Bernard Bell
American law clerk
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Bernard Bell 's Degrees
- Doctorate Law Harvard University
Why Is Bernard Bell Influential?
(Suggest an Edit or Addition)According to Wikipedia, Bernard Bell is the Associate Dean for Academic Affairs and Faculty Professor of Law and Herbert Hannoch Scholar at Rutgers School of Law–Newark. Career Bell received a B.A. cum laude from Harvard and a J.D. from Stanford, where he was notes editor of the Stanford Law Review and a member of the Order of the Coif. He clerked for Judge Amalya L. Kearse of the U.S. Court of Appeals for the Second Circuit and for U.S. Supreme Court Justice Byron R. White and then practiced with Sullivan & Cromwell in New York City. Before coming to Rutgers in 1994, he served as senior litigation counsel and, earlier, as Assistant U.S. Attorney in the U.S. Attorney's Office for the Southern District of New York.
Bernard Bell 's Published Works
Published Works
- Human testosterone-binding globulin is a dimer composed of two identical protomers that are differentially glycosylated. (1989) (36)
- The microheterogeneity of androgen-binding protein in rat serum and epididymis is due to differences in glycosylation of their subunits. (1988) (23)
- Analysis of the oligosaccharides on androgen-binding proteins: Implications concerning their role in structure/function relationships (1991) (22)
- Monoclonal antibodies to rat androgen-binding protein recognize both of its subunits and cross-react with rabbit and human testosterone-binding globulin. (1988) (11)
- The apparent molecular weight of androgen-binding protein (ABP) in the blood of immature rats differs from that of ABP in the epididymis. (1987) (4)
- The microheterogeneity of rabbit testosterone-binding globulin is due to differential glycosylation of its single protomer. (1989) (4)
- Androgen‐Binding Protein in Rat Serum Is Glycosylated Differently than That in Epididymis a (1987) (2)
- Androgen‐Binding Protein (ABP) in the Blood of Immature Rats Differs in Apparent Molecular Weight from ABP in the Epididw (1987) (0)
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