Výsledky vyhledávání - "Limited proteolysi"

Lysines Acetylome and Methylome Profiling of H3 and H4 Histones in Trichostatin A-Treated Stem Cells

Autor: Flora Cozzolino, Ilaria Iacobucci, Maria Chiara Monti, Vittoria Monaco, Tiziana Angrisano

Publikováno v: International Journal of Molecular Sciences
Volume 22
Issue 4
International Journal of Molecular Sciences, Vol 22, Iss 2063, p 2063 (2021)

Trichostatin A ([R-(E,E)]-7-[4-(dimethylamino) phenyl]-N-hydroxy- 4,6-dimethyl- 7-oxo-2,4-heptadienamide, TSA) affects chromatin state through its potent histone deacetylase inhibitory activity. Interfering with the removal of acetyl groups from lysi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3059b51d9b9170c317b5211378889afc
https://pubmed.ncbi.nlm.nih.gov/33669725

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Description of the topographical changes associated to the different stages of the DsbA catalytic cycle

Autor: Eric Quéméneur, Floriana Vinci, Piero Pucci, Joël Couprie, Mireille Moutiez

Publikováno v: Protein Science
Protein Science, 2002, 11 (7), pp.1600-1612. ⟨10.1110/ps.4960102⟩

This paper provides a description of the surface topography of DsbA, the bacterial disulfide-bond forming enzyme, in the different phases of its catalytic cycle. Three representative states, that is, oxidized and reduced protein and a covalent comple

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df7b59f2aad844c3fea1a13436808b3c
https://doi.org/10.1110/ps.4960102

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Multiple disulfide bridges modulate conformational stability and flexibility in hyperthermophilic archaeal purine nucleoside phosphorylase

Autor: Giovanna Cacciapuoti, Elisa Martino, Georges Feller, Maria Libera Bagarolo, Marina Porcelli

5′-Deoxy-5′-methylthioadenosine phosphorylase from Sulfolobus solfataricus is a hexameric hyperthermophilic protein containing in each subunit two pairs of disulfide bridges, a CXC motif, and one free cysteine. The contribution of each disulfide

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ec3bdae52d17c7f14950dc685f81164
http://hdl.handle.net/11591/332345

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Assessment of the conformational features of vasoactive intestinal peptide in solution by limited proteolysis experiments

Autor: Alessandra Dicitore, Anna Marabotti, Angelo Facchiano, Pasquale Ferranti, Maria Cartenì, Paola Stiuso, Marilena Lepretti

Publikováno v: Biopolymers
81 (2006): 110–119. doi:10.1002/bip.20385
info:cnr-pdr/source/autori:Stiuso P., Marabotti A., Facchiano A., Lepretti M., Dicitore A., Ferranti P., Carteni M./titolo:Assessment of the conformational features of vasoactive intestinal peptide in solution by limited proteolysis experiments./doi:10.1002%2Fbip.20385/rivista:Biopolymers (Print)/anno:2006/pagina_da:110/pagina_a:119/intervallo_pagine:110–119/volume:81

The structural features of vasoactive intestinal peptide (VIP) and of its Gln16-diaminopropane derivative (VIP-DAP) in solution were investigated by limited proteolysis experiments with trypsin and thermolysin. The proteolysis of the native peptide b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f07f98a6bd990eed167ac369c94e39f1
http://hdl.handle.net/11591/190104

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Limited proteolysis in the investigation of beta2-microglobulin amyloidogenic and fibrillar states

Autor: Piero Pucci, Sofia Giorgetti, Maria Chiara Monti, Vittorio Bellotti, Angela Amoresano

Amyloid fibrils of patients treated with regular haemodialysis essentially consists of beta2-microglobulin (beta2-m) and its truncated species DeltaN6beta2-m lacking six residues at the amino terminus. The truncated fragment shows a higher propensity

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3832e1c0dae6ffdd34ab8ab081883faf
http://hdl.handle.net/11588/204414

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The regions of the sequence most exposed to the solvent within the amyloidogenic state of a protein initiate the aggregation process

Autor: Giulia Calloni, Fabrizio Chiti, Barbara Lelj Garolla di Bard, Piero Pucci, Gianpietro Ramponi, Maria Chiara Monti, Angela Amoresano

Publikováno v: Journal of molecular biology. 336(1)

Formation of misfolded aggregates is an essential part of what proteins can do. The process of protein aggregation is central to many human diseases and any aggregating event needs to be prevented within a cell and in protein design. In order to aggr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a73ab9c537f53ea3f80d920e614515ee
https://pubmed.ncbi.nlm.nih.gov/14741220

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Topological investigation of amyloid fibrils obtained from β2-microglobulin

Autor: Anne Clark, Vittorio Bellotti, Serena Principe, Gianpaolo Merlini, Maria Chiara Monti, Piero Pucci, Angela Amoresano, Sofia Giorgetti, Palma Mangione

Amyloid fibrils of patients treated with regular hemodialysis essentially consists of beta2-microglobulin (beta2-m) and its truncated species DeltaN6beta2-m lacking six residues at the amino terminus. The truncated fragment has a more flexible three-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::daf247a69585844e4fdce3048a208cba
https://europepmc.org/articles/PMC2373708/

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Conformational analysis of putative regulatory subunit D of the toluene/o-xylene-monooxygenase complex from Pseudomonas stutzeri OX1

Autor: Alberto Di Donato, Eugenio Notomista, Piero Pucci, Paola Barbieri, Roberta Scognamiglio, Fabrizio Dal Piaz, Anna Tramontano

A gene cluster isolated from Pseudomonas stutzeri OX1 genomic DNA and containing six ORFs codes for toluene/o-xylene-monooxygenase. The putative regulatory D subunit was expressed in Escherichia coli and purified. Its protein sequence was verified by

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64d02a4704fb2ed90fd42f94421bdc77
https://europepmc.org/articles/PMC2374142/

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Selective and asymmetric action of trypsin on the dimeric forms of seminal Rnase

Autor: F. Dal Piaz, Piero Pucci, C. De Lorenzo, Giuseppe D'Alessio, A. Di Maro, Renata Piccoli

Publikováno v: Scopus-Elsevier

Dimeric seminal RNase (BS-RNase) is an equilibrium mixture of conformationally different quaternary structures, one characterized by the interchange between subunits of their N-terminal ends (the MXM form); the other with no interchange (the M=M form

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77397d317da032ac9cc14f4fa6e0378d
http://hdl.handle.net/11588/155528

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