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Items: 1 to 20 of 96

1.

Structural basis for substrate specificity and catalysis of human histone acetyltransferase 1.

Wu H, Moshkina N, Min J, Zeng H, Joshua J, Zhou MM, Plotnikov AN.

Proc Natl Acad Sci U S A. 2012 Jun 5;109(23):8925-30. doi: 10.1073/pnas.1114117109. Erratum in: Proc Natl Acad Sci U S A. 2013 Nov 5;110(45):18339.

2.

Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily.

Dutnall RN, Tafrov ST, Sternglanz R, Ramakrishnan V.

Cell. 1998 Aug 21;94(4):427-38.

3.

Crystal structure of an aminoglycoside 6'-N-acetyltransferase: defining the GCN5-related N-acetyltransferase superfamily fold.

Wybenga-Groot LE, Draker K, Wright GD, Berghuis AM.

Structure. 1999 May;7(5):497-507.

PMID:
10378269
4.

Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A.

Clements A, Rojas JR, Trievel RC, Wang L, Berger SL, Marmorstein R.

EMBO J. 1999 Jul 1;18(13):3521-32.

5.
6.

The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase gcn5p.

Owen DJ, Ornaghi P, Yang JC, Lowe N, Evans PR, Ballario P, Neuhaus D, Filetici P, Travers AA.

EMBO J. 2000 Nov 15;19(22):6141-9.

7.

Molecular basis for the autoregulation of the protein acetyl transferase Rtt109.

Stavropoulos P, Nagy V, Blobel G, Hoelz A.

Proc Natl Acad Sci U S A. 2008 Aug 26;105(34):12236-41. doi: 10.1073/pnas.0805813105.

8.

Crystal structure of the histone acetyltransferase Hpa2: A tetrameric member of the Gcn5-related N-acetyltransferase superfamily.

Angus-Hill ML, Dutnall RN, Tafrov ST, Sternglanz R, Ramakrishnan V.

J Mol Biol. 1999 Dec 17;294(5):1311-25.

PMID:
10600387
9.

Atomic resolution structure of human α-tubulin acetyltransferase bound to acetyl-CoA.

Taschner M, Vetter M, Lorentzen E.

Proc Natl Acad Sci U S A. 2012 Nov 27;109(48):19649-54. doi: 10.1073/pnas.1209343109.

10.

Structure of Arabidopsis thaliana At1g77540 protein, a minimal acetyltransferase from the COG2388 family.

Tyler RC, Bitto E, Berndsen CE, Bingman CA, Singh S, Lee MS, Wesenberg GE, Denu JM, Phillips GN Jr, Markley JL.

Biochemistry. 2006 Dec 5;45(48):14325-36.

11.

Crystal structure of Helicobacter pylori pseudaminic acid biosynthesis N-acetyltransferase PseH: implications for substrate specificity and catalysis.

Ud-Din AI, Liu YC, Roujeinikova A.

PLoS One. 2015 Mar 17;10(3):e0115634. doi: 10.1371/journal.pone.0115634.

12.

Kinetic mechanism of human histone acetyltransferase P/CAF.

Tanner KG, Langer MR, Denu JM.

Biochemistry. 2000 Oct 3;39(39):11961-9.

PMID:
11009610
13.
14.

Catalysis and substrate selection by histone/protein lysine acetyltransferases.

Berndsen CE, Denu JM.

Curr Opin Struct Biol. 2008 Dec;18(6):682-9. doi: 10.1016/j.sbi.2008.11.004. Review.

15.

Structure of histone acetyltransferases.

Marmorstein R.

J Mol Biol. 2001 Aug 17;311(3):433-44. Review.

PMID:
11492997
16.

Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide.

Rojas JR, Trievel RC, Zhou J, Mo Y, Li X, Berger SL, Allis CD, Marmorstein R.

Nature. 1999 Sep 2;401(6748):93-8.

PMID:
10485713
17.

Structure and catalytic mechanism of the human histone methyltransferase SET7/9.

Xiao B, Jing C, Wilson JR, Walker PA, Vasisht N, Kelly G, Howell S, Taylor IA, Blackburn GM, Gamblin SJ.

Nature. 2003 Feb 6;421(6923):652-6.

PMID:
12540855
18.

The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate.

Yan Y, Harper S, Speicher DW, Marmorstein R.

Nat Struct Biol. 2002 Nov;9(11):862-9.

PMID:
12368900
19.

Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator.

Trievel RC, Rojas JR, Sterner DE, Venkataramani RN, Wang L, Zhou J, Allis CD, Berger SL, Marmorstein R.

Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8931-6.

20.

Crystallographic analysis of substrate binding and catalysis in dihydrolipoyl transacetylase (E2p).

Mattevi A, Obmolova G, Kalk KH, Teplyakov A, Hol WG.

Biochemistry. 1993 Apr 20;32(15):3887-901.

PMID:
8471601

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