Interaction with the Src homology (SH3-SH2) region of the Src-family kinase Hck structures the HIV-1 Nef dimer for kinase activation and effector recruitment (Q30009331)

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scientific article published on 13 August 2014

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English	Interaction with the Src homology (SH3-SH2) region of the Src-family kinase Hck structures the HIV-1 Nef dimer for kinase activation and effector recruitment	scientific article published on 13 August 2014

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scholarly article

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Europe PubMed Central

21 May 2017

Interaction with the Src homology (SH3-SH2) region of the Src-family kinase Hck structures the HIV-1 Nef dimer for kinase activation and effector recruitment (English)

1 reference

Europe PubMed Central

21 May 2017

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author name string

John Jeff Alvarado

1

1 reference

Europe PubMed Central

21 May 2017

Sreya Tarafdar

2

1 reference

Europe PubMed Central

21 May 2017

Joanne I Yeh

3

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Europe PubMed Central

21 May 2017

Thomas E Smithgall

4

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Europe PubMed Central

21 May 2017

language of work or name

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publication date

13 August 2014

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Europe PubMed Central

21 May 2017

number of pages

15

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Journal of Biological Chemistry

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Europe PubMed Central

21 May 2017

289

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Europe PubMed Central

21 May 2017

41

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Europe PubMed Central

21 May 2017

28539-28553

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Europe PubMed Central

21 May 2017

describes a project that uses

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Europe PubMed Central

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC4192505/fullTextXML

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How HIV-1 Nef hijacks the AP-2 clathrin adaptor to downregulate CD4

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HIV-1 Nef interaction influences the ATP-binding site of the Src-family kinase, Hck

1 reference

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Interactions of the HIV/SIV pathogenicity factor Nef with SH3 domain-containing host cell proteins

1 reference

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Crystal Structure of the Src Family Kinase Hck SH3-SH2 Linker Regulatory Region Supports an SH3-dominant Activation Mechanism

1 reference

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1 reference

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The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling

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1 reference

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The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase

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Binding, domain orientation, and dynamics of the Lck SH3-SH2 domain pair and comparison with other Src-family kinases

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Domain assembly, surface accessibility and sequence conservation in full length HIV-1 Nef.

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HIV-1 Nef protein protects infected primary cells against killing by cytotoxic T lymphocytes.

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The Nef protein of human immunodeficiency virus establishes superinfection immunity by a dual strategy to downregulate cell-surface CCR5 and CD4.

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NMRPipe: a multidimensional spectral processing system based on UNIX pipes

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PROCHECK: a program to check the stereochemical quality of protein structures

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Direct Determination of Changes of Interdomain Orientation on Ligation: Use of the Orientational Dependence of15N NMR Relaxation in Abl SH(32)†

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Using Biacore to measure the binding kinetics of an antibody-antigen interaction

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12 December 2020

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The CD4C/HIV(Nef)transgenic model of AIDS

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https://pubmed.ncbi.nlm.nih.gov/25122770

12 December 2020

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inferred from PubMed ID database lookup

Processing of X-ray diffraction data collected in oscillation mode

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https://pubmed.ncbi.nlm.nih.gov/25122770

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Nef harbors a major determinant of pathogenicity for an AIDS-like disease induced by HIV-1 in transgenic mice

1 reference

https://pubmed.ncbi.nlm.nih.gov/25122770

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Identifiers

10.1074/JBC.M114.600031

1 reference

Europe PubMed Central

21 May 2017

0 references

1 reference

Europe PubMed Central

21 May 2017

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