FimC is a periplasmic PapD-like chaperone that directs assembly of type 1 pili in bacteria - Wikidata - awgldk - TriplyDB

FimC is a periplasmic PapD-like chaperone that directs assembly of type 1 pili in bacteria

FimC is a periplasmic PapD-like chaperone that directs assembly of type 1 pili in bacteria

http://www.wikidata.org/entity/Q28249354

about

Structural basis of chaperone-subunit complex recognition by the type 1 pilus assembly platform FimD.Quality control of disulfide bond formation in pilus subunits by the chaperone FimC NMR solution structure of the periplasmic chaperone FimC Bacterial outer membrane ushers contain distinct targeting and assembly domains for pilus biogenesis.Functional flexibility of the FimH adhesin: insights from a random mutant library Small-molecule inhibitors target Escherichia coli amyloid biogenesis and biofilm formation.Sequestration of zinc oxide by fimbrial designer chelators Characterization of FasG segments required for 987P fimbria-mediated binding to piglet glycoprotein receptors.Adhesive threads of extraintestinal pathogenic Escherichia coli.Secretion and assembly of regular surface structures in Gram-negative bacteria.Ramifications of kinetic partitioning on usher-mediated pilus biogenesis Mast cell degranulation induced by type 1 fimbriated Escherichia coli in mice.Molecular strategies for fimbrial expression and assembly.Pilicide ec240 disrupts virulence circuits in uropathogenic Escherichia coli.FimH adhesin of type 1 pili is assembled into a fibrillar tip structure in the Enterobacteriaceae.Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes.PapD-like chaperones provide the missing information for folding of pilin proteins.Genes for CS2 pili of enterotoxigenic Escherichia coli and their interchangeability with those for CS1 pili.The structural gene encoding human enterotoxigenic Escherichia coli PCFO20 is homologous to that for porcine 987P Molecular basis of two subfamilies of immunoglobulin-like chaperones PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbA Identification and characterization of a gene cluster mediating enteroaggregative Escherichia coli aggregative adherence fimbria I biogenesis.Nucleotide sequence of the afimbrial-adhesin-encoding afa-3 gene cluster and its translocation via flanking IS1 insertion sequences.Pathotyping avian pathogenic Escherichia coli strains in Korea.Cloning of fimH and fliC and expression of the fusion protein FimH/FliC from Uropathogenic Escherichia coli (UPEC) isolated in Iran.The mast cell tumor necrosis factor alpha response to FimH-expressing Escherichia coli is mediated by the glycosylphosphatidylinositol-anchored molecule CD48.Regulation of fim genes in uropathogenic Escherichia coli.A tale of two pili: assembly and function of pili in bacteria.Drug and Vaccine Development for the Treatment and Prevention of Urinary Tract Infections.The Escherichia coli P and Type 1 Pilus Assembly Chaperones PapD and FimC Are Monomeric in Solution.Uropathogenic E. coli adhesin-induced host cell receptor conformational changes: implications in transmembrane signaling transduction.Localization of a domain in the FimH adhesin of Escherichia coli type 1 fimbriae capable of receptor recognition and use of a domain-specific antibody to confer protection against experimental urinary tract infection Positive selection identifies an in vivo role for FimH during urinary tract infection in addition to mannose binding.Adhesive organelles of Gram-negative pathogens assembled with the classical chaperone/usher machinery: structure and function from a clinical standpoint.Bacterial surface appendages as targets for novel antibacterial therapeutics.The gaf fimbrial gene cluster of Escherichia coli expresses a full-size and a truncated soluble adhesin protein.Uropathogenic Escherichia coli induces extrinsic and intrinsic cascades to initiate urothelial apoptosis Genetic characterization of Escherichia coli type 1 pilus adhesin mutants and identification of a novel binding phenotype Impairment of the biomechanical compliance of P pili: a novel means of inhibiting uropathogenic bacterial infections?The export systems of type 1 and F1C fimbriae are interchangeable but work in parental pairs

P2860

Q24529567-C6A6EF38-E161-46AB-9E46-85D91C93779E Q27681723-09D0D76D-ADB8-465B-A0AD-19DDA000BBFD Q27765723-5F9F1CA2-5B4F-4B75-BC94-53178599B443 Q30165131-A0CC3099-814F-4B44-8FB7-0822BDEE1828 Q30859071-19DE0F11-21FC-42DC-8251-37466D54E9E6 Q30885749-9AF5766C-F2D7-4822-A864-B115916E6B3F Q31440668-37C5E7BB-02B9-4F90-BDF1-CF0BC4D1EA4E Q33551932-1A3A4982-1219-4E8E-88EE-E4EFDEE0AC3B Q33554744-B5C51301-9BFB-45E7-BC2B-E0237FBB51AC Q33820597-A02A5073-D645-45DB-9D8A-273AF9088106 Q33888670-57096E76-0222-44E8-9158-96135CC8F557 Q34140243-AD1F2466-2F87-45B3-848A-1A32F86337FA Q34246945-704FE7AD-68A8-4F59-8BCA-B6E4737B40E4 Q34440901-F148D7DA-036A-4E00-8252-0BF88E3D5D5B Q34566388-D360650F-4D71-455D-9904-B4BCE86FDD26 Q34756531-DD6AD046-3C27-4CC4-8F83-22BB04422F0C Q35166061-0D6354CC-0CBD-4A3F-921F-F4EA87D104BD Q35457102-747A7CF6-AF9C-4635-9355-833E7FBAA1B1 Q35481439-C0A73E25-58F8-4DA4-9D5A-D99FF048D1ED Q35904132-E0EB2324-C144-407B-9CA1-73219A5463D3 Q35922206-9E388233-DD4C-425B-AC65-5FAD9D12E47D Q35968044-6E06DDEA-2435-4262-9335-B05BD6D5021F Q35983847-D7F88892-210A-4441-ADAB-D21BD9ED0F34 Q36066877-56065580-CFBF-41CE-BCAD-290EE9666C50 Q36211391-EA6228F8-A53C-4E72-B6F8-111107D23B40 Q36416493-22E58A2F-0AA5-49F0-A5CE-249D1CE97E65 Q36802922-FD83089E-B0FA-4DE7-AE6A-40182569149B Q36908459-74AE2119-717B-4E5D-98C8-743480309B9F Q36951570-5157C746-6209-4459-86A0-48A4B5DC979D Q37174241-84800B11-C7F9-42A4-9F5E-0D9DCA46EFCB Q37371352-8EC86CDA-F9BF-4E92-835A-AD961A520AF1 Q37371765-685B23E0-21EF-4B35-8280-1502253FF024 Q37478977-C671EE9C-033D-4377-B99C-748BBA7FA98A Q37673260-892231BB-AD81-447D-90CA-4AC4CF52CD4A Q38243219-FD6DD09F-8CAB-423F-9651-906EDDCF1B6B Q38305389-34167519-5F15-4B68-8ED0-7981F50528CC Q38481141-3D1C4663-BE04-42A3-B294-42E90A500540 Q39500248-6FAFBA4F-E4F8-4411-9066-C55BA925EBF9 Q39665383-FB977F60-1852-4F6D-A8C3-1EE724CA5528 Q39835431-CE361014-073A-4BB3-AACA-FD76B639DB81

P2860

FimC is a periplasmic PapD-like chaperone that directs assembly of type 1 pili in bacteria

http://www.wikidata.org/entity/Q28249354

description

1993 nî lūn-bûn

@nan

1993 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

1993 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

1993年の論文

@ja

1993年論文

@yue

1993年論文

@zh-hant

1993年論文

@zh-hk

1993年論文

@zh-mo

1993年論文

@zh-tw

1993年论文

@wuu

name

FimC is a periplasmic PapD-lik ...... bly of type 1 pili in bacteria

@ast

FimC is a periplasmic PapD-lik ...... bly of type 1 pili in bacteria

@en

FimC is a periplasmic PapD-lik ...... bly of type 1 pili in bacteria

@nl

type

label

FimC is a periplasmic PapD-lik ...... bly of type 1 pili in bacteria

@ast

FimC is a periplasmic PapD-lik ...... bly of type 1 pili in bacteria

@en

FimC is a periplasmic PapD-lik ...... bly of type 1 pili in bacteria

@nl

prefLabel

FimC is a periplasmic PapD-lik ...... bly of type 1 pili in bacteria

@ast

FimC is a periplasmic PapD-lik ...... bly of type 1 pili in bacteria

@en

FimC is a periplasmic PapD-lik ...... bly of type 1 pili in bacteria

@nl

P1433

Q28249354-7371230B-088F-4226-B0A2-D6D04F405851

P1476

Q28249354-BA59EFCD-C86B-4E06-AD2C-068B754D124D

P2093

Q28249354-0593B255-5CD5-4F7E-B05F-59DB31532496

Q28249354-376F03C6-55DF-4442-9CF5-128141F4AAAC

Q28249354-61CB46B1-6637-4AB4-A7D3-585DAF542FCA

Q28249354-82C69E49-669E-4F3C-A85E-D439FD3F9350

Q28249354-BE2276F9-70E6-45B8-8E5F-11FF19E63F2B

Q28249354-EEEC941E-AEA3-420B-A11F-0835ADA04B8B

P2860

Q28249354-110A0CE6-BEE4-4BB5-B9F1-60C28B370E61

Q28249354-21F9D525-2FEB-4C59-A92C-9CED25A2F767

Q28249354-2BC0EB74-2CCE-4293-9E59-BE9C16779865

Q28249354-2E0176F7-D932-4689-9C97-667AA3AE2FD5

Q28249354-4DD16DA0-66BB-4902-8F5D-C088F6B45DDF

Q28249354-53AC9DD2-0A4A-4811-BA90-064EB989293B

Q28249354-5CA9A52A-4F6E-4A34-9144-4A803C07CA32

Q28249354-5DDA7248-65AD-43BD-9A6D-0E70E651D5E7

Q28249354-5F30B887-CC7D-4229-B441-2FA89EB85E1F

Q28249354-6609A9CA-632C-43C3-A807-286C802F724D

P304

Q28249354-05EEEFF0-9FC7-44EC-A597-B8EB798C624E

P31

Q28249354-B6FCDC25-1D4E-4CBD-8FF9-3FF3CBA7742E

P356

Q28249354-59CDBEB0-FB10-4EDC-9838-345B9834D566

P407

Q28249354-9220374C-1F5E-4689-A2C6-448C004D9DD5

P433

Q28249354-B2EF4FE1-655B-4CC6-AA56-9D3AD5925BED

P478

Q28249354-00E92392-A1E5-482F-93FC-8CCC62125F98

P577

Q28249354-DD3810C5-FB80-4890-ADF1-30D83FCE75E6

P5875

Q28249354-FF49A4C6-AC0E-41A7-AE2C-B83DE49C3C32

P698

Q28249354-DFAB4314-04C6-4B72-A269-4C55B44C7BB4

P921

Q28249354-44A462E8-13D0-4F5D-9146-C5CDED982BF2

P932

Q28249354-63B735C3-DF79-4C0B-949E-875D0FD523A8

P356

PNAS.90.18.8397

P1433

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

P1476

FimC is a periplasmic PapD-lik ...... bly of type 1 pili in bacteria

@en

P2093

A V Nicholes

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

C H Jones

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

J S Pinkner

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

L N Slonim

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

S J Hultgren

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

S N Abraham

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

P2860

Crystal structure of chaperone protein PapD reveals an immunoglobulin fold

A complementation analysis of the restriction and modification of DNA in Escherichia coli

Three pure chaperone proteins of Escherichia coli--SecB, trigger factor and GroEL--form soluble complexes with precursor proteins in vitro.

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

Adherence of Escherichia coli to human mucosal cells mediated by mannose receptors.

The PapG protein is the alpha-D-galactopyranosyl-(1----4)-beta-D-galactopyranose-binding adhesin of uropathogenic Escherichia coli

Adhesin presentation in bacteria requires molecular chaperones and ushers.

Lesions in two Escherichia coli type 1 pilus genes alter pilus number and length without affecting receptor binding

P304

8397-401

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

P31

scholarly article

P356

10.1073/PNAS.90.18.8397

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

P407

P433

18

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

P478

90

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

P577

1993-09-15T00:00:00Z

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

P5875

15095587

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

P698

8104335

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

P921

molecular chaperones

P932

47363

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