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: PROTEÍNAS; FÍSICA DA MATÉRIA CONDENSADA
- Language: Inglês
- Imprenta:
- Publisher place: Copenhagen
- Date published: 1996
- Source:
- Título do periódico: Acta Crystallographica a
- Volume/Número/Paginação/Ano: v.52, p.res.ps04.01.13, 1996
- Conference titles: Congress and General Assembly of the International Union of Crystallography
-
ABNT
OLIVA, Glaucius; SOUZA, D H F; ARAÚJO, Ana Paula Ulian de; JESUS, W D P. Crystal structure of t. Cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenase: implications for the catalytic mechanism and new potential target sites for selective inhibition. Acta Crystallographica a[S.l: s.n.], 1996. -
APA
Oliva, G., Souza, D. H. F., Araújo, A. P. U. de, & Jesus, W. D. P. (1996). Crystal structure of t. Cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenase: implications for the catalytic mechanism and new potential target sites for selective inhibition. Acta Crystallographica a. Copenhagen. -
NLM
Oliva G, Souza DHF, Araújo APU de, Jesus WDP. Crystal structure of t. Cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenase: implications for the catalytic mechanism and new potential target sites for selective inhibition. Acta Crystallographica a. 1996 ;52 res.ps04.01.13. -
Vancouver
Oliva G, Souza DHF, Araújo APU de, Jesus WDP. Crystal structure of t. Cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenase: implications for the catalytic mechanism and new potential target sites for selective inhibition. Acta Crystallographica a. 1996 ;52 res.ps04.01.13. - Analise cristalografica da anidrase carbonica bovina nativa
- 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
- 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
- The refined crystal structure of carbonic anhydrase from bovine erythrocytes at 2.5 'ANGSTRON' resolution
- 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
- Cristalizacao e investigacao preliminar por raios-x da anidrase carbonica bovina nativa
- Structure of carbonic anhydrase from bovine erythrocytes at 2.5 'ANGSTRON' resolution
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