Joseph W. Landry, Ph.D.

Affiliations: 
2002 Stony Brook University, Stony Brook, NY, United States 
Area:
Genetics
Google:
"Joseph Landry"

Parents

Sign in to add mentor
Rolf Sternglanz grad student 2002 SUNY Stony Brook
 (Characterization of histone modifying enzymes.)
BETA: Related publications

Publications

You can help our author matching system! If you notice any publications incorrectly attributed to this author, please sign in and mark matches as correct or incorrect.

Mayes K, Qiu Z, Alhazmi A, et al. (2014) ATP-dependent chromatin remodeling complexes as novel targets for cancer therapy. Advances in Cancer Research. 121: 183-233
Alkhatib SG, Landry JW. (2011) The nucleosome remodeling factor. Febs Letters. 585: 3197-207
Wang CL, Landry J, Sternglanz R. (2008) A yeast sir2 mutant temperature sensitive for silencing. Genetics. 180: 1955-62
Landry J, Sutton A, Hesman T, et al. (2003) Set2-catalyzed methylation of histone H3 represses basal expression of GAL4 in Saccharomyces cerevisiae. Molecular and Cellular Biology. 23: 5972-8
Landry J, Sternglanz R. (2003) Enzymatic assays for NAD-dependent deacetylase activities. Methods (San Diego, Calif.). 31: 33-9
Landry J, Sternglanz R. (2003) Yeast Fms1 is a FAD-utilizing polyamine oxidase. Biochemical and Biophysical Research Communications. 303: 771-6
Min J, Landry J, Sternglanz R, et al. (2001) Crystal structure of a SIR2 homolog-NAD complex. Cell. 105: 269-79
Tanner KG, Landry J, Sternglanz R, et al. (2000) Silent information regulator 2 family of NAD- dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose. Proceedings of the National Academy of Sciences of the United States of America. 97: 14178-82
Landry J, Slama JT, Sternglanz R. (2000) Role of NAD+ in the deacetylase activity of the SIR2-like proteins Biochemical and Biophysical Research Communications. 278: 685-690
Landry J, Sutton A, Tafrov ST, et al. (2000) The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases Proceedings of the National Academy of Sciences of the United States of America. 97: 5807-5811
See more...