Literature DB >> 17150588

Three-dimensional structure of S-adenosyl-L-homocysteine hydrolase from Plasmodium falciparum.

Nobutada Tanaka1, Masayuki Nakanishi, Yoshio Kusakabe, Katsura Shiraiwa, Saori Yabe, Yasutomo Ito, Yukio Kitade, Kazuo T Nakamura.   

Abstract

Structural information of Plasmodium falciparum S-adenosyl-L-homocysteine hydrolase (PfSAHH) has been expected to provide new-type chemotherapeutic agents against malaria. Here we report the crystal structure of PfSAHH. The present structure should provide opportunities to design potent and selective PfSAHH inhibitors.

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Year:  2004        PMID: 17150588     DOI: 10.1093/nass/48.1.281

Source DB:  PubMed          Journal:  Nucleic Acids Symp Ser (Oxf)        ISSN: 0261-3166


  2 in total

1.  Efficacy of S-adenosylhomocysteine hydrolase inhibitors, D-eritadenine and (S)-DHPA, against the growth of Cryptosporidium parvum in vitro.

Authors:  Vlasta Ctrnáctá; Jason M Fritzler; Mária Surinová; Ivan Hrdý; Guan Zhu; Frantisek Stejskal
Journal:  Exp Parasitol       Date:  2010-04-20       Impact factor: 2.011

2.  Structural insight into binding mode of inhibitor with SAHH of Plasmodium and human: interaction of curcumin with anti-malarial drug targets.

Authors:  Dev Bukhsh Singh; Seema Dwivedi
Journal:  J Chem Biol       Date:  2016-08-15
  2 in total

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