Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes (2021)
- Authors:
- USP affiliated authors: BORGES, JÚLIO CÉSAR - IQSC ; SILVA, PAULO ROBERTO DAS DORES DA - IQSC ; COTO, AMANDA LAÍS DE SOUZA - IQSC ; SILVA, NOELI SOARES MELO DA - IQSC
- Unidade: IQSC
- DOI: 10.1007/s12192-021-01210-8
- Subjects: LIPOSSOMOS; FOSFOLIPÍDEOS
- Keywords: Hsp70; HSPA8; HSPA1A; HSP90AA1; Membranes; Chaperones
- Agências de fomento:
- Language: Inglês
- Imprenta:
- Source:
- Título: Cell Stress & Chaperones
- ISSN: 1355-8145
- Volume/Número/Paginação/Ano: p. 26, n. 4, p. 671-684, 2021
- Este periódico é de assinatura
- Este artigo é de acesso aberto
- URL de acesso aberto
- Cor do Acesso Aberto: hybrid
- Licença: cc-by-nc-nd
-
ABNT
DORES-SILVA, Paulo Roberto et al. Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes. Cell Stress & Chaperones, n. 4, p. 671-684, 2021Tradução . . Disponível em: https://doi.org/10.1007/s12192-021-01210-8. Acesso em: 27 dez. 2025. -
APA
Dores-Silva, P. R., Cauvi, D. M., Coto, A. L. S., Silva, N. S. M. da, Borges, J. C., & De Maio, A. (2021). Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes. Cell Stress & Chaperones, ( 4), 671-684. doi:10.1007/s12192-021-01210-8 -
NLM
Dores-Silva PR, Cauvi DM, Coto ALS, Silva NSM da, Borges JC, De Maio A. Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes [Internet]. Cell Stress & Chaperones. 2021 ;( 4): 671-684.[citado 2025 dez. 27 ] Available from: https://doi.org/10.1007/s12192-021-01210-8 -
Vancouver
Dores-Silva PR, Cauvi DM, Coto ALS, Silva NSM da, Borges JC, De Maio A. Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes [Internet]. Cell Stress & Chaperones. 2021 ;( 4): 671-684.[citado 2025 dez. 27 ] Available from: https://doi.org/10.1007/s12192-021-01210-8 - Obtaining and structural studies of human BiP thermal aggregate
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- Biophysical and biochemical characterization of human 70 kDa heat shock proteins (hHSP70)
- Small-angle X-ray scattering (SAXS) studies on the HSP70 chaperone family
- The regulation of the thermal stability and affinity of the HSPA5 (Grp78/BiP) by clients and nucleotides is modulated by domains coupling
- Thermal aggregates of human mortalin and Hsp70-1A behave as supramolecular assemblies
- Human mortalin (HSPA9, mt-HSP70) interacts with liposomes made of negatively charged phospholipids similar to those present in the mitochondrial membrane
- Interaction of HSPA5 (Grp78, BIP) with negatively charged phospholipid membranes via oligomerization involving the N-terminal end domain
- Structural and functional studies of Hsp70 Escort Protein 1 (Hep1): a chaperone for a chaperone!
- Teaching an old dog new tricks: new strategies for saxs data analysis of proteins in solution
Informações sobre o DOI: 10.1007/s12192-021-01210-8 (Fonte: oaDOI API)
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