Structural and functional characterization and rational modification of L-asnase_Mosmolytes: a new biopharmaceutical for the acute lymphoblastic leukemia treatment? (2015)
- Authors:
- USP affiliated authors: PESSOA JUNIOR, ADALBERTO - FCF ; SOUZA, GISELE MONTEIRO DE - FCF
- Unidade: FCF
- Assunto: LEUCEMIA (TRATAMENTO)
- Language: Inglês
- Imprenta:
- Publisher: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq)
- Publisher place: São Paulo
- Date published: 2015
- Source:
- Título do periódico: Abstracts Book
- Conference titles: Congress of the International Union for Biochemistry and Molecular Biology - IUBMB
-
ABNT
SCHULTZ, L. S et al. Structural and functional characterization and rational modification of L-asnase_Mosmolytes: a new biopharmaceutical for the acute lymphoblastic leukemia treatment? 2015, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq), 2015. . Acesso em: 26 abr. 2024. -
APA
Schultz, L. S., Costa, I. M., Pessoa Junior, A., Monteiro, G., & Oliveira, M. A. (2015). Structural and functional characterization and rational modification of L-asnase_Mosmolytes: a new biopharmaceutical for the acute lymphoblastic leukemia treatment? In Abstracts Book. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq). -
NLM
Schultz LS, Costa IM, Pessoa Junior A, Monteiro G, Oliveira MA. Structural and functional characterization and rational modification of L-asnase_Mosmolytes: a new biopharmaceutical for the acute lymphoblastic leukemia treatment? Abstracts Book. 2015 ;[citado 2024 abr. 26 ] -
Vancouver
Schultz LS, Costa IM, Pessoa Junior A, Monteiro G, Oliveira MA. Structural and functional characterization and rational modification of L-asnase_Mosmolytes: a new biopharmaceutical for the acute lymphoblastic leukemia treatment? Abstracts Book. 2015 ;[citado 2024 abr. 26 ] - Evaluation of bacterial expression strains for the production of recombinant L-asparaginase, an antileukemic enzyme from Escherichia coli
- Evaluation of the activity and resistance to proteolytic cleavage of recombinat L-asparaginase obtained by error-prone polymerase chain reaction
- Enzima da levedura do pão pode ser alternativa para tratar leucemia infantil
- Effect of different osmolyte concentrations in the L-asparaginase II activity
- Influence and effect of osmolytes in biopharmaceutical formulations
- Mutant L-asparaginase of Dickeya chrysanthemi (Erwinia chrysanthemi) with better biochemical parameters
- Functional and structural evaluation of the antileukaemic enzyme L-asparaginase II expressed at low temperature by different Escherichia coli strains
- Saccharomyces cerevisiae L-asparaginase 1: rational modifications aiming the modulation of kinetic characteristics over different substrates
- Producing L-asparaginase of Erwinia chrysanthemi improved by synthetic evolution of proteins
- Osmolytes stabilize L-asparaginase II without changing its secondary structure
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