Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Filipe E. P. Rodrigues"'
Autor:
Nuno F. B. Oliveira, Filipe E. P. Rodrigues, João N. M. Vitorino, Patrícia F. N. Faísca, Miguel Machuqueiro
Publikováno v:
Journal of Chemical Information and Modeling.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7371c08d271fee08f60cfe73011599cc
https://doi.org/10.1021/acs.jcim.3c00399
https://doi.org/10.1021/acs.jcim.3c00399
Autor:
Nuno F. B. Oliveira, Filipe E. P. Rodrigues, João N. M. Vitorino, Patrícia F. N. Faísca, Miguel Machuqueiro
Protein aggregation is a complex process that strongly depends on environmental conditions and has considerable structural heterogeneity, not only at the level of fibril structure but also at the level of molecular oligomerization. Since the first st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::038d1193d094ccf1791281597f541fd6
https://doi.org/10.1101/2022.12.28.522115
https://doi.org/10.1101/2022.12.28.522115
Autor:
Irina S. Moreira, Filipe E. P. Rodrigues, João N. M. Vitorino, Rita Melo, Nícia Rosário-Ferreira, Tomás Silva, Salete J. Baptista, Miguel Machuqueiro, Sara G. F. Ferreira, Bruno L. Victor, Carlos A. V. Barreto
Publikováno v:
ACS Synthetic Biology
SARS-CoV-2 triggered a worldwide pandemic disease, COVID-19, for which an effective treatment has not yet been settled. Among the most promising targets to fight this disease is SARS-CoV-2 main protease (Mpro), which has been extensively studied in t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae055efe8e468d82bf310dff97193ff3
https://doi.org/10.1021/acssynbio.1c00368
https://doi.org/10.1021/acssynbio.1c00368
Autor:
João G. N. Sequeira, Filipe E. P. Rodrigues, Telmo G. D. Silva, Pedro B. P. S. Reis, Miguel Machuqueiro
Publikováno v:
The journal of physical chemistry. B. 126(40)
The impact of pH on proteins is significant but often neglected in molecular dynamics simulations. Constant-pH Molecular Dynamics (CpHMD) is the state-of-the-art methodology to deal with these effects. However, it still lacks widespread adoption by t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::189b36b71f1000a34dfd5095a061730b
https://pubmed.ncbi.nlm.nih.gov/36190807
https://pubmed.ncbi.nlm.nih.gov/36190807
Autor:
Filipe E. P. Rodrigues, João N. M. Vitorino, Nuno F. B. Oliveira, Rui J. S. Loureiro, Miguel Machuqueiro, Patrícia F. N. Faísca
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 19, Iss, Pp 5160-5169 (2021)
The D76N mutant of the β 2 m protein is a biologically motivated model system to study protein aggregation. There is strong experimental evidence, supported by molecular simulations, that D76N populates a highly dynamic conformation (which we origin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8731cc82599df95426f713349e03ad5
https://doi.org/10.1016/j.csbj.2021.09.003
https://doi.org/10.1016/j.csbj.2021.09.003
Autor:
Guilherme G. Moreira, António E. N. Ferreira, Guenter Fritz, Ana P. Carapeto, Isabel Cardoso, Filipe E. P. Rodrigues, Cláudio M. Gomes, Mário Rodrigues, Joana S. Cristóvão, Miguel Machuqueiro
Publikováno v:
Chemical Communications. 57:379-382
S100B is an extracellular protein implicated in Alzheimer's Disease and a suppressor of amyloid-β aggregation. Herein we report a mechanism tying Cu2+ binding to a change in assembly state yielding disulfide cross-linked oligomers with higher anti-a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::24337c620f3fffac3ac0a7d6783b1489
https://doi.org/10.1039/d0cc06842j
https://doi.org/10.1039/d0cc06842j
Autor:
Filipe E. P. Rodrigues, Patrícia F. N. Faísca, João N. M. Vitorino, Miguel Machuqueiro, Rui J. S. Loureiro, Nuno F. B. Oliveira
The D76N mutant of the β2m protein is a biologically motivated model system to study protein aggregation. There is strong experimental evidence, supported by molecular simulations, that D76N populates a highly dynamic conformation (which we original
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::70009d9b44474defb4c16b39bfb30add
https://doi.org/10.1101/2021.07.14.452361
https://doi.org/10.1101/2021.07.14.452361
Autor:
Nuno F B, Oliveira, Filipe E P, Rodrigues, João N M, Vitorino, Rui J S, Loureiro, Patrícia F N, Faísca, Miguel, Machuqueiro
Publikováno v:
Computational and Structural Biotechnology Journal
Graphical abstract
Highlights • β2m D76N mutant populates an aggregation-prone monomer (I2) with unstructured termini. • MD and MM-PBSA indicate that I2 dimers are stabilized by hydrophobic interactions. • The termini regions and BC- and
Highlights • β2m D76N mutant populates an aggregation-prone monomer (I2) with unstructured termini. • MD and MM-PBSA indicate that I2 dimers are stabilized by hydrophobic interactions. • The termini regions and BC- and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::12f218f516670d153acafc992fac1732
https://pubmed.ncbi.nlm.nih.gov/34630936
https://pubmed.ncbi.nlm.nih.gov/34630936
Publikováno v:
International Journal of Molecular Sciences
International Journal of Molecular Sciences, Vol 22, Iss 3629, p 3629 (2021)
Volume 22
Issue 7
International Journal of Molecular Sciences, Vol 22, Iss 3629, p 3629 (2021)
Volume 22
Issue 7
S100B is an astrocytic extracellular Ca2+-binding protein implicated in Alzheimer’s disease, whose role as a holdase-type chaperone delaying Aβ42 aggregation and toxicity was recently uncovered. Here, we employ computational biology approaches to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a45183bb91f37d329aae7954177ce80f
http://europepmc.org/articles/PMC8037576
http://europepmc.org/articles/PMC8037576
Autor:
Joana S, Cristóvão, Guilherme G, Moreira, Filipe E P, Rodrigues, Ana P, Carapeto, Mário S, Rodrigues, Isabel, Cardoso, António E N, Ferreira, Miguel, Machuqueiro, Guenter, Fritz, Cláudio M, Gomes
Publikováno v:
Chemical communications (Cambridge, England). 57(3)
S100B is an extracellular protein implicated in Alzheimer's Disease and a suppressor of amyloid-β aggregation. Herein we report a mechanism tying Cu2+ binding to a change in assembly state yielding disulfide cross-linked oligomers with higher anti-a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8afa14e9c60d7e9b0c51f3aa3ef966f0
https://pubmed.ncbi.nlm.nih.gov/33326534
https://pubmed.ncbi.nlm.nih.gov/33326534