http://www.cnr.it/ontology/cnr/individuo/prodotto/ID168135
Biomimetic chemistry on tandem protein/lipid damages under reductive radical stress (Articolo in rivista)
- Type
- Label
- Biomimetic chemistry on tandem protein/lipid damages under reductive radical stress (Articolo in rivista) (literal)
- Anno
- 2008-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.2533/chimia.2008.721 (literal)
- Alternative label
Scaloni, Andrea (5); Ferreri, Carla (5); Torreggiani, Armida (5); Salzano, Anna Maria (1); CHATGILIALOGLU, CHRYSSOSTOMOS (6); Capdevila, Mercè (4); Atrian, Silvia (3); Bobrowski, Krzysztof (2); Houée-Levin, Chantai (6) (2008)
Biomimetic chemistry on tandem protein/lipid damages under reductive radical stress
in CHIMIA International Journal for Chemistry
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Scaloni, Andrea (5); Ferreri, Carla (5); Torreggiani, Armida (5); Salzano, Anna Maria (1); CHATGILIALOGLU, CHRYSSOSTOMOS (6); Capdevila, Mercè (4); Atrian, Silvia (3); Bobrowski, Krzysztof (2); Houée-Levin, Chantai (6) (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- ISI Web of Science (WOS) (literal)
- Scopu (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- (1) Proteomics and Mass Spectrometry Laboratory - ISPAAM; (2) Institute of Nuclear Chemistry and Technology - ; (3) Departament de Genètica - Facultat de Biologia; (4) Departament de Química - Facultat de Ciències; (5) ISOF - Consiglio Nazionale Delle Ricerche; (6) Laboratoire de Chimie Physique - UMR 8000 (literal)
- Titolo
- Biomimetic chemistry on tandem protein/lipid damages under reductive radical stress (literal)
- Abstract
- The study of radical stress in the biological environment needs a comprehensive vision of all possible
reactive species and their mechanisms. Among them, reductive stress is evaluated for its selective target of sulfurcontaining
compounds. The selective attack of reducing species like Ho atoms or eaq
-/H+ to sulfur-containing amino
acid residues has been proved in different substrates, peptides and proteins. The transformations include methionine
to ?-aminobutyric acid and cysteine/cystine residues to alanine, as recognized in several sequences so far,
such as RNase A, lysozyme, Met-enkephalin, amyloid ?-peptide and metallothioneins. The amino acid desulfurization
is accompanied by the formation of low-molecular-weight sulfur-centered radicals that may cause geometrical
cis-trans isomerization of unsaturated fatty acid residues in lipid bilayer. Thus, tandem protein/lipid damage is
accomplished. Progress in research has given us a more comprehensive overview of the protein modifications and
their roles, and the chemical biology approach will make its vital contribution to the study of free radical reactions,
linking chemistry to biology and medicine. (literal)
- Prodotto di
- Autore CNR
- Insieme di parole chiave
Incoming links:
- Prodotto
- Autore CNR di
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
- Insieme di parole chiave di