Half-barrels derived from a (beta/alpha)(8) barrel beta-Glycosidase undergo an activation process (2015)
- Authors:
- Autor USP: MARANA, SANDRO ROBERTO - IQ
- Unidade: IQ
- DOI: 10.1371/journal.pone.0139673
- Subjects: ENZIMAS; PROTEÍNAS
- Language: Inglês
- Imprenta:
- Publisher place: San Francisco
- Date published: 2015
- Source:
- Este periódico é de acesso aberto
- Este artigo é de acesso aberto
- URL de acesso aberto
- Cor do Acesso Aberto: gold
- Licença: cc-by
-
ABNT
BETON, Daniela e MARANA, Sandro Roberto. Half-barrels derived from a (beta/alpha)(8) barrel beta-Glycosidase undergo an activation process. PLOS ONE, v. 10, n. 10, p. 1-6 art. e0139673, 2015Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0139673. Acesso em: 15 maio 2024. -
APA
Beton, D., & Marana, S. R. (2015). Half-barrels derived from a (beta/alpha)(8) barrel beta-Glycosidase undergo an activation process. PLOS ONE, 10( 10), 1-6 art. e0139673. doi:10.1371/journal.pone.0139673 -
NLM
Beton D, Marana SR. Half-barrels derived from a (beta/alpha)(8) barrel beta-Glycosidase undergo an activation process [Internet]. PLOS ONE. 2015 ; 10( 10): 1-6 art. e0139673.[citado 2024 maio 15 ] Available from: https://doi.org/10.1371/journal.pone.0139673 -
Vancouver
Beton D, Marana SR. Half-barrels derived from a (beta/alpha)(8) barrel beta-Glycosidase undergo an activation process [Internet]. PLOS ONE. 2015 ; 10( 10): 1-6 art. e0139673.[citado 2024 maio 15 ] Available from: https://doi.org/10.1371/journal.pone.0139673 - Optimum temperature may be a misleading parameter in enzyme characterization and application
- Enzyme optimum temperature: constant or relative parameter?
- Role of the triad N46, S106 and T107 and the surface charges in the determination of the acidic pH optimum of digestive lysozymes from Musca domestica
- Additivity of mutational effects on the catalytic activity of a 'beta'glycosidase
- Role of residue E190 in modulating aglycone specificity of a 'beta'-glycosidase from spodoptera frugiperda (SFBGLI50-AF 052729) of family 1
- In vitro evolution of beta-glucosidase from Spodoptera frugiperda, aiming at second generation ethanol
- Data supporting the hypothesis that contact pathways modulate the substrate specificity of a β-glucosidase
- Mapping of amino acid residues involved in the thermal stability of a beta-glucosidase
- Standardization of a method of In vitro evolution of beta-glycosidases
- The role in the substrate specificity and catalysis of residues forming the substrate aglycone-binding site of a 'beta'-glycosidase
Informações sobre o DOI: 10.1371/journal.pone.0139673 (Fonte: oaDOI API)
How to cite
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
