Zobrazeno 1 - 10 of 41 pro vyhledávání: '"Ana Rosa Viguera"'
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Akademický článek
The Isolation of New Pore-Forming Toxins from the Sea Anemone Actinia fragacea Provides Insights into the Mechanisms of Actinoporin Evolution
Autor: Koldo Morante, Augusto Bellomio, Ana Rosa Viguera, Juan Manuel González-Mañas, Kouhei Tsumoto, Jose M. M. Caaveiro
Publikováno v: Toxins, Vol 11, Iss 7, p 401 (2019)
Random mutations and selective pressure drive protein adaptation to the changing demands of the environment. As a consequence, nature favors the evolution of protein diversity. A group of proteins subject to exceptional environmental stress and known
Externí odkaz: https://doaj.org/article/f1c44771913946f1a4b329d3891bea35
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2
Fine-tuning of the Hsc70-based Human Protein Disaggregase Machinery by the Distinctive C-terminal Extension of Apg2
Autor: Yovana Cabrera, Ganeko Bernardo-Seisdedos, Leire Dublang, David Albesa-Jové, Natalia Orozco, Ana Rosa Viguera, Oscar Millet, Arturo Muga, Fernando Moro
Publikováno v: Journal of molecular biology. 434(22)
Apg2, one of the three cytosolic Hsp110 chaperones in humans, supports reactivation of unordered and ordered protein aggregates by Hsc70 (HspA8). Together with DnaJB1, Apg2 serves to nucleate Hsc70 molecules into sites where productive entropic pulli
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9fec813633b8563d076faa84b6f6930
https://pubmed.ncbi.nlm.nih.gov/36167183
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3
The Isolation of New Pore-Forming Toxins from the Sea Anemone Actinia fragacea Provides Insights into the Mechanisms of Actinoporin Evolution
Autor: Jose M. M. Caaveiro, Augusto Bellomio, Ana Rosa Viguera, Juan Manuel González-Mañas, Koldo Morante, Kouhei Tsumoto
Publikováno v: Toxins, Vol 11, Iss 7, p 401 (2019)
Toxins
Volume 11
Issue 7
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Random mutations and selective pressure drive protein adaptation to the changing demands of the environment. As a consequence, nature favors the evolution of protein diversity. A group of proteins subject to exceptional environmental stress and known
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b3bb51503dfef39f2fe8ca6830617d9
https://www.mdpi.com/2072-6651/11/7/401
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4
Functional characterization of Val60, a key residue involved in the membrane-oligomerization of fragaceatoxin C, an actinoporin fromActinia fragacea
Autor: Koldo Morante, Kouhei Tsumoto, Ana Rosa Viguera, Jose M. M. Caaveiro, Juan Manuel González-Mañas
Publikováno v: FEBS Letters. 589:1840-1846
Actinoporins are pore-forming toxins produced by different sea anemones that self-assemble within the membranes of their target cells and compromise their function as a permeability barrier. The recently published three-dimensional structures of two
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07bbc27414d71ca5dcb4fb881c70dea3
https://doi.org/10.1016/j.febslet.2015.06.012
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5
Purification and characterization of the colicin A immunity protein in detergent micelles
Autor: Marián Alonso-Mariño, Ane Metola, Ana Rosa Viguera, Félix M. Goñi, Lena Mäler, Ana M. Bouchet, Tammo Diercks
Publikováno v: Biochimica et biophysica acta. Biomembranes. 1859(11)
The immunity proteins against pore-forming colicins represent a family of integral membrane proteins that reside in the inner membrane of producing cells. Cai, the colicin A immunity protein, was characterized here in detergent micelles by circular d
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::47415af4f3e65570de4c8025f987829b
https://pubmed.ncbi.nlm.nih.gov/28803731
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6
Membrane Permeabilization Induced by Sphingosine: Effect of Negatively Charged Lipids
Autor: Jesús Sot, Juan C. Gómez-Fernández, Alejandro Torrecillas, Ana Rosa Viguera, Félix M. Goñi, M. Isabel Collado, Alicia Alonso, Noemi Jiménez-Rojo
Publikováno v: Biophysical Journal. 106:2577-2584
Sphingosine [(2S, 3R, 4E)-2-amino-4-octadecen-1, 3-diol] is the most common sphingoid long chain base in sphingolipids. It is the precursor of important cell signaling molecules, such as ceramides. In the last decade it has been shown to act itself a
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd25ac011188a2ed49bf733a214c2c4c
https://doi.org/10.1016/j.bpj.2014.04.038
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7
Par j 1 and Par j 2, the two major allergens in Parietaria judaica, bind preferentially to monoacylated negative lipids
Autor: Juan A. Asturias, Ana Rosa Viguera, Alberto Martínez, R. González‐Rioja, Félix M. Goñi
Publikováno v: FEBS Journal. 276:1762-1775
Par j 1 and Par j 2 proteins are the two major allergens in Parietaria judaica pollen, one of the main causes of allergic diseases in the Mediterranean area. Each of them contains eight cysteine residues organized in a pattern identical to that found
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a54eb85d2c474871fdc900ebc11858ff
https://doi.org/10.1111/j.1742-4658.2009.06911.x
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8
The C-terminal transmembrane domain of human phospholipid scramblase 1 is essential for the protein flip-flop activity and Ca2+-binding
Autor: Ana Rosa Viguera, José Luis R. Arrondo, Lissete Sánchez-Magraner, F.-Xabier Contreras, Nagore Andraka, Diego M. A. Guérin, Félix M. Goñi, Itziar M.D. Posada, Hugo L. Monaco
Human phospholipid scramblase 1 (SCR) is a 318 amino acid protein that was originally described as catalyzing phospholipid transbilayer (flip-flop) motion in plasma membranes in a Ca2+-dependent, ATP-independent way. Further studies have suggested an
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c30ad8275f1996b2714985cf5d34b25
http://hdl.handle.net/11562/663759
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9
Thermodynamic Analysis of α-spectrin SH3 and Two of Its Circular Permutants with Different Loop Lengths: Discerning the Reasons for Rapid Folding in Proteins
Autor: Vladimir V. Filimonov, Ana Rosa Viguera, Jose C. Martínez, Matthias Wilmanns, Pedro L. Mateo, Rita Berisio, Luis Serrano
Publikováno v: Biochemistry. 38:549-559
The temperature dependences of the unfolding-refolding reaction of a shorter version of the alpha-spectrin SH3 domain (PWT) used as a reference and of two circular permutants (with different poly-Gly loop lengths at the newly created fused loop) have
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::768365d071dbcb0752311f464ed68c53
https://doi.org/10.1021/bi981515u
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10
Elucidating the folding problem of α-helices: local motifs, long-range electrostatics, ionic-strength dependence and prediction of NMR parameters 1 1Edited by A. R. Fersht
Autor: Luis Serrano, Ana Rosa Viguera, Emmanuel Lacroix
Publikováno v: Journal of Molecular Biology. 284:173-191
The information about the conformational behavior of monomeric helical peptides in solution, as well as the alpha-helix stability in proteins, has been previously utilized to derive a database with the energy contributions for various interactions ta
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5e95d07f9ac580a63828123010b2af41
https://doi.org/10.1006/jmbi.1998.2145
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