Molecular Basis of Antimony Treatment in Leishmaniasis (Articolo in rivista)

Type

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

Label

• Molecular Basis of Antimony Treatment in Leishmaniasis (Articolo in rivista) (literal)

Anno

• 2009-01-01T00:00:00+01:00 (literal)

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

• 10.1021/jm900185q (literal)

Alternative label

• Baiocco P; Colotti G; Franceschini S; Ilari A. (2009)
  Molecular Basis of Antimony Treatment in Leishmaniasis
  in Journal of medicinal chemistry; ACS, American chemical society, Washington, DC (Stati Uniti d'America)
  (literal)

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

• Baiocco P; Colotti G; Franceschini S; Ilari A. (literal)

Pagina inizio

• 2603 (literal)

Pagina fine

• 2612 (literal)

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

• 52 (literal)

Rivista

• Journal of medicinal chemistry (Rivista)

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

• 8 (literal)

Note

• ISI Web of Science (WOS) (literal)

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

• 1. Ist Biol & Patol Mol, CNR, I-00185 Rome, Italy 2. Sapienza Univ Roma, Dept Biochem Sci, I-00185 Rome, Italy (literal)

Titolo

• Molecular Basis of Antimony Treatment in Leishmaniasis (literal)

Abstract

• Leishmaniasis is a disease that affects 2 million people and kills 70000 persons every year. It is caused by Leishmania species, which are human protozoan parasites of the trypanosomatidae family. Trypanosomatidae differ from the other eukaryotes in their specific redox metabolism because the glutathione/glutathione reductase system is replaced by the unique trypanothione/trypanothione reductase system. The current treatment of leishmaniasis relies mainly on antimonial drugs. The crystal structures of oxidized trypanothione reductase (TR) from Leishmania infantum and of the complex of reduced TR with NADPH and Sb(III), reported in this paper, disclose for the first time the molecular mechanism of action of antimonial drugs against the parasite. Sb(III), which is coordinated by the two redox-active catalytic cysteine residues (Cys52 and Cys57), one threonine residue (Thr335), and His461' of the 2-fold symmetry related subunit in the dimer, strongly inhibits TR activity. Because TR is essential for the parasite survival and virulence and it is absent in mammalian cells, these findings provide insights toward the design of new more affordable and less toxic drugs against Leishmaniasis. (literal)

Editore

• ACS, American chemical society (Editore)

Prodotto di

• Biologia strutturale e bioinformatica: struttura-funzione, dinamica e riconoscimento in proteine (SV.P14.008.001) (Modulo)
• Institute of molecular biology and pathology (IBPM) (Istituto)

Autore CNR

• GIANNI COLOTTI (Unità di personale interno)
• ANDREA ILARI (Unità di personale interno)

Insieme di parole chiave

• Parole chiave di "Molecular Basis of Antimony Treatment in Leishmaniasis" (Insieme di parole chiave)

Incoming links:

Prodotto

• Institute of molecular biology and pathology (IBPM) (Istituto)
• Biologia strutturale e bioinformatica: struttura-funzione, dinamica e riconoscimento in proteine (SV.P14.008.001) (Modulo)

Autore CNR di

• GIANNI COLOTTI (Unità di personale interno)
• ANDREA ILARI (Unità di personale interno)

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

• Journal of medicinal chemistry (Rivista)

Editore di

• ACS, American chemical society (Editore)

Insieme di parole chiave di

• Parole chiave di "Molecular Basis of Antimony Treatment in Leishmaniasis" (Insieme di parole chiave)