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William J. Rutter

Researcher at University of California, San Francisco

Publications -  329
Citations -  60039

William J. Rutter is an academic researcher from University of California, San Francisco. The author has contributed to research in topics: Gene & DNA. The author has an hindex of 108, co-authored 329 publications receiving 59560 citations. Previous affiliations of William J. Rutter include University of Washington & Eötvös Loránd University.

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Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease.

TL;DR: In this article, the rat pancreas RNA was used as a source for the purification of alpha-amylase messenger ribonucleic acid (RBA) using 2-mercaptoethanol.
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Number and evolutionary conservation of α- and β-tubulin and cytoplasmic β- and γ-actin genes using specific cloned cDNA probes

TL;DR: Bacterial clones containing inserted DNA sequences specific for α- Tubulin, β-tubulin,β-Actin and γ-actin have been constructed from mRNA of embryonic chick brain and are able to hybridize under stringent conditions to DNA of all vertebrates tested, as well as to sea urchin DNA, but not to yeast DNA.
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The human insulin receptor cDNA: The structural basis for hormone-activated transmembrane signalling

TL;DR: A cloned approximately 5 kb cDNA (human placenta) contains the coding sequences for the insulin receptor; the nucleotide sequence predicts a 1382 amino acid precursor and the overall structure is reminiscent of the EGF receptor.
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Rat Insulin Genes: Construction of Plasmids Containing the Coding Sequences

TL;DR: Recombinant bacterial plasmids have been constructed that contain complementary DNA prepared from rat islets of Langerhans messenger RNA that contain cloned sequences representing the complete coding region of rat proinsulin I, part of the preproinsulin II prepeptide, and the untranslated 3' terminal region of the mRNA.
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Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose

TL;DR: It is shown that replacement of one or both of the twin tyrosines (residues 1162 and 1163) with phenylalanine results in a dramatic reduction in or loss of insulin-activated autophosphorylation and kinase activity in vitro.