Y. He

发表

Topological changes in the CYP3A4 active site probed with phenyldiazene: effect of interaction with NADPH-cytochrome P450 reductase and cytochrome b5 and of site-directed mutagenesis.

J. Halpert, Y. Yamaguchi, K. K. Khan, 2004, Drug metabolism and disposition: the biological fate of chemicals.

TOPOLOGICAL CHANGES IN THE CYP 3 A 4 ACTIVE SITE PROBED WITH PHENYLDIAZENE : EFFECT OF INTERACTION WITH NADPH-CYTOCHROME P 450 REDUCTASE AND CYTOCHROME B 5 AND OF SITE-DIRECTED MUTAGENESIS

J. Halpert, Y. Yamaguchi, K. K. Khan, 2003 .

CYP3A4 is a vitamin D-24- and 25-hydroxylase: analysis of structure function by site-directed mutagenesis.

J. Halpert, N. Bell, Ram P. Gupta, 2005, The Journal of clinical endocrinology and metabolism.

Activation of the anticancer prodrugs cyclophosphamide and ifosfamide: identification of cytochrome P450 2B enzymes and site-specific mutants with improved enzyme kinetics.

D. Waxman, J. Halpert, Jack T. Lin, 2004, Molecular pharmacology.

An open conformation of mammalian cytochrome P450 2B4 at 1.6-Å resolution

James R. Halpert, Eric F. Johnson, J. Halpert, 2003, Proceedings of the National Academy of Sciences of the United States of America.

KIT kinase mutants show unique mechanisms of drug resistance to imatinib and sunitinib in gastrointestinal stromal tumor patients

Yan Zhang, Mark R. Emmett, Alan G. Marshall, 2009, Proceedings of the National Academy of Sciences.

deletion of 7 . 1 kb of DNA . hormone deficiency with a A Chinese familial growth

Shi Chen, Y. He, Ya Xin Wang, 2004 .

Expanding control of the tumor cell cycle with a CDK2/4/6 inhibitor.

X. Mu, J. Bienkowska, Zhou Zhu, 2021, Cancer cell.

Spectrum and Degree of CDK Drug Interactions Predicts Clinical Performance

Ping Chen, Simon Bergqvist, Xiu Yu, 2016, Molecular Cancer Therapeutics.

Polycomb repressive complex 2 structure with inhibitor reveals a mechanism of activation and drug resistance

K. Gajiwala, P. Kung, A. Brooun, 2016, Nature Communications.

Discovery of PF-06873600, a CDK2/4/6 Inhibitor for the Treatment of Cancer.

J. Lapek, Sherry L. Niessen, M. McTigue, 2021, Journal of medicinal chemistry.

Ack1: Activation and Regulation by Allostery

K. Gajiwala, R. Ferre, K. Maegley, 2013, PloS one.

Role of Residue 363 and 206 in Conversion of Cytochrome P450 2B1 from a Steroid 16-Hydroxylase to a 15α-Hydroxylase

J. Halpert, Y. He, Z. Lou, 1994 .

Secobarbital-mediated Inactivation of Cytochrome P450 2B1 and Its Active Site Mutants

Grazyna D. Szklarz, James R. Halpert, Maria Almira Correia, 1996, The Journal of Biological Chemistry.

Analysis of homotropic and heterotropic cooperativity of diazepam oxidation by CYP3A4 using site-directed mutagenesis and kinetic modeling.

J. Halpert, James R Halpert, You Ai He, 2003, Archives of biochemistry and biophysics.

Structure of Mammalian Cytochrome P450 2B4 Complexed with 4-(4-Chlorophenyl)imidazole at 1.9-Å Resolution

Eric F. Johnson, J. Halpert, C. Stout, 2004, Journal of Biological Chemistry.

Structure of mammalian cytochrome P450 2B4

Eric F. Johnson, J. Halpert, C. Stout, 2000 .

Identification and functional characterization of eight CYP3A4 protein variants.

H. Klenk, J. Brockmöller, J. Halpert, 2001, Pharmacogenetics.

Phenylalanine and tryptophan scanning mutagenesis of CYP3A4 substrate recognition site residues and effect on substrate oxidation and cooperativity.

J. Halpert, J R Halpert, Q Wang, 2001, Biochemistry.

Dual role of human cytochrome P450 3A4 residue Phe-304 in substrate specificity and cooperativity.

J. Halpert, J R Halpert, G R Harlow, 2000, The Journal of pharmacology and experimental therapeutics.

Site-directed mutagenesis of cytochrome P450eryF: implications for substrate oxidation, cooperativity, and topology of the active site.

J. Halpert, K. K. Khan, Y. He, 2002, Chemical research in toxicology.

Identification of three key residues in substrate recognition site 5 of human cytochrome P450 3A4 by cassette and site-directed mutagenesis.

J. Halpert, G. Szklarz, G D Szklarz, 1997, Biochemistry.

Site-directed mutagenesis of putative substrate recognition sites in cytochrome P450 2B11: importance of amino acid residues 114, 290, and 363 for substrate specificity.

J. Halpert, G. Szklarz, L. Kaminsky, 1994, Molecular pharmacology.

Role of residue 478 as a determinant of the substrate specificity of cytochrome P450 2B1.

J. Halpert, Y. He, K. Kedzie, 1992, Biochemistry.

Molecular basis for a functionally unique cytochrome P450IIB1 variant.

S. Grimm, J. Halpert, J. Regan, 1991, The Journal of biological chemistry.