Výsledky vyhledávání - "F.X. Gomis-Ruth"

Structure-based mechanism of cysteine-switch latency and of catalysis by pappalysin-family metallopeptidases

Autor: Miroslaw Ksiazek, Arturo Rodríguez-Banqueri, Jan Potempa, F.X. Gomis-Ruth, Tibisay Guevara

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
instname
IUCrJ, Vol 7, Iss 1, Pp 18-29 (2020)
Digital.CSIC: Repositorio Institucional del CSIC
Consejo Superior de Investigaciones Científicas (CSIC)
IUCrJ

Tannerella forsythia is an oral dysbiotic periodontopathogen involved in severe human periodontal disease. As part of its virulence factor armamentarium, at the site of colonization it secretes mirolysin, a metallopeptidase of the unicellular pappaly

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57cd8b99a7fa67f83b978036f790ef66
http://hdl.handle.net/10261/241436

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Coupling Factors in Macromolecular Type-IV Secretion Machineries

Autor: F de la Cruz, Maria Solà, F.X. Gomis-Ruth, Miquel Coll

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
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Type IV secretion systems (T4SSs) are bacterial multiprotein organelles specialised in the transfer of (nucleo)protein complexes across cell membranes. They are essential for conjugation, bacterial-induced tumour formation in plant cells, as observed

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c908fda5c4cd30668e8be1ca947d3aa
https://doi.org/10.2174/1381612043384817

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Solving a 300 kDa multimeric protein by low-resolution MAD phasing and averaging/phase extension

Autor: F.X. Gomis-Ruth, Miquel Coll

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
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The structure of the conjugative coupling protein TrwBΔN70 from Escherichia coli plasmid R388 was solved using two crystal forms. This large multimeric membrane protein of 437 residues per monomer is involved in cell-to-cell single-strand DNA transf

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d44dd963b2a0690d708ec99f85e1cb9
https://doi.org/10.1107/s0907444901004887

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The bacterial conjugation protein TrwB resembles ring helicases and F1-ATPase

Autor: Rosa Pérez-Luque, Marta Coll, Elena Cabezón, Gabriel Moncalián, F de la Cruz, F.X. Gomis-Ruth, Adolfo González

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
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The transfer of DNA across membranes and between cells is a central biological process; however, its molecular mechanism remains unknown. In prokaryotes, trans-membrane passage by bacterial conjugation, is the main route for horizontal gene transfer.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a1d723f54f01c788630b5382860a3ee
https://doi.org/10.1038/35054586

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Insights into MMP-TIMP Interactions

Autor: Wolfram Bode, F.X. Gomis-Ruth, Hideaki Nagase, Frank Grams, Carlos Fernandez-Catalan, Klaus Maskos, Harald Tschesche

Publikováno v: Annals of the New York Academy of Sciences. 878:73-91

The proteolytic activity of the matrix metalloproteinases (MMPs) involved in extracellular matrix degradation must be precisely regulated by their endogenous protein inhibitors, the tissue inhibitors of metalloproteinases (TIMPs). Disruption of this

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c13008c12f640e75a50494af60be138
https://doi.org/10.1111/j.1749-6632.1999.tb07675.x

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The three-dimensional structure of human RNase 4, unliganded and complexed with d(up), reveals the basis for its uridine selectivity

Autor: F.X. Gomis-Ruth, Miquel Coll, Rosa Peracaula, R. De Llorens, Yoshiaki Tsushima, Simon Terzyan, Hidenori Yamada, Masaharu Seno

Publikováno v: Journal of Molecular Biology. 285:205-214

The RNase 4 family is unique among RNase enzymes, displaying the highest level of sequence similarity and encompassing the shortest polypeptide chain. It is the only one showing high specificity. The human representative is an intracellular and plasm

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::631ad5fef0c1e63dcd1bdc534882a93b
https://doi.org/10.1006/jmbi.1998.2288

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Crystal structure of yellow meal worm α-amylase at 1.64 Å resolution

Autor: Stefan Strobl, F.X. Gomis-Ruth, M. Betz, Georg Wiegand, Rudi Glockshuber, Klaus Maskos, Robert Huber

Publikováno v: Journal of Molecular Biology. 278:617-628

The three-dimensional structure of the alpha-amylase from Tenebrio molitor larvae (TMA) has been determined by molecular replacement techniques using diffraction data of a crystal of space group P212121 (a=51.24 A; b=93.46 A; c=96.95 A). The structur

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e1ed9e32d670c5dc641969b80761c2b7
https://doi.org/10.1006/jmbi.1998.1667

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Structures of adamalysin II with peptidic inhibitors. Implications for the design of tumor necrosis factor α convertase inhibitors

Autor: Edgar F. Meyer, Lawrence F. Kress, V. Politi, F.X. Gomis-Ruth

Publikováno v: Protein Science. 7:283-292

Croralus adamanteus snake venom adamalysin I1 is the structural prototype of the adamalysin or ADAM family comprising proteolytic domains of snake venom metatloproteinases, multimodular mammalian reproductive tract proteins, and tumor necrosis factor

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::8388f9e62f6c0637ca7236a3225c194b
https://doi.org/10.1002/pro.5560070207

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