The Golgi matrix proteins have a high propensity to form liquid droplets (2023)
- Authors:
- USP affiliated authors: MENDES, LUIS FELIPE SANTOS - IFSC ; COSTA FILHO, ANTÔNIO JOSÉ DA - FFCLRP ; OLIVEIRA, CAROLINA GIMENES - FFCLRP
- Unidades: IFSC; FFCLRP
- Subjects: MEMBRANAS (BIOLOGIA); PROTEÍNAS; COMPLEXO DE GOLGI
- Keywords: GRASPs; Liquid liquid phase separation; Unconventional protein secretion
- Agências de fomento:
- Language: Inglês
- Imprenta:
- Source:
- Título: Anais eletrônicos
- Conference titles: Annual Meeting of the Brazilian Biophysical Society - SBBf
-
ABNT
OLIVEIRA, Carolina Gimenes e MENDES, Luís Felipe Santos e COSTA FILHO, Antonio José da. The Golgi matrix proteins have a high propensity to form liquid droplets. 2023, Anais.. Campinas: Galoá, 2023. Disponível em: https://proceedings.science/sbbf-2023/papers/the-golgi-matrix-proteins-have-a-high-propensity-to-form-liquid-droplets?lang=en. Acesso em: 12 fev. 2026. -
APA
Oliveira, C. G., Mendes, L. F. S., & Costa Filho, A. J. da. (2023). The Golgi matrix proteins have a high propensity to form liquid droplets. In Anais eletrônicos. Campinas: Galoá. Recuperado de https://proceedings.science/sbbf-2023/papers/the-golgi-matrix-proteins-have-a-high-propensity-to-form-liquid-droplets?lang=en -
NLM
Oliveira CG, Mendes LFS, Costa Filho AJ da. The Golgi matrix proteins have a high propensity to form liquid droplets [Internet]. Anais eletrônicos. 2023 ;[citado 2026 fev. 12 ] Available from: https://proceedings.science/sbbf-2023/papers/the-golgi-matrix-proteins-have-a-high-propensity-to-form-liquid-droplets?lang=en -
Vancouver
Oliveira CG, Mendes LFS, Costa Filho AJ da. The Golgi matrix proteins have a high propensity to form liquid droplets [Internet]. Anais eletrônicos. 2023 ;[citado 2026 fev. 12 ] Available from: https://proceedings.science/sbbf-2023/papers/the-golgi-matrix-proteins-have-a-high-propensity-to-form-liquid-droplets?lang=en - Investigating structural determinants for protein condensate formation in the saccharomyces cerevisiae GRASP
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- A gold revision of the Golgi dynamics (GOLD) domain structure and associated cell functionalities
- Exploring liquid-liquid phase separation in the organisation of golgi matrix proteins
- The overlooked impact of N-terminal acetylation on biomolecular condensation
- Myristoylation and its effects on the human Golgi Reassembly and Stacking Protein 55
- Tetramethyl-phenanthroline copper complexes in the development of drugs to treat cancer: synthesis, characterization and cytotoxicity studies of a series of copper(II)-l-dipeptide-3,4,7,8-tetramethyl-phenanthroline complexes
- Molecular interaction of neocuproine and its copper(II) complex with model membranes
- Conformational flexibility of GRASPs and their constituent PDZ subdomains reveals structural basis of their promiscuous interactome
- Structural analysis and anchoring mechanism of the transmembrane emp24 domain-containing proteins
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