Bradeion 'beta': heterologoes expression and purification (2002)
- Authors:
- USP affiliated authors: ARAUJO, ANA PAULA ULIAN DE - IFSC ; GARRATT, RICHARD CHARLES - IFSC
- Unidade: IFSC
- Subjects: BIOQUÍMICA; NEOPLASIAS; PROTEÍNAS
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Programa e Resumos
- Conference titles: Reunião Anual da Socidade Brasileira de Bioquímica e Biologia Molecular
-
ABNT
GARCIA, W. et al. Bradeion 'beta': heterologoes expression and purification. 2002, Anais.. São Paulo: SBBq, 2002. . Acesso em: 19 set. 2024. -
APA
Garcia, W., Araújo, A. P. U. de, Tanaka, M., & Garratt, R. C. (2002). Bradeion 'beta': heterologoes expression and purification. In Programa e Resumos. São Paulo: SBBq. -
NLM
Garcia W, Araújo APU de, Tanaka M, Garratt RC. Bradeion 'beta': heterologoes expression and purification. Programa e Resumos. 2002 ;[citado 2024 set. 19 ] -
Vancouver
Garcia W, Araújo APU de, Tanaka M, Garratt RC. Bradeion 'beta': heterologoes expression and purification. Programa e Resumos. 2002 ;[citado 2024 set. 19 ] - Crystallographic structure of the enzyme Fe-superoxide dismutase from Trypanossoma cruzi at 1.9 'angstron' resolution: a potential target for development of novel drugs against chagas disease
- Biophysical characterization of human septin 2 and its binding to phosphatidylinositol-4,5-biophosphate
- A draft of the human septin interactome
- Structural investigation of the human septin 2/6/7/9 hetero complex
- Automontagem de filamentos de septinas estudada por microscopia eletrônica
- Preliminary EM studies of the assembly of septin filaments
- Studies of SEPT2-SEPT6 heterocomplex: revealing the molecular determinants involved in the interaction
- Estudos de estabilidade e agregação da septina 3
- Design of potentials TcFeSOD inhibitors based on the crystallographic structure of the enzyme Fe-superoxide dismutase from Trypanosoma cruzi at 1.9 'angstron' resolution
- An intermediate structure in the thermal unfolding of the GTPase domain of human septin 4 (SEPT4/Bradeion-'beta') forms amyloid-like filaments in vitro
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