2004 - Fellow of the American Association for the Advancement of Science (AAAS)
1974 - Fellow of Alfred P. Sloan Foundation
Biochemistry, Ribosome, Protein biosynthesis, Stereochemistry and Biophysics are his primary areas of study. His study in Biochemistry concentrates on Peptide sequence, Enzyme, Inorganic pyrophosphatase, Escherichia coli and Ribonucleotide reductase. His work deals with themes such as Ribosomal RNA and Transfer RNA, which intersect with Ribosome.
His research integrates issues of Messenger RNA, EF-G, Förster resonance energy transfer, Protein engineering and Lysis in his study of Protein biosynthesis. Barry S. Cooperman combines subjects such as Molecule and Chymotrypsin with his study of Stereochemistry. His Biophysics research is multidisciplinary, relying on both Translation, Prokaryotic initiation factor-2, Eukaryotic translation, Thiostrepton and GTP'.
His scientific interests lie mostly in Biochemistry, Ribosome, Stereochemistry, Transfer RNA and Ribosomal protein. Protein subunit, Escherichia coli, Ribonucleotide reductase, Enzyme and Binding site are the subjects of his Biochemistry studies. His Ribosome research incorporates elements of Ribosomal RNA, Biophysics, Puromycin, Protein biosynthesis and Translation.
His Biophysics study which covers Crystallography that intersects with Molecule. His Stereochemistry study also includes
Barry S. Cooperman focuses on Ribosome, Transfer RNA, Protein biosynthesis, Biophysics and Translation. The study of Biochemistry and RNA are components of his Ribosome research. His Biochemistry study frequently draws connections between related disciplines such as Fluorophore.
The various areas that Barry S. Cooperman examines in his Transfer RNA study include Crystallography, Fluorescence and Chromosomal translocation. His study in Protein biosynthesis is interdisciplinary in nature, drawing from both Amino acid, Single-molecule FRET, Protein subunit, Cell-free system and Cell biology. Barry S. Cooperman interconnects GTPase, Ribosomal RNA, Molecular biology, Base pair and Genetic code in the investigation of issues within Translation.
His primary areas of study are Ribosome, Protein biosynthesis, Biochemistry, Transfer RNA and Biophysics. His specific area of interest is Ribosome, where he studies Ribosomal protein. The concepts of his Protein biosynthesis study are interwoven with issues in Protein subunit, Alkyne, Cell biology, Combinatorial chemistry and Azide.
His is doing research in A-site, GTPase, Dihydrouridine, Oligonucleotide and Cytidine, both of which are found in Biochemistry. Barry S. Cooperman has researched Transfer RNA in several fields, including Uridine, Covalent bond, Escherichia coli, Molecular biology and Förster resonance energy transfer. His research in Biophysics intersects with topics in RNA and Peptide Elongation Factor G.
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A double-stranded RNA unwinding activity introduces structural alterations by means of adenosine to inosine conversions in mammalian cells and Xenopus eggs.
Richard W. Wagner;Joseph E. Smith;Barry S. Cooperman;Kazuko Nishikura.
Proceedings of the National Academy of Sciences of the United States of America (1989)
Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop
Anzhi Wei;Harvey Rubin;Barry S. Cooperman;David W. Christianson.
Nature Structural & Molecular Biology (1994)
Evolutionary conservation of the active site of soluble inorganic pyrophosphatase.
Barry S. Cooperman;Alexander A. Baykov;Reijo Lahti.
Trends in Biochemical Sciences (1992)
Kinetically competent intermediates in the translocation step of protein synthesis.
Dongli Pan;Stanislav V. Kirillov;Stanislav V. Kirillov;Barry S. Cooperman.
Molecular Cell (2007)
Cloning, expression, purification, and biological activity of recombinant native and variant human alpha 1-antichymotrypsins.
H. Rubin;Zhi Mei Wang;E. B. Nickbarg;S. Mclarney.
Journal of Biological Chemistry (1990)
Photoincorporation of tetracycline into Escherichia coli ribosomes. Identification of the major proteins photolabeled by native tetracycline and tetracycline photoproducts and implications for the inhibitory action of tetracycline on protein synthesis.
Robert A. Goldman;Tayyaba Hasan;Clifford C. Hall;William A. Strycharz.
Biochemistry (1983)
The structural basis for pyrophosphatase catalysis.
Pirkko Heikinheimo;Jukka Lehtonen;Alexander Baykov;Reijo Lahti.
Structure (1996)
Reaction of human skin chymotrypsin-like proteinase chymase with plasma proteinase inhibitors.
N M Schechter;J L Sprows;O L Schoenberger;G S Lazarus.
Journal of Biological Chemistry (1989)
Dynamics of translation by single ribosomes through mRNA secondary structures
Chunlai Chen;Haibo Zhang;Steven L Broitman;Michael Reiche.
Nature Structural & Molecular Biology (2013)
The mechanism of action of yeast inorganic pyrophosphatase.
Barry S. Cooperman.
Methods in Enzymology (1982)
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