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1
Crystal structure of fumarate hydratase from Leishmania major
Crystal structure of fumarate hydratase from Leishmania major
Material Type:
Artigo de Congresso 		Adicionar ao Meu Espaço

Crystal structure of fumarate hydratase from Leishmania major

P. R. Feliciano C. L Drennan; Maria Cristina Nonato; Gordon Research Conference on Diffraction Methods in Structural Biology (2012 Lewiston)

Abstracts Lewiston, 2012

Lewiston 2012

Localização: FCFRP - Fac. Ciên. Farm. Ribeirão Preto    (pcd 2301014 Estantes Deslizantes ) e outros locais(Acessar)

2
Molecular cloning, expression and purification of cabohydrate recognition domains (CRDs) from human galectin-4
Molecular cloning, expression and purification of cabohydrate recognition domains (CRDs) from human galectin-4
Material Type:
Artigo de Congresso 		Adicionar ao Meu Espaço

Molecular cloning, expression and purification of cabohydrate recognition domains (CRDs) from human galectin-4

A. L. R. L. Zimbardi Maria Cristina Nonato; Annual Metting of SBBq (37. 2008 Águas de Lindóia); Congress of the Pan-American Association for Biochemistry and Molecular Biology (PABMB) (11. 2008 Águas de Lindóia)

Abstracts São Paulo : SBBq, 2008

São Paulo SBBq 2008

Localização: FCFRP - Fac. Ciên. Farm. Ribeirão Preto    (pcd 1678638 ) e outros locais(Acessar)

3
Preliminary biochemical characterization of dihydroorotate dehydrogenase from Xylella fastidiosa strain 9A5C
Preliminary biochemical characterization of dihydroorotate dehydrogenase from Xylella fastidiosa strain 9A5C
Material Type:
Artigo de Congresso 		Adicionar ao Meu Espaço

Preliminary biochemical characterization of dihydroorotate dehydrogenase from Xylella fastidiosa strain 9A5C

A. L. Souza Maria Cristina Nonato; Annual Metting of SBBq (37. 2008 Águas de Lindóia); Congress of the Pan-American Association for Biochemistry and Molecular Biology (PABMB) (11. 2008 Águas de Lindóia)

Abstracts São Paulo : SBBq, 2008

São Paulo SBBq 2008

Localização: FCFRP - Fac. Ciên. Farm. Ribeirão Preto    (pcd 1678818 ) e outros locais(Acessar)

4
Structure of APO T.cruzi glyceraldehyde-3-phosphate dehydrogenase implications for drug design
Structure of APO T.cruzi glyceraldehyde-3-phosphate dehydrogenase implications for drug design
Material Type:
Artigo de Congresso 		Adicionar ao Meu Espaço

Structure of APO T.cruzi glyceraldehyde-3-phosphate dehydrogenase implications for drug design

Glaucius Oliva B. G Guimaraes; Luis Fernando Delboni; Maria Cristina Nonato; Mônica Tallarico Pupo; Fernando Pavao; Jair Mafezolli; P. C Vieira; Congress and General Assembly of the International Union of Crystallography (18. 1999 Glasgow)

Abstracts Glasgow, 1999

Glasgow 1999

Item não circula. Consulte sua biblioteca.(Acessar)

5
Biomolecular interactions from the perspective of the electron spin
Biomolecular interactions from the perspective of the electron spin
Material Type:
Artigo de Congresso 		Adicionar ao Meu Espaço

Biomolecular interactions from the perspective of the electron spin

Fabio Dyszy Ana P Citadini; Sheila G Couto; Andressa Patrícia Alves Pinto; José L Lima; Daniel F Silva; Ana Paula Ulian de Araújo; Maria Cristina Nonato; Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq (39. 2010 Foz do Iguaçu)

Abstracts Foz do Iguaçu, 2010

Foz do Iguaçu 2010

Localização: FCFRP - Fac. Ciên. Farm. Ribeirão Preto    (pcd 1830983 estantes deslizantes ) e outros locais(Acessar)

6
Crystallization and structure determination of EcTI, a serine protease inhibitor from enterolobium
Crystallization and structure determination of EcTI, a serine protease inhibitor from enterolobium
Material Type:
Artigo de Congresso 		Adicionar ao Meu Espaço

Crystallization and structure determination of EcTI, a serine protease inhibitor from enterolobium

Richard Charles Garratt Maria Cristina Nonato; Marcos Bonfadini; Leila Maria Beltramini; I. F. C Batista; M. U Sampaio; C. A. M Sampaio; Congress and General Assembly of the International Union of Crystallography (18. 1999 Glasgow)

Abstracts Glasgow, 1999

Glasgow 1999

Item não circula. Consulte sua biblioteca.(Acessar)

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