Massimo Coletta
Overview
Explore the profile of Massimo Coletta including associated specialties, affiliations and a list of published articles.
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148
Citations
1541
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Recent Articles
1.
Ascenzi P, De Simone G, Zingale G, Coletta M
J Inorg Biochem
. 2025 Jan;
265:112829.
PMID: 39854981
Nitrite (NO) interacts with myoglobin (Mb) and hemoglobin (Hb) behaving as a ligand of both the ferrous (i.e., Mb(II) and Hb(II)) and ferric (i.e., Mb(III) and Hb(III)) forms. However, while...
2.
Tundo G, Cavaterra D, Pandino I, Zingale G, Giammaria S, Boccaccini A, et al.
Int J Mol Sci
. 2024 Sep;
25(18).
PMID: 39337505
Glaucoma is chronic optic neuropathy whose pathogenesis has been associated with the altered metabolism of Trabecular Meshwork Cells, which is a cell type involved in the synthesis and remodeling of...
3.
Messias A, Capece L, De Simone G, Coletta M, Ascenzi P, Estrin D
Inorg Chem
. 2024 May;
63(21):9907-9918.
PMID: 38754069
Nitrobindins (Nbs) are all-β-barrel heme proteins present along the evolutionary ladder. They display a highly solvent-exposed ferric heme group with the iron atom being coordinated by the proximal His residue...
4.
Coletta M, Bolognesi M, Ascenzi P
J Inorg Biochem
. 2023 Nov;
250:112423.
PMID: 37953207
No abstract available.
5.
Pandino I, Giammaria S, Zingale G, Roberti G, Michelessi M, Coletta M, et al.
Mol Aspects Med
. 2023 Nov;
94:101226.
PMID: 37950974
Glaucoma represents a group of progressive neurodegenerative diseases characterized by the loss of retinal ganglion cells (RGCs) and their axons with subsequent visual field impairment. The disease develops through largely...
6.
De Simone G, Di Masi A, Pasquadibisceglie A, Coletta A, Sebastiani F, Smulevich G, et al.
J Inorg Biochem
. 2023 Nov;
250:112387.
PMID: 37914583
Most hemoproteins display an all-α-helical fold, showing the classical three on three (3/3) globin structural arrangement characterized by seven or eight α-helical segments that form a sandwich around the heme....
7.
Messias A, Pasquadibisceglie A, Alonso de Armino D, De Simone G, Polticelli F, Coletta M, et al.
J Inorg Biochem
. 2023 Aug;
248:112336.
PMID: 37572543
Nitrobindins (Nbs) represent an evolutionary conserved all-β-barrel heme-proteins displaying a highly solvent-exposed heme-Fe(III) atom, coordinated by a proximal His residue. Interestingly, even if the distal side is exposed to the...
8.
De Simone G, Monaca S, Fattibene P, Bocedi A, Coletta M, Ascenzi P
J Inorg Biochem
. 2023 Aug;
247:112338.
PMID: 37549473
NO binding to horse heart cytochrome c (hhcyt c) has been investigated as a function of pH by both optical absorption and EPR spectroscopies. Lowering pH from 3.5 to 1.5...
9.
De Simone G, Di Masi A, Tundo G, Coletta M, Ascenzi P
Int J Mol Sci
. 2023 Apr;
24(7).
PMID: 37047528
Nitrobindins (Nbs) are all-β-barrel heme proteins spanning from bacteria to . They inactivate reactive nitrogen species by sequestering NO, converting NO to HNO, and promoting peroxynitrite isomerization to NO. Here,...
10.
Tundo G, Cascio P, Milardi D, Santoro A, Graziani G, Lacal P, et al.
Pharmacol Ther
. 2022 Dec;
241:108329.
PMID: 36526014
The immunoproteasome is a specialized form of proteasome equipped with modified catalytic subunits that was initially discovered to play a pivotal role in MHC class I antigen processing and immune...