically disordered protein via the autotransporter pathway.Mechanistic link between β barrel assembly and the initiation of autotransporter secretion.Intimin and invasin export their C-terminus to the bacterial cell surface using an inverse mechanism compared to classical autotransport.Single-cell characterization of autotransporter-mediated Escherichia coli surface display of disulfide bond-containing proteins.Residues in a conserved α-helical segment are required for cleavage but not secretion of an Escherichia coli serine protease autotransporter passenger domain.A conserved aromatic residue in the autochaperone domain of the autotransporter Hbp is critical for initiation of outer membrane translocationType V Secretion: the Autotransporter and Two-Partner Secretion PathwaysUpaH is a newly identified autotransporter protein that contributes to biofilm formation and bladder colonization by uropathogenic Escherichia coli CFT073Interaction of an autotransporter passenger domain with BamA during its translocation across the bacterial outer membrane.The Moraxella catarrhalis autotransporter McaP is a conserved surface protein that mediates adherence to human epithelial cells through its N-terminal passenger domain.Topology and maturation of filamentous haemagglutinin suggest a new model for two-partner secretion.Surface display of proteins by gram-negative bacterial autotransporters.Analysis of a beta-helical region in the p55 domain of Helicobacter pylori vacuolating toxin.Two-Partner Secretion: Combining Efficiency and Simplicity in the Secretion of Large Proteins for Bacteria-Host and Bacteria-Bacteria InteractionsHigh-resolution structure of infectious prion protein: the final frontierThe T7-related Pseudomonas putida phage φ15 displays virion-associated biofilm degradation properties.Reconstitution of Helicobacter pylori VacA toxin from purified componentsPrevalence and genetic characterization of pertactin-deficient Bordetella pertussis in Japan.Secretion of a bacterial virulence factor is driven by the folding of a C-terminal segment.
P2860
Q24595049-050F55B3-8017-43A0-AE21-EE992A9A0838Q24621416-87F29E0B-BCE5-4EAE-B05E-3756A1359C10Q26748278-8E7F4AF1-8765-49EA-9EE5-593A12F6278CQ26828625-79D48B40-F290-4B0D-B19B-E88BF123B476Q27011231-8A261FB7-123C-4079-8BBA-BF4E80457337Q27648699-62926B73-818F-443C-98CF-97F4CC95E2B6Q27649311-E36A93D7-54AA-433F-976C-A540E6A9A244Q27655729-6DF5E42E-4147-4ED2-A751-591AAED3EB45Q27666695-B21E16F7-7C3E-43A7-ABE9-F3435F1BAC71Q27667004-020CA21B-A95B-4A2F-B08D-7C7DD1A43294Q27674666-380F9E12-06AC-473D-8527-B09E32D28A3EQ27678868-2F3E1B9F-10AA-48BA-BF5A-1D0E97F4F4A5Q27679430-47A1E2C6-D568-42DC-9F72-F5C428ABAD51Q30152749-CEAA38C6-9872-473A-9248-ADD9811F3C49Q30152834-D7973F3D-F0DB-485A-AB2C-171D149DB90EQ30152947-7C616B15-F141-443C-9456-6C0E0ADE8CD5Q30152950-2A5047E2-46F4-42D2-8BF9-F37F96FD80E0Q30153344-6F91D9FE-5AB3-420A-AA2B-18F85E189FC5Q30153376-CB2614CB-F9F1-43DB-A20C-DC371AF2FC02Q30153404-B5A49D11-077A-40C4-97B2-870C678EDC96Q30153486-81B1F507-1BC1-4847-9A0E-0D8057E88FCCQ30153491-2B62DF24-3CD7-487A-8D85-CB8A9F9A4A31Q30155134-FE69A69C-4FDB-4285-B6C1-576140FA14B5Q30155205-92ED2446-8558-4D7E-A70B-616592645065Q30155216-24048A3B-174D-4F14-886C-8BD31FAFB5B2Q30155539-0299D30D-847D-4060-9CA4-DAD8462C65FBQ30156002-DB1D9AD0-6493-4AB1-97CA-FFBDD25A7E80Q30156047-E4E6DFC0-2DD0-4A8C-B876-8C7045EF249CQ30156964-3E899AF8-ACBE-4554-BB26-4C33EDBC2176Q30157080-E5775C2B-F7FA-4903-B432-967CCAC755D3Q30159574-705F89C3-F42C-4F9C-9CFD-70EE3544390EQ30159632-BD20C766-2DD8-4542-8AA7-2FB0BE471AF6Q33247360-073F7F62-F95A-4F3A-BE77-446E7782BF7DQ33533647-ED5B4F7B-4E5A-48C2-AEDA-00A22C646045Q33650510-C48946D5-48F3-4F4D-8C0A-CC5EC991FE91Q33725453-66C8B1FA-F41F-415A-B3D4-31A0F08313E8Q33883634-C97314CF-38E1-4D34-9FC1-62816C167229Q34020343-3D9BAC51-51A8-48DA-BA3E-995EFC695BCFQ34163792-E98D20E8-34F5-4A91-BB7C-22C5906093D4Q34200224-093B9220-ABCE-43D8-9B84-E4D7F61C7711
P2860
Pertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins.
description
2006 nî lūn-bûn
@nan
2006 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի մարտին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Pertactin beta-helix folding m ...... g of autotransporter proteins.
@ast
Pertactin beta-helix folding m ...... g of autotransporter proteins.
@en
type
label
Pertactin beta-helix folding m ...... g of autotransporter proteins.
@ast
Pertactin beta-helix folding m ...... g of autotransporter proteins.
@en
prefLabel
Pertactin beta-helix folding m ...... g of autotransporter proteins.
@ast
Pertactin beta-helix folding m ...... g of autotransporter proteins.
@en
P2093
P2860
P356
P1476
Pertactin beta-helix folding m ...... g of autotransporter proteins.
@en
P2093
Andrew V McDonnell
Christopher C Schuster
Kelli A Sorg
Mary C Finn
Mirco Junker
P2860
P304
P356
10.1073/PNAS.0507923103
P407
P577
2006-03-20T00:00:00Z