Jack Lubowsky
SUNY Downstate Medical Center
14 Papers
174 Citations
Jack Lubowsky 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 8, co-authored 14 publications.
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Papers
Bilateral skin conductance, finger pulse volume, and EEG orienting response to tones of differing intensities in chronic schizophrenics and controls.
Alvin S. Bernstein,Kenneth W. Taylor,Paul Starkey,Samuel Juni,Jack Lubowsky,Herbert M. Paley +5 more
TL;DR: Skin conductance, finger pulse volume, and EEG orienting responses were examined to repeated tones of either 60− or 90-dB intensity in chronic schizophrenics, nonschizophrenic psychiatric patients, and normals and showed no drug-associated effect on any OR variable under study.
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A Limiting Factor in the “Normalization” of Schizophrenic Orienting Response Dysfunction
TL;DR: Schizophrenic subjects showed greater consistency of OR nonresponsiveness in SCR and FPV, and nonsignificantly greater consistency in criterion alpha block, pointing to a deficit in orienting response (OR) rather than in peripheral response.
•Journal Article
Sexual Instrumentation
John L. Semmlos,Jack Lubowsky +1 more
TL;DR: The application of engineering tools to life science problems has both generated the incentive and provided the means for quantitative measurement of physiological variables, and this trend is clearly demonstrated in the development of instrumentation to quantify human sexual response.
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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.
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