Zobrazeno 1 - 10
of 35
pro vyhledávání: '"Manuel Bañó-Polo"'
Autor:
Marina Rius-Salvador, Maria Jesús García-Múrria, Luciana Rusu, Manuel Bañó-Polo, Rubén León, Ron Geller, Ismael Mingarro, Luis Martinez-Gil
Publikováno v:
PLoS ONE, Vol 19, Iss 2, p e0297291 (2024)
BackgroundThe oral cavity is the site of entry and replication for many respiratory viruses. Furthermore, it is the source of droplets and aerosols that facilitate viral transmission. It is thought that appropriate oral hygiene that alters viral infe
Externí odkaz:
https://doaj.org/article/fd6f37fd8c7548c78d5d5cc2a9dd991a
Autor:
Manuel Bañó-Polo, Luis Martínez-Gil, Manuel M. Sánchez del Pino, Alberto Massoli, Ismael Mingarro, Rubén Léon, Maria Jesus Garcia-Murria
Publikováno v:
Journal of Oral Microbiology, Vol 14, Iss 1 (2022)
Background SARS-CoV-2 is continuously disseminating worldwide. The development of strategies to break transmission is mandatory. Aim of the study To investigate the potential of cetylpyridinium chloride (CPC) as a viral inhibitor. Methods SARS-CoV-2
Externí odkaz:
https://doaj.org/article/986436ed09c94f63ad5cf2a601d8b1cf
Autor:
Eva Riveira-Muñoz, Edurne Garcia-Vidal, Manuel Bañó-Polo, Rubén León, Vanessa Blanc, Bonaventura Clotet, Ester Ballana
Publikováno v:
Viruses, Vol 15, Iss 7, p 1433 (2023)
The oral cavity is particularly susceptible to viral infections that are self-recovering in most cases. However, complications may appear in severe cases and/or immunocompromised subjects. Cetylpyridinium chloride (CPC)-containing mouthwashes are abl
Externí odkaz:
https://doaj.org/article/369548407c944a0b83b348f0014a3819
Publikováno v:
ACS Omega, Vol 5, Iss 1, Pp 556-560 (2019)
Externí odkaz:
https://doaj.org/article/6c6bbeb063a549e2ad44b51acb3b3466
Autor:
Manuel Bañó-Polo, Carlos Baeza-Delgado, Silvia Tamborero, Anthony Hazel, Brayan Grau, IngMarie Nilsson, Paul Whitley, James C. Gumbart, Gunnar von Heijne, Ismael Mingarro
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-9 (2018)
Integral membrane proteins are assembled into the ER membrane via the ribosome-translocon channel. Here authors use in vitro translation assays and MD simulations to show that folding in the ribosome is favorable for TM helices, but unfavorable for s
Externí odkaz:
https://doaj.org/article/3c5b89887b174ab79e5d3eb70d8006cc
Autor:
Patrizia Marinelli, Susanna Navarro, Ricardo Graña-Montes, Manuel Bañó-Polo, María Rosario Fernández, Elena Papaleo, Salvador Ventura
Publikováno v:
Redox Biology, Vol 14, Iss , Pp 566-575 (2018)
Oxidatively modified forms of proteins accumulate during aging. Oxidized protein conformers might act as intermediates in the formation of amyloids in age-related disorders. However, it is not known whether this amyloidogenic conversion requires an e
Externí odkaz:
https://doaj.org/article/52f15ab330134b4ca3d418acebb475c1
Autor:
Christina M. Brock, Manuel Bañó-Polo, Maria J. Garcia-Murria, Ismael Mingarro, Maria Esteve-Gasent
Publikováno v:
BMC Microbiology, Vol 17, Iss 1, Pp 1-17 (2017)
Abstract Background The bacterial spirochete Borrelia burgdorferi is the causative agent of the most commonly reported arthropod-borne illness in the United States, Lyme disease. A family of proteins containing von Willebrand Factor A (VWFA) domains
Externí odkaz:
https://doaj.org/article/7d53c685a81f4d8ab56d6f82e275066b
Publikováno v:
ACS Omega, Vol 5, Iss 1, Pp 556-560 (2019)
ACS Omega
ACS Omega
A peptide corresponding to bacteriorhodopsin (bR) helix C, later named pHLIP, inserts across lipid bilayers as a monomeric α-helix at acidic pH, but is an unstructured surface-bound monomer at neutral pH. As a result of such pH-responsiveness, pHLIP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ac9f114855d20515c35153c98d01287
https://doi.org/10.1021/acsomega.9b03126
https://doi.org/10.1021/acsomega.9b03126
Autor:
Manuel Bañó-Polo, Carlos Baeza-Delgado, Mar Orzáez, Marc A Marti-Renom, Concepción Abad, Ismael Mingarro
Publikováno v:
PLoS ONE, Vol 7, Iss 9, p e44263 (2012)
The vast majority of membrane proteins are anchored to biological membranes through hydrophobic α-helices. Sequence analysis of high-resolution membrane protein structures show that ionizable amino acid residues are present in transmembrane (TM) hel
Externí odkaz:
https://doaj.org/article/5e1a8c01d8404c34b9effa12b9e1c187
Combining Structural Aggregation Propensity and Stability Predictions To Redesign Protein Solubility
Autor:
Marcos Gil-Garcia, Salvador Ventura, Michał H. Jamróz, Nathalia Varejão, Sebastian Kmiecik, Manuel Bañó-Polo, Aleksander Kuriata, David Reverter, Marta Díaz-Caballero, Jara Lascorz, Bertrand Morel, Susanna Navarro
Publikováno v:
Molecular Pharmaceutics. 15:3846-3859
The aggregation propensity of each particular protein seems to be shaped by evolution according to its natural abundance in the cell. The production and downstream processing of recombinant polypeptides implies attaining concentrations that are order
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a833ba5fdf751309738fc96b600c763
https://doi.org/10.1021/acs.molpharmaceut.8b00341
https://doi.org/10.1021/acs.molpharmaceut.8b00341