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Items: 1 to 20 of 119

1.

Structural basis of lysine-acetylated HIV-1 Tat recognition by PCAF bromodomain.

Mujtaba S, He Y, Zeng L, Farooq A, Carlson JE, Ott M, Verdin E, Zhou MM.

Mol Cell. 2002 Mar;9(3):575-86.

2.

HIV-1 tat transcriptional activity is regulated by acetylation.

Kiernan RE, Vanhulle C, Schiltz L, Adam E, Xiao H, Maudoux F, Calomme C, Burny A, Nakatani Y, Jeang KT, Benkirane M, Van Lint C.

EMBO J. 1999 Nov 1;18(21):6106-18.

3.

Tat acetylation modulates assembly of a viral-host RNA-protein transcription complex.

D'Orso I, Frankel AD.

Proc Natl Acad Sci U S A. 2009 Mar 3;106(9):3101-6. doi: 10.1073/pnas.0900012106.

4.

Enhancement of nuclear factor-kappa B acetylation by coactivator p300 and HIV-1 Tat proteins.

Furia B, Deng L, Wu K, Baylor S, Kehn K, Li H, Donnelly R, Coleman T, Kashanchi F.

J Biol Chem. 2002 Feb 15;277(7):4973-80.

5.

Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones.

Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F.

Virology. 2000 Nov 25;277(2):278-95.

6.

HIV-1 Tat interactions with p300 and PCAF transcriptional coactivators inhibit histone acetylation and neurotrophin signaling through CREB.

Wong K, Sharma A, Awasthi S, Matlock EF, Rogers L, Van Lint C, Skiest DJ, Burns DK, Harrod R.

J Biol Chem. 2005 Mar 11;280(10):9390-9.

7.

Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA.

Deng L, Wang D, de la Fuente C, Wang L, Li H, Lee CG, Donnelly R, Wade JD, Lambert P, Kashanchi F.

Virology. 2001 Oct 25;289(2):312-26.

8.
9.

Differential acetylation of Tat coordinates its interaction with the co-activators cyclin T1 and PCAF.

Brès V, Tagami H, Péloponèse JM, Loret E, Jeang KT, Nakatani Y, Emiliani S, Benkirane M, Kiernan RE.

EMBO J. 2002 Dec 16;21(24):6811-9.

10.

Tat acetyl-acceptor lysines are important for human immunodeficiency virus type-1 replication.

Brès V, Kiernan R, Emiliani S, Benkirane M.

J Biol Chem. 2002 Jun 21;277(25):22215-21.

11.

Transcriptional synergy between Tat and PCAF is dependent on the binding of acetylated Tat to the PCAF bromodomain.

Dorr A, Kiermer V, Pedal A, Rackwitz HR, Henklein P, Schubert U, Zhou MM, Verdin E, Ott M.

EMBO J. 2002 Jun 3;21(11):2715-23.

12.

Acetylation of the HIV-1 Tat protein by p300 is important for its transcriptional activity.

Ott M, Schnölzer M, Garnica J, Fischle W, Emiliani S, Rackwitz HR, Verdin E.

Curr Biol. 1999 Dec 16-30;9(24):1489-92.

13.

p73 Interacts with human immunodeficiency virus type 1 Tat in astrocytic cells and prevents its acetylation on lysine 28.

Amini S, Mameli G, Del Valle L, Skowronska A, Reiss K, Gelman BB, White MK, Khalili K, Sawaya BE.

Mol Cell Biol. 2005 Sep;25(18):8126-38.

14.

Acetylation of Tat defines a cyclinT1-independent step in HIV transactivation.

Kaehlcke K, Dorr A, Hetzer-Egger C, Kiermer V, Henklein P, Schnoelzer M, Loret E, Cole PA, Verdin E, Ott M.

Mol Cell. 2003 Jul;12(1):167-76.

15.
16.

Tat acetylation: a regulatory switch between early and late phases in HIV transcription elongation.

Ott M, Dorr A, Hetzer-Egger C, Kaehlcke K, Schnolzer M, Henklein P, Cole P, Zhou MM, Verdin E.

Novartis Found Symp. 2004;259:182-93; discussion 193-6, 223-5. Review.

PMID:
15171254
17.

Bromodomain: an acetyl-lysine binding domain.

Zeng L, Zhou MM.

FEBS Lett. 2002 Feb 20;513(1):124-8. Review.

18.

Insights on HIV-1 Tat:P/CAF bromodomain molecular recognition from in vivo experiments and molecular dynamics simulations.

Pantano S, Marcello A, Ferrari A, Gaudiosi D, Sabò A, Pellegrini V, Beltram F, Giacca M, Carloni P.

Proteins. 2006 Mar 1;62(4):1062-73.

PMID:
16362936
19.

Aqueous solution structure of a hybrid lentiviral Tat peptide and a model of its interaction with HIV-1 TAR RNA.

Mujeeb A, Parslow TG, Yuan YC, James TL.

J Biomol Struct Dyn. 1996 Feb;13(4):649-60.

PMID:
8906885
20.

Multiple modes of transcriptional regulation by the HIV-1 Tat transactivator.

Marcello A, Zoppé M, Giacca M.

IUBMB Life. 2001 Mar;51(3):175-81. Review.

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