Cellular receptors for mammalian viruses.

Autor: Ana Valero-Rello, Carlos Baeza-Delgado, Iván Andreu-Moreno, Rafael Sanjuán

Publikováno v: PLoS Pathogens, Vol 20, Iss 2, p e1012021 (2024)

The interaction of viral surface components with cellular receptors and other entry factors determines key features of viral infection such as host range, tropism and virulence. Despite intensive research, our understanding of these interactions rema

Externí odkaz: https://doaj.org/article/678c87ff9f2e4811b67d0602fb19204f

Transmembrane but not soluble helices fold inside the ribosome tunnel

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

A practical solution to estimate the sample size required for clinical prediction models generated from observational research on data

Autor: Carlos Baeza-Delgado, Leonor Cerdá Alberich, José Miguel Carot-Sierra, Diana Veiga-Canuto, Blanca Martínez de las Heras, Ben Raza, Luis Martí-Bonmatí

Publikováno v: European radiology experimental. 6(1)

Background Estimating the required sample size is crucial when developing and validating clinical prediction models. However, there is no consensus about how to determine the sample size in such a setting. Here, the goal was to compare available meth

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c7d7d50b46482fcebd115d16047ecf8
https://pubmed.ncbi.nlm.nih.gov/35641659

Biological insertion of computationally designed short transmembrane segments

Autor: Carlos Baeza-Delgado, Marc A. Marti-Renom, Ismael Mingarro, Gunnar von Heijne

Publikováno v: Scientific Reports
Baeza Delgado, Carlos Heijne, Gunnar von Marti-Renom, Marc A. Mingarro Muñoz, Ismael 2016 Biological insertion of computationally designed short transmembrane segments Scientific Reports 6 23397 1 9
RODERIC. Repositorio Institucional de la Universitat de Valéncia
instname

The great majority of helical membrane proteins are inserted co-translationally into the ER membrane through a continuous ribosome-translocon channel. The efficiency of membrane insertion depends on transmembrane (TM) helix amino acid composition, th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4422288e00d96427d2428b60b67d5076
http://europepmc.org/articles/PMC4796907

Polar/Ionizable Residues in Transmembrane Segments: Effects on Helix-Helix Packing

Autor: Ismael Mingarro, Marc A. Marti-Renom, Manuel Bañó-Polo, Carlos Baeza-Delgado, Concepción Abad, Mar Orzáez

Publikováno v: Plos One
r-CIPF. Repositorio Institucional Producción Científica del Centro de Investigación Principe Felipe (CIPF)
instname
Bañó Polo, Manuel Baeza Delgado, Carlos Orzáez Calatayud, María del Mar Marti Renom, Marc Abad Mazario, Concepción Mingarro Muñoz, Ismael 2012 Polar/Ionizable Residues in Transmembrane Segments: Effects on Helix-Helix Packing Plos One 7 9 e44263
PLoS ONE, Vol 7, Iss 9, p e44263 (2012)
r-CIPF: Repositorio Institucional Producción Científica del Centro de Investigación Principe Felipe (CIPF)
Centro de Investigación Principe Felipe (CIPF)
RODERIC. Repositorio Institucional de la Universitat de Valéncia
PLoS ONE

The vast majority of membrane proteins are anchored to biological membranes through hydrophobic alpha-helices. Sequence analysis of high-resolution membrane protein structures show that ionizable amino acid residues are present in transmembrane (TM)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fed59d6bc74b1e8290b0cf878104bec1
https://fundanet.cipf.es/Publicaciones/ProdCientif/PublicacionFrw.aspx?id=2109