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Items: 1 to 20 of 149


HIV-1 infection of T cells and macrophages are differentially modulated by virion-associated Hck: a Nef-dependent phenomenon.

Cornall A, Mak J, Greenway A, Tachedjian G.

Viruses. 2013 Sep 18;5(9):2235-52. doi: 10.3390/v5092235.


Identification of a highly conserved valine-glycine-phenylalanine amino acid triplet required for HIV-1 Nef function.

Meuwissen PJ, Stolp B, Iannucci V, Vermeire J, Naessens E, Saksela K, Geyer M, Vanham G, Arien KK, Fackler OT, Verhasselt B.

Retrovirology. 2012 Apr 27;9:34. doi: 10.1186/1742-4690-9-34.


The identification of a small molecule compound that reduces HIV-1 Nef-mediated viral infectivity enhancement.

Chutiwitoonchai N, Hiyoshi M, Mwimanzi P, Ueno T, Adachi A, Ode H, Sato H, Fackler OT, Okada S, Suzu S.

PLoS One. 2011;6(11):e27696. doi: 10.1371/journal.pone.0027696. Epub 2011 Nov 15.


Interaction between Hck and HIV-1 Nef negatively regulates cell surface expression of M-CSF receptor.

Hiyoshi M, Suzu S, Yoshidomi Y, Hassan R, Harada H, Sakashita N, Akari H, Motoyoshi K, Okada S.

Blood. 2008 Jan 1;111(1):243-50. Epub 2007 Sep 24.


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.

Alvarado JJ, Tarafdar S, Yeh JI, Smithgall TE.

J Biol Chem. 2014 Oct 10;289(41):28539-53. doi: 10.1074/jbc.M114.600031. Epub 2014 Aug 13.


Nef alleles from all major HIV-1 clades activate Src-family kinases and enhance HIV-1 replication in an inhibitor-sensitive manner.

Narute PS, Smithgall TE.

PLoS One. 2012;7(2):e32561. doi: 10.1371/journal.pone.0032561. Epub 2012 Feb 29.


Single-domain antibody-SH3 fusions for efficient neutralization of HIV-1 Nef functions.

Bouchet J, Hérate C, Guenzel CA, Vérollet C, Järviluoma A, Mazzolini J, Rafie S, Chames P, Baty D, Saksela K, Niedergang F, Maridonneau-Parini I, Benichou S.

J Virol. 2012 May;86(9):4856-67. doi: 10.1128/JVI.06329-11. Epub 2012 Feb 15.


Structure, dynamics, and Hck interaction of full-length HIV-1 Nef.

Jung J, Byeon IJ, Ahn J, Gronenborn AM.

Proteins. 2011 May;79(5):1609-22. doi: 10.1002/prot.22986. Epub 2011 Mar 1.


Oligomerization is required for HIV-1 Nef-induced activation of the Src family protein-tyrosine kinase, Hck.

Ye H, Choi HJ, Poe J, Smithgall TE.

Biochemistry. 2004 Dec 21;43(50):15775-84.


Subtle Dynamic Changes Accompany Hck Activation by HIV-1 Nef and are Reversed by an Antiretroviral Kinase Inhibitor.

Wales TE, Hochrein JM, Morgan CR, Emert-Sedlak LA, Smithgall TE, Engen JR.

Biochemistry. 2015 Oct 20;54(41):6382-91. doi: 10.1021/acs.biochem.5b00875. Epub 2015 Oct 6.


Allosteric loss-of-function mutations in HIV-1 Nef from a long-term non-progressor.

Trible RP, Emert-Sedlak L, Wales TE, Ayyavoo V, Engen JR, Smithgall TE.

J Mol Biol. 2007 Nov 16;374(1):121-9. Epub 2007 Sep 11.


Overlapping effector interfaces define the multiple functions of the HIV-1 Nef polyproline helix.

Kuo LS, Baugh LL, Denial SJ, Watkins RL, Liu M, Garcia JV, Foster JL.

Retrovirology. 2012 May 31;9:47. doi: 10.1186/1742-4690-9-47.


SH3-mediated Hck tyrosine kinase activation and fibroblast transformation by the Nef protein of HIV-1.

Briggs SD, Sharkey M, Stevenson M, Smithgall TE.

J Biol Chem. 1997 Jul 18;272(29):17899-902.

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