A. A. Carmen

HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription.

M. Grunstein, R. Kobayashi, B. Turner, 1996, Proceedings of the National Academy of Sciences of the United States of America.

Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin.

J Wu, M. Grunstein, A. A. Carmen, 2001, Molecular cell.

The regulation of gene activity by histones and the histone deacetylase RPD3.

M. Grunstein, S. Rundlett, A. A. Carmen, 1998, Cold Spring Harbor symposia on quantitative biology.

HDA2 and HDA3 are related proteins that interact with and are essential for the activity of the yeast histone deacetylase HDA1

M. Grunstein, R. Kobayashi, A. A. Carmen, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Acetylation of the Yeast Histone H4 N Terminus Regulates Its Binding to Heterochromatin Protein SIR3*

Lisa Milne, Michael Grunstein, M. Grunstein, 2002, The Journal of Biological Chemistry.

Yeast HOS3 forms a novel trichostatin A-insensitive homodimer with intrinsic histone deacetylase activity.

M. Grunstein, P. Griffin, S. Rundlett, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Transcriptional repression by UME6 involves deacetylation of lysine 5 of histone H4 by RPD3

M. Grunstein, B. Turner, S. Rundlett, 1998, Nature.

HDA1 and HDA3 Are Components of a Yeast Histone Deacetylase (HDA) Complex*

M. Grunstein, S. Rundlett, A. A. Carmen, 1996, The Journal of Biological Chemistry.

The upstream repression sequence from the yeast enolase gene ENO1 is a complex regulatory element that binds multiple trans-acting factors including REB1.

M. Holland, A. A. Carmen, 1994, The Journal of biological chemistry.

Transcriptional regulation by an upstream repression sequence from the yeast enolase gene ENO1

M. Holland, C. S. Park, A. A. Carmen, 1995, Yeast.