Molecular recognition by CDC25B phosphatases (2019)
- Authors:
- USP affiliated authors: MARANA, SANDRO ROBERTO - IQ ; ARANTES, GUILHERME MENEGON - IQ
- Unidade: IQ
- Subjects: BIOLOGIA MOLECULAR; PROTEÍNAS
- Agências de fomento:
- Language: Inglês
- Imprenta:
- Publisher: Sociedade Brasileira de Biofísica/SBBf
- Publisher place: Santos
- Date published: 2019
- Source:
- Título: Abstracts
- Conference titles: Congresso da Sociedade Brasileira de Biofísica
-
ABNT
REIS, André Anversa Oliveira et al. Molecular recognition by CDC25B phosphatases. 2019, Anais.. Santos: Sociedade Brasileira de Biofísica/SBBf, 2019. . Acesso em: 28 dez. 2025. -
APA
Reis, A. A. O., Sayegh, R. S. R., Marana, S. R., & Arantes, G. M. (2019). Molecular recognition by CDC25B phosphatases. In Abstracts. Santos: Sociedade Brasileira de Biofísica/SBBf. -
NLM
Reis AAO, Sayegh RSR, Marana SR, Arantes GM. Molecular recognition by CDC25B phosphatases. Abstracts. 2019 ;[citado 2025 dez. 28 ] -
Vancouver
Reis AAO, Sayegh RSR, Marana SR, Arantes GM. Molecular recognition by CDC25B phosphatases. Abstracts. 2019 ;[citado 2025 dez. 28 ] - 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
- Mutations close to a hub residue affect the distant active site of a GH1 beta-glucosidase
- 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
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