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

Data up to Jan 2025

Published1993
Citations134
References25

Total Citations Per Year

Abstract

References (25)

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

1969 • 3,866 citations

THE STRUCTURE, FUNCTION, SYNTHESIS AND GENETIC CONTROL OF BACTERIAL PILI AND A MOLECULAR MODEL FOR DNA AND RNA TRANSPORT IN GRAM NEGATIVE BACTERIA*

1965 • 762 citations

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

1977 • 678 citations

P pili in uropathogenic E. coli are composite fibres with distinct fibrillar adhesive tips

1992 • 338 citations

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

1989 • 317 citations

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

1987 • 293 citations

Crystal structure of chaperone protein PapD reveals an immunoglobulin fold

1989 • 292 citations

CHAPERONE-ASSISTED ASSEMBLY AND MOLECULAR ARCHITECTURE OF ADHESIVE PILI

1991 • 236 citations

Organization and expression of genes responsible for type 1 piliation in Escherichia coli

1984 • 220 citations

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

1993 • 212 citations

Role of type 1 pili and effects of phase variation on lower urinary tract infections produced by Escherichia coli

1985 • 199 citations

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

1989 • 182 citations

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

1993 • 148 citations

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

1991 • 131 citations

Conserved immunoglobulin-like features in a family of periplasmic pilus chaperones in bacteria.

1992 • 123 citations

Identification and characterization of genes determining receptor binding and pilus length of Escherichia coli type 1 pili

1987 • 121 citations

Identification of two ancillary subunits of Escherichia coli type 1 fimbriae by using antibodies against synthetic oligopeptides of fim gene products

1987 • 116 citations

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

1992 • 116 citations

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

1992 • 90 citations

Globoside-specific adhesins of uropathogenic Escherichia coli are encoded by similar trans-complementable gene clusters

1985 • 81 citations

Adhesin presentation in bacteria requires molecular chaperones and ushers

1992 • 61 citations

Neutrophil activation by nascent FimH subunits of type 1 fimbriae purified from the periplasm of Escherichia coli.

1993 • 58 citations

Dependence of secretion and assembly of type 1 fimbrial subunits of Escherichia coli on normal protein export

1984 • 41 citations

A novel secretion apparatus for the assembly of adhesive bacterial pili

1993 • 35 citations

Mannose‐sensitive haemagglutination in the absence of piliation in Escherichia coli

1990 • 28 citations

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FimC is a periplasmic PapD-like chaperone that directs assembly of type 1 pili in… (1993) – Proceedings of the National Academy of Sciences | Metascience Observatory Explorer