E
Eric F. Johnson
Researcher at Scripps Research Institute
Publications - 227
Citations - 20512
Eric F. Johnson is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: Cytochrome & Microsome. The author has an hindex of 70, co-authored 222 publications receiving 19543 citations. Previous affiliations of Eric F. Johnson include Salk Institute for Biological Studies & University of Illinois at Urbana–Champaign.
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Journal ArticleDOI
ABT-263: A Potent and Orally Bioavailable Bcl-2 Family Inhibitor
Christin Tse,Alexander R. Shoemaker,Jessica Adickes,Mark G. Anderson,Jun Chen,Sha Jin,Eric F. Johnson,Kennan C. Marsh,Michael J. Mitten,Paul Nimmer,Lisa R. Roberts,Stephen K. Tahir,Yu Xiao,Xiufen Yang,Haichao Zhang,Stephen W. Fesik,Saul H. Rosenberg,Steven W. Elmore +17 more
TL;DR: The biological properties and rationale for clinical trials evaluating ABT-263 in small-cell lung cancer and B-cell malignancies are provided and the oral efficacy should provide dosing flexibility to maximize clinical utility both as a single agent and in combination regimens are reported.
Journal ArticleDOI
The P450 superfamily: update on new sequences, gene mapping, and recommended nomenclature.
Daniel W. Nebert,David R. Nelson,Minor J. Coon,Ronald W. Estabrook,René Feyereisen,Yoshiaki Fujii-Kuriyama,Frank J. Gonzalez,F P Guengerich,Irwin C. Gunsalus,Eric F. Johnson +9 more
TL;DR: A modest revision of the initially proposed and updated and updated nomenclature system based on evolution of the superfamily P450 is proposed.
Journal ArticleDOI
The P450 gene superfamily: recommended nomenclature.
Daniel W. Nebert,Milton Adesnik,Minor J. Coon,Ronald W. Estabrook,Frank J. Gonzalez,F P Guengerich,Irwin C. Gunsalus,Eric F. Johnson,Byron Kemper,Wayne Levin +9 more
TL;DR: A nomenclature for the P450 gene superfamily is proposed based on evolution, and recommendations include Roman numerals for distinct gene families, capital letters for subfamilies, and Arabic numeral for individual genes.
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The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05-A resolution.
Jason Yano,Michael R. Wester,Guillaume A. Schoch,Keith J. Griffin,C. David Stout,Eric F. Johnson +5 more
TL;DR: The structure of P450 3A4 should facilitate a better understanding of the substrate selectivity of the enzyme, and may diminish the efficiency of substrate oxidation, which may be improved by space restrictions imposed by the presence of a second substrate molecule.
Journal ArticleDOI
Mammalian microsomal cytochrome P450 monooxygenase : structural adaptations for membrane binding and functional diversity
TL;DR: The first structure of a mammalian microsomal P450 was described in this article, which suggests that the association of P450s with the endoplasmic reticulum involves a hydrophobic surface of the protein formed by noncontiguous portions of the polypeptide chain.