G.R. Bommineni

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Trends

Author Order

Document Type

Co-Authors

Peter J. Tonge

Stony Brook University

J. Schiebel

Philipps University of Marburg

Caroline Kisker

University of Würzburg

Kanishk Kapilashrami

Incyte (United States)

C. Schaefer

University of Würzburg

András Fekete

Budapest University of Technology and Economics

M.J. Mueller

Ludwig-Maximilians-Universität München

Anthony Chang

Children's Hospital of Orange County

Carlos Simmerling

Stony Brook University

Victoria Perrone

Stony Brook University

Cooperative Institutions

Stony Brook University

University of Science and Technology of China

State University of New York

University of Würzburg

National Institutes of Health

Incyte (United States)

Memorial Sloan Kettering Cancer Center

Stony Brook Medicine

Chinese Academy of Sciences

Columbia University

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Field

Crystal structure of S. aureus FabI in complex with NADP and 2- phenoxy-5-(2-propenyl)phenol

J. Schiebel Anthony Chang G.R. Bommineni Peter J. Tonge Caroline Kisker

Propenyl

Crystal (programming language)

10.2210/pdb4bnf/pdb

Cite

Citations (0)

Crystal structure of S. aureus FabI in complex with NADP and 2-(2- aminophenoxy)-5-hexylphenol

J. Schiebel Anthony Chang G.R. Bommineni Peter J. Tonge Caroline Kisker

Crystal (programming language)

10.2210/pdb4bni/pdb

Cite

Citations (0)

Thiolactomycin-based β-Ketoacyl-AcpM Synthase A (KasA) Inhibitors

Journal of Biological Chemistry (2013)

Kanishk Kapilashrami G.R. Bommineni CarlA. Machutta Pilho Kim Cheng‐Tsung Lai

Thiolactomycin (TLM) is a natural product inhibitor of KasA, the β-ketoacyl synthase A from Mycobacterium tuberculosis. To improve the affinity of TLM for KasA, a series of TLM analogs have been synthesized based on interligand NOEs between TLM and a pantetheine analog when both are bound simultaneously to the enzyme. Kinetic binding data reveal that position 3 of the thiolactone ring is a suitable position for elaboration of the TLM scaffold, and the structure-activity relationship studies provide information on the molecular features that govern time-dependent inhibition in this enzyme system. These experiments also exemplify the utility of transient one-dimensional NOE spectroscopy for obtaining interligand NOEs compared with traditional steady state two-dimensional NOESY spectroscopy.

Natural product

10.1074/jbc.m112.414516

Cite

Citations (32)

The effect of isoleucine to alanine mutation on InhA enzyme crystallization pattern and substrate binding loop conformation and flexibility

H.-J. Li C.T. Lai N. Liu Wancheng Yu Sejal Shah

INHA

Alanine

Isoleucine

10.2210/pdb5coq/pdb

Cite

Citations (0)