D
David M. Neville
Researcher at Laboratory of Molecular Biology
Publications - 152
Citations - 14951
David M. Neville is an academic researcher from Laboratory of Molecular Biology. The author has contributed to research in topics: Immunotoxin & Transplantation. The author has an hindex of 58, co-authored 152 publications receiving 14745 citations. Previous affiliations of David M. Neville include Scott & White Hospital & University of Wisconsin-Madison.
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Molecular Weight Determination of Protein-Dodecyl Sulfate Complexes by Gel Electrophoresis in a Discontinuous Buffer System
TL;DR: The retardation coefficient is shown both empirically and theoretically to be a uniform function of molecular weight of protein-SDS complexes over specified ranges, providing a rationale for determining molecular weight from plots of the negative logarithm of relative mobility against molecular weight.
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Insulin-Dependent Regulation of Insulin Receptor Concentrations: A Direct Demonstration in Cell Culture
TL;DR: The data suggest a reciprocal relationship between insulin in the extracellular fluid and the concentration of insulin receptors per cell, which is mediated at the target cell itself by intracellular insulin-sensitive regulatory processes and directly affects target-cell sensitivity to hormone.
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Isolation of an organ specific protein antigen from cell-surface membrane rat liver
TL;DR: The liver membrane protein could not be detected in extracts of Morris hepatoma but was found to be present in a highly differentiated second generation hepatoma induced by diacetyl amino fluorene.
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Insulin interactions with its receptors: experimental evidence for negative cooperativity.
TL;DR: A simple method is reported to detect cooperative interactions in the binding of polypeptide hormones to their membrane receptors, and Insulin receptors on cultured lymphocytes and liver plasma membranes show negative cooperative interactions.
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Monoiodoinsulin: Demonstration of its biological activity and binding to fat cells and liver membranes
TL;DR: 125I-insulin binding to liver membranes was inhibited by unlabeled insulin at physiological concentrations, and monoiodoinsulin prepared by this method was bound to isolated fat cells and to purified plasma membranes from liver.