Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases (2014)
- Authors:
- USP affiliated authors: POLIKARPOV, IGOR - IFSC ; MARANA, SANDRO ROBERTO - IQ
- Unidades: IFSC; IQ
- DOI: 10.1371/journal.pone.0096627
- Subjects: ENZIMAS (ESTUDO); PROTEÍNAS; AMINOÁCIDOS
- Language: Inglês
- Imprenta:
- Publisher place: San Francisco
- Date published: 2014
- Source:
- Status:
- Artigo publicado em periódico de acesso aberto (Gold Open Access)
- Versão do Documento:
- Versão publicada (Published version)
- Acessar versão aberta:
-
ABNT
TAMAKI, Fábio K. et al. Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases. PLOS One, v. 9, n. 5, p. e96627-1-e96627-8, 2014Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0096627. Acesso em: 01 abr. 2026. -
APA
Tamaki, F. K., Textor, L. C., Polikarpov, I., & Marana, S. R. (2014). Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases. PLOS One, 9( 5), e96627-1-e96627-8. doi:10.1371/journal.pone.0096627 -
NLM
Tamaki FK, Textor LC, Polikarpov I, Marana SR. Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases [Internet]. PLOS One. 2014 ; 9( 5): e96627-1-e96627-8.[citado 2026 abr. 01 ] Available from: https://doi.org/10.1371/journal.pone.0096627 -
Vancouver
Tamaki FK, Textor LC, Polikarpov I, Marana SR. Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases [Internet]. PLOS One. 2014 ; 9( 5): e96627-1-e96627-8.[citado 2026 abr. 01 ] Available from: https://doi.org/10.1371/journal.pone.0096627 - Effects on the thermal stability and enzymatic activity caused by substitutions of co-variant amino acids of the 'beta'-glucosidase from Spodoptera frugiperda
- Functional study of amino acid positions presenting coupled frequencies in Spodoptera frujiperda beta-glucosidase
- Effects on the thermal stability and enzymatic activity caused by substitutions of co-variant amino acids of the 'beta'-glucosidase from Spodoptera frugiperda
- Sets of co-variant positions in β-glucosidases are involved in modulating the activity and the thermal stability
- Functional sectors involved in thermal stability and activity in beta-glucosidases
- Biochemical characterization and low-resolution SAXS molecular envelope of GH1 β-Glycosidase from Saccharophagus degradans
- Differences in gluco and galacto substrate-binding interactions in a dual 6Pβ-Glucosidase/6Pβ-Galactosidase glycoside hydrolase 1 enzyme from Bacillus licheniformis
- Characterization of the interdependency between residues that bind the substrate in a 'beta'-glycosidase
- Enzyme kinetics of the β-glucosidase from Spodoptera frugiperda in two different ionic strengths
- Protein structure network and thermal stability
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