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Biology and Biochemistry

D-Index
72
Citations
22039
World Ranking
6203
National Ranking
2917

Overview

David M. Neville is affiliated with the National Institutes of Health in the United States. Their professional activities are centered within this institution, which plays a significant role in public health research and biomedical sciences.

The records available do not list recent papers authored by David M. Neville, nor information on frequent co-authors or venues where publications have been consistently presented. Similarly, there is no detailed data on book publications or distinct fields and subfields of study documented for this researcher.

Without specific details on main fields or subfields of study, it is not possible to outline particular scientific domains or specialties associated with David M. Neville. Likewise, no specific research topics have been noted, so no further thematic summarization can be provided.

There are no recorded awards linked to David M. Neville, indicating either that this information is not publicly documented or that no awards have been conferred within the data timeframe.

This profile maintains an objective approach, presenting only the confirmed affiliations and the absence of additional detailed academic contributions or accolades for David M. Neville based on the current data.

Best Publications

  • Molecular Weight Determination of Protein-Dodecyl Sulfate Complexes by Gel Electrophoresis in a Discontinuous Buffer System

    David M. Neville

  • Insulin-Dependent Regulation of Insulin Receptor Concentrations: A Direct Demonstration in Cell Culture

    James R. Gavin;Jesse Roth;David M. Neville;Pierre De Meyts

  • Isolation of an organ specific protein antigen from cell-surface membrane rat liver

    David M. Neville

  • Insulin interactions with its receptors: experimental evidence for negative cooperativity.

    Pierre De Meyts;Jesse Roth;David M. Neville;James R. Gavin

  • Monoiodoinsulin: Demonstration of its biological activity and binding to fat cells and liver membranes

    Pierre Freychet;Jesse Roth;David M. Neville

  • Insulin Receptors in the Liver: Specific Binding of [ 125 I]insulin to the Plasma Membrane and Its Relation to Insulin Bioactivity

    Pierre Freychet;Jesse Roth;David M. Neville

  • Glycoproteins of Cell Surfaces A COMPARATIVE STUDY OF THREE DIFFERENT CELL SURFACES OF THE RAT

    Hartmut Glossmann;David M. Neville

  • Insulin-Receptor Interaction in the Obese-Hyperglycemic Mouse: A MODEL OF INSULIN RESISTANCE

    Kahn Cr;Neville Dm;Roth J

  • Insulin interactions with liver plasma membranes. Independence of binding of the hormone and its degradation.

    Pierre Freychet;Ronald Kahn;Jesse Roth;David M. Neville

  • Quantitative Aspects of the Insulin-Receptor Interaction in Liver Plasma Membranes

    C. Ronald Kahn;Pierre Freychet;Jesse Roth;David M. Neville

  • Insulin Receptor Deficiency in Genetic and Acquired Obesity

    Soli Ah;Kahn Cr;Neville Dm;Roth J

  • [9] Molecular weight determination of membrane protein and glycoprotein subunits by discontinuous gel electrophoresis in dodecyl sulfate

    David M. Neville;Hartmut Glossmann

  • Alterations in insulin binding induced by changes in vivo in the levels of glucocorticoids and growth hormone.

    C. Ronald Kahn;Ira D. Goldfine;David M. Neville;Pierre De Meyts

  • ACTINOMYCIN BINDING TO DNA: MECHANISM AND SPECIFICITY.

    Martin Gellert;Carl E. Smith;David Neville;Gary Felsenfeld

  • Stable mixed chimerism and tolerance using a nonmyeloablative preparative regimen in a large-animal model

    Christene A. Huang;Yasushi Fuchimoto;Rachel Scheier-Dolberg;Michael C. Murphy

  • Mixed chimerism and tolerance without whole body irradiation in a large animal model

    Yasushi Fuchimoto;Christene A. Huang;Kazuhiko Yamada;Akira Shimizu;Akira Shimizu

  • Anti-Thy 1.2 monoclonal antibody linked to ricin is a potent cell-type-specific toxin

    Richard J. Youle;David M. Neville

  • Receptors for Insulin, NSILA-s, and Growth Hormone: Applications to Disease States in Man

    Jesse Roth;C. Ronald Kahn;Maxine A. Lesniak;Phillip Gorden

  • FN18-CRM9 immunotoxin promotes tolerance in primate renal allografts.

    Stuart J. Knechtle;Daniel Vargo;John Fechner;Yuan Zhai

  • Ex-vivo treatment of donor bone marrow with anti-T-cell immunotoxins for prevention of graft-versus-host disease.

    A.H Filipovich;A.H Filipovich;R.J Youle;R.J Youle;D.M Neville;D.M Neville;D.A Vallera;D.A Vallera

Frequent Co-Authors

Jesse Roth
Jesse Roth National Institutes of Health
Richard J. Youle
Richard J. Youle National Institutes of Health
David H. Sachs
David H. Sachs Columbia University
Stuart J. Knechtle
Stuart J. Knechtle Duke University
C. Ronald Kahn
C. Ronald Kahn Harvard University
Hartmut Glossmann
Hartmut Glossmann Innsbruck Medical University
Daniel A. Vallera
Daniel A. Vallera University of Minnesota
John H. Kersey
John H. Kersey University of Minnesota
David K. C. Cooper
David K. C. Cooper University of Pittsburgh
Pierre De Meyts
Pierre De Meyts Novo Nordisk (Denmark)

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