Chaperone-assisted pilus assembly and bacterial attachment. (Q34066527)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11042452 AND SRC:MED&resulttype=core&format=json

1 November 2019

review article

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title

Chaperone-assisted pilus assembly and bacterial attachment (English)

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1 November 2019

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4

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1 November 2019

author name string

F G Sauer

1

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1 November 2019

M Barnhart

2

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1 November 2019

D Choudhury

3

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1 November 2019

G Waksman

5

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1 November 2019

S J Hultgren

6

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1 November 2019

publication date

1 October 2000

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Current Opinion in Structural Biology

1 November 2019

published in

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11042452 AND SRC:MED&resulttype=core&format=json

1 November 2019

volume

10

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1 November 2019

issue

5

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1 November 2019

page(s)

548-556

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Bacterial adhesins: common themes and variations in architecture and assembly.

1 November 2019

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Type 1 fimbrial expression enhances Escherichia coli virulence for the urinary tract

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Prevention of mucosal Escherichia coli infection by FimH-adhesin-based systemic vaccination

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Cloning, expression, and sequence analysis of the Haemophilus influenzae type b strain M43p pilin gene

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Identification of a gene essential for piliation in Haemophilus influenzae type b with homology to the pilus assembly platform genes of gram-negative bacteria.

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Haemophilus influenzae pili are composite structures assembled via the HifB chaperone

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Identification of two minor subunits in the pilus of Haemophilus influenzae

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PapD, a periplasmic transport protein in P-pilus biogenesis

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

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7 January 2021

The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems

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7 January 2021

Periplasmic chaperone recognition motif of subunits mediates quaternary interactions in the pilus

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7 January 2021

Evidence for donor strand complementation in the biogenesis of Haemophilus influenzae haemagglutinating pili

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7 January 2021

PapD-like chaperones provide the missing information for folding of pilin proteins

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7 January 2021

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

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Development of pilus organelle subassemblies in vitro depends on chaperone uncapping of a beta zipper.

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Structural basis of pilus subunit recognition by the PapD chaperone.

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7 January 2021

Structural basis of chaperone self-capping in P pilus biogenesis

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

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7 January 2021

The PapC usher forms an oligomeric channel: Implications for pilus biogenesis across the outer membrane

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7 January 2021

Ramifications of kinetic partitioning on usher-mediated pilus biogenesis

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7 January 2021

Crystal structure of chaperone protein PapD reveals an immunoglobulin fold

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NMR solution structure of the periplasmic chaperone FimC

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Probing conserved surfaces on PapD

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

YscB of Yersinia pestis functions as a specific chaperone for YopN.

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7 January 2021

Role of SycD, the chaperone of the Yersinia Yop translocators YopB and YopD.

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7 January 2021

Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures

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7 January 2021

Involvement of cellular caveolae in bacterial entry into mast cells.

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7 January 2021

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Identifiers

DOI

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11042452 AND SRC:MED&resulttype=core&format=json

1 November 2019

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