Výsledky vyhledávání - "Luis F.S. Mendes"

The exquisite structural biophysics of the Golgi Reassembly and Stacking Proteins

Autor: Antonio J. Costa-Filho, Natália A. Fontana, Luis F.S. Mendes, Vladimir N. Uversky, S. Thirupathi Reddy

Publikováno v: International Journal of Biological Macromolecules. 164:3632-3644

Golgi Reassembly and Stacking Proteins (GRASPs) were firstly described as crucial elements in determining the structure of the Golgi complex. However, data have been accumulating over the years showing GRASPs can actually participate in various cell

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::50cbb44a59aef645ac50f3784ef63fa1
https://doi.org/10.1016/j.ijbiomac.2020.08.203

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Structural and thermodynamic analyses of human TMED1 (p24γ1) Golgi dynamics

Autor: Mariana R. B. Batista, Antonio J. Costa-Filho, M. Cristina Nonato, Danielly C. A. M. Mota, Luis G.M. Basso, Luis F.S. Mendes, Renan M. Mori, Iara Aimê Cardoso

Publikováno v: Biochimie. 192

The transmembrane emp24 domain-containing (TMED) proteins, also called p24 proteins, are members of a family of sorting receptors present in all representatives of the Eukarya and abundantly present in all subcompartments of the early secretory pathw

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93fe7ad114ab30c78d4567c176b70cab
https://pubmed.ncbi.nlm.nih.gov/34634369

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Resurrecting Golgi proteins to grasp Golgi ribbon formation and self-association under stress

Autor: Mariana R. B. Batista, Mariana C. Micheletto, Lucas Bleicher, Antonio J. Costa-Filho, Emanuel Kava, Luis F.S. Mendes

Publikováno v: International journal of biological macromolecules. 194

The Golgi complex is a membranous organelle located in the heart of the eukaryotic secretory pathway. A subfamily of the Golgi matrix proteins, called GRASPs, are key players in the stress-induced unconventional secretion, the Golgi dynamics during m

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::558200ffd1dafa789aa614df0f02ad71
https://pubmed.ncbi.nlm.nih.gov/34861272

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The GRASP domain in golgi reassembly and stacking proteins: differences and similarities between lower and higher Eukaryotes

Autor: Luis F.S. Mendes, Jose L. S. Lopes, Fernando A. Melo, Marjorie C. L. C. Freire, Carolina Gimenes Oliveira, Antonio J. Costa-Filho, Natália A. Fontana

Publikováno v: Web of Science
Repositório Institucional da UNESP
Universidade Estadual Paulista (UNESP)
instacron:UNESP

Made available in DSpace on 2020-12-10T19:35:32Z (GMT). No. of bitstreams: 0 Previous issue date: 2019-09-01 Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) The

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1afaf53bf6b705dbdcd3941d80edf5a
https://doi.org/10.1111/febs.14869

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Development of copper(II)-diimine-iminodiacetate mixed ligand complexes as potential antitumor agents

Autor: Luis F.S. Mendes, Natalia Alvarez, María H. Torre, M. Gabriela Kramer, Javier Ellena, Gianella Facchin, Antonio J. Costa-Filho

Publikováno v: Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP

In order to seek for new compounds with antitumor activity, our research group is focused on copper complexes with mixed ligands. This work presents the synthesis and characterization of eight compounds with general formula [Cu(iminodiacetate)(diimin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::18918645311036f0a882c5b3964fae40
https://doi.org/10.1016/j.ica.2018.07.052

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Myristoylation and its effects on the human Golgi Reassembly and Stacking Protein 55

Autor: Antonio J. Costa-Filho, Luis F.S. Mendes, Emanuel Kava, Mariana R. B. Batista

Publikováno v: Biophysical Chemistry. 279:106690

GRASP55 is a myristoylated protein localized in the medial/trans-Golgi faces and involved in the Golgi structure maintenance and the regulation of unconventional secretion pathways. It is believed that GRASP55 achieves its main functionalities in the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12f8f38aed3a73e88ce0ebde889baabe
https://doi.org/10.1016/j.bpc.2021.106690

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Lipid membranes and acyl-CoA esters promote opposing effects on acyl-CoA binding protein structure and stability

Autor: Raquel Fonseca-Maldonado, Luis G.M. Basso, Luis F.S. Mendes, Antonio J. Costa-Filho, Mariana C. Micheletto

Publikováno v: Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP

Acyl-CoA Binding Proteins (ACBP) form a housekeeping family of proteins that is responsible for the buffering of long chain acyl-coenzyme A esters (LCFA-CoA) inside the cell. Even though numerous studies have focused on the characterization of differ

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ff66b8e0d1a1ea6b892c127c752c038
https://doi.org/10.1016/j.ijbiomac.2017.03.197

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Synthesis, structural characterization and cytotoxic activity against tumor cells of heteroleptic copper (I) complexes with aromatic diimines and phosphines

Autor: Luis F.S. Mendes, Gianella Facchin, Javier Ellena, Antonio J. Costa-Filho, Eduardo Kremer, María H. Torre, M. Gabriela Kramer, Márcio P. de Araujo, Carolina Noble, Natalia Alvarez

Publikováno v: Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP

Copper coordination complexes are increasingly recognized as potential drugs for therapeutic use in various diseases, especially in cancer. In an attempt to find new leaders for the development of antitumor Cu compounds, heteroleptic Cu(I) complexes

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad18b3aff00b3609c3dfedbc6d2bae80
https://doi.org/10.1016/j.ica.2017.06.050

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Synthesis and structural characterization of a series of ternary copper(II)-L-dipeptide-neocuproine complexes. Study of their cytotoxicity against cancer cells including MDA-MB-231, triple negative breast cancer cells

Autor: Javier Ellena, Luis F.S. Mendes, Gianella Facchin, Alzir A. Batista, Celisnolia M. Leite, Diana Viña, Antonio J. Costa-Filho, Natalia Alvarez

Publikováno v: Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP

This work presents the synthesis and characterization of eight copper complexes [Cu(L-dipeptide)(neo)]·nH2O (neo = neocuproine) and their cytotoxic activities against tumor cell lines. The crystalline structure of [Cu(gly-val)(neo)]·3H2O, [Cu(gly-l

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2dac0c729ff7518ce5bebff2fd446f0e
https://pubmed.ncbi.nlm.nih.gov/31812025

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Exploring Structural Aspects of the Human Golgi Matrix Protein GRASP55 in Solution

Autor: S. Thirupathi Reddy, Natália A. Fontana, Antonio J. Costa-Filho, Luis F.S. Mendes

Publikováno v: Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP

In mammalian cells, the Golgi apparatus is a central hub for intracellular trafficking, sorting and post-translational modifications of proteins and lipids. The Golgi reassembly and stacking proteins (GRASPs) are somehow involved in the Golgi stackin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10e5984ff96cc8a5b6839921ff19fe16
https://doi.org/10.1101/594572

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