The Chlamydia effector TarP mimics the mammalian leucine-aspartic acid motif of paxillin to subvert the focal adhesion kinase during invasion (Q30409633)

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English	The Chlamydia effector TarP mimics the mammalian leucine-aspartic acid motif of paxillin to subvert the focal adhesion kinase during invasion	scientific article

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scholarly article

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Europe PubMed Central

PMC publication ID

13 October 2017

The Chlamydia effector TarP mimics the mammalian leucine-aspartic acid motif of paxillin to subvert the focal adhesion kinase during invasion (English)

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Europe PubMed Central

PMC publication ID

13 October 2017

object named as

Ivan Campeotto

3

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Rey A Carabeo

6

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author name string

Tristan Thwaites

1

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Europe PubMed Central

PMC publication ID

13 October 2017

Ana T Nogueira

2

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Europe PubMed Central

PMC publication ID

13 October 2017

Ana P Silva

4

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Europe PubMed Central

PMC publication ID

13 October 2017

Scott S Grieshaber

5

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Europe PubMed Central

PMC publication ID

13 October 2017

language of work or name

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publication date

5 September 2014

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Europe PubMed Central

PMC publication ID

13 October 2017

Journal of Biological Chemistry

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Europe PubMed Central

PMC publication ID

13 October 2017

289

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Europe PubMed Central

PMC publication ID

13 October 2017

44

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

30426-30442

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Europe PubMed Central

PMC publication ID

13 October 2017

describes a project that uses

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Europe PubMed Central

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC4215226/fullTextXML

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Insights into the biological functions of Dock family guanine nucleotide exchange factors

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Chlamydia trachomatis Tarp harbors distinct G and F actin binding domains that bundle actin filaments

1 reference

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10.1074/JBC.M114.604876

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

ResearchGate publication ID

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