P U B L I C A T I O N S

Cosgrove, M.S. (2007) Histone proteomics and the epigenetic regulation of nucleosome mobility. Expert Review of Proteomics 4, 465-478. (Invited Perspective).

Fry, C.J., Norris, A., Cosgrove, M.S., Boeke, J.D., and Peterson, C.L. (2006) The LRS and SIN domains: Two structurally equivalent but functionally distinct nucleosome surfaces required for transcriptional silencing. Mol. Cell. Biol. 26, 9045-9059.

Cosgrove, M.S. (2006) PHinDing a new histone effector domain. Structure 14, 1096-1098.

Cosgrove M.S., Bever, K., Avalos, J.L. Muhammad, S., Zhang,X. and Wolberger, C.(2006). The Structural Basis of Sirtuin Substrate Affinity. Biochemistry 45, 7511-7521.

Hyland, E.M., Cosgrove, M.S., Molina, H., Wang, D., Pandey, A., Cotter, R.J., and Boeke, J.D. (2005). Insights into the role of histone H3 and H4 core modifiable residues in Saccharomyces cerevisiae. Mol. Cell. Biol. 25, 10060-10070.

Cosgrove, MS, and Wolberger C (2005) How does the histone code work? Biochemistry and Cell Biology 83, 468-476 (featured on the cover).

Cosgrove, MS, Boeke JD, and Wolberger C (2004) Regulated nucleosome mobility and the histone code. Nature Structural & Molecular Biology 11, 1037-1043. (Highlighted on the Nature Milestones Gene Expression website)

Park, JH, Cosgrove, MS, Youngman E, Wolberger C, and Boeke JD(2002) A core nucleosome surface crucial for transcriptional silencing. Nature Genetics 32, 273-9. (Recommended reading by the Faculty of 1000 website)

Avalos JL, Celic I, Muhammand S, Cosgrove, MS, Boeke JD, and Wolberger C (2002) Structure of a Sir2 enzyme bound to an acetylated p53 peptide. Molecular Cell 10, 523-535 (featured on the cover).

Cosgrove, MS, Loh SN, Ha JH and Levy HR (2002) The catalytic mechanism of glucose 6-phosphate dehydrogenases: assignment and 1H NMR spectroscopy pH tiration of the catalytic histidine residue in the 109 kD Leuconostoc mesenteroides enzyme. Biochemistry 41, 6939-6945.

Naylor CE, Gover S, Basak AK, Cosgrove, MS, Levy HR, and Adams MJ (2001) NADP+ and NAD+ binding to the dual coenzyme specific enzyme Leuconostoc mesenteroides glucose 6-phospate dehydrogenase: different inter-domain hinge angles are seen in different binary and ternary complexes. Acta Cryst. D57, 635-648.

Cosgrove, MS, Gover S, Naylor CE, Vanderputte-Rutten L, Adams MJ and Levy HR (2000) An examinatin of the role of Asp-177 in the His-Asp catalytic dyad of glucose 6-phosphate dehydrogenase of Leuconostoc mesenteroides: X-ray structure and pH dependence of kinetic parameters of the D177N mutant enzyme. Biochemistry 39, 15002-15011.

Vought V, Ciccone T, Davino MH, Fairbairn L, Lin Y, Cosgrove, MS, Adams MJ and Levy HR (2000) Delineation of the roles of amino acids involved in the catalytic functions of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase. Biochemistry 39, 15012-15021.

Cosgrove, MS, Naylor C, Paludan S, Adams MJ, and Levy HR (1998) On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry 37, 2759-2767.