Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Samantha M. Martins"'
Ações educativas e logística reversa de medicamentos descartados na cidade universitária de Macaé-RJ
Autor:
Juliana G. Valente, Bárbara S Santos, Denise O. Guimarães, Maria Cs Verdam, Thaís Ms Pereira, Raiane L Santos, Samantha M. Martins, Raissa Mf Oliveira, Maximiliano da Silva Sangoi, Marina Cardoso Nemitz, Marlon Rs Campos, Thiago Barth, Marcos Fm Gomes, Vítor Todeschini, Anna Kms Machado, Julia R Sales, Chayanne S Chagas
Publikováno v:
Cadernos do Desenvolvimento Fluminense. :193-215
Os medicamentos podem constituir risco à saúde pública e ao meio ambiente se descartados incorretamente. Neste cenário vem sendo desenvolvido o projeto “Descarte de medicamentos: diagnóstico, educação e gerenciamento em domicílios e estabel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2dd127d0f99a9601117e9b89744454fa
https://doi.org/10.12957/cdf.2021.59617
https://doi.org/10.12957/cdf.2021.59617
Autor:
Leandro L. da Silva, Ivana C. R. Leal, Fernando Armani Aguiar, Shaft Corrêa Pinto, Laura L Calassara, Cecília P M Condack, Samantha M. Martins, Michelle Frazão Muzitano, Luzineide W. Tinoco, Ludmilla C Do Espírito Santo Nery, Beatriz F Leite, Juliana M Raimundo
Publikováno v:
Natural Product Research. 35:5480-5483
The aim of this study was to perform the isolation and characterization of vasodilatory flavonoids from Tapirira guianensis Aubl. (Annacardiaceae) leaves. In this context, ethyl acetate fraction (E...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7bab9a8669d8cf4ae2448e0eca7a77a0
https://doi.org/10.1080/14786419.2020.1784170
https://doi.org/10.1080/14786419.2020.1784170
Autor:
Laura L, Calassara, Shaft C, Pinto, Cecília P M, Condack, Beatriz F, Leite, Ludmilla C do E S, Nery, Luzineide W, Tinoco, Fernando A, Aguiar, Ivana C R, Leal, Samantha M, Martins, Leandro L da, Silva, Juliana M, Raimundo, Michelle F, Muzitano
Publikováno v:
Natural product research. 35(23)
The aim of this study was to perform the isolation and characterization of vasodilatory flavonoids from
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a08f328e5875cc5f4ca40168c91e2ae7
https://pubmed.ncbi.nlm.nih.gov/32586127
https://pubmed.ncbi.nlm.nih.gov/32586127
Autor:
Sergio T. Ferreira, Surza Lucia Gonçalves da Rocha, Samantha M. Martins, Gilberto B. Domont, Richard H. Valente, Oliver Holub, Ana G.C. Neves-Ferreira, Alex Chapeaurouge, Jonas Perales
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1794:1379-1386
We have investigated the folding of DM43, a homodimeric metalloproteinase inhibitor isolated from the serum of the South American opossum Didelphis marsupialis. Denaturation of the protein induced by GdnHCl (guanidine hydrochloride) was monitored by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5078945b7e1bc40ecca8941d599993e4
https://doi.org/10.1016/j.bbapap.2009.03.010
https://doi.org/10.1016/j.bbapap.2009.03.010
Autor:
Samantha M. Martins, Dóris J. Frosoni, Sergio T. Ferreira, Fernanda G. De Felice, Ana Maria Blanco Martinez
Publikováno v:
Journal of Biological Chemistry. 281:26121-26128
Prion diseases are fatal neurodegenerative disorders associated with conformational conversion of the cellular prion protein, PrP(C), into a misfolded, protease-resistant form, PrP(Sc). Here we show, for the first time, the oligomerization and fibril
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a76d0fce623396d8ff53f82edbf359ed
https://doi.org/10.1074/jbc.m605367200
https://doi.org/10.1074/jbc.m605367200
Publikováno v:
European Journal of Biochemistry. 269:5484-5491
The structures and stabilities of recombinant chicken muscle troponin I (TnI) and T (TnT) were investigated by a combination of bis-ANS binding and equilibrium unfolding studies. Unlike most folded proteins, isolated TnI and TnT bind the hydrophobic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ee70564bd5cbdb5876d914ccd44a8bf6
https://doi.org/10.1046/j.1432-1033.2002.03248.x
https://doi.org/10.1046/j.1432-1033.2002.03248.x
Publikováno v:
Bioscience Reports. 20:369-381
ATPdiphosphohydrolases (ATPDases) are ubiquitous enzymes capable of hydrolyzing nucleoside di- and triphosphates. Although a number of possible physiological roles have been proposed for ATPDases, detailed studies on structure-function relationships
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c436dcd54bac903536af4ac699b7b26
https://doi.org/10.1023/a:1010330017583
https://doi.org/10.1023/a:1010330017583
Autor:
Jean-Christophe Houzel, William L. Klein, Andre F. Batista, Samantha M. Martins, Natalia M. Lyra e Silva, Leticia Forny-Germano, Jordano Brito-Moreira, Sergio T. Ferreira, Fernanda G. De Felice, Douglas P. Munoz
Publikováno v:
Alzheimer's & Dementia. 8
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8cfa90dae9ee80d4748c4af4b51c0789
https://doi.org/10.1016/j.jalz.2012.05.557
https://doi.org/10.1016/j.jalz.2012.05.557
Autor:
Samantha M. Martins, Sergio T. Ferreira, Helena Brentani, Fabio F. Oliveira, Léo Freitas-Correa, Dirce Maria Carraro, Fernanda G. De Felice, Soniza Vieira Alves-Leon, Andrea C. Paula-Lima, Leonardo M. Saraiva, Cesar Torres, Adriano Sebollela, Louise Danielle de Carvalho Mota, Jorge Marcondes de Souza
Publikováno v:
The Journal of biological chemistry. 287(10)
Cognitive decline in Alzheimer disease (AD) is increasingly attributed to the neuronal impact of soluble oligomers of the amyloid-β peptide (AβOs). Current knowledge on the molecular and cellular mechanisms underlying the toxicity of AβOs stems la
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb508ec00531dbb517ffe12babe1d197
https://pubmed.ncbi.nlm.nih.gov/22235132
https://pubmed.ncbi.nlm.nih.gov/22235132
Publikováno v:
The Journal of biological chemistry. 278(50)
Prion diseases are associated with conformational conversion of the cellular prion protein, PrPC, into a misfolded form, PrPSc. We have investigated the equilibrium unfolding of the structured domain of recombinant murine prion protein, comprising re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3df7fa80f2e0d901fb78f5c7f62f3f4
https://pubmed.ncbi.nlm.nih.gov/14525996
https://pubmed.ncbi.nlm.nih.gov/14525996