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Massimo Coletta

Researcher at University of Rome Tor Vergata

Publications -  254
Citations -  5803

Massimo Coletta is an academic researcher from University of Rome Tor Vergata. The author has contributed to research in topics: Heme & Ferrous. The author has an hindex of 38, co-authored 246 publications receiving 5160 citations. Previous affiliations of Massimo Coletta include University of Salerno & University of Camerino.

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Human matrix metalloproteinases: an ubiquitarian class of enzymes involved in several pathological processes.

TL;DR: An extensive review of the different MMPs structural and functional features is integrated with their pathological role in several types of diseases, spanning from cancer to cardiovascular diseases and to neurodegeneration.
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The Bovine Basic Pancreatic Trypsin Inhibitor (Kunitz Inhibitor): A Milestone Protein

TL;DR: The structural, inhibition, and bio-medical aspects of BPTI are reported, which include inhibition of nitric oxide synthase type-I and -II action and impairs K+ transport by Ca2+-activated K+ channels.
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Insights into cytochrome c-cardiolipin interaction. Role played by ionic strength.

TL;DR: This paper found that formation of the cytochrome c-cardiolipin complex occurs via two distinct transitions, implying a high-affinity site and a low-Affinity site in the complex, and ascribes it to the high activation barrier met by the protein when restoring the native Fe(III)-M80 axial bond.
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Aβ(31–35) and Aβ(25–35) fragments of amyloid beta-protein induce cellular death through apoptotic signals: Role of the redox state of methionine-35

TL;DR: Taken together, this result indicate that Aβ(31–35) and A β(25– 35) peptides in non‐aggregated form, i.e., predominantly monomeric, are strongly neurotoxic, having the ability to enter within the cells, determining mitochondrial damage with an evident trigger of apoptotic signals.
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Extended cardiolipin anchorage to cytochrome c : a model for protein–mitochondrial membrane binding

TL;DR: A spectroscopic and kinetic study of the wild type and the Asn52Ile mutant of iso-1-cytochrome c from yeast is undertaken to investigate the interaction of cy tochrome c with CL vesicles, considered here a model for the CL-containing mitochondrial membrane.