Structure of Bordetella pertussis virulence factor P.69 pertactin
about
The Chlamydophila abortus genome sequence reveals an array of variable proteins that contribute to interspecies variationMolecular pathogenesis, epidemiology, and clinical manifestations of respiratory infections due to Bordetella pertussis and other Bordetella subspecies.The translocation domain in trimeric autotransporter adhesins is necessary and sufficient for trimerization and autotransportationDetection of spatial correlations in protein structures and molecular complexesCharacterization of two potentially universal turn motifs that shape the repeated five-residues fold--crystal structure of a lumenal pentapeptide repeat protein from Cyanothece 51142Structure and distribution of pentapeptide repeats in bacteriaBacterial 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.1.68-A crystal structure of endopolygalacturonase II from Aspergillus niger and identification of active site residues by site-directed mutagenesisThe iota-carrageenase of Alteromonas fortis. A beta-helix fold-containing enzyme for the degradation of a highly polyanionic polysaccharideThe structure of the Haemophilus influenzae HMW1 pro-piece reveals a structural domain essential for bacterial two-partner secretionCrystal structure of the Helicobacter pylori vacuolating toxin p55 domainAutotransporter structure reveals intra-barrel cleavage followed by conformational changesSelective Ligand Recognition by a Diversity-Generating Retroelement Variable ProteinAutotransporter 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 mechanismStructure of the Streptococcus pneumoniae Surface Protein and Adhesin PfbAThe antigen 43 structure reveals a molecular Velcro-like mechanism of autotransporter-mediated bacterial clumpingX-ray crystal structure of the passenger domain of plasmid encoded toxin(Pet), an autotransporter enterotoxin from enteroaggregative Escherichia coli (EAEC)Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptorsThe tree-dimensional structure of aspergillus niger pectin lyase B at 1.7-A resolutionSupramolecular structure in full-length Alzheimer's beta-amyloid fibrils: evidence for a parallel beta-sheet organization from solid-state nuclear magnetic resonance.Site-specific identification of non-beta-strand conformations in Alzheimer's beta-amyloid fibrils by solid-state NMRA structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMRSolid-state NMR as a probe of amyloid structureA model for Ure2p prion filaments and other amyloids: the parallel superpleated beta-structureType VI secretion system translocates a phage tail spike-like protein into target cells where it cross-links actinCrystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme MachineryLooks can be deceiving: recent insights into the mechanism of protein secretion by the autotransporter pathway.Stepwise folding of an autotransporter passenger domain is not essential for its secretionMechanistic link between β barrel assembly and the initiation of autotransporter secretion.Two-partner secretion of gram-negative bacteria: a single β-barrel protein enables transport across the outer membraneAutotransporter protein secretion.Residues in a conserved α-helical segment are required for cleavage but not secretion of an Escherichia coli serine protease autotransporter passenger domain.Channel properties of the translocator domain of the autotransporter Hbp of Escherichia coli.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 CFT073
P2860
Q22065749-17F83E32-6D55-48A7-8A50-CBF090CB0005Q24522458-F200D562-C807-4DDA-9B5B-90687B461E25Q24595049-102DB67C-0B2A-4947-B70C-1AA6BCD537BDQ24602698-AF88B93E-B5A8-48EA-B4DB-08FE197AF912Q24648111-C92C4B98-520A-43D6-898E-6901C9DB6B20Q24673061-F5DF935D-556D-4C02-BAE7-C527600B6BD3Q26828625-142E0772-DF3E-45B7-AE93-1B3CC0D73896Q27011231-A97CC894-792D-4A91-B99B-2C5E5C86EC1DQ27619983-C4F89CE5-10E7-4938-AAD4-F44B36B2267CQ27633983-5D487137-5154-40B6-ADAE-E2C4AF988F88Q27647289-11B6A6CE-4C2A-438F-8D3C-286093ED5915Q27648699-73081FED-07F7-48A5-9C1B-93F7D77E7193Q27648993-BE6CFA85-0E4F-4729-B1A9-931228B88F6CQ27650753-303E0366-BDB0-45F5-B552-1960961B0890Q27666695-CBEAAEC1-4A78-4BB0-8859-4C34276696CCQ27667004-07CD6328-9582-4418-AFA4-38FB339DF3AFQ27674666-9C73DC9D-0B28-48BB-B108-584E309170CAQ27678868-57B89BDB-5933-4891-AAF1-A53E93AB2A39Q27679237-9B23C580-0F6C-4771-9DC8-2FBFF12C1BFBQ27680876-E91EF049-CA71-4A6C-85F3-92189DC461BBQ27681742-14831ECA-D058-4693-89C9-8A302F16D063Q27733696-850374C7-0502-4931-BAFA-AA52DA5CE70EQ27748827-810EADD7-0B76-48CD-A997-1E7365204213Q28386697-2A6A9AA8-CFE9-4517-9947-56CAAE197533Q28386707-F9D2C5E9-D009-462B-AF2C-16028CE49690Q28387681-E1B9C5B3-5261-43B5-B0B0-43107251B263Q28388671-F7A0FC8C-8EA7-4DE9-AECF-03EA7FE40B8EQ28395735-3F837D75-861A-4186-8EC7-F2DAF0BA12A8Q28485710-7AFC54D5-8B44-43CE-8712-70651DE0F365Q28554698-3F36044F-A972-49DF-91CF-5544D62A86D1Q30152947-485AC4ED-CA75-490C-90F4-F4A0B9C4FB0FQ30153486-4FAC5068-3F42-48CC-B77A-F11B7BE017A2Q30155134-3357F72D-55F8-4C61-AF7C-F0298C6E1987Q30155419-32DE112C-09EE-49B7-81B9-6A680C671681Q30155423-D9A14395-6DE3-420B-AB0F-5EF7AE71093DQ30155539-341EA746-5B31-472C-AFDA-4FD581CF0799Q30155854-A95E46E6-9CF2-4B84-BA67-C7BD25BB46AEQ30156002-2B11C950-929E-4BD3-B41F-80EF23AAA3CCQ30156047-46D65D3F-7B4B-4B16-AE03-343649B2BACBQ30156964-23298A5F-BC5E-492A-BC84-EA212D49DC81
P2860
Structure of Bordetella pertussis virulence factor P.69 pertactin
description
1996 nî lūn-bûn
@nan
1996 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Structure of Bordetella pertussis virulence factor P.69 pertactin
@ast
Structure of Bordetella pertussis virulence factor P.69 pertactin
@en
Structure of Bordetella pertussis virulence factor P.69 pertactin
@nl
type
label
Structure of Bordetella pertussis virulence factor P.69 pertactin
@ast
Structure of Bordetella pertussis virulence factor P.69 pertactin
@en
Structure of Bordetella pertussis virulence factor P.69 pertactin
@nl
prefLabel
Structure of Bordetella pertussis virulence factor P.69 pertactin
@ast
Structure of Bordetella pertussis virulence factor P.69 pertactin
@en
Structure of Bordetella pertussis virulence factor P.69 pertactin
@nl
P2093
P356
P1433
P1476
Structure of Bordetella pertussis virulence factor P.69 pertactin
@en
P2093
I G Charles
N F Fairweather
N W Isaacs
P2888
P356
10.1038/381090A0
P407
P577
1996-05-02T00:00:00Z
P6179
1038170248