P. Lou

发表

Discovery and optimization of anthranilic acid sulfonamides as inhibitors of methionine aminopeptidase-2: a structural basis for the reduction of albumin binding.

Scott A. Erickson, S. Davidsen, A. Petros, 2006, Journal of medicinal chemistry.

Efficient hydrogen production via sunlight-driven thermal formic acid decomposition over a porous film of molybdenum carbide

Yaguang Li, Shufang Wang, Cuncai Lv, 2021, Journal of Materials Chemistry A.

Physiologically relevant metal cofactor for methionine aminopeptidase-2 is manganese.

D. Egan, Chang H. Park, J. Henkin, 2003, Biochemistry.

Development of sulfonamide compounds as potent methionine aminopeptidase type II inhibitors with antiproliferative properties.

Scott A. Erickson, K. Comess, A. Vasudevan, 2006, Bioorganic & medicinal chemistry letters.

3-Amino-2-hydroxyamides and related compounds as inhibitors of methionine aminopeptidase-2.

Scott A. Erickson, Jyoti R. Patel, Chang H. Park, 2004, Bioorganic & medicinal chemistry letters.

Selective inhibition of endothelial cell proliferation by fumagillin is not due to differential expression of methionine aminopeptidases

J. Henkin, Jieyi Wang, P. Lou, 2000, Journal of cellular biochemistry.

Lead optimization of methionine aminopeptidase-2 (MetAP2) inhibitors containing sulfonamides of 5,6-disubstituted anthranilic acids.

Gary T. Wang, Chang H. Park, Jieyi Wang, 2007, Bioorganic & medicinal chemistry letters.

Paclitaxel at ultra low concentrations inhibits angiogenesis without affecting cellular microtubule assembly

J. Henkin, Jieyi Wang, R. Lesniewski, 2003, Anti-cancer drugs.

Tumor suppression by a rationally designed reversible inhibitor of methionine aminopeptidase-2.

Scott A. Erickson, J. Maris, Chang H. Park, 2003, Cancer research.

Ectopic expression of methionine aminopeptidase-2 causes cell transformation and stimulates proliferation

S. Davidsen, Qian Zhang, L. Tucker, 2008, Oncogene.