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Article

Spatial clustering of the curlin secretion lipoprotein requires curli fiber assembly.

Journal of bacteriology - 1 Jan 2009

Epstein Elisabeth Ashman, Reizian Margeaux A, Chapman Matthew R

Abstract excerpt

Gram-negative bacteria assemble functional amyloid surface fibers called curli. CsgB nucleates the major curli subunit protein, CsgA, into a self-propagating amyloid fiber on the cell surface. The CsgG lipoprotein is sufficient for curlin transport across the outer membrane and is hypothesized to be the central molecule of the curli fiber secretion and assembly complex. We tested the hypothesis that the curli...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 19011034
DOI: 10.1128/JB.01244-08
PMCID: PMC2620823

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Spatial clustering of the curlin secretion lipoprotein requires curli fiber assembly.PMID 19011034Read ↗

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Structure-Function Analysis of the Curli Accessory Protein CsgE Defines Surfaces Essential for Coordinating Amyloid Fiber Formation.Semantic proximity Read ↗

Electrostatically-guided inhibition of Curli amyloid nucleation by the CsgC-like family of chaperonesSemantic proximity Read ↗

Structural and functional characterization of the Curli adaptor protein CsgFSemantic proximity Read ↗

The Production of Curli Amyloid Fibers Is Deeply Integrated into the Biology of Escherichia coli.Semantic proximity Read ↗

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