Dimerization of the Agrobacterium tumefaciens VirB4 ATPase and the effect of ATP-binding cassette mutations on the assembly and function of the T-DNA transporter (Q41923043)

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scientific article published on June 1999

Language	Label	Description	Also known as
English	Dimerization of the Agrobacterium tumefaciens VirB4 ATPase and the effect of ATP-binding cassette mutations on the assembly and function of the T-DNA transporter	scientific article published on June 1999

Statements

scholarly article

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

Dimerization of the Agrobacterium tumefaciens VirB4 ATPase and the effect of ATP-binding cassette mutations on the assembly and function of the T-DNA transporter (English)

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

Agrobacterium tumefaciens

object named as

Agrobacterium tumefaciens

1 reference

based on heuristic

inferred from title

author name string

T A Dang

1

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

X R Zhou

2

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

B Graf

3

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

P J Christie

4

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

language of work or name

0 references

publication date

1 June 1999

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

Molecular Microbiology

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

32

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

6

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

1239-1253

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

Stability of the Agrobacterium tumefaciens VirB10 protein is modulated by growth temperature and periplasmic osmoadaption

1 reference

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Agrobacterium tumefaciens-mediated transformation of filamentous fungi

1 reference

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Natural competence for DNA transformation in Helicobacter pylori: identification and genetic characterization of the comB locus

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ATP-binding-cassette (ABC) transport systems: functional and structural aspects of the ATP-hydrolyzing subunits/domains

1 reference

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The Ti plasmid increases the efficiency of Agrobacterium tumefaciens as a recipient in virB-mediated conjugal transfer of an IncQ plasmid

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Type III protein secretion systems in bacterial pathogens of animals and plants

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Suppression of mutant phenotypes of the Agrobacterium tumefaciens VirB11 ATPase by overproduction of VirB proteins

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Agrobacterium tumefaciens T-complex transport apparatus: a paradigm for a new family of multifunctional transporters in eubacteria

1 reference

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The lipoprotein VirB7 interacts with VirB9 in the membranes of Agrobacterium tumefaciens

1 reference

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Characterization of membrane and protein interaction determinants of the Agrobacterium tumefaciens VirB11 ATPase

1 reference

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The VirB4 ATPase of Agrobacterium tumefaciens is a cytoplasmic membrane protein exposed at the periplasmic surface

1 reference

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Interactions between VirB9 and VirB10 membrane proteins involved in movement of DNA from Agrobacterium tumefaciens into plant cells

1 reference

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Agrobacterium-plant cell DNA transport: have virulence proteins, will travel

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Agrobacterium tumefaciens VirB7 and VirB9 form a disulfide-linked protein complex

1 reference

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Intermolecular disulfide bonds stabilize VirB7 homodimers and VirB7/VirB9 heterodimers during biogenesis of the Agrobacterium tumefaciens T-complex transport apparatus.

1 reference

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The Agrobacterium tumefaciens VirB7 lipoprotein is required for stabilization of VirB proteins during assembly of the T-complex transport apparatus

1 reference

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The Agrobacterium tumefaciens virB7 gene product, a proposed component of the T-complex transport apparatus, is a membrane-associated lipoprotein exposed at the periplasmic surface

1 reference

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Temperature affects the T-DNA transfer machinery of Agrobacterium tumefaciens

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The Agrobacterium tumefaciens virB4 gene product is an essential virulence protein requiring an intact nucleoside triphosphate-binding domain

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ABC transporters: bacterial exporters

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Identifiers

10.1046/J.1365-2958.1999.01436.X

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

ResearchGate publication ID

0 references

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