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

Enzymatic and Structural Characterization of the Major Endopeptidase in the Venus Flytrap Digestion Fluid

Autor: Ernst Meinjohanns, Marie V. Lukassen, Irene Garcia-Ferrer, Line R. Thomsen, Jan J. Enghild, F. Xavier Gomis-Rüth, Carsten Scavenius, Kristian W. Sanggaard, Tania A. Nielsen, Ida B. Thøgersen, Michael W. Risør, Tibisay Guevara, Litten Sørensen Rossen

Publikováno v: Risor, M W, Thomsen, L R, Sanggaard, K W, Nielsen, T A, Thøgersen, I B, Lukassen, M V, Rossen, L, Garcia-Ferrer, I, Guevara, T, Scavenius, C, Meinjohanns, E, Gomis-Ruth, F X & Enghild, J J 2016, ' Enzymatic and structural characterization of the major endopeptidase in the Venus flytrap digestion fluid ', Journal of Biological Chemistry, vol. 291, pp. 2271-2287 . https://doi.org/10.1074/jbc.M115.672550
Digital.CSIC. Repositorio Institucional del CSIC
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Michael W. Risor et al.
Carnivorous plants primarily use aspartic proteases during digestion of captured prey. In contrast, the major endopeptidases in the digestive fluid of the Venus flytrap (Dionaea muscipula) are cysteine proteases (dionain-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e8e9980bb5602f1b984711648c30df4
https://doi.org/10.1074/jbc.m115.672550

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Autor: Irene, Garcia-Ferrer, Aniebrys, Marrero, F Xavier, Gomis-Rüth, Theodoros, Goulas

Publikováno v: Sub-cellular biochemistry. 83

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Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a24d3f6a60964f11410740fd3ca15d2f
https://pubmed.ncbi.nlm.nih.gov/28271476

Differential inhibition of restriction enzyme cleavage by chromophore-modified analogues of the antitumour antibiotics mithramycin and chromomycin reveals structure–activity relationships

Autor: Sylvia Mansilla, Irene Garcia-Ferrer, José Portugal, Carmen Méndez, José A. Salas

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
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Differential cleavage at three restriction enzyme sites was used to determine the specific binding to DNA of the antitumour antibiotics mithramycin A (MTA), chromomycin A3 (CRO) and six chromophore-modified analogues bearing shorter side chains attac

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9618b9ce509f3c319ff7a514a9ab33de
https://doi.org/10.1016/j.bcp.2010.01.005

Combining phase information in reciprocal space for molecular replacement with partial models

Autor: Claudia Millán, Theodoros Goulas, Massimo Sammito, George M. Sheldrick, Irene Garcia-Ferrer, Isabel Usón

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
instname

© 2015 International Union of Crystallography. ARCIMBOLDO allows ab initio phasing of macromolecular structures below atomic resolution by exploiting the location of small model fragments combined with density modification in a multisolution frame.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ccfc543e49f6228ab43010c8a44236d3
http://hdl.handle.net/10261/123890