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Metallo-ß-lactamases: structural features, antibiotic recognition, inhibition, and inhibitor design.
Wang, Jing-Fang; Chou, Kuo-Chen.
Afiliación
  • Wang JF; Key Laboratory of Systems Biomedicine (Ministry of Education), Shanghai Center for Systems Biomedicine, Shanghai Jiao Tong University, Shanghai 200240, China. jfwang@gordonlifescience.org
Curr Top Med Chem ; 13(10): 1242-53, 2013.
Article en En | MEDLINE | ID: mdl-23647546
Owing to their ability in destroying or slowing down the growth of bacteria, antibiotics have been widely used to treat the bacterial infections. However, because of the long-term and irresponsible use of antibiotics, resistance to antibiotics has become a serious problem directly threatening the public health worldwide. To fight against and resist ß- lactam antibiotics, bacteria usually employed ß-lactamases, especially the metallo-ß-lactamases, to hydrolyze the C-N bond of the ß-lactam ring so as to inactivate the antibiotics. In this minireview, we are to summarize the structural features of the metallo-ß-lactamases, as well as their antibiotic binding modes and resistance mechanisms, in hopes that the discussion and analysis presented in this paper can stimulate new strategies to overcome the resistance problem and find novel inhibitors against the metallo-ß-lactamases.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Beta-Lactamasas / Diseño de Fármacos / Inhibidores Enzimáticos / Inhibidores de beta-Lactamasas / Antibacterianos Límite: Animals / Humans Idioma: En Revista: Curr Top Med Chem Asunto de la revista: QUIMICA Año: 2013 Tipo del documento: Article País de afiliación: China
Buscar en Google
Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Beta-Lactamasas / Diseño de Fármacos / Inhibidores Enzimáticos / Inhibidores de beta-Lactamasas / Antibacterianos Límite: Animals / Humans Idioma: En Revista: Curr Top Med Chem Asunto de la revista: QUIMICA Año: 2013 Tipo del documento: Article País de afiliación: China
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