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Walker T. McGraw

Researcher at Boston University

Publications -  8
Citations -  1085

Walker T. McGraw is an academic researcher from Boston University. The author has contributed to research in topics: Porphyromonas gingivalis & Gingipain. The author has an hindex of 8, co-authored 8 publications receiving 1047 citations. Previous affiliations of Walker T. McGraw include University of Natal & University of Georgia.

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Purification, Characterization, and Sequence Analysis of a Potential Virulence Factor from Porphyromonas gingivalis, Peptidylarginine Deiminase

TL;DR: It is proposed that PAD, acting in concert with arginine-specific proteinases from P. gingivalis, promotes the growth of the pathogen in the periodontal pocket, initially by enhancing its survivability and then by assisting the organism in its circumvention of host humoral defenses.
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Lysine- and arginine-specific proteinases from Porphyromonas gingivalis. Isolation, characterization, and evidence for the existence of complexes with hemagglutinins.

TL;DR: Two proteinases with arginine and lysine specificity were isolated from a high molecular mass fraction of the P. gingivalis culture fluid and Lys-gingipain was found to be a cysteine proteinase with optimal activity and stability at pH 8.0-8.5 and was extensively characterized in terms of its specificity and activation characteristics.
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Characterization of the binding activities of proteinase-adhesin complexes from Porphyromonas gingivalis

TL;DR: With specific proteinase inhibitors, it was shown that hemagglutination by either proteinase-adhesin complex could occur independently of proteinase activity, indicating that adherence to these proteins and not the hemagGLutination activity was a primary property of the adhesin activity component of complexes.
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Metalloendopeptidase EC 3.4.24.15 is necessary for Alzheimer's amyloid-beta peptide degradation.

TL;DR: It is shown here that conditioned medium of MP24.15 antisense-transfected SKNMC neuroblastoma has significantly higher levels of Aβ, and pharmacological modulation of either enzyme may provide a means of regulating Aβ in the brain.
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Heparin-dependent Modification of the Reactive Center Arginine of Antithrombin and Consequent Increase in Heparin Binding Affinity*

TL;DR: The results support the proposal that antithrombin circulates in a constrained conformation, which when released, in this study by perturbation of the bonding of P1 Arg to the body of the molecule, allows the reactive site loop to take up the active inhibitory conformation with exposure of the P1Arg.