Zobrazeno 1 - 10 of 56 pro vyhledávání: '"Joan L. Arolas"'
1
A unique network of attack, defence and competence on the outer membrane of the periodontitis pathogen Tannerella forsythia
Autor: Mirosław Książek, Theodoros Goulas, Danuta Mizgalska, Arturo Rodríguez-Banqueri, Ulrich Eckhard, Florian Veillard, Irena Waligórska, Małgorzata Benedyk-Machaczka, Alicja M. Sochaj-Gregorczyk, Mariusz Madej, Ida B. Thøgersen, Jan J. Enghild, Anna Cuppari, Joan L. Arolas, Iñaki de Diego, Mar López-Pelegrín, Irene Garcia-Ferrer, Tibisay Guevara, Vincent Dive, Marie-Louise Zani, Thierry Moreau, Jan Potempa, F. Xavier Gomis-Rüth
Publikováno v: Chemical Science
Chemical Science, 2023, 14 (4), pp.869-888. ⟨10.1039/d2sc04166a⟩
Książek, M, Goulas, T, Mizgalska, D, Rodríguez-Banqueri, A, Eckhard, U, Veillard, F, Waligórska, I, Benedyk-Machaczka, M, Sochaj-Gregorczyk, A M, Madej, M, Thøgersen, I B, Enghild, J J, Cuppari, A, Arolas, J L, de Diego, I, López-Pelegrín, M, Garcia-Ferrer, I, Guevara, T, Dive, V, Zani, M L, Moreau, T, Potempa, J & Gomis-Rüth, F X 2023, ' A unique network of attack, defence and competence on the outer membrane of the periodontitis pathogen Tannerella forsythia ', Chemical Science, vol. 14, no. 4, pp. 869-888 . https://doi.org/10.1039/d2sc04166a
Periodontopathogenic Tannerella forsythia uniquely secretes six peptidases of disparate catalytic classes and families that operate as virulence factors during infection of the gums, the KLIKK-peptidases. Their coding genes are immediately downstream
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7698e6876d479a7bef16c93ae86818e9
https://ruj.uj.edu.pl/xmlui/handle/item/308078
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2
Akademický článek
The pCri System: a vector collection for recombinant protein expression and purification.
Autor: Theodoros Goulas, Anna Cuppari, Raquel Garcia-Castellanos, Scott Snipas, Rudi Glockshuber, Joan L Arolas, F Xavier Gomis-Rüth
Publikováno v: PLoS ONE, Vol 9, Iss 11, p e112643 (2014)
A major bottleneck in structural, biochemical and biophysical studies of proteins is the need for large amounts of pure homogenous material, which is generally obtained by recombinant overexpression. Here we introduce a vector collection, the pCri Sy
Externí odkaz: https://doaj.org/article/f2488450042447068930619d6eaab567
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3
Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin
Autor: Ariadna Rodriguez Chamorro, Andrea Ghisleni, Pierantonio Doto, Eneda Hollerl, Borja Mateos, Wiktor Kozminski, Robert Konrat, Kristina Djinović-Carugo, Miriam Pedron, Dmitri I. Svergun, Friedel Drepper, Anna Zawadzka-Kazimierczuk, Julius Kostan, Bettina Warscheid, Bojan Zagrovic, Georgine Faulkner, Claudia Schreiner, Joan L. Arolas, G. Mlynek, Euripedes de Almeida Ribeiro, Thomas Peterbauer, Cy M. Jeffries, Antonio Sponga, Leonhard Geist, Anton A. Polyansky, Mathias Gautel, Thomas C. Schwarz
Publikováno v: Science Advances
Science advances 7(22), eabg7653-(2021). doi:10.1126/sciadv.abg7653
'Science Advances ', vol: 7, pages: eabg7653-1-eabg7653-20 (2021)
Science advances 7(22), eabg7653 - (2021). doi:10.1126/sciadv.abg7653
In sarcomeres, α-actinin cross-links actin filaments and anchors them to the Z-disk. FATZ (filamin-, α-actinin-, and telethonin-binding protein of the Z-disk) proteins inter
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6df15fcff097138a51c1137346fd138
http://europepmc.org/articles/PMC8163081
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4
Calcium modulates the domain flexibility and function of an α-actinin similar to the ancestral α-actinin
Autor: Thomas C. Marlovits, Joan L. Arolas, Claudia Schreiner, Euripedes de Almeida Ribeiro, Anita Salmazo, Eirini A. Gkougkoulia, Kristina Djinović-Carugo, Julius Kostan, Alok Bhattacharya, Karolina Zielinska, Luciano Ciccarelli, Martin Puchinger, Mrigya Babuta, Muhammad Bashir Khan, Nikos Pinotsis
Publikováno v: Proc Natl Acad Sci U S A
The actin cytoskeleton, a dynamic network of actin filaments and associated F-actin–binding proteins, is fundamentally important in eukaryotes. α-Actinins are major F-actin bundlers that are inhibited by Ca(2+) in nonmuscle cells. Here we report t
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97abbd845a59cb5cc5eb265ba92d6d99
https://pubmed.ncbi.nlm.nih.gov/32848067
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5
Multiple Architectures and Mechanisms of Latency in Metallopeptidase Zymogens
Autor: F. Xavier Gomis-Rüth, Anna Cuppari, Joan L. Arolas, Theodoros Goulas
Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
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Metallopeptidases cleave polypeptides bound in the active-site cleft of catalytic domains through a general base/acid mechanism. This involves a solvent molecule bound to a catalytic zinc and general regulation of the mechanism through zymogen-based
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80d701a763227374236731576b22a6bc
https://doi.org/10.1021/acs.chemrev.8b00030
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8
Expression and purification of integral membrane metallopeptidase HtpX
Autor: Joan L. Arolas, F. Xavier Gomis-Rüth, Yoshinori Akiyama, Theodoros Goulas, Raquel García-Castellanos
Publikováno v: Protein Expression and Purification
Protein Expression and Purification; Vol 99
Digital.CSIC. Repositorio Institucional del CSIC
instname
Little is known about the catalytic mechanism of integral membrane (IM) peptidases. HtpX is an IM metallopeptidase that plays a central role in protein quality control by preventing the accumulation of misfolded proteins in the membrane. Here we repo
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d9e1ff86ff35acb6903523f0f13428e
https://doi.org/10.1016/j.pep.2014.04.008
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