The Machinery for Oxidative Protein Folding in Thermophiles (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• The Machinery for Oxidative Protein Folding in Thermophiles (Articolo in rivista) (literal)

Anno

• 2008-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1089/ars.2007.1855 (literal)

Alternative label

• Pedone E, Limauro D, Bartolucci S (2008)
  The Machinery for Oxidative Protein Folding in Thermophiles
  in Antioxidants & redox signalling
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Pedone E, Limauro D, Bartolucci S (literal)

Pagina inizio

• 157 (literal)

Pagina fine

• 170 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 10 (literal)

Rivista

• Antioxidants & redox signalling (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#descrizioneSinteticaDelProdotto

• pubblicazione scientifica (literal)

Note

• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• CNR, Ist Biostrutture & Bioimmagini, I-80134 Naples, Italy Univ Naples Federico 2, Dip Biol Strutturale & Funz, Naples, Italy (literal)

Titolo

• The Machinery for Oxidative Protein Folding in Thermophiles (literal)

Abstract

• Disulfide bonds are required for the stability and function of many proteins. A large number of thiol-disulfide oxidoreductases, belonging to the thioredoxin superfamily, catalyze protein disulfide bond formation in all living cells, from bacteria to humans. The protein disulfide isomerase (PDI) is the eukaryotic factor that catalyzes oxidative protein folding in the endoplasmic reticulum; by contrast, in prokaryotes, a family of disulfide bond (Dsb) proteins have an equivalent outcome in the bacterial periplasm. Recently the results from genome analysis suggested an important role for disulfide bonds in the structural stabilization of intracellular proteins from thermophiles. A specific protein disulfide oxidoreductase (PDO) has a key role in intracellular disulfide shuffling in thermophiles. Here we focus on the structural and functional characterization of PDO correlated with the multifunctional eukaryotic PDI. In addition, we highlight the chimeric nature of the machinery for oxidative protein folding in thermophiles in comparison with the mesophilic bacterial and eukaryal counterparts (literal)

Prodotto di

• Sistemi sintetici riconoscibili da target biologici (PM.P01.003.001) (Modulo)
• Institute of biostructure and bioimaging (IBB) (Istituto)

Autore CNR

• EMILIA MARIA PEDONE (Persona)

Incoming links:

Prodotto

• Institute of biostructure and bioimaging (IBB) (Istituto)
• Sistemi sintetici riconoscibili da target biologici (PM.P01.003.001) (Modulo)

Autore CNR di

• EMILIA MARIA PEDONE (Persona)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Antioxidants & redox signalling (Rivista)