Výsledky vyhledávání - "Karen F Discola"

Akademický článek

Structural insights on the efficient catalysis of hydroperoxide reduction by Ohr: Crystallographic and molecular dynamics approaches.

Autor: Erika Piccirillo, Thiago G P Alegria, Karen F Discola, José R R Cussiol, Renato M Domingos, Marcos A de Oliveira, Leandro de Rezende, Luis E S Netto, Antonia T-do Amaral

Publikováno v: PLoS ONE, Vol 13, Iss 5, p e0196918 (2018)

Organic hydroperoxide resistance (Ohr) enzymes are highly efficient Cys-based peroxidases that play central roles in bacterial response to fatty acid hydroperoxides and peroxynitrite, two oxidants that are generated during host-pathogen interactions.

Externí odkaz: https://doaj.org/article/99244d479e80482aa4aa579b00b09e4a

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Structural basis of eukaryotic cell targeting by type III secretion system (T3SS) effectors

Autor: David Neves, Alexander Pflug, Andréa Dessen, Karen F. Discola, Tommaso Tosi

Publikováno v: Research in Microbiology
Research in Microbiology, Elsevier, 2013, 164 (6), pp.605-19
Research in Microbiology, 2013, 164 (6), pp.605-19

International audience; Type III secretion systems (T3SS) are macromolecular complexes that translocate a wide number of effector proteins into eukaryotic host cells. Once within the cytoplasm, many T3SS effectors mimic the structure and/or function

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7cd76c88908013340150e0bb54244623
https://doi.org/10.1016/j.resmic.2013.03.019

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FtsZ filament capping by MciZ, a developmental regulator of bacterial division

Autor: Alexandre Martins, Harold P. Erickson, Valdir Blasios, Frederico J. Gueiros-Filho, Alexandre W. Bisson-Filho, Andréa Dessen, Wanius Garcia, Maurício L. Sforça, Patricia Castellen, Karen F. Discola, Ana Carolina de Mattos Zeri

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2015, 112 (17), pp.E2130-8
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
Proceedings of the National Academy of Sciences of the United States of America, 2015, 112 (17), pp.E2130-8

International audience; Cytoskeletal structures are dynamically remodeled with the aid of regulatory proteins. FtsZ (filamentation temperature-sensitive Z) is the bacterial homolog of tubulin that polymerizes into rings localized to cell-division sit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d4605d26a3d8869836b1fe530f18b12
https://hal.univ-grenoble-alpes.fr/hal-01149454

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Membrane and chaperone recognition by the major translocator protein PopB of the type III secretion system of Pseudomonas aeruginosa

Autor: Viviana Job, Jean-Pierre Simorre, Karen F. Discola, Ina Attree, François Boulay, Andreas Förster, Andréa Dessen

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, 2014, 289 (6), pp.3591-601
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2014, 289 (6), pp.3591-601
HAL

International audience; The type III secretion system is a widespread apparatus used by pathogenic bacteria to inject effectors directly into the cytoplasm of eukaryotic cells. A key component of this highly conserved system is the translocon, a pore

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e7effd9c5c04da0aead8d8953ea3bb9
https://hal.univ-grenoble-alpes.fr/hal-01109809

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Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl-based redox modification of the 20S proteasome

Autor: Gustavo M, Silva, Luis E S, Netto, Karen F, Discola, Gilberto M, Piassa-Filho, Daniel C, Pimenta, José A, Bárcena, Marilene, Demasi

Publikováno v: The FEBS journal. 275(11)

The yeast 20S proteasome is subject to sulfhydryl redox alterations, such as the oxidation of cysteine residues (Cys-SH) into cysteine sulfenic acid (Cys-SOH), followed by S-glutathionylation (Cys-S-SG). Proteasome S-glutathionylation promotes partia

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a7db1a11226aa38251fbacded0699bfa
https://pubmed.ncbi.nlm.nih.gov/18435761

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