Outer-membrane PapC molecular usher discriminately recognizes periplasmic chaperone-pilus subunit complexes. - Wikidata - awgldk - TriplyDB

Outer-membrane PapC molecular usher discriminately recognizes periplasmic chaperone-pilus subunit complexes.

Outer-membrane PapC molecular usher discriminately recognizes periplasmic chaperone-pilus subunit complexes.

http://www.wikidata.org/entity/Q36257636

about

Mechanisms of protein export across the bacterial outer membrane Crystal structure of the FimD usher bound to its cognate FimC-FimH substrate Permissive linker insertion sites in the outer membrane protein of 987P fimbriae of Escherichia coli Structural basis of chaperone self-capping in P pilus biogenesis Crystal Structure of the P Pilus Rod Subunit PapA Fiber formation across the bacterial outer membrane by the chaperone/usher pathway Design and Synthesis of C-2 Substituted Thiazolo and Dihydrothiazolo Ring-Fused 2-Pyridones: Pilicides with Increased Antivirulence Activity Structural and Functional Characterization of Pseudomonas aeruginosa CupB Chaperones The Structure of the PapD-PapGII Pilin Complex Reveals an Open and Flexible P5 Pocket NMR solution structure of the periplasmic chaperone FimC FimC is a periplasmic PapD-like chaperone that directs assembly of type 1 pili in bacteria Cpx signaling pathway monitors biogenesis and affects assembly and expression of P pili The PprA-PprB two-component system activates CupE, the first non-archetypal Pseudomonas aeruginosa chaperone-usher pathway system assembling fimbriae Molecular basis of usher pore gating in Escherichia coli pilus biogenesis Domain activities of PapC usher reveal the mechanism of action of an Escherichia coli molecular machine.The role of chaperone-subunit usher domain interactions in the mechanism of bacterial pilus biogenesis revealed by ESI-MS.Modulating effects of the plug, helix, and N- and C-terminal domains on channel properties of the PapC usher.The 'P-usher', a novel protein transporter involved in fimbrial assembly and TpsA secretion.Topology of the outer membrane usher PapC determined by site-directed fluorescence labeling.Bacterial outer membrane ushers contain distinct targeting and assembly domains for pilus biogenesis.Nitazoxanide Inhibits Pilus Biogenesis by Interfering with Folding of the Usher Protein in the Outer Membrane An Overview of Two-Component Signal Transduction Systems Implicated in Extra-Intestinal Pathogenic E. coli Infections Secretion and assembly of regular surface structures in Gram-negative bacteria.Characterization of the Escherichia coli AF/R1 pilus operon: novel genes necessary for transcriptional regulation and for pilus-mediated adherence.Ramifications of kinetic partitioning on usher-mediated pilus biogenesis Periplasmic chaperone recognition motif of subunits mediates quaternary interactions in the pilus Bacterial adhesins: common themes and variations in architecture and assembly.CS5 pilus biosynthesis genes from enterotoxigenic Escherichia coli O115:H40.Characterization of the adhesin of Escherichia coli F18 fimbriae.Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli Escherichia coli DegP protease cleaves between paired hydrophobic residues in a natural substrate: the PapA pilin Bacterial adhesion pili are heterologous assemblies of similar subunits Assembly of CS1 pili: the role of specific residues of the major pilin, CooA Identification and characterization of assembly proteins of CS5 pili from enterotoxigenic Escherichia coli Protein secretion in the absence of ATP: the autotransporter, two-partner secretion and chaperone/usher pathways of gram-negative bacteria (review).A minor 987P protein different from the structural fimbrial subunit is the adhesin Identification of hifD and hifE in the pilus gene cluster of Haemophilus influenzae type b strain Eagan.FimH adhesin of type 1 pili is assembled into a fibrillar tip structure in the Enterobacteriaceae.Chaperoning Anfinsen: the steric foldases.Growth kinetics of bacterial pili from pairwise pilin association rates.

P2860

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P2860

Outer-membrane PapC molecular usher discriminately recognizes periplasmic chaperone-pilus subunit complexes.

http://www.wikidata.org/entity/Q36257636

description

1993 nî lūn-bûn

@nan

1993年の論文

@ja

1993年学术文章

@wuu

1993年学术文章

@zh-cn

1993年学术文章

@zh-hans

1993年学术文章

@zh-my

1993年学术文章

@zh-sg

1993年學術文章

@yue

1993年學術文章

@zh

1993年學術文章

@zh-hant

name

Outer-membrane PapC molecular ...... erone-pilus subunit complexes.

@ast

Outer-membrane PapC molecular ...... erone-pilus subunit complexes.

@en

type

label

Outer-membrane PapC molecular ...... erone-pilus subunit complexes.

@ast

Outer-membrane PapC molecular ...... erone-pilus subunit complexes.

@en

prefLabel

Outer-membrane PapC molecular ...... erone-pilus subunit complexes.

@ast

Outer-membrane PapC molecular ...... erone-pilus subunit complexes.

@en

P1433

Q36257636-9C155996-246D-4BF6-BB77-F70FEFE290F1

P1476

Q36257636-42946683-68F5-45A7-A4E9-EF0B2368A933

P2093

Q36257636-242B330E-D8E7-4F62-B75E-356ED4A7D61D

Q36257636-EFF1462A-318E-4CD0-9D88-D5B54DDBB57D

P2860

Q36257636-039EBD1A-2CC0-49F8-990F-AC577FB57068

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P304

Q36257636-841938EB-4033-4908-BFB7-FF09075113B9

P31

Q36257636-A5D9CED7-43FC-40EA-9EEA-0DA8DA3B9319

P356

Q36257636-D920AAA6-A1B8-46FA-83FD-26FCA7C0E560

P407

Q36257636-E04AE21A-BEBE-4AB6-8971-876FB0905C0E

P433

Q36257636-6FF9802E-1BF7-4C92-AB44-7B8F02DF52D9

P478

Q36257636-520AB265-6EA8-4540-A6A6-736AF4EBF629

P50

Q36257636-290D6BD7-186E-4BB7-B691-FCB7E929227C

Q36257636-56ED9A6A-E505-4157-927C-76C771592580

P577

Q36257636-3A558084-F7A5-4124-8D1B-AAE274B1FC9B

P5875

Q36257636-AFE8C118-487D-427E-8CF2-5C10F57D12E2

P698

Q36257636-9F022C4F-50AC-4060-8E22-5C25FC145A59

P921

Q36257636-304D74A9-1EC6-4C82-AB0A-F46B0A351E09

P932

Q36257636-847D2848-1464-489F-B711-FD7F2C6CC6FD

P356

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Outer-membrane PapC molecular ...... perone-pilus subunit complexes

@en

P2093

K W Dodson

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

S J Hultgren

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

P2860

Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector

Genes on the 90-kilobase plasmid of Salmonella typhimurium confer low-affinity cobalamin transport: relationship to fimbria biosynthesis genes.

The PapG adhesin of uropathogenic Escherichia coli contains separate regions for receptor binding and for the incorporation into the pilus.

Interactive surface in the PapD chaperone cleft is conserved in pilus chaperone superfamily and essential in subunit recognition and assembly.

Initiation of assembly and association of the structural elements of a bacterial pilus depend on two specialized tip proteins

Nucleotide sequence of the papA gene encoding the Pap pilus subunit of human uropathogenic Escherichia coli

Construction and expression of recombinant plasmids encoding type 1 or D-mannose-resistant pili from a urinary tract infection Escherichia coli isolate

Chaperone-assisted assembly and molecular architecture of adhesive pili.

Tissue tropism of Escherichia coli adhesins in human extraintestinal infections.

Immunoglobulin-like PapD chaperone caps and uncaps interactive surfaces of nascently translocated pilus subunits.

P304

3670-3674

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

P31

scholarly article

P356

10.1073/PNAS.90.8.3670

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

P407

P433

8

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

P478

90

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

P50

F Jacob-Dubuisson

P577

1993-04-01T00:00:00Z

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

P5875

15102573

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

P698

8097321

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

P921

molecular chaperones

P932

46363

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