Crystal structure of t. Cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenase: implications for the catalytic mechanism and new potential target sites for selective inhibition (1996)
- Authors:
- USP affiliated authors: JESUS, WANDA DRAGHETTA PERUSSI DE - IFSC ; OLIVA, GLAUCIUS - IFSC ; ARAUJO, ANA PAULA ULIAN DE - IFSC
- Unidade: IFSC
- Subjects: COMPOSTOS ORGANOMETÁLICOS (QUÍMICA INORGÂNICA); BIOFÍSICA; PROTEÍNAS
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Resumos
- Conference titles: Reuniao Anual da Sociedade Brasileira de Bioquimica e Biologia Molecular
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ABNT
SOUZA, D H F et al. Crystal structure of t. Cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenase: implications for the catalytic mechanism and new potential target sites for selective inhibition. 1996, Anais.. São Paulo: Sbbq, 1996. . Acesso em: 28 mar. 2024. -
APA
Souza, D. H. F., Araújo, A. P. U. de, Jesus, W. D. P., & Oliva, G. (1996). Crystal structure of t. Cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenase: implications for the catalytic mechanism and new potential target sites for selective inhibition. In Resumos. São Paulo: Sbbq. -
NLM
Souza DHF, Araújo APU de, Jesus WDP, Oliva G. Crystal structure of t. Cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenase: implications for the catalytic mechanism and new potential target sites for selective inhibition. Resumos. 1996 ;[citado 2024 mar. 28 ] -
Vancouver
Souza DHF, Araújo APU de, Jesus WDP, Oliva G. Crystal structure of t. Cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenase: implications for the catalytic mechanism and new potential target sites for selective inhibition. Resumos. 1996 ;[citado 2024 mar. 28 ] - Structure of carbonic anhydrase from bovine erytrocytes at 2.5 'ANGSTRON' resolution
- Structure of carbonic anhydrase from bovine erythrocytes at 2.5 'ANGSTRON' resolution
- Determinacao estrutural da anidrase carbonica bovina
- Molecular replacement at its limits? the structure determination of t. Cruzi g- glyceraldehyde -3-phosphate dehydrogenase, 12 monomers in the asymmetric unit and 41% data completeness at 3.5'ANGSTRON' resolution
- Analise cristalografica da anidrase carbonica bovina nativa
- Expression in E. coli, purification and crystallization of the Trypanosoma cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenase
- Crystallization and preliminary crystallographic studies of bovine carbonic anhydrase
- Molecular replacement at its limits? the structure determination of t. Cruzi g-glyceraldehyde-3-phosphate dehydrogenase, 12 monomers in the asymmetric unit and 41% data completeness at 3.5'ANGSTRON' resolution
- The refined crystal structure of carbonic anhydrase from bovine erythrocytes at 2.5 'ANGSTRON' resolution
- Expression in e. Coli, purification and crystallization of the Trypanosoma cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenase
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