Mutations close to a hub residue affect the distant active site of a GH1 beta-glucosidase (2018)
- Authors:
- USP affiliated authors: ARANTES, GUILHERME MENEGON - IQ ; MARANA, SANDRO ROBERTO - IQ
- Unidade: IQ
- DOI: 10.1371/journal.pone.0198696
- Subjects: GLICOSÍDEOS; MUTAÇÃO
- Agências de fomento:
- Language: Inglês
- Imprenta:
- Publisher place: San Francisco
- Date published: 2018
- 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
SOUZA, Valquiria Pianheri et al. Mutations close to a hub residue affect the distant active site of a GH1 beta-glucosidase. PLOS ONE, v. 13, n. 6, p. 1-12 art. e0198696, 2018Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0198696. Acesso em: 28 dez. 2025. -
APA
Souza, V. P., Ikegami, C. M., Arantes, G. M., & Marana, S. R. (2018). Mutations close to a hub residue affect the distant active site of a GH1 beta-glucosidase. PLOS ONE, 13( 6), 1-12 art. e0198696. doi:10.1371/journal.pone.0198696 -
NLM
Souza VP, Ikegami CM, Arantes GM, Marana SR. Mutations close to a hub residue affect the distant active site of a GH1 beta-glucosidase [Internet]. PLOS ONE. 2018 ; 13( 6): 1-12 art. e0198696.[citado 2025 dez. 28 ] Available from: https://doi.org/10.1371/journal.pone.0198696 -
Vancouver
Souza VP, Ikegami CM, Arantes GM, Marana SR. Mutations close to a hub residue affect the distant active site of a GH1 beta-glucosidase [Internet]. PLOS ONE. 2018 ; 13( 6): 1-12 art. e0198696.[citado 2025 dez. 28 ] Available from: https://doi.org/10.1371/journal.pone.0198696 - Protein thermal denaturation is modulated by central residues in the protein structure network
- Role of highly connected residues (hubs) of enzyme structural networks on the substrate specificity
- Study of the correlation between structural network and structural and catalytic properties of beta-glucosidases
- Molecular recognition by CDC25B phosphatases
- Combining NMR and computer simulations to evaluate Cdc25B protein flexbility
- Conformational flexibility of the complete catalytic domain of Cdc25B phosphatases
- Expression, purification and buffering conditions of Cdc25B for NMR data acquisition
- Ligand binding and conformational dynamics of CDC25B phosphatase
- Combining free energy simulations and NMR chemical-shift perturbation to identify transient cation−π contacts in proteins
- Theoretical modeling of low-energy electronic absorption bands in reduced cobaloximes
Informações sobre o DOI: 10.1371/journal.pone.0198696 (Fonte: oaDOI API)
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