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Stefano Bettati

Researcher at University of Parma

Publications -  133
Citations -  3353

Stefano Bettati is an academic researcher from University of Parma. The author has contributed to research in topics: Oxygen binding & Allosteric regulation. The author has an hindex of 30, co-authored 126 publications receiving 2948 citations. Previous affiliations of Stefano Bettati include National Institutes of Health & National Research Council.

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Pyridoxal 5-Phosphate Enzymes as Targets for Therapeutic Agents

TL;DR: The relevance of recent genomic analysis of PLP-dependent enzymes for the selection of drug targets is discussed, and enzymes that have been recently characterized and proposed as drug targets are reported.
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A tertiary two-state allosteric model for hemoglobin.

TL;DR: The model is consistent with the results of solution, gel, and single crystal oxygen binding studies, but underestimates the population of doubly-liganded molecules determined in low-temperature electrophoresis experiments.
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T State Hemoglobin Binds Oxygen Noncooperatively with Allosteric Effects of Protons, Inositol Hexaphosphate, and Chloride

TL;DR: In this article, the T state of hemoglobin in silica gels was determined to have a reduced affinity compared with solution, with no Bohr effect and with no influence of other allosteric effectors.
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Evolution of allosteric models for hemoglobin

TL;DR: Comparing various allosteric models to explain cooperative oxygen binding to hemoglobin shows the preponderance of experimental evidence favors the TTS model which postulates an equilibrium between high (r)‐ and low (t)‐affinity tertiary conformations that are present in both the T and R quaternary structures.
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New insights into allosteric mechanisms from trapping unstable protein conformations in silica gels

TL;DR: In this paper, the authors investigated the kinetic properties of unstable conformations transiently trapped by encapsulation in silica gels and found that after nanosecond photodissociation of carbon monoxide, a large fraction of the subunits of the T quaternary structure had kinetic properties almost identical to those of sub units of the R quaternaries.