J
John E. Shively
Researcher at Beckman Research Institute
Publications - 178
Citations - 9190
John E. Shively is an academic researcher from Beckman Research Institute. The author has contributed to research in topics: Carcinoembryonic antigen & Peptide sequence. The author has an hindex of 44, co-authored 178 publications receiving 8792 citations. Previous affiliations of John E. Shively include Los Alamos National Laboratory.
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Journal ArticleDOI
A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes.
Nancy A. Thornberry,Herbert G. Bull,Jimmy R. Calaycay,Kevin T. Chapman,Andrew D. Howard,Matthew J. Kostura,Douglas K. Miller,Susan M. Molineaux,Jeffrey R. Weidner,John G. Aunins,Keith O. Elliston,Julia M. Ayala,Francesca J. Casano,Jayne Chin,Gloria J.-F. Ding,Linda A. Egger,Erin P. Gaffney,Guadalupe A. Limjuco,Oksana C. Palyha,S.M. Raju,Anna M. Rolando,J. Paul Salley,Ting-Ting Yamin,Terry D. Lee,John E. Shively,Malcolm MacCross,Richard A. Mumford,John A. Schmidt,Michael J. Tocci +28 more
TL;DR: Purification and cloning of the complementary DNA indicates that IL-lβ-converting enzyme is composed of two nonidentical subunits that are derived from a single proenzyme, possibly by autoproteolysis.
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Characterization of a major form of rat hepatic microsomal cytochrome P-450 induced by isoniazid.
D E Ryan,L Ramanathan,S Iida,Paul E. Thomas,M Haniu,John E. Shively,Charles S. Lieber,Wayne Levin +7 more
TL;DR: Cytochrome P-450j has been purified to electrophoretic homogeneity from isoniazid-treated adult male rats; and this enzyme appears to be a major protein induced in hepatic microsomes after administration of isoniaZid, as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
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Tumor localization of anti-CEA single-chain Fvs: improved targeting by non-covalent dimers
Anna M. Wu,Wengang Chen,Andrew Raubitschek,Lawrence E. Williams,Michael Neumaier,Rainer Fischer,Shi-zhen Hu,Tamara Odom-Maryon,Jeffrey Y.C. Wong,John E. Shively +9 more
TL;DR: Non-covalent dimers of scFV are stable, easy to produce and show excellent targeting as compared to monomeric scFv, probably due to increased mass and valency.
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Human aromatase: cDNA cloning, Southern blot analysis, and assignment of the gene to chromosome 15.
Shiuan Chen,Marc Besman,Robert S. Sparkes,Susan Zollman,Ivana Klisak,T. K. Mohandas,Peter F. Hall,John E. Shively +7 more
TL;DR: The amino acid sequence of human placental aromatase was determined in part (about 40%) by microsequencing methods and contains the highly conserved heme-binding domain, thus confirming the essential structural requirements for this class of protein.
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The amino acid sequence of a fluorescein-labeled peptide from the active site of (Na,K)-ATPase.
TL;DR: The labeling of (Na,K)-ATPase by fluorescein 5'-isothiocyanate was associated with the irreversible inhibition of enzymatic activity, and both the labeling of the tryptic peptide and inhibition of activity were prevented when the reaction was performed in the presence of ATP.