Subhangi Ghosh, Ph.D.

Affiliations: 
2011 Biological Sciences Purdue University, West Lafayette, IN, United States 
Google:
"Subhangi Ghosh"
Mean distance: 9.68
 
SNBCP

Parents

Sign in to add mentor
Jeffrey T. Bolin grad student 2011 Purdue
 (Structural studies of BphD LBb400 variants: Insights into the reaction mechanism of MCP hydrolases.)
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.

Khachatryan V, Sirunyan AM, Tumasyan A, et al. (2016) Search for Resonant Production of High-Mass Photon Pairs in Proton-Proton Collisions at sqrt[s]=8 and 13 TeV. Physical Review Letters. 117: 051802
Khachatryan V, Sirunyan AM, Tumasyan A, et al. (2016) Search for Narrow Resonances in Dijet Final States at sqrt[s]=8  TeV with the Novel CMS Technique of Data Scouting. Physical Review Letters. 117: 031802
Khachatryan V, Sirunyan AM, Tumasyan A, et al. (2016) Event generator tunes obtained from underlying event and multiparton scattering measurements. The European Physical Journal. C, Particles and Fields. 76: 155
Khachatryan V, Sirunyan AM, Tumasyan A, et al. (2016) Measurement of the [Formula: see text] production cross section in the all-jets final state in pp collisions at [Formula: see text][Formula: see text]. The European Physical Journal. C, Particles and Fields. 76: 128
Olek AT, Rayon C, Makowski L, et al. (2014) The structure of the catalytic domain of a plant cellulose synthase and its assembly into dimers. The Plant Cell. 26: 2996-3009
Ruzzini AC, Bhowmik S, Ghosh S, et al. (2013) A substrate-assisted mechanism of nucleophile activation in a Ser-His-Asp containing C-C bond hydrolase. Biochemistry. 52: 7428-38
Ruzzini AC, Bhowmik S, Yam KC, et al. (2013) The lid domain of the MCP hydrolase DxnB2 contributes to the reactivity toward recalcitrant PCB metabolites. Biochemistry. 52: 5685-95
Ruzzini AC, Ghosh S, Horsman GP, et al. (2012) Identification of an acyl-enzyme intermediate in a meta-cleavage product hydrolase reveals the versatility of the catalytic triad. Journal of the American Chemical Society. 134: 4615-24
See more...