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Charles R. Manclark

Researcher at Food and Drug Administration

Publications -  54
Citations -  3601

Charles R. Manclark is an academic researcher from Food and Drug Administration. The author has contributed to research in topics: Bordetella pertussis & Pertussis toxin. The author has an hindex of 30, co-authored 54 publications receiving 3570 citations. Previous affiliations of Charles R. Manclark include United States Department of the Army & North Carolina State University.

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Nature and Rates of Adverse Reactions Associated with DTP and DT Immunizations in Infants and Children

TL;DR: In 784 DT and 15,752 DTP immunizations given to children 0 to 6 years of age who were prospectively studied for reactions occurring within 48 hours following immunization, minor reactions were significantly more frequent following DTP vaccine.
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Stimulation and inhibition of adenylyl cyclases mediated by distinct regulatory proteins

TL;DR: It is shown here that Cyc− S49 cells contain a substrate for ADP-ribosylation by pertussis toxin and that the toxin alters GTP dependent inhibition of cyc− adenyl cyclase activity, and it is concluded that Ni is a distinct and separate regulatory component of adenylyl cyclase.
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Pertussis toxin. Affinity purification of a new ADP-ribosyltransferase.

TL;DR: A rapid purification procedure has been developed for the preparation of pertussis toxin in high yields andStructural, amino acid, and immunologic analyses indicate that toxin prepared from strain 165 is indistinguishable from toxins prepared from other strains.
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Pertussis toxin substrate, the putative Ni component of adenylyl cyclases, is an alpha beta heterodimer regulated by guanine nucleotide and magnesium

TL;DR: This work believes that it has purified a guanine nucleotide- and Mg2+-binding inhibitory regulatory component of adenylyl cyclases--i.e., the Ni.
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Ns and Ni, the stimulatory and inhibitory regulatory components of adenylyl cyclases. Purification of the human erythrocyte proteins without the use of activating regulatory ligands.

TL;DR: Methods were developed to adequately extract, separate and, without the use of NaF as stabilizing agent, purify to better than 90% purity human erythrocyte Ns and Ni, the stimulatory and inhibitory guanine nucleotide- and Mg-binding regulatory components of adenylyl cyclases, as well as a protein containing Mr = 35,000 subunits.