Spatial clustering of the curlin secretion lipoprotein requires curli fiber assembly - Wikidata - wikimedia - TriplyDB

Spatial clustering of the curlin secretion lipoprotein requires curli fiber assembly

Spatial clustering of the curlin secretion lipoprotein requires curli fiber assembly

http://www.wikidata.org/entity/Q28300992

about

Diversity, biogenesis and function of microbial amyloids Extending the usability of the phasing power of diselenide bonds: SeCys SAD phasing of CsgC using a non-auxotrophic strain Atomic Resolution Insights into Curli Fiber Biogenesis Outer membrane lipoprotein biogenesis: Lol is not the end.Assembly of the secretion pores GspD, Wza and CsgG into bacterial outer membranes does not require the Omp85 proteins BamA or TamA.New insight into the molecular control of bacterial functional amyloids Uropathogenic Escherichia coli modulates immune responses and its curli fimbriae interact with the antimicrobial peptide LL-37.Functional amyloid formation by Streptococcus mutans.Characterization of Salmonella type III secretion hyper-activity which results in biofilm-like cell aggregation.Curli biogenesis: order out of disorder.Modulation of curli assembly and pellicle biofilm formation by chemical and protein chaperones.The bacterial curli system possesses a potent and selective inhibitor of amyloid formation.A small RNA that regulates motility and biofilm formation in response to changes in nutrient availability in Escherichia coli.The Biology of the Escherichia coli Extracellular Matrix Enteric YaiW is a surface-exposed outer membrane lipoprotein that affects sensitivity to an antimicrobial peptide.The Chlamydia pneumoniae Adhesin Pmp21 Forms Oligomers with Adhesive Properties.Fold modulating function: bacterial toxins to functional amyloids.Giving structure to the biofilm matrix: an overview of individual strategies and emerging common themes.The Role of Functional Amyloids in Multicellular Growth and Development of Gram-Positive Bacteria.Functional amyloid: turning swords into plowshares CsgE is a curli secretion specificity factor that prevents amyloid fibre aggregation.Uncharacterized bacterial structures revealed by electron cryotomography.The Production of Curli Amyloid Fibers Is Deeply Integrated into the Biology of Escherichia coli.Amyloid-Like β-Aggregates as Force-Sensitive Switches in Fungal Biofilms and Infections.Alternative pathways for Escherichia coli biofilm formation revealed by sRNA overproduction.Electron microscopic observations of prokaryotic surface appendages.Identification of BamC on the Surface of E. coli.

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P2860

Spatial clustering of the curlin secretion lipoprotein requires curli fiber assembly

http://www.wikidata.org/entity/Q28300992

description

2009 nî lūn-bûn

@nan

2009 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Spatial clustering of the curlin secretion lipoprotein requires curli fiber assembly

@ast

Spatial clustering of the curlin secretion lipoprotein requires curli fiber assembly

@en

Spatial clustering of the curlin secretion lipoprotein requires curli fiber assembly

@nl

type

label

Spatial clustering of the curlin secretion lipoprotein requires curli fiber assembly

@ast

Spatial clustering of the curlin secretion lipoprotein requires curli fiber assembly

@en

Spatial clustering of the curlin secretion lipoprotein requires curli fiber assembly

@nl

prefLabel

Spatial clustering of the curlin secretion lipoprotein requires curli fiber assembly

@ast

Spatial clustering of the curlin secretion lipoprotein requires curli fiber assembly

@en

Spatial clustering of the curlin secretion lipoprotein requires curli fiber assembly

@nl

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P1433

Journal of Bacteriology

P1476

Spatial clustering of the curlin secretion lipoprotein requires curli fiber assembly

@en

P2093

Elisabeth Ashman Epstein

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

Margeaux A Reizian

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

Matthew R Chapman

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

P2860

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

In vitro polymerization of a functional Escherichia coli amyloid protein.

Wza the translocon for E. coli capsular polysaccharides defines a new class of membrane protein.

Salmonella enteritidis agfBAC operon encoding thin, aggregative fimbriae

The curli nucleator protein, CsgB, contains an amyloidogenic domain that directs CsgA polymerization.

Curli biogenesis and function

Functional amyloid--from bacteria to humans.

Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein.

Structural and topographical studies of the type IV bundle-forming pilus assembly complex of enteropathogenic Escherichia coli.

Nucleator-dependent intercellular assembly of adhesive curli organelles in Escherichia coli.

P304

608-15

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scholarly article

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10.1128/JB.01244-08

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P433

2

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191

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2009-01-01T00:00:00Z

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23475367

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19011034

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2620823

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