The Legionella pneumophila IcmR protein exhibits chaperone activity for IcmQ by preventing its participation in high-molecular-weight complexes (Q47208585)

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scientific article published in June 2001

Language	Label	Description	Also known as
English	The Legionella pneumophila IcmR protein exhibits chaperone activity for IcmQ by preventing its participation in high-molecular-weight complexes	scientific article published in June 2001

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

11 January 2018

http://europepmc.org/abstract/MED/11401716

The Legionella pneumophila IcmR protein exhibits chaperone activity for IcmQ by preventing its participation in high-molecular-weight complexes (English)

1 reference

Europe PubMed Central

PubMed publication ID

11 January 2018

http://europepmc.org/abstract/MED/11401716

molecular chaperones

0 references

Legionella pneumophila

1 reference

based on heuristic

inferred from title

Ralph R. Isberg

2

object named as

Isberg RR

1 reference

Europe PubMed Central

PubMed publication ID

11 January 2018

http://europepmc.org/abstract/MED/11401716

author name string

Duménil G

1

1 reference

Europe PubMed Central

PubMed publication ID

11 January 2018

http://europepmc.org/abstract/MED/11401716

language of work or name

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publication date

1 June 2001

1 reference

Europe PubMed Central

PubMed publication ID

11 January 2018

http://europepmc.org/abstract/MED/11401716

Molecular Microbiology

1 reference

Europe PubMed Central

PubMed publication ID

11 January 2018

http://europepmc.org/abstract/MED/11401716

40

1 reference

Europe PubMed Central

PubMed publication ID

11 January 2018

http://europepmc.org/abstract/MED/11401716

5

1 reference

Europe PubMed Central

PubMed publication ID

11 January 2018

http://europepmc.org/abstract/MED/11401716

1113-1127

1 reference

Europe PubMed Central

PubMed publication ID

11 January 2018

http://europepmc.org/abstract/MED/11401716

From flagellum assembly to virulence: the extended family of type III export chaperones

1 reference

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Altered intracellular targeting properties associated with mutations in the Legionella pneumophila dotA gene

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The Legionella pneumophila icm locus: a set of genes required for intracellular multiplication in human macrophages

1 reference

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Yersinia enterocolitica type III secretion. On the role of SycE in targeting YopE into HeLa cells

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Bacterial type IV secretion: conjugation systems adapted to deliver effector molecules to host cells

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The Agrobacterium tumefaciens virE2 gene product is a single-stranded-DNA-binding protein that associates with T-DNA.

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Deviant expression of Rab5 on phagosomes containing the intracellular pathogens Mycobacterium tuberculosis and Legionella pneumophila is associated with altered phagosomal fate

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Substrate-specific binding of hook-associated proteins by FlgN and FliT, putative chaperones for flagellum assembly

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The transfer region of IncI1 plasmid R64: similarities between R64 tra and legionella icm/dot genes

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21 January 2018

Identification and subcellular localization of the Legionella pneumophila IcmX protein: a factor essential for establishment of a replicative organelle in eukaryotic host cells

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21 January 2018

Extracellular association and cytoplasmic partitioning of the IpaB and IpaC invasins of S. flexneri

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A series of wide-host-range low-copy-number vectors that allow direct screening for recombinants

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Translocation of Helicobacter pylori CagA into gastric epithelial cells by type IV secretion

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Legionella pneumophila DotA protein is required for early phagosome trafficking decisions that occur within minutes of bacterial uptake

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Host cell killing and bacterial conjugation require overlapping sets of genes within a 22-kb region of the Legionella pneumophila genome.

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21 January 2018

Cooperative binding of Agrobacterium tumefaciens VirE2 protein to single-stranded DNA.

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Legionella pneumophila replication vacuoles mature into acidic, endocytic organelles

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VirE1 protein mediates export of the single-stranded DNA-binding protein VirE2 from Agrobacterium tumefaciens into plant cells

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SycE, a chaperone-like protein of Yersinia enterocolitica involved in Ohe secretion of YopE.

1 reference

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Individual chaperones required for Yop secretion by Yersinia

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Customized secretion chaperones in pathogenic bacteria

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1 reference

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21 January 2018

Identifiers

10.1046/J.1365-2958.2001.02454.X

1 reference

Europe PubMed Central

PubMed publication ID

11 January 2018

http://europepmc.org/abstract/MED/11401716

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

11 January 2018

http://europepmc.org/abstract/MED/11401716

ResearchGate publication ID

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