Matthew Avitable
SUNY Downstate Medical Center
12 Papers
111 Citations
Matthew Avitable is an academic researcher from SUNY Downstate Medical Center. The author has contributed to research in topics: Conformational change & Amino acid. The author has an hindex of 6, co-authored 12 publications.
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Papers
Matrix vesicle enzymes in human osteoarthritis
Thomas A. Einhorn,Stanley L. Gordon,Scott A. Siegel,Charles F. Hummel,Matthew Avitable,Robert P. Carty +5 more
TL;DR: The results suggest that OA, growth plate, and even normal articular cartilage all have the potential to undergo calcification as long as both phosphate and pyrophosphate ions can be generated at sufficiently high levels.
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Conformation of the metastasis-inhibiting laminin pentapeptide.
Paul W. Brandt-Rauf,Matthew R. Pincus,Robert P. Carty,Jack Lubowsky,Matthew Avitable,John A. Carucci,Randall B. Murphy +6 more
TL;DR: Con conformational energy analysis has been used to determine the three-dimensional structures of Tyr-Ile-Gly-Ser-Arg peptides, and results indicate that the substitution of Glu for the terminal Arg produces a significant conformational change in the peptide backbone at the middle Gly residue.
14
Structural effects of amino acid substitutions on the P21 proteins: Evidence for a malignant conformation
TL;DR: Substitution for Gly 12 of other amino acids that have widely disparate helix-nucleating potentials and completely different side chains all produce this identical lowest energy conformation and suggests the existence of a “malignancy-causing” conformation for the P21 proteins.
13
The relationship between the sick role and functional ability: one center's experience.
TL;DR: Results suggest that individuals who have the strongest coping skills and the least resentment toward their illness seem best able to gain strength and reject the sick role as a permanent identity.
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Correlation of structure with transforming activity of the P21 proteins with substitutions of L-amino acids for Gly at position 13
TL;DR: From analysis of the interactions preventing the Asp 13-containing peptide from adopting the “normal” conformation, it is predicted that substitutions of amino acids with branched side chains atCβ, such as Val, Ile, and Thr, should promote cell transformation.
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