Insulin degrading enzyme activates the 20S proteasome and competes with canonical regulatory particles

Autor: Sbardella, D, Tundo, Gr, Marcoux, J, Coletta, A, Di Pierro, D, Grasso, Giuseppe, Santoro, Am, Ciaccio, C, Marini, S, Bousquet Dubouch, M. P., Van Endert, P, Coletta, M.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______4731::25b3bc5d09b2c6df9511063663c02dd6
http://hdl.handle.net/20.500.11769/109279

Insulin-degrading Enzyme (IDE): A NOVEL HEAT SHOCK-LIKE PROTEIN*

Autor: Tundo, Gr, Sbardella, D, Ciaccio, C, Bianculli, A, Orlandi, A, Desimio, Mg, Arcuri, G, Coletta, M, Marini, S

Insulin-degrading enzyme (IDE) is a highly conserved zinc metallopeptidase that is ubiquitously distributed in human tissues, and particularly abundant in the brain, liver, and muscles. IDE activity has been historically associated with insulin and �

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::12ff0be6056e0679ca345d8f98f58e4c
https://europepmc.org/articles/PMC3554900/

Enzyme catalysis: the case of the prostate-specific antigen

Autor: Paola Cozza, Stefano Marini, Luigi Tomao, Alessandra di Masi, Magda Gioia, Grazia R. Tundo, Chiara Ciaccio, Massimo Coletta, Diego Sbardella, Paolo Ascenzi, Giovanni Francesco Fasciglione

Publikováno v: Rendiconti Lincei. 28:229-237

Proteases are a class of enzymes that lower the activation energy for the cleavage of the peptide bonds by polarizing the carbonyl group. The catalytic mechanism of proteases is characterized by the formation and the dissociation of a tetrahedral acy

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8a1a0ce9b71bf6f9f4de8a7c80a7b04
https://doi.org/10.1007/s12210-017-0602-6

Functional and structural roles of the N-terminal extension in Methanosarcina acetivorans protoglobin

Autor: Massimo Coletta, Martino Bolognesi, Grazia R. Tundo, Alessandra Pesce, Luc Moens, Sylvia Dewilde, Paolo Ascenzi, L. Tilleman, Marco Nardini, Laura Bertolacci, Chiara Ciaccio

Publikováno v: Biochimica et biophysica acta. Proteins and proteomics 1834 (2013): 1813–1823. doi:10.1016/j.bbapap.2013.02.026
info:cnr-pdr/source/autori:Ciaccio C, Pesce A, Tundo GR, Tilleman L, Bertolacci L, Dewilde S, Moens L, Ascenzi P, Bolognesi M, Nardini M, Coletta M/titolo:Functional and structural roles of the N-terminal extension in Methanosarcina acetivorans protoglobin/doi:10.1016%2Fj.bbapap.2013.02.026/rivista:Biochimica et biophysica acta. Proteins and proteomics/anno:2013/pagina_da:1813/pagina_a:1823/intervallo_pagine:1813–1823/volume:1834
Biochimica et biophysica acta : proteins and proteomics

Functional and structural properties of protoglobin from Methanosarcina acetivorans, whose Cys(101)E20 residue was mutated to Ser (MaPgb*), and of mutants missing either the first 20 N-terminal amino acids (MaPgb*-Delta N20 mutant), or the first 33 N

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::027310c82de596128154ffebbcf90357
https://doi.org/10.1016/j.bbapap.2013.02.026

Warfarin modulates the nitrite reductase activity of ferrous human serum heme-albumin

Autor: Grazia R. Tundo, Gabriella Fanali, Mauro Fasano, Massimo Coletta, Paolo Ascenzi

Human serum heme–albumin (HSA–heme–Fe) displays reactivity and spectroscopic properties similar to those of heme proteins. Here, the nitrite reductase activity of ferrous HSA–heme–Fe [HSA–heme–Fe(II)] is reported. The value of the secon

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a9d62fb325606b7d8ce92f2a67259b0
https://hdl.handle.net/11590/135047