The regulation of the thermal stability and affinity of the HSPA5 (Grp78/BiP) by clients and nucleotides is modulated by domains coupling (2024)
- Authors:
- USP affiliated authors: BORGES, JÚLIO CÉSAR - IQSC ; SILVA, NOELI SOARES MELO DA - IQSC ; OLIVEIRA, CARLOS SABINO DE - IQSC ; SILVA, PAULO ROBERTO DAS DORES DA - IQSC
- Unidade: IQSC
- DOI: 10.1016/j.bbapap.2024.141034
- Subjects: PROTEÍNAS; BIOQUÍMICA
- Keywords: HSPA5; Molecular chaperone; BiP; Grp78; Bidirectional heterotrophic allosteric mechanism
- Agências de fomento:
- Language: Inglês
- Imprenta:
- Source:
- Título: Biochimica et Biophysica Acta. Proteins and Proteomics
- ISSN: 1570-9639
- Volume/Número/Paginação/Ano: v.1872, p.141034, 2024
- Este periódico é de acesso aberto
- Este artigo NÃO é de acesso aberto
-
ABNT
SILVA, Noeli Soares Melo da et al. The regulation of the thermal stability and affinity of the HSPA5 (Grp78/BiP) by clients and nucleotides is modulated by domains coupling. Biochimica et Biophysica Acta. Proteins and Proteomics, v. 1872, p. 141034, 2024Tradução . . Disponível em: https://doi.org/10.1016/j.bbapap.2024.141034. Acesso em: 10 fev. 2026. -
APA
Silva, N. S. M. da, Siebeneichler, B., Oliveira, C. S. de, Dores-Silva, P. R., & Borges, J. C. (2024). The regulation of the thermal stability and affinity of the HSPA5 (Grp78/BiP) by clients and nucleotides is modulated by domains coupling. Biochimica et Biophysica Acta. Proteins and Proteomics, 1872, 141034. doi:10.1016/j.bbapap.2024.141034 -
NLM
Silva NSM da, Siebeneichler B, Oliveira CS de, Dores-Silva PR, Borges JC. The regulation of the thermal stability and affinity of the HSPA5 (Grp78/BiP) by clients and nucleotides is modulated by domains coupling [Internet]. Biochimica et Biophysica Acta. Proteins and Proteomics. 2024 ;1872 141034.[citado 2026 fev. 10 ] Available from: https://doi.org/10.1016/j.bbapap.2024.141034 -
Vancouver
Silva NSM da, Siebeneichler B, Oliveira CS de, Dores-Silva PR, Borges JC. The regulation of the thermal stability and affinity of the HSPA5 (Grp78/BiP) by clients and nucleotides is modulated by domains coupling [Internet]. Biochimica et Biophysica Acta. Proteins and Proteomics. 2024 ;1872 141034.[citado 2026 fev. 10 ] Available from: https://doi.org/10.1016/j.bbapap.2024.141034 - Immunization with recombinant enolase of Sporothrix spp. (rSsEno) confers effective protection against sporotrichosis in mice
- Calcium interaction with HSPA1A Nucleotide Binding Domain
- Biophysical and biochemical characterization of human 70 kDa heat shock proteins (hHSP70)
- Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes
- Small-angle X-ray scattering (SAXS) studies on the HSP70 chaperone family
- A Sporothrix spp. enolase derived multi-epitope vaccine confers protective response in BALB/c mice challenged with Sporothrix brasiliensis
- Structural studies of the recombinant enolase of sporothrix SPP
- Human mortalin (HSPA9, mt-HSP70) interacts with liposomes made of negatively charged phospholipids similar to those present in the mitochondrial membrane
- Structural and functional studies of Hsp70 Escort Protein 1 (Hep1): a chaperone for a chaperone!
- Thermal aggregates of human mortalin and Hsp70-1A behave as supramolecular assemblies
Informações sobre o DOI: 10.1016/j.bbapap.2024.141034 (Fonte: oaDOI API)
Download do texto completo
| Tipo | Nome | Link | |
|---|---|---|---|
 |
P21205.pdf |
How to cite
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
