Lab presentation
The work carried out in the Proteolysis Lab is centred on the analysis of the molecular determinants of function and regulation of proteolysis at the protein level. We study peptidases and their zymogens, mostly from host-microbiome interactions, as well as their complexes with small-molecule and protein inhibitors. Another line of research deals with the molecular analysis of other interaction mediators between animal hosts and their microbiomes. Employed techniques include molecular biology, biochemistry, biophysics, and X-ray crystallography, among others. Our lab is fully furnished with state-of-the-art equipment, which enables us to carry out cutting-edge science projects.
One recent project has focused on coeliac disease (CoD), a chronic autoimmune enteropathy that affects individuals with genetic and environmental sensitization to dietary gluten, namely a group of cereal prolamin storage proteins rich in proline and glutamine. Prolamins that trigger CoD include gliadin and glutenin in wheat, hordein in barley, and secalin in rye. Intestinal damage is inflicted by as little as ~10 mg of dietary gluten per day, which is <0.1% of the amount found in a typical western diet. CoD is a global health burden across all age ranges, with a worldwide serological prevalence of 1.4% that increases by 7.5% every year.
The disease is caused by partially degraded gluten peptides, which are immunogenic and include a 33-residue fragment of wheat α-gliadin (33-mer) that is kind of a standard in the field. These peptides resist further cleavage by digestive peptidases owing to their high proline content. In coeliacs, they cross the mucosal epithelium of the small intestine, where glutamine residues are deamidated by tissue transglutaminase. This enhances the affinity of the peptides for particular alleles of the human leukocyte antigen receptor, which are a requisite for the development of CoD. Receptor binding triggers a severe pro-inflammatory autoimmune response mediated by T cells, with resulting intestinal phenotypes including intraepithelial lymphocytosis, crypt hyperplasia, atrophy of small-intestine villi and mucosal inflammation. These lead, in turn, to the chronic malabsorption of nutrients, diarrhoea, vomiting, bloating, abdominal pain and intestinal lymphomas. Moreover, there are extra-intestinal manifestations, which include delayed puberty, osteoporosis, axonal neuropathy and cerebellar ataxia. Overall, CoD patients face a reduced life expectancy.
Currently, there is no treatment for CoD, so patients must adhere to a lifelong strict gluten-free diet, which restores the normal architecture of the intestinal villi. However, gluten-free diets do not provide balanced nutrition, and many coeliacs suffer intestinal symptoms even with adherence to such dietary restrictions. Moreover, gluten is found in most processed foods and medicines, making dietary compliance challenging in western societies. This has created a demand for effective CoD therapies.
One promising approach is the development of endopeptidases that cleave the immunogenic gluten peptides and would thus act as bona fide glutenases for oral enzyme therapy, reminiscent of lactase tablets for lactose intolerance. Such an approach would also benefit patients suffering from non-coeliac gluten sensitivity, which has a worldwide prevalence of up to 13%, and irritable bowel syndrome, with a prevalence of ~0.5%. A candidate glutenase must fulfil stringent criteria for clinical application. First, it should work in the stomach during digestion, before the gastric bolus passes into the duodenum and initiates the autoimmune response, and thus must remain stable and active in the acidic gastric environment (pH ~2.5) as well as resisting gastric pepsin. Second, a reasonable dose should efficiently digest gliadin and the immunogenic gluten peptides when combined with pepsin under gastric conditions, which requires the processing of large quantities of dietary protein. Third, it should not harm intestinal structures or inhibit nutrient absorption, and thus ideally should be inactive at the slightly acidic postprandial pH of the duodenum.
Recently, in a collaboration with the Synthetic Structural Biology group headed by Ulrich Eckhard within the institute and the group of Francisco José Pérez Cano from the Faculty of Pharmacy and Food Science of the University of Barcelona, we studied neprosin, a peptidase from a carnivorous pitcher plant, as a potential glutenase for therapy in CoD based on previous pioneering work by the group of David Schriemer from the University of Calgary in Canada (https://profiles.ucalgary.ca/david-schriemer). He hypothesized neprosin might have a function in protein metabolism during prey digestion and/or defence. In combination with other peptidases from the digestive fluid, neprosin was further identified as part of a potential glutenase preparation. Finally, purified neprosin was also considered a useful reagent for proteomics.
We established an efficient human recombinant production system to produce high yields of pure neprosin in human cells. We determined that neprosin is a new member of the glutamate peptidase class, with two unique glutamate residues acting as a catalytic dyad, which is distantly reminiscent of the two aspartates of acid peptidases. Moreover, we reported the crystal structure of the neprosin zymogen and its mature form in product-mimicking complexes. In this way, we further unveiled the molecular determinants of latency, its mechanism of activation, as well as its thermal stability, pH profile, general proteolytic and peptidolytic activities, and susceptibility to a panel of peptidase inhibitors. We also tested cleavage of gliadin and the 33-mer in vitro to evaluate the ability of neprosin to act as a solo glutenase. Moreover, we evaluated the effect in mice and found that co-administration of gliadin and the neprosin zymogen at the ratio 500:1 reduced the abundance of the immunogenic gluten peptides in the small intestine by up to 90%. Neprosin therefore founds a family of eukaryotic glutamate endopeptidases that a priori fulfils requisites for a therapeutic glutenase.
Read the whole story freely under https://www.nature.com/articles/s41467-022-32215-1.
Lab people
F. Xavier Gomis Ruth
Dr. Gomis-Rüth is the head of Proteolysis Laboratory at the Institute of Molecular Biology of Barcelona (IBMB) and is presently Director of the Department of Structural Biology.
Dr. Gomis-Rüth graduated in chemical engineering (1989) by the Institut Químic de Sarrià, Universitat Ramon Llull, of Barcelona. In 1989-1992, he worked in protein crystallography, mainly on proteolytic enzymes, under the supervision of W. Bode and R. Huber, Nobel Prize for Chemistry in 1988, at the Max-Planck Institute of Biochemistry (MPIB) in Martinsried (Germany). In 1992 he obtained a PhD from the Ludwig-Maximilian University of Munich (Germany), and, at the end of 1992, he moved to Barcelona to continue working in structural biochemistry and biophysics of proteases with F.X. Avilés at the Universitat Autònoma de Barcelona. During this time, he held EMBO and Marie Curie long-term fellowships. In 1995-1996, he worked again at the MPIB, and, in 1997, he joined the group of M. Coll of the Spanish Research Council (CSIC). He became tenured scientific collaborator of CSIC in 1999 and set up his own laboratory. In 2004, he became research scientist and in 2008 he became full professor.
A detailed CV can be obtained here.
Tibisay Guevara Puig
Soraia dos Reis Mendes
Arturo Rodríguez Banqueri
Juan Sebastián Ramírez Larrota
Elisabeth Subirats
Past students
Selected publications
S. Trillo-Muyo, S. Martínez-Rodríguez, J.L. Arolas & F.X. Gomis-Rüth * (2013). Mechanism of action of a Janus-faced single-domain protein inhibitor simultaneously targeting two peptidase classes. Chem. Sci., 4, 791-797
D. Luque, T. Goulas, C.P. Mata, S.R. Mendes, F.X. Gomis-Rüth * & J.R. Castón (2022). Cryo-EM structures shows the mechanistic basis of pan-peptidase inhibition by human α2-macroglobulin. Proc. Natl. Acad. Sci. USA, 119, e2200102119.
L. del Amo-Maestro, S.R. Mendes, A. Rodríguez-Banqueri, L. Garzon-Flores, M. Girbal, M.J. Rodríguez-Lagunas, T. Guevara, A. Franch, F.J. Pérez-Cano, U. Eckhard & F.X. Gomis-Rüth * (2022). Molecular and in vivo studies of a glutamate-class prolyl-endopeptidase for coeliac disease therapy. Nat. Commun., 13, 4446. Press release from the institution: https://www.csic.es/es/actualidad-del-csic/identifican-una-molecula-que-podria-servir-para-tratar-la-celiaquia.Wide coverage in Catalan, Galician, Basque and Spanish online, audiovisual and printed media, including “Diari de Girona”, “La Voz de Galicia”, “Segre”, “El Progreso”, “La Vanguardia”, “Cambio 16”, “Diario de Jerez”, “Diario de Cádiz”, “Diario de Sevilla”, “El Mundo Deportivo”, “Sport”, “El Periódico de Aragón”, “Diario de Mallorca”, “Diario de Ibiza”, “El Periódico”, “RTVE”, ”LaSexta”, ”TeleMadrid”, “EFE”, etc. Radio interview for “Onda Cero” (Madrid, Spain). Highlighted in Quickcuts, the official publication of the International Proteolysis Society (https://www.protease.org/QuickCuts/QuickCuts_2022_November.pdf).
T.M. Chidyausiku, S.R. Mendes, J.C. Klima, M. Nadal, U. Eckhard, J. Roel-Touris, S. Houliston, T. Guevara, H.K. Haddox, A. Moyer, C.H. Arrowsmith, F.X. Gomis-Rüth *, D. Baker & E. Marcos (2022). De novo design of immunoglobulin-like domains. Nat. Commun., 13, 5661
M. Książek, T. Goulas, D. Mizgalska, A. Rodríguez-Banqueri, U. Eckhard, F. Veillard, I. Waligórska, M. Benedyk-Machaczka, A.M. Sochaj-Gregorczyk, M. Madej, I.B. Thøgersen, J.J. Enghild, A. Cuppari, J.L. Arolas, I. de Diego, M. López-Pelegrín, I. Garcia-Ferrer, T. Guevara, V. Dive, M.L. Zani, T. Moreau, J. Potempa&F.X. Gomis-Rüth * (2023). A unique network of attack, defence and competence on the outer membrane of the periodontitis pathogen Tannerella forsythia. Chem. Sci., 14, 869-888. Press release form the institution (www.csic.es/es/actualidad-del-csic/un-estudio-del-csic-aporta-nuevas-pistas-sobre-las-causas-de-la-periodontitis)and highlight in “Butlletí CSIC a Catalunya”, Vol 175, 30.1.2023–5.2.2023 (delegacion.catalunya.csic.es/un-trabajo-del-csic-aporta-nuevas-pistas-sobre-las-causas-de-la-periodontitis/?lang=ca).
Intermolecular latency regulates the essential C-terminal signal peptidase and sortase of the P. gingivalis Type-IX Secretion System.
D. Mizgalska, T. Goulas, A. Rodríguez-Banqueri, F. Veillard, M. Madej, E. Małecka, K. Szczesniak, M. Ksiazek, M. Widziołek, T. Guevara, U. Eckhard, M. Solà, J. Potempa & F.X. Gomis-Rüth * (2021). Proc. Natl. Acad. Sci. USA, 118, e2103573118. ( Wide coverage in Catalan and Spanish online and printed media, including “Diari de Girona”, “El Periódico de Catalunya”, “La Vanguardia”, “La República”, “Diario Médico”, “MSN”, as well as through a radio interview (Radio Ecca; Canary Islands) and a notice in “El Dentista Moderno” (https://www.eldentistamoderno.com/file/view/28575#bn/1 page 72 )
The crystal structure of a 250-kDa heterotetrameric particle explains inhibition of sheddase meprin β by endogenous fetuin-B.
Eckhard, H. Körschgen, N. von Wiegen, W. Stöcker & F.X. Gomis-Rüth
Proc. Natl. Acad. Sci. USA, 118(14):e2023839118. (2021)
Multiple architectures and mechanisms of latency in metallopeptidase zymogens
J.L. Arolas, T. Goulas, A. Cuppari & F.X. Gomis-Rüth
Chem. Rev., 118, 5581-5597. (2018)
Structural and functional insights into Escherichia coli α2-macroglobulin endopeptidase snap-trap inhibition.
I. Garcia-Ferrer, P. Arêde, J. Gómez-Blanco, D. Luque, S. Duquerroy, J.R. Castón, T. Goulas & F.X. Gomis-Rüth.
Proc. Natl. Acad. Sci. USA , 112, 8290-8295 (2015)
(highlighted by the Spanish Biophysical Society as one of four Papers of the Month by SBE Members in July; Biofísica Magazine, issue #2, May-August 2015, http://biofisica.info/garcia-ferrer-gomis-ruth-pnas-112-8290/; selected by the Spanish Society of Biochemistry and Molecular Biology as The Article of the Month, January 2016, https://revista.sebbm.es).
LysargiNase mirrors trypsin for identification of protein C-termini and methylation sites.
P.F. Huesgen, P.F. Lange, L.D. Rogers, N. Solis, U. Eckhard, O. Kleifeld, T. Goulas, F.X. Gomis-Rüth & C.M. Overall
Nat. Meth., 2015. 12, 55-58. (2015)
Multiple stable conformations account for reversible concentration-depedent oligomerization and autoinhibition of a metamorphic metallopeptidase.
López-Pelegrín, M. Cerdà-Costa, A. Cintas-Pedrola, F. Herranz-Trillo, P. Bernadó, J.R. Peinado, J.L. Arolas & F.X. Gomis-Rüth.
Angew. Chem. Int. Ed., 53, 10624-10630 (2014)
(chosen for the frontispiece of the section on communications).
Structural basis for the sheddase function of human meprin β metalloproteinase at the plasma membrane.
J.L. Arolas, C. Broder, T. Jefferson, T. Guevara, E.E. Sterchi, W. Bode, W. Stöcker, C. Becker-Pauly & F.X. Gomis-Rüth.
Proc. Natl. Acad. Sci. USA, 109, 16131-16136. (2012)
The crystal structure of human α2-macroglobulin reveals a unique molecular cage.
Marrero, S. Duquerroy, S. Trapani, T. Goulas, T. Guevara, G.R. Andersen, J. Navaza, L. Sottrup-Jensen & F.X. Gomis-Rüth.
Angew. Chem. Int. Ed., 51, 3340-3344 (2012)
(chosen by the journal as a Very Important Paper and for the issue cover; comment in C. Meyer, W. Hinrichs & U. Hahn, Human α2-macroglobulin–another variation on the venus flytrap, Angew. Chem. Int. Ed., 51, 5045-5047).
Structural evidence for standard-mechanism inhibition in metallopeptidases from a complex poised to re-synthesize a peptide bond.
J.L. Arolas, T.O. Botelho, A. Vilcinskas & F.X. Gomis-Rüth. (2011)
Angew. Chem. Int. Ed., 50, 10357-10360.
Structure, function and latency regulation of a bacterial enterotoxin potentially derived from a mammalian adamalysin/ADAM xenolog.
T. Goulas, J.L. Arolas & F.X. Gomis-Rüth
Proc. Natl. Acad. Sci. USA, 108, 1856-1861. (2011)
Plasmid replication initiator RepB forms a hexamer reminiscent of ring helicases and has mobile nuclease domains.
D.R. Boer, J.A. Ruíz-Masó, J.R. López-Blanco, A.G. Blanco, M. Vives-Llàcer, P. Chacón, I. Usón, F. X. Gomis-Rüth, M. Espinosa, O. Llorca, G. del Solar & M. Coll
EMBO J., 28(11):1666-78 (2009)
Macrophage elastase (MMP-12) kills bacteria within murine macrophages.
A.M. Houghton, W.O. Hartzell, C.S. Robbins, F.X. Gomis-Rüth & S.D. Shapiro.
Nature, 460, 637-641. (2009)
Mammalian metallopeptidase inhibition at the defense barrier of Ascaris parasite.
L. Sanglas, F.X. Avilés, R. Huber, F.X. Gomis-Rüth & J.L. Arolas.
Proc. Natl. Acad. Sci. USA, 106, 1743-1747. (2009)
Unique structure and stability of HmuY, a novel heme-binding protein of Porphyromonas gingivalis.
H. Wójtowicz, T. Guevara, C. Tallant, M. Olczak, A. Sroka, J. Potempa, M. Solà, T. Olczak & F. X. Gomis-Rüth
PLoS Pathog., 5, e1000419. (2009)
Structure of activated thrombin-activatable fibrinolysis inhibitor, a molecular link between coagulation and fibrinolysis.
Sanglas, Z. Valnickova, J.L. Arolas, I. Pallarés, T. Guevara, M. Solà, T. Kristensen, J.J. Enghild, F.X. Avilés & F.X. Gomis-Rüth.
Mol. Cell, 31, 598-606. (2008)
Structure of human carboxypeptidase A4 with its endogenous protein inhibitor, latexin.
I. Pallarés, R. Bonet, R. García-Castellanos, S. Ventura, F.X. Avilés, J. Vendrell & F.X. Gomis-Rüth
Proc. Natl. Acad. Sci. USA, 102, 3978-3983. (2005)
Recognition and processing of the origin of transfer DNA by conjugative relaxase TrwC.
A. Guasch, M. Lucas, M. Cabezas, R. Pérez-Luque, F.X. Gomis-Rüth, F. de la Cruz & M. Coll
Nat. Struct. Biol., 10, 1002-1010. (2003)
The bacterial conjugation protein TrwB resembles ring helicases and F1-ATPase
F.X. Gomis-Rüth, G. Moncalián, R. Pérez-Luque, A. González, E. Cabezón, F. de la Cruz & M. Coll.
Nature, 409, 637-641. (2001)
Crystal structure of avian carboxypeptidase D domain II: a prototype for the regulatory metallocarboxypeptidase family.
F.X. Gomis-Rüth, V. Companys, Y. Qian, L.D. Fricker, J. Vendrell, F.X. Avilés & M. Coll
EMBO J., 18, 5817-5826. (1999)
Structure of proline iminopeptidase from Xanthomonas campestris pv. citri : a prototype for the prolyl oligopeptidase family.
F.J. Medrano, J. Alonso, J.L. García, A. Romero, W. Bode & F.X. Gomis-Rüth
EMBO J., 17, 1-9. (1998)
The structure of plasmid-encoded transcriptional repressor CopG, unliganded and bound to its operator.
F.X. Gomis-Rüth, M. Solà, P. Acebo, A. Párraga, A. Guasch, R. Eritja, A. González, M. Espinosa, G. del Solar & M. Coll
EMBO J., 17, 7404-7415. (1998)
Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1.
F.X. Gomis-Rüth, K. Maskos, M. Betz, A. Bergner, R. Huber, K. Suzuki, N. Yoshida, H. Nagase, K. Brew, G.P. Bourenkov, H. Bartunik & W. Bode.
Nature, 389, 77-81. (1997)
The three-dimensional structure of the native ternary complex of bovine pancreatic procarboxypeptidase A with proproteinase E and chymotrypsinogen C.
F. X. Gomis-Rüth, M. Gómez, W. Bode, R. Huber & F. X. Avilés
EMBO J., 14, 4387-4394. (1995)
Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d).
D. Zhang, I. Bothos, F.X. Gomis-Rüth, R. Doll, C. Blood, F.G. Njoroge, J.W. Fox, W. Bode & E.F. Meyer
Proc. Natl. Acad. Sci. USA, 91, 8447-8451. (1994)
First structure of a snake venom metalloproteinase: a prototype for matrix metalloproteinases/
F.X. Gomis-Rüth, L.F. Kress & W. Bode
EMBO J., 12, 4151-4157. (1993)
Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases.
W. Bode, F.X. Gomis-Rüth, R. Huber, R. Zwilling & W. Stöcker
Nature, 358, 164-167. (1992)
All publications
R. Caliandro, I. de Diego & F.X. Gomis-Rüth * (2022). Crystal structure report of the ImmR transcriptional regulator DNA-binding domain of the Bacillus subtilis ICEBs1 transposon. Sci. Rep., 12, 5258.
A. Jiménez-Alesanco, U. Eckhard, M. Asencio del Río, S. Vega, T. Guevara, A. Vázquez-Campoy, F.X. Gomis-Rüth * & O. Abián (2022). Repositioning small molecule drugs as allosteric inhibitors of the BFT-3 toxin from enterotoxigenic Bacteroides fragilis. Prot. Sci., 31, e4427
T.M. Chidyausiku, S.R. Mendes, J.C. Klima, M. Nadal, U. Eckhard, J. Roel-Touris, S. Houliston, T. Guevara, H.K. Haddox, A. Moyer, C.H. Arrowsmith, F.X. Gomis-Rüth *, D. Baker & E. Marcos (2022). De novo design of immunoglobulin-like domains. Nat. Commun., 13, 5661
T. Guevara, A. Rodríguez-Banqueri, W. Stöcker, C. Becker-Pauly & F.X. Gomis-Rüth * (2022). Zymogenic latency in a ~250-million-year-old astacin metallopeptidase. Acta Crystallgr., D78, 1347-1357
L. del Amo-Maestro, S.R. Mendes, A. Rodríguez-Banqueri, L. Garzon-Flores, M. Girbal, M.J. Rodríguez-Lagunas, T. Guevara, A. Franch, F.J. Pérez-Cano, U. Eckhard & F.X. Gomis-Rüth * (2022). Molecular and in vivo studies of a glutamate-class prolyl-endopeptidase for coeliac disease therapy. Nat. Commun., 13, 4446. Press release from the institution: https://www.csic.es/es/actualidad-del-csic/identifican-una-molecula-que-podria-servir-para-tratar-la-celiaquia.Wide coverage in Catalan, Galician, Basque and Spanish online, audiovisual and printed media, including “Diari de Girona”, “La Voz de Galicia”, “Segre”, “El Progreso”, “La Vanguardia”, “Cambio 16”, “Diario de Jerez”, “Diario de Cádiz”, “Diario de Sevilla”, “El Mundo Deportivo”, “Sport”, “El Periódico de Aragón”, “Diario de Mallorca”, “Diario de Ibiza”, “El Periódico”, “RTVE”, ”LaSexta”, ”TeleMadrid”, “EFE”, etc. Radio interview for “Onda Cero” (Madrid, Spain). Highlighted in Quickcuts, the official publication of the International Proteolysis Society (https://www.protease.org/QuickCuts/QuickCuts_2022_November.pdf)
F.X. Gomis-Rüth * & W. Stöcker (2023). Structural and evolutionary insights into astacin metallopeptidases. Front. Molec. Biosci., 9, 1080836.
D. Luque, T. Goulas, C.P. Mata, S.R. Mendes, F.X. Gomis-Rüth * & J.R. Castón (2022). Cryo-EM structures shows the mechanistic basis of pan-peptidase inhibition by human α2-macroglobulin. Proc. Natl. Acad. Sci. USA, 119, e2200102119
A. Rodríguez-Banqueri, M. Moliner-Culubret, S.R. Mendes, T. Guevara, U. Eckhard & F.X. Gomis-Rüth * (2023). Structural insights into latency of the metallopeptidase ulilysin (lysargiNase) and its unexpected inhibition by a sulfonyl-fluoride inhibitor of serine peptidases. Dalton Trans., 52, 3610-3622. Selected for the quarterly HOT article collection, which represents the top 10% of research published in the journal (https://pubs.rsc.org/en/journals/articlecollectionlanding?sercode=dt&themeid=2a26afe9-b42c-440b-a3d4-d1e001db330d).
S.R. Mendes, F.X. Gomis-Rüth * & T. Goulas (2023). Frozen fresh blood plasma preserves the functionality of native human α2-macroglobulin. Sci. Rep., 13, 4579.
Książek, T. Goulas, D. Mizgalska, A. Rodríguez-Banqueri, U. Eckhard, F. Veillard, I. Waligórska, M. Benedyk-Machaczka, A.M. Sochaj-Gregorczyk, M. Madej, I.B. Thøgersen, J.J. Enghild, A. Cuppari, J.L. Arolas, I. de Diego, M. López-Pelegrín, I. Garcia-Ferrer, T. Guevara, V. Dive, M.L. Zani, T. Moreau, J. Potempa & F.X. Gomis-Rüth * (2023). A unique network of attack, defence and competence on the outer membrane of the periodontitis pathogen Tannerella forsythia. Chem. Sci., 14, 869-888. doi: 10.1039/D2SC04166A
S.R. Mendes, U. Eckhard, A. Rodríguez-Banqueri, T. Guevara, P. Czermak, E. Marcos, A. Vilcinskas & F. Xavier Gomis-Rüth * (2022). An engineered protein-based submicromolar competitive inhibitor of the Staphylococcus aureus virulence factor aureolysin. Comp. Struct. Biotechnol. J., 20, 534-544.
D. Mizgalska, T. Goulas, A. Rodríguez-Banqueri, F. Veillard, M. Madej, E. Małecka, K. Szczesniak, M. Ksiazek, M. Widziołek, T. Guevara, U. Eckhard, M. Solà, J. Potempa & F.X. Gomis-Rüth * (2021). Proc. Natl. Acad. Sci. USA, 118, e2103573118. ( Wide coverage in Catalan and Spanish online and printed media, including “Diari de Girona”, “El Periódico de Catalunya”, “La Vanguardia”, “La República”, “Diario Médico”, “MSN”, as well as through a radio interview (Radio Ecca; Canary Islands) and a notice in “El Dentista Moderno” (https://www.eldentistamoderno.com/file/view/28575#bn/1 page 72 )
Eckhard, H. Körschgen, N. von Wiegen, W. Stöcker & F.X. Gomis-Rüth
Proc. Natl. Acad. Sci. USA, 118(14):e2023839118. (2021)
Del Amo-Maestro L, A. Sagar, P. Pompach, T. Goulas, C. Scavenius, D.S. Ferrero, M. Castrillo-Briceño, M. Taulés, J.J. Enghild, P. Bernadó & F.X. Gomis-Rüth.
Mol. Biol., 433(13):166954. (2021)
Madej, Z. Nowakowska, M. Ksiazek, A.M. Lasica, D. Mizgalska, M. Nowak, A. Jacula, M. Bzowska, C. Scavenius, J.J. Enghild, J. Aduse-Opoku, M.A. Curtis, F.X. Gomis-Rüth & J. Potempa.
mBio, 12(1):e02262-20. (2021)
S.R. Mendes, L. Del Amo-Maestro, L. Marino-Puertas, I. Diego, T. Goulas & F.X. Gomis-Rüth.
Sci. Rep., 10(1):6317. (2020)
Guevara, A. Rodriguez-Banqueri, M. Ksiazek, J. Potempa & Gomis-Rüth FX.
IUCrJ, 7(Pt 1):18-29. (2020)
Guevara, H. Körschgen, A. Cuppari, C. Schmitz, M. Kuske, I. Yiallouros, J. Floehr, W. Jahnen-Dechent, W. Stöcker & F.X. Gomis-Rüth.
Sci. Rep., 9(1):14683. (2019)
G. Bereta, T. Goulas, M. Madej, E. Bielecka, M. Solà, J. Potempa & F.X. Gomis-Rüth
Prot. Sci. 28, 478-486 (2019) (highlighted at the front of the issue under https://onlinelibrary.wiley.
Marino-Puertas L, Del Amo-Maestro L, Taulés M, Gomis-Rüth FX, Goulas T.
Sci Rep. 24;9(1):9186. (2019)
Del Amo-Maestro L, Marino-Puertas L, Goulas T, Gomis-Rüth FX.
Sci Rep. 17;9(1):8660 (2019)
Guevara T, Rodríguez-Banqueri A, Lasica AM, Ksiazek M, Potempa BA, Potempa J, Gomis-Rüth FX.
Sci Rep. 20;9(1):4935. (2019)
Structure of mammalian plasma fetuin-B and its mechanism of selective metallopeptidase inhibition
Cuppari A, Körschgen H, Fahrenkamp D, Schmitz C, Guevara T, Karmilin K, Kuske M, Olf M, Dietzel E, Yiallouros I, de Sanctis D, Goulas T, Weiskirchen R, Jahnen-Dechent W, Floehr J, Stoecker W, Jovine L, Gomis-Rüth FX.
IUCrJ. 28;6(Pt 2):317-330. (2019)
Multiple architectures and mechanisms of latency in metallopeptidase zymogens
J.L. Arolas, T. Goulas, A. Cuppari & F.X. Gomis-Rüth
Chem. Rev., 118, 5581-5597. (2018)
Third time lucky? Getting a grip on matrix metalloproteinases
Gomis-Rüth FX.
J Biol Chem. 27;292(43):17975-17976. (2017)
García-Castellanos R, Nielsen NS, Runager K, Thøgersen IB, Lukassen MV, Poulsen ET, Goulas T, Enghild JJ, Gomis-Rüth FX.
Structure. 7;25(11):1740-1750.e2. (2017)
Goulas T, Ksiazek M, Garcia-Ferrer I, Sochaj-Gregorczyk AM, Waligorska I, Wasylewski M, Potempa J, Gomis-Rüth FX.
J Biol Chem. 30;292(26):10883-10898. (2017)
Matrix metalloproteinases outside vertebrates
Marino-Puertas L, Goulas T, Gomis-Rüth FX.
Biochim Biophys Acta. 1864(11 Pt A):2026-2035. (2017)
α2-Macroglobulins: Structure and Function
Garcia-Ferrer I, Marrero A, Gomis-Rüth FX, Goulas T.
Subcell Biochem. 83:149-183. (2017)
Structural and functional insight into pan-endopeptidase inhibition by α2-macroglobulins
Goulas T, Garcia-Ferrer I, Marrero A, Marino-Puertas L, Duquerroy S, Gomis-Rüth FX.
Biol Chem. 398(9):975-994. (2017)
A. Pomowski, I. Usón, Z. Nowakowska, F. Veillard, M.N. Sztukowska, T. Guevara, T. Goulas, D. Mizgalska, M. Nowak, B. Potempa, J.A. Huntington, J. Potempa & & F.X. Gomis-Rüth.
J. Biol. Chem., 292, 5724-5735 (2017)
(highlighted in the March 2017 issue of the JBC Editorial Member Digest, “Bringing the gingipain”)
A.M. Lasica, T. Goulas, D. Mizgalska, X. Zhou, I. de Diego, M. Ksiazek, M. Madej, Y. Guo, T. Guevara, M. Nowak, B. Potempa, A. Goel, M. Sztukowska, A.T. Prabhakar, M. Bzowska, M. Widziolek, I.B. Thøgersen, J.J. Enghild, M. Simonian, A.W. Kulczyk, K.-A. Nguyen, J. Potempa & F.X. Gomis-Rüth
Sci. Rep., 6, 37708 (2016)
(highlighted by the Spanish Biophysical Society as one of Papers of the Month in November 2016 in Biofísica Magazine, issue #6, September-December 2016)
T. Goulas, I. Garcia-Ferrer, J.A. Hutcherson, B.A. Potempa, J. Potempa, D.A. Scott & F.X. Gomis-Rüth
Mol. Oral Microbiol., 31, 472-485. (2016)
I. De Diego, M. Ksiazek, D. Mizgalska, L. Koneru, P. Golik, B. Szmigielski, M. Nowak, Z. Nowakowska, B. Potempa, J.A. Houston, J.J. Enghild, I.B. Thøgersen, J. Gao, A.H. Kwan, J. Trewhella, G. Dubin, F.X. Gomis-Rüth, K.-A. Nguyen & J. Potempa.
Sci. Rep., 6, 23123. (2016)
M.W. Risør, L.R. Thomsen, K.W. Sanggaard, T.A. Nielsen, I.B. Thøgersen, M.V. Lukassen, L. Rossen, I. Garcia-Ferrer, T. Guevara, C. Scavenius, E. Meinjohanns, F.X. Gomis-Rüth & J.J. Enghild
J. Biol. Chem., 291, 2271-2287 (2016)
(highlighted in the May 2016 issue of the magazine of the American Society for Biochemistry and Molecular Biology, ASBMB Today)
J.L. Arolas, T. Goulas, A.P. Pomerantsev, S.H. Leppla & F.X. Gomis-Rüth.
Structure, 24, 25-36. (2016)
(Preview in the same journal issue: Schacherl, M. & Baumann, U. (2016). Feeding anthrax: the crystal structure of Bacillus anthracis InhA protease. Structure, 24, 1-2).
I. Garcia-Ferrer, P. Arêde, J. Gómez-Blanco, D. Luque, S. Duquerroy, J.R. Castón, T. Goulas & F.X. Gomis-Rüth.
Proc. Natl. Acad. Sci. USA , 112, 8290-8295 (2015)
(highlighted by the Spanish Biophysical Society as one of four Papers of the Month by SBE Members in July; Biofísica Magazine, issue #2, May-August 2015, http://biofisica.info/garcia-ferrer-gomis-ruth-pnas-112-8290/; selected by the Spanish Society of Biochemistry and Molecular Biology as The Article of the Month, January 2016, https://revista.sebbm.es).
T. Goulas, D. Mizgalska, I. Garcia-Ferrer, T. Kantyka, T. Guevara, B. Szmigielski, A. Sroka, C. Millán, I. Usón, F. Veillard, B. Potempa, P. Mydel, M. Solà, J. Potempa & F.X. Gomis-Rüth
Sci. Rep., 5, 11969 (2015)
(highlighted by the Spanish Biophysical Society as one of four Papers of the Month by SBE Members in July in Biofísica Magazine, issue #2, May-August 2015; http://biofisica.info/garcia-ferrer-gomis-ruth-pnas-112-8290/)
T. Goulas, I. Garcia-Ferrer, J.A. Hutcherson, B.A. Potempa, J. Potempa, D.A. Scott & F.X. Gomis-Rüth.
Mol. Oral Microbiol., doi: 10.1111/omi.12140. (2015)
LysargiNase mirrors trypsin for identification of protein C-termini and methylation sites.
P.F. Huesgen, P.F. Lange, L.D. Rogers, N. Solis, U. Eckhard, O. Kleifeld, T. Goulas, F.X. Gomis-Rüth & C.M. Overall
Nat. Meth., 2015. 12, 55-58. (2015)
A novel mechanism of latency in matrix metalloproteinases.
M. López-Pelegrín, M. Ksiazek, A.Y. Karim, T. Guevara, Joan L. Arolas, J. Potempa & F.X. Gomis-Rüth
J. Biol. Chem., 290, 4728-4740. (2015)
The pCri system: a vector collection for recombinant protein expression and purification.
T. Goulas, A. Cuppari, R. García-Castellanos, S. Snipas, R. Glockshuber, J.L. Arolas & F.X. Gomis-Rüth.
PLoS ONE, 9, e112643. (2014)
I. De Diego, F. Veillard, M.N. Sztukowska, T. Guevera, B. Potempa, A. Pomowski, J.A. Huntington, J. Potempa & F.X. Gomis-Rüth
J. Biol. Chem., 289, 32291-32302. (2014)
T. Goulas, I. Garcia-Ferrer, S. García-Piqué, L. Sottrup-Jensen & F.X. Gomis-Rüth
Mol. Oral Microbiol., 29, 354-364. (2014)
Expression and purification of integral membrane metallopeptidase HtpX.
J.L. Arolas, R. García-Castellanos, T. Goulas, Y. Akiyama & F.X. Gomis-Rüth
Prot. Expr. Purif., 99, 113-118. (2014)
López-Pelegrín, M. Cerdà-Costa, A. Cintas-Pedrola, F. Herranz-Trillo, P. Bernadó, J.R. Peinado, J.L. Arolas & F.X. Gomis-Rüth.
Angew. Chem. Int. Ed., 53, 10624-10630 (2014)
(chosen for the frontispiece of the section on communications).
Architecture and function of metallopeptidase catalytic domains.
N. Cerdà-Costa & F.X. Gomis-Rüth
Prot. Sci., 23, 123-144. (2014)
M. López-Pelegrín, N. Cerdà-Costa, F. Martínez-Jiménez, A. Cintas-Pedrola, A. Canals, J.R. Peinado, M.A. Martí-Renom, C. López-Otin, J.L. Arolas & F.X. Gomis-Rüth
J. Biol. Chem., 288, 21279-21294. (2013)
Structure-function studies of the staphylococcal methicillin resistance anti-repressor, MecR2.
P. Arêde, T. Botelho, T. Guevera, I. Usón, D.C. Oliveira & F.X. Gomis-Rüth
J. Biol. Chem., 2013; 288, 21267-21278. (2013)
F. Veillard, M. Sztukowska, D. Mizgalska, M. Ksiazek, J.A. Houston, B. Potempa, J.J. Enghild, I.B. Thøgersen, F.X. Gomis-Rüth & J. Potempa.
Biochim. Biophys. Acta – Gen. Subj., 1830, 4218-4228. (2013)
I. De Diego, F. T. Veillard, T. Guevara, B. Potempa, M. Sztukowska, J. Potempa & F.X. Gomis-Rüth
J. Biol. Chem., 288, 14287-14296. (2013)
T. Guevara, M. Ksiazek, P.D. Skottrup, N. Cerda-Costa, S. Trillo-Muyo, I. de Diego, E. Riise, J. Potempa & F.X. Gomis- Rüth.
Acta Cryst., F69, 472-476. (2013)
Ultra-tight crystal packing of a 10-KDa protein.
S. Trillo-Muyo, A. Jasilionis, M. Domagalski, M. Chruszcz, W. Minor, N. Kuisiene, J.L. Arolas, M. Solà & F.X. Gomis-Rüth (2013).
Acta Cryst., D69, 464-470. (2013)
S. Trillo-Muyo, S. Martínez-Rodríguez, J.L. Arolas & F.X. Gomis-Rüth
Chem. Sci., 4, 791-797. (2013)
J.L. Arolas, C. Broder, T. Jefferson, T. Guevara, E.E. Sterchi, W. Bode, W. Stöcker, C. Becker-Pauly & F.X. Gomis-Rüth.
Proc. Natl. Acad. Sci. USA, 109, 16131-16136. (2012)
Functional and structural insights into astacin metallopeptidases.
F.X. Gomis-Rüth, S. Trillo-Muyo & W. Stöcker
Biol. Chem., 393, 1027-1041. (2012)
A standard orientation for metallopeptidases.
F.X. Gomis-Rüth, T.O. Botelho & W. Bode
Biochim. Biophys. Acta – Prot. & Proteom., 1824, 157-163. (2012)
The crystal structure of human α2-macroglobulin reveals a unique molecular cage.
Marrero, S. Duquerroy, S. Trapani, T. Goulas, T. Guevara, G.R. Andersen, J. Navaza, L. Sottrup-Jensen & F.X. Gomis-Rüth.
Angew. Chem. Int. Ed., 51, 3340-3344 (2012)
(chosen by the journal as a Very Important Paper and for the issue cover; comment in C. Meyer, W. Hinrichs & U. Hahn, Human α2-macroglobulin–another variation on the venus flytrap, Angew. Chem. Int. Ed., 51, 5045-5047).
J.L. Arolas, T.O. Botelho, A. Vilcinskas & F.X. Gomis-Rüth. (2011)
Angew. Chem. Int. Ed., 50, 10357-10360.
T.O. Botelho, T. Guevara, A. Marrero, P. Arêde, V.S. Fluxà, J.-L. Reymond, D.C. Oliveira & F.X. Gomis-Rüth
J. Biol. Chem., 286, 25697-25709. (2011)
N. Cerdà-Costa, T. Guevara, A.Y. Karim, M. Ksiazek, K.-A. Nguyen, J.L. Arolas,, J. Potempa & F.X. Gomis-Rüth
Mol. Microbiol., 79, 119-132. (2011)
T. Goulas, J.L. Arolas & F.X. Gomis-Rüth
Proc. Natl. Acad. Sci. USA, 108, 1856-1861. (2011)
Z. Valnickova, L. Sanglas, J.L. Arolas, S.V. Petersen, C. Schar, D. Otzen, F.X. Avilés, F.X. Gomis-Rüth & J.J. Enghild
J. Biol. Chem., 285, 38243-38250. (2010)
S. Tanco, J.L. Arolas, T. Guevara, J. Lorenzo, F.X. Avilés & F.X. Gomis-Rüth
J. Mol. Biol., 401, 465-477. (2010)
L. Sanglas, J.L. Arolas, Z. Valnickova, F.X. Avilés, J.J. Enghild & F.X. Gomis-Rüth
J. Thromb. Haemost., 8, 1056-1065 (2010)
(Comment in the same issue: A. Gils, Hot spots in TAFIa, J. Thromb. Haemost., 8, 1054-1055).
Proenzyme structure and activation of astacin metallopeptidase.
T. Guevara, I. Yiallouros, R. Kappelhoff, S. Bissdorf, W. Stöcker & F.X. Gomis-Rüth.
J. Biol. Chem., 285, 13958-13965. (2010)
On the relevance of the Met-turn methionine in metzincins.
C. Tallant, R. García-Castellanos, U. Baumann & F.X. Gomis-Rüth.
J. Biol. Chem., 285, 13951-13957. (2010)
Matrix metalloproteinases: fold and function of their catalytic domains.
C. Tallant, A. Marrero & F.X. Gomis-Rüth.
Biochim. Biophys. Acta – Mol. Cell Res., 1803, 20-28. (2010)
D.R. Boer, J.A. Ruíz-Masó, J.R. López-Blanco, A.G. Blanco, M. Vives-Llàcer, P. Chacón, I. Usón, F. X. Gomis-Rüth, M. Espinosa, O. Llorca, G. del Solar & M. Coll
EMBO J, 28(11):1666-78 (2009)
Macrophage elastase (MMP-12) kills bacteria within murine macrophages.
A.M. Houghton, W.O. Hartzell, C.S. Robbins, F.X. Gomis-Rüth & S.D. Shapiro.
Nature, 460, 637-641. (2009)
Unique structure and stability of HmuY, a novel heme-binding protein of Porphyromonas gingivalis.
H. Wójtowicz, T. Guevara, C. Tallant, M. Olczak, A. Sroka, J. Potempa, M. Solà, T. Olczak & F. X. Gomis-Rüth
PLoS Pathog., 5, e1000419. (2009)
Catalytic domain architecture of metzincin metalloproteases.
F.X. Gomis-Rüth
J. Biol. Chem., 284, 15353-15357. (2009)
K. Runager, R. García-Castellanos, Z. Valnickova, T. Kistensen, N.C. Nielsen, G.K. Klintworth, F.X. Gomis-Rüth & J.J. Enghild
Acta Cryst., F65, 299-303. (2009)
Mammalian metallopeptidase inhibition at the defense barrier of Ascaris parasite.
L. Sanglas, F.X. Avilés, R. Huber, F.X. Gomis-Rüth & J.L. Arolas.
Proc. Natl. Acad. Sci. USA, 106, 1743-1747. (2009)
G. Niemirowicz, D. Fernández, M. Solà, J.J. Cazzulo, F.X. Avilés & F.X. Gomis-Rüth
Mol. Microbiol., 70, 853-866. (2008)
Structure and function of metallocarboxypeptidases
F.X. Gomis-Rüth
Crit. Rev. Biochem. Mol. Biol., 43, 319-345. (2008)
N. Mallorquí-Fernández, S.P. Manandhar, G. Mallorquí-Fernández, I. Usón, K. Wawrzonek, T. Kantyka, M. Solà, I.B. Thøgersen, J.J. Enghild, J. Potempa & F.X. Gomis-Rüth
J. Biol. Chem., 283, 2871-2882. (2008)
Sanglas, Z. Valnickova, J.L. Arolas, I. Pallarés, T. Guevara, M. Solà, T. Kristensen, J.J. Enghild, F.X. Avilés & F.X. Gomis-Rüth.
Mol. Cell, 31, 598-606. (2008)
Activity of ulilysin, an archaeal PAPP-A-related gelatinase and IGBP protease.
C. Tallant, R. García-Castellanos, A. Marrero, F. Canals, Y. Yang, J.L. Reymond, M. Solà, U. Baumann & F.X. Gomis-Rüth.
Biol. Chem, 388, 1243-1253. (2007)
A. Bayés, D. González, M. Solà, A. Marrero, S. García-Piqué, F.X. Avilés, J. Vendrell & F.X. Gomis-Rüth
Biochemistry, 46, 6921-6930. (2007)
R. Arribas-Bosacoma, S.-K. Kim, C. Ferrer-Orta, A.G. Blanco, P.J.B. Pereira, F.X. Gomis-Rüth, B.L. Wanner, M. Coll & M. Solà
J. Mol. Biol., 366, 626-641. (2007)
R. García-Castellanos, C. Tallant, A. Marrero, M. Solà, U.Baumann & F.X. Gomis-Rüth
Arch. Biochem. Biophys., 457, 57-72. (2007)
Cut and move: Protein machinery for DNA processing in bacterial conjugation.
F. X. Gomis-Rüth & M. Coll
Curr. Op. Struct. Biol., 16, 744-752. (2006)
T. Guevara, N. Mallorquí-Fernández, R. García-Castellanos, S. García-Piqué, G.E. Petersen, C. Lauritzen, J. Pedersen, J. Arnau, F. X. Gomis-Rüth & M. Solà
Biol. Chem., 387, 1479-1486. (2006)
The cofactor-induced pre-active conformation in PhoB.
M. Solà, D.L. Drew, A.G. Blanco, F.X. Gomis-Rüth & M. Coll
Acta Cryst., D62, 1046-1057. (2006)
A. Marrero, G. Mallorquí-Fernández, T. Guevara, R. García-Castellanos & F.X. Gomis-Rüth
J. Mol. Biol., 361, 506-521. (2006)
C. Tallant, R. García-Castellanos, J. Seco, U. Baumann & F.X. Gomis-Rüth
J. Biol. Chem., 281, 17920-17928. (2006)
D. Mouradov, A. Craven, J.K. Forwood, J.U. Flanagan, R. García-Castellanos, F.X. Gomis-Rüth, J.L. Martin, B. Kobe & T. Huber
Protein Eng. Des. Sel. (PEDS), 19, 9-16. (2006)
R. García-Castellanos, R. Bonet-Figueredo, I. Pallarés, S. Ventura, F.X. Avilés, J. Vendrell & F.X. Gomis-Rüth
Cell. Mol. Life Sci., 62, 1996-2014. (2005)
Structure of human carboxypeptidase A4 with its endogenous protein inhibitor, latexin.
I. Pallarés, R. Bonet, R. García-Castellanos, S. Ventura, F.X. Avilés, J. Vendrell & F.X. Gomis-Rüth
Proc. Natl. Acad. Sci. USA, 102, 3978-3983. (2005)
The eight-cysteine motif, a versatile structure in plant proteins.
M. José-Estanyol, F.X. Gomis-Rüth & P. Puigdomènech
Plant Physiol.Biochem., 42, 355-365. (2004)
Staphylococcal methicillin resistance: fine focus on folds and functions.
G. Mallorquí-Fernández, A. Marrero, S. García-Piquè, R. García-Castellanos & F.X. Gomis-Rüth
FEMS Microbiol. Lett., 235, 1-8. (2004)
Coupling factors in macromolecular type IV secretion machineries.
F.X. Gomis-Rüth, M. Solà, F. de la Cruz & M. Coll
Curr. Pharm. Des., 10, 1551-1565. (2004)
R. García-Castellanos, G. Mallorquí-Fernández, A. Marrero, J. Potempa, M. Coll & F.X. Gomis-Rüth.
J. Biol. Chem., 279, 17888-17896. (2004)
Recognition and processing of the origin of transfer DNA by conjugative relaxase TrwC.
A. Guasch, M. Lucas, M. Cabezas, R. Pérez-Luque, F.X. Gomis-Rüth, F. de la Cruz & M. Coll
Nat. Struct. Biol., 10, 1002-1010. (2003)
R. García-Castellanos, A. Marrero, G. Mallorquí-Fernández, J. Potempa, M. Coll & F.X. Gomis-Rüth
J. Biol. Chem., 278, 39897-39905. (2003)
Structure of xylanase Xys1Δ from Streptomyces halstedii.
A. Canals, M.C. Vega, F.X. Gomis-Rüth, M. Díaz, R.I. Santamaría & M. Coll
Acta Cryst., D59, 1447-1453. (2003)
Structural aspects of the metzincin clan of metalloendopeptidases.
F. X. Gomis-Rüth
Mol. Biotech., 24, 157-202. (2003)
F. X. Gomis-Rüth, A. Dessen, J. Timmins, A. Bracher, L. Kolesnikowa, S. Becker, H.-D. Klenk & W. Weissenhorn
Structure, 11, 423-433. (2003)
G. del Solar, A.M. Hernández-Arriaga, F.X. Gomis-Rüth, M. Coll & M. Espinosa
J. Bacteriol., 184, 4943-4951. (2002)
P.J.B. Pereira, S. Segura-Martín, B. Oliva, C. Ferrer-Orta, F.X. Avilés, M. Coll, F.X. Gomis-Rüth & J. Vendrell.
J. Mol. Biol., 321, 537-547. (2002)
F.X. Gomis-Rüth, A. Bayés, G. Sotiropoulou, G. Pampalakis, T. Tsetsenis, V. Villegas, F.X. Avilés & M. Coll
J. Biol. Chem., 277, 27273-27281. (2002)
Bacterial conjugation: a two-step mechanism for DNA transport.
M. Llosa, F.X. Gomis-Rüth, M. Coll & F. de la Cruz
Mol. Microbiol., 45, 1-8. (2002)
Structure and role of coupling proteins in conjugal DNA transfer.
F.X. Gomis-Rüth, F. de la Cruz & M. Coll
Res. Microbiol., 153, 199-204. (2002)
Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator.
A.G. Blanco, M. Solà, F.X. Gomis-Rüth & M. Coll
Structure, 10, 701-713. (2002)
(Comment in Structure Previews by K. Volz).
F.X. Gomis-Rüth, G. Moncalián, F. de la Cruz & M. Coll
J. Biol. Chem., 277, 7556-7566. (2002)
A. Guasch, J. Pous, B. Ibarra, F.X. Gomis-Rüth, J.M. Valpuesta, N. Sousa, J.L. Carrascosa & M. Coll
J. Mol. Biol., 315, 663-676. (2002)
P.J.B. Pereira, M.C. Vega, E. González-Rey, R. Fernández-Carazo, S. Macedo-Ribeiro, F. X. Gomis-Rüth, A. González & M. Coll
EMBO Rep., 3, 88-94. (2002)
The structure of TrwB, a gatekeeper in bacterial conjugation.
F.X. Gomis-Rüth & M. Coll
Int. J. Biochem. Cell Biol., 33, 839-843. (2001)
The bacterial conjugation protein TrwB resembles ring helicases and F1-ATPase.
F.X. Gomis-Rüth, G. Moncalián, R. Pérez-Luque, A. González, E. Cabezón, F. de la Cruz & M. Coll.
Nature, 409, 637-641. (2001)
M. Costa, M. Solà, G. Del Solar, R. Eritja, A.M. Hernández-Arriaga, M. Espinosa, F.X. Gomis-Rüth & M. Coll
J. Mol. Biol., 310, 403-417. (2001)
Solving a 300 kDa multimeric protein by low-resolution MAD phasing and averaging/phase extension.
F.X. Gomis-Rüth & M. Coll
Acta Cryst., D57, 800-805. (2001)
P. Aloy, V. Companys, J. Vendrell, F.X. Avilés, L.D. Fricker, M. Coll & F.X. Gomis-Rüth
J. Biol. Chem., 276, 16177-16184. (2001)
V. Knäuper, M.L. Stewart, F.X. Gomis-Rüth, B. Smith, A. Lyons, A.J.P. Docherty & G. Murphy
Eur. J. Biochem., 268, 1888-1896. (2001)
Three-dimensional crystal structure of human RNase 1ΔN7 at 1.9 Å.
J. Pous, G. Mallorquí-Fernández, R. Peracaula, S.S. Terzyan, J. Futami, H. Tada, H. Yamada, M. Seno, R. de Llorens, F.X. Gomis-Rüth & M. Coll
Acta Cryst., D57, 498-505. (2001)
Three-dimensional structure of human eosinophil cationic protein (RNase 3) at 1.75 Å resolution.
G. Mallorquí-Fernández, J. Pous, R. Peracaula, T. Maeda, H. Tada, H. Yamada, M. Seno, R. de Llorens, F.X. Gomis-Rüth & M. Coll
J. Mol. Biol., 300, 1297-1309. (2000)
F.X. Gomis-Rüth, V. Companys, Y. Qian, L.D. Fricker, J. Vendrell, F.X. Avilés & M. Coll
EMBO J., 18, 5817-5826. (1999)
Two wavelength MAD phasing: in search of the optimal wavelengths.
A. González, J.-D. Pédelacq, M. Solà, F.X. Gomis-Rüth, M. Coll, J.P. Samama & S. Benini
Acta Cryst., D55, 1449-1458. (1999)
Three-dimensional crystal structure of the transcription factor PhoB receiver domain.
M. Solà, F.X. Gomis-Rüth, L. Serrano, A. González & M. Coll
J. Mol. Biol., 285, 675-687. (1999)
S.S. Terzyan, R. Peracaula, R. de Llorens, Y. Tsushima, H. Yamada, M. Seno, F.X. Gomis-Rüth & M. Coll
J. Mol. Biol., 285, 205-214. (1999)
F.X. Gomis-Rüth, M. Solà, P. Acebo, A. Párraga, A. Guasch, R. Eritja, A. González, M. Espinosa, G. del Solar & M. Coll
EMBO J., 17, 7404-7415. (1998)
M. Solà, F.X. Gomis-Rüth, A. Guasch, L. Serrano & M. Coll
Acta Cryst., D54, 1460-1463. (1998)
S. Strobl, K. Maskos, G. Wiegand, R. Huber, F.X. Gomis-Rüth & R. Glockshuber
Structure, 6, 911-921. (1998)
F.X. Gomis-Rüth, M. Solà, R. Pérez-Luque, P. Acebo, M.T. Alda, A. González, M. Espinosa, G. del Solar & M. Coll
FEBS Lett., 425, 161-165. (1998)
Crystal structure of the yellow meal worm α-amylase at 1.64 Å resolution.
S. Strobl, K. Maskos, M. Betz, G. Wiegand, R. Huber, F.X. Gomis-Rüth & R. Glockshuber
J. Mol. Biol., 278, 617-628. (1998)
F.X. Gomis-Rüth, M. Gómez-Ortiz, J. Vendrell, S. Ventura, W. Bode, R. Huber & F.X. Avilés
Eur. J. Biochem., 251, 839-844. (1998)
F.X. Gomis-Rüth, E.F. Meyer, L.F. Kress & V. Politi
Prot. Sci., 7, 283-292. (1998)
F.J. Medrano, J. Alonso, J.L. García, A. Romero, W. Bode & F.X. Gomis-Rüth
EMBO J., 17, 1-9. (1998)
M. Cirilli, C. Gallina, E. Gavuzzo, C. Giordano, F.X. Gomis-Rüth, B. Gorini, L.F. Kress, F. Mazza, M. Paglialunga Paradisi, G. Pochetti & V. Politi
FEBS Lett., 418, 319-322. (1997)
Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1.
F.X. Gomis-Rüth, K. Maskos, M. Betz, A. Bergner, R. Huber, K. Suzuki, N. Yoshida, H. Nagase, K. Brew, G.P. Bourenkov, H. Bartunik & W. Bode.
Nature, 389, 77-81. (1997)
M. Pieper, M. Betz, N. Budisa, F.X. Gomis-Rüth, W. Bode & H. Tschesche
J. Prot. Chem., 16, 637-650. (1997)
M. Betz, P. Huxley, S.J. Davies, Y. Mushtaq, M. Pieper, H. Tschesche, W. Bode & F.X. Gomis-Rüth
Eur. J. Biochem., 247, 356-363. (1997)
S. Strobl, F.X. Gomis-Rüth, K. Maskos, G. Frank, R. Huber & R. Glockshuber
FEBS Lett., 409, 109-114. (1997)
F.X. Gomis-Rüth, M. Gómez-Ortiz, J. Vendrell, S. Ventura, W. Bode, R. Huber & F.X. Avilés
J. Mol. Biol., 269, 861-880. (1997)
Pancreatic procarboxypeptidases: oligomeric structures and activation processes revisited.
S. Ventura, F.X. Gomis-Rüth, A. Puigserver, F.X. Avilés & J. Vendrell
Biol. Chem., 378, 161-165. (1997)
C. Hammann, G. van Pouderoyen, H. Nar, F.X. Gomis-Rüth, A. Messerschmidt, R. Huber, T. den Blaauwen & G.W. Canters
J. Mol. Biol., 266, 357-366. (1997)
M. Gómez-Ortiz, F.X. Gomis-Rüth, R. Huber & F.X. Avilés
FEBS Lett., 400, 336-340. (1996)
F.J. Medrano, J. Alonso, J.L. García, W. Bode & F.X. Gomis-Rüth
FEBS Lett., 400, 91-93. (1996)
F.X. Gomis-Rüth, U. Gohlke, M. Betz, V. Knäuper, G. Murphy, C. López-Otín & W. Bode.
J. Mol. Biol., 264, 556-566. (1996)
Protein crystal density by volume measurement and amino acid analysis.
R. Kiefersauer, J. Stetefeld, F.X. Gomis-Rüth, M.J. Romão, F. Lottspeich & R. Huber
J. Appl. Crystallogr., 29, 311-317. (1996)
U. Gohlke, F.X. Gomis-Rüth, T. Crabbe, G. Murphy, A.J.P. Docherty & W. Bode
FEBS Lett., 378, 126 -130. (1996)
F. X. Gomis-Rüth, M. Gómez, W. Bode, R. Huber & F. X. Avilés
EMBO J., 14, 4387-4394. (1995)
F.X. Gomis-Rüth, I. Fita , R. Kiefersauer, R. Huber , F.X. Avilés & J. Navaza
Acta Cryst., D51, 819-823. (1995)
F. X. Gomis-Rüth, M. Gómez, S. Ventura, J. Vendrell & F. X. Avilés
FEBS Lett., 367, 211-213. (1995)
W. Stöcker, F. Grams, U. Baumann, P. Reinemer, F.X. Gomis-Rüth, D.B. McKay & W. Bode
Prot. Sci., 4, 823-840. (1995)
D. Zhang, I. Bothos, F.X. Gomis-Rüth, R. Doll, C. Blood, F.G. Njoroge, J.W. Fox, W. Bode & E.F. Meyer
Proc. Natl. Acad. Sci. USA, 91, 8447-8451. (1994)
F.X. Gomis-Rüth, L.F. Kress, J. Kellermann, I. Mayr, X. Lee, R. Huber & W. Bode
J. Mol. Biol., 239, 513-544. (1994)
F.X. Gomis-Rüth, F. Grams, I. Yallouros, H. Nar, U. Küsthardt, R. Zwilling, W. Bode & W. Stöcker
J. Biol. Chem., 269, 17111-17117. (1994)
F.X. Gomis-Rüth, L.F. Kress & W. Bode
EMBO J., 12, 4151-4157. (1993)
W. Bode, F.X. Gomis-Rüth & W. Stöcker
FEBS Lett., 331, 134-140. (1993)
W. Stöcker, F.X. Gomis-Rüth, W. Bode & R. Zwilling
Eur. J. Biochem., 214, 215-231. (1993)
F.X. Gomis-Rüth, W. Stöcker, R. Huber, R. Zwilling & W. Bode
J. Mol. Biol., 229, 945-968. (1993)
B. Laber, F.X. Gomis-Rüth, M.J. Romão & R. Huber
Biochem. J., 288, 691-695. (1992)
M.J. Romão, D. Turk, F.X. Gomis-Rüth, R. Huber, G. Schumacher, H. Möllering & L. Rüssmann
J. Mol. Biol., 226, 1111-1130. (1992)
Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases.
W. Bode, F.X. Gomis-Rüth, R. Huber, R. Zwilling & W. Stöcker
Nature, 358, 164-167. (1992)
Atropoisomería en la serie 11H -dibenzo[b,e]azepínica. Parte III. 11-oxo derivados N-aril sustituidos.
J. Irurre, F. Marquillas, E. Narbón, C. Puig & X. Gomis
An. Quim., 88, 601-606. (1992)
Book chapters
α2-Macroglobulins: structure and function
I. Garcia-Ferrer, A. Marrero, F.X. Gomis-Rüth & T. Goulas (J.R. Harris & J. Marles-Wright, eds.)
In Macromolecular Protein Complexes, 2017. Subcellular Biochemistry series, Vol. 83 , Springer, Cham (Switzerland), pp. 149-183.
A traves del cristal: Cómo la cristalografía ha cambiado la vision del mundo
F. X. Gomis-Rüth (M. Martínez-Ripoll, J.A. Hermoso & A. Albert, eds.)
Peptidasas: nanomáquinas para el procesado de proteínas, 2014. Los Libros de la Catarata, CSIC, Madrid, pp. 89-97.
Astacins: proteases in development and tissue differentiation
W. Stöcker & F. X. Gomis-Rüth (K. Brix & W. Stöcker, eds.)
Proteases: Structure and Function, 2013. Springer Verlag, Vienna (Austria), pp. 235-263.
J.L. Arolas & F. X. Gomis-Rüth (V.N. Uversky, R.H. Kretsinger & E.A. Permyakov, eds.)
Encyclopedia of Metalloproteins, 2013. Springer Verlag, Heidelberg, pp. 2473-2479
F. X. Gomis-Rüth (V.N. Uversky, R.H. Kretsinger & E.A. Permyakov, eds.)
Encyclopedia of Metalloproteins, 2013. Springer Verlag, Heidelberg, pp. 2345-2349 .
J. Potempa, F. X. Gomis-Rüth & A.Y. Karim (N.D. Rawlings & G.S. Salvesen, eds.)
Handbook of Proteolytic Enzymes, 2013, Academic Press, Oxford, pp. 883-886 .
T. Goulas & F. X. Gomis-Rüth (N.D. Rawlings & G.S. Salvesen, eds.)
Handbook of Proteolytic Enzymes, 2013, Academic Press, Oxford, pp. 887-891
270 Ulilysin (Methanosarcina acetivorans)
U. Baumann & F. X. Gomis-Rüth (N.D. Rawlings & G.S. Salvesen, eds.)
Handbook of Proteolytic Enzymes, 2013, Academic Press, Oxford, pp. 1208-1211
L.D. Fricker & F. X. Gomis-Rüth (N.D. Rawlings & G.S. Salvesen, eds.)
Handbook of Proteolytic Enzyme, 2013. Academic Press, Oxford, pp. 1307-1310
T.O. Botelho & F. X. Gomis-Rüth (N.D. Rawlings & G.S. Salvesen, eds.)
Handbook of Proteolytic Enzymes, 2013, Academic Press, Oxford, pp. 1651-1654
Em cura la grip: L’estructura tridimensional de proteïnes com a motlle per el desenvolupament de fàrmacs.
F. X. Gomis-Rüth & M. Solà (Sílvia Pujals Riatós & Eduardo Sabidó Aguadé, eds.)
Què fa la biotecnologia per a mi?, 2010. Xarxa de Referència en Biotecnologia, Generalitat de Catalunya, pp.27-36 (e-Book chapter).
Atomic structure of a molecular switch for blood coagulation and fibrinolysis.
L. Sanglas, Z. Valnickova, J.L. Arolas, I. Pallarés, T. Guevara, M. Solà, T. Kristensen, J.J. Enghild, F.X. Avilés & F.X. Gomis-Rüth (Gary Admans, ed.)
ESRF Highlights 2008, 2009 ESRF, Grenoble, pp.66-67
F. X. Gomis-Rüth (W. Bode, M. Cygler & A. Messerschmidt, eds.)
Handbook of Metalloproteins – Volume III, 2004, John Wiley & Sons, Chichester, pp. 631-646
Structural basis for the function of astacin and related zinc peptidases
W. Stöcker, I. Yallouros, D. Köhler, S. Gredel, R. Zwilling, V. Dive, W. Bode, F.X. Gomis-Rüth& F. Grams (W. Stöcker & R. Zwilling, eds.).
The Astacins – Structure and Function of a New Protein Family, 1997. Verlag Dr. Kovac, Hamburg, pp. 147-163
Comparison of the crystallographic structure of rattlesnake venom adamalysin II with other members of the metzincin-superfamily of metalloendopeptidases and thermolysin
F.X. Gomis-Rüth, W. Stöcker & W. Bode (W. Stöcker & R. Zwilling, eds.)
The Astacins – Structure and Function of a New Protein Family, 1997. Verlag Dr. Kovac, Hamburg, pp. 329-348.
The metzincins: a new superfamily of zinc endopeptidases.
W. Bode, F. Grams, P. Reinemer, F.X. Gomis-Rüth, U. Baumann, D.B. McKay & W. Stöcker (W. Stöcker & R. Zwilling, eds.)
The Astacins – Structure and Function of a New Protein Family, 1997. Verlag Dr. Kovac, Hamburg, pp. 29-43.
Other Publications
Mechanistic insights into the action of a bacterial protease inhibitor (P35-019).
I. Garcia-Ferrer, P. Arêde-Rei, T. Goulas & F.X. Gomis-Rüth.
FEBS J., 282 (Suppl. 1), 328-328 (Published conference abstract). (2015)
Molecular plasticity controls proteolytic activity.
M. López-Pelegrín, N. Cerdà-Costa, A. Cintas-Pedrola, F. Herranz-Trillo, P. Bernadó, J.R. Peinado, J.L. Arolas & F.X. Gomis-Rüth
ALBA Activity Report 2014, Alba Synchrotron, Cerdanyola del Vallès (Barcelona), pp. 15-16 (Annual report of activity). (2015)
A different look for AB5 toxins.
F. X. Gomis-Rüth.
Structure, 21, 1909-1910 (Preview of an article in the same issue). (2013)
Structural features of the replication initiator protein RepB of the promiscuous plasmid pMV158.
J.A. Ruiz-Maso, D.R. Boer, J.R. López-Blanco, A.G. Blanco, M. Vives-Llacer, P. Chacón, I. Usón, F.X. Gomis-Rüth, M. Espinosa, O. Llorca, G. del Solar & M. Coll.
FEBS J., 276 (Suppl. 1), 387-387 (Published conference abstract). (2009)
Biochemical and structural characterisation of human ECI and its complex with human carboxypeptidase A4.
I. Pallarés, R. Bonet, R. García-Castellanos, S. Ventura, F.X. Avilés, J. Vendrell & F.X. Gomis-Rüth
FEBS J., 272 (Suppl. 1), 96-97 (Published conference abstract; poster A2-064P). (2005)
Resistencia bacteriana a los antibióticos.
F. X. Gomis-Rüth & Miquel Coll. Diario de Sevilla, 15-03-2001, pp. 48-49 (Newspaper article).
Insights into MMP-TIMP interactions.
W. Bode, C. Fernández-Catalán, F. Grams, F.X. Gomis-Rüth, H. Nagase, H. Tschesche & K. Maskos.
Ann. N.Y. Acad. Sci., 878, 73-91 (Published conference abstract). (1999)
Cristal.lografia de proteines.
A. Guasch, N. Verdaguer, F.X. Gomis-Rüth, I. Fita & M. Coll
Treballs de la Societat Catalana de Biologia, 48, 13-23 (Special issue of the Catalan Biological Society). (1998).
The metzincin-superfamily of zinc-peptidases. In Intracellular Protein Catabolism
W. Bode, F. Grams, P. Reinemer, F.X. Gomis-Rüth, U. Baumann, D.B. McKay & W. Stöcker (K. Suzuki & J.S. Bond, eds.)
Book Series Advances in Experimental Medicine and Biology, Vol. 389, Plenum Publishing Co., New York, pp. 1 – 11 (Published conference abstract). (1996)
The metzincins: a superfamily of structurally related metalloproteinases.
W. Bode, F. Grams, P. Reinemer, F.X. Gomis-Rüth, U. Baumann, D.B. McKay & W. Stöcker
Zoology – Analysis of Complex Systems, 99, 237-246 (Published conference abstract). (1995/1996)
W. Bode, L. Kress & F.X. Gomis-Rüth
Brazilian J. Med. Biol. Res., 27, 2049-2068 (Published conference abstract). (1994)
The three-dimensional structure of astacin: implications for the structure of astacins and for the zinc ligation of other metalloproteinases.
W. Bode, F.X. Gomis-Rüth, R. Zwilling & W. Stöcker
In Proteolysis and Protein Turnover (A.J. Barrett & J.S. Bond, eds.), Portland Press Inc., Cambridge, pp. 13-24 (Published conference abstract). (1993).
Kinetic investigation and X-ray structure analysis of metal-substituted derivatives of the zinc-endopeptidase astacin reveals a correlation between metal-ligand geometry and catalytic activity.
S. Stöcker, I. Yallouros, R. Zwilling, F.X. Gomis-Rüth, F. Grams & W. Bode
Biol. Chem. Hoppe-Seyler, 374, 682-683 (Published conference abstract). (1993)
Biochemische und kristallographische Arbeiten an zwei Enzymen: Dihydrodipicolinat-Synthase und Astacin.
F.X. Gomis-Rüth
Faculty of Chemistry and Pharmacy, University Ludwig-Maximilian, Munich (Germany) (Ph.D.-Thesis). (1992).
Astacin: Archetype of a novel protein-family.
S. Stöcker, F.X. Gomis-Rüth, R. Huber, R. Zwilling & W. Bode
Verh. Dtsch. Zool. Ges.,85, 170-170 (Published conference abstract) (1992)
S. Stöcker, F.X. Gomis-Rüth, R. Huber, R. Zwilling & W. Bode
Biol. Chem. Hoppe-Seyler, 373, 654-654 (Published conference abstract). (1992)
Síntesis, resolución en atropoisómeros y análisis conformacional en derivados 11-carboximetilénicos de 11H-dibenzo[b,e]azepin-6-onas y 6-tionas N-substituidas.
F.X. Gomis-Rüth
Department of Organic Chemistry, Chemistry Institute of Sarrià (IQS), Barcelona (Spain) (M.Sc.-Thesis) (1989).
Project funding
Ongoing Projects
R&D Proof-of-concept project, State Agency of Research (AEI), Ministry of Science and Innovation. “Validation and further development of a glutenase for the treatment of coeliac disease (CELIASTOP)”. Ref. PDC2022-133344-I00. Total (incl. indirect costs): €133,400. Role: PI. 01.12.2022 – 30.11.2024.
Proyecto PDC2022-133344-I00 financiado por:
Consolidated Research Groups of Catalunya Grant, Generalitat of Catalunya. Ref. 2021SGR423. “Structural and Computational Protein Biochemistry (BIOSTROMP)”. Total awarded: €40,000. Role: Coordinator. 01.01.2023 – 31.12.2025.
R&D project, State Plan, section Molecular and Cellular Biology, Ministry of Science and Innovation. “Biochemistry of proteolysis: function, regulation and structure of biomedically and biotechnologically relevant peptidases and their inhibitors.” Ref.: PID2019-107725RB-I00. Total awarded (incl. indirect costs): €242,000. Role: PI. 1.6.2020-31.5.2023.
Proyecto PID2019-107725RB-I00 financiado por:
Concluded Projects
(last 5 years)
Reference: 201815
Title: Tackling periodontal pathogen Porphyromonas gingivalis through its type-IX secretion system sortase
Total awarded: €195,500 (1.1.2019 – 31.12.2021)
Role: PI
“Fundació La Marató de TV3” Research Project, Edition 2017 – Biomedical Research Projects in Infectious Diseases
Research Contract with the Fraunhofer Gesellschaft in collaboration with Prof. Andreas Vilcinskas from the Fraunhofer Institute of Molecular Biology and Applied Ecology, Gießen (Germany), entitled “Structure and function analysis of variants of the inducible metalloproteinase inhibitor (IMPI) from Galleria mellonella to target pathogenic M4 metallopeptidases.” Total amount (incl. indirect costs): €100,000. Role: Subcontractor. 31.10.2019-30.9.2022.
Reference: 16GW0183K
Title: Validation of the γ-glutamylpolyamine synthetase GlnA3 as a promising target for the development of novel anti-tubercular drugs (GPS-TBT)
Total awarded: €30,000 (1.2.2018 – 31.12.2021)
Role: Subcontractor
German Ministry of Education and Research.
Reference: 2017SGR3
Title: Proteolysis Lab
Total awarded: €19,750 (1.1.2017 – 31.12.2019)
Role: PI
Consolidated Research Groups of Catalunya Grant, Generalitat of Catalunya.
Reference: MDM-2014-0435
Title: Appointment of the Department of Structural Biology of IBMB as a “María de Maeztu Unit of Excellence”
Total awarded: €2,000,000 (1.7.2015 – 31.12.2019)
Role: co-PI (out of just 7 PIs)
Spanish Ministry of Economy and Competitivity.
Reference: BFU2015-64487-R
Title: Biochemistry of proteolysis: function, regulation and structure of peptidases of biomedical relevance and their inhibitors
Total awarded: €340,000 (1.1.2016-31.12.2019)
Role: PI
R&D project, State Plan, section Molecular and Cellular Biology, Ministry of Economy and Competitivity\
Proyecto BFU2015-64487-R financiado por:
Reference: FP7-PEOPLE-2011-290246 “RAPID”
Title: RAPID-Rheumatoid arthritis and periodontal inflammatory disease
Total awarded to subgroup: €380,367 (1.4.2013 – 31.3.2017)
Role: Co-PI and Coordinator of Subproject (WP) nº 6 (Coordinator: Thomas Dietrich (Birmingham, UK)
European Union Marie Curie Initial Training Network (ITN) Project
Reference: FP7-HEALTH-2012-306029-2 “TRIGGER”
Title: King of hearts, joints and lungs; periodontal pathogens as etiologic factor in RA, CVD and COPD and their impact on treatment strategies
Total awarded: €519,041 (1.4.2013 – 31.3.2017)
Role: Co-PI and Coordinator of Subproject (WP) nº 6
European Union STREP FP7 Project
Reference: 2014SGR9
Title: Proteolysis Lab
Total awarded: €15,000 (2014 – 2016)
Role: Coordinator
Consolidated Research Groups of Catalunya Grant, Generalitat of Catalunya.
Reference: BIO2013-49320-EXP
Title: Redesign of therapeutic proteins with enhanced stability through incorporation of non-natural amino acids
Total awarded: €60,000 (1.9.2014-31.8.2016,extended to 31.1.2017)
Role: PI
R&D project, State Plan, program Explora technology, section Biotechnology, Ministry of Economy and Competitivity.
Reference: CSD2006-00015
Title: The Crystallization Factory
Total awarded: €5,000,000. Grant awarded to subgroup: €171,308 (6.12.2006-6.12.2014)
Role: Co-PI (coordinator: J.M. García Ruiz)
“Consolider-Ingenio” Project 2010, first call (2006). Ministry of Education and Science.
Reference: FP7-HEALTH-2010-261460 “Gums&Joints”
Title: Protein citrullination as a link between periodontal diseases and rheumatoid arthritis (RA) and target for development of novel drugs to treat RA
Grant awarded to subgroup: €504,510 (1.11.2010 – 31.10.2014)
Role: Co-PI and Coordinator of Subproject (WP) nº 3 (coordinator: Peter Mydel; Bergen, Norway)
European Union STREP FP7 Project
Reference: “Fundació La Marató de TV3” Research Project 100732
Title: Clinical, genetic, epidemiological, pathophysiological and translational studies of spinocerebellar ataxias
Grant awarded to subproject: €176,500 (1.1.2011 – 30.6.2014, after 6-month extension)
Role: Co-PI (coordinator: Antoni Matilla Dueñas; IICSGTP, Badalona)
“Fundació La Marató de TV3” Research Project, Edition 2009 – Biomedical Research Projects in Minority Diseases.
Reference: 2009SGR1036
Title: Structural biology: computational methods and structure-function analysis of proteins of biomedical and biotechnological interest (MEBIO)
Total awarded: €42,640 (2009 – 2013, extended until 31.3.2014)
Role: Coordinator and co-PI.
Consolidated Research Groups of Catalunya Grant, Generalitat of Catalunya.
Reference: 210RT0390
Title: Multidisciplinary network for the study of disorders of movement: Parkinson’s disease and spinocerebellar ataxias
Total awarded: €128,000 (2009 – 2013)
Role: Co-PI.
Programme for the Development of Science and Technology in Latin-American (CYTED).
Reference: FP7-HEALTH-F3-2009-223101 “AntiPathoGN”
Title: Identification and validation of novel drug targets in Gram-negative bacteria by global search: a trans-system approach
Grant awarded to subgroup: €300,000 (1.2.2009 – 30.6.2013, after 6-month extension)
Role: Co-PI, Responsible for the Third Part of Subproject nº 2 (coordinator: Xavier Daura; UAB, Barcelona)
European STREP FP7 Project
Reference: BIO2009-10334
Title: Structural biology of hydrolases of therapeutic interest (IV)
Total awarded: €295,000. (1.1.2010-31.12.2012)
Role: PI.
R&D project, National Biotechnology Plan, Ministry of Science and Technology.
Vacancies/Jobs
Lab corner
Products
- Ulilysin, also knwon as LysargiNase, was developed in the Proteolysis Lab, originally by Ulrich Baumann during a sabatical stay in 2005 (1-4). In a collaboration with the group of Chris Overall from the University of British Columbia in Vancouver (Canada), this metallopeptidase was assessed as a very valuable reagent for proteomics (5). We are currently marketing original LysargiNase produced by the discoverers through Millipore/Merck ( http://www.merckmillipore.com/
ES/es/product/LysargiNase,MM_ NF-EMS0008 ).
(1) C. Tallant, R. García-Castellanos, J. Seco, U. Baumann & F.X. Gomis-Rüth * (2006). Molecular analysis of ulilysin, the structural prototype of a new family of metzincin metalloproteases. J. Biol. Chem., 281, 17920-17928.
(2) R. García-Castellanos, C. Tallant, A. Marrero, M. Solà, U. Baumann & F.X. Gomis-Rüth * (2007). Substrate specificity of a metalloprotease of the pappalysin family revealed by an inhibitor and a product complex. Arch. Biochem. Biophys., 457, 57-72.
(3) C. Tallant, R. García-Castellanos, A. Marrero, F. Canals, Y. Yang, J.L. Reymond, M. Solà, U. Baumann & F.X. Gomis-Rüth * (2007). Activity of ulilysin, an archaeal PAPP-A-related gelatinase and IGBP protease. Biol. Chem, 388, 1243-1253.
(4) A. Rodríguez-Banqueri, M. Moliner-Culubret, S.R. Mendes, T. Guevara, U. Eckhard & F.X. Gomis-Rüth * (2023). Structural insights into latency of the metallopeptidase ulilysin (lysargiNase) and its unexpected inhibition by a sulfonyl-fluoride inhibitor of serine peptidases. Dalton Trans., 52, 3610-3622.
(5) P.F. Huesgen, P.F. Lange, L.D. Rogers, N. Solis, U. Eckhard, O. Kleifeld, T. Goulas, F.X. Gomis-Rüth & C.M. Overall (2015). LysargiNase mirrors trypsin for identification of protein C-termini and methylation sites. Nat. Meth., 12, 55-58
- We also developed the pCri plasmid system for the recombinant overexpression of proteins in several hosts (1). It can be acquired via Addgene, see https://www.addgene.org/kits/
pcrisystem. Comments in http://blog.addgene.org/ easing-the-protein- purification-process-with-pcri .
(1) T. Goulas, A. Cuppari, R. García-Castellanos, S. Snipas, R. Glockshuber, J.L. Arolas & F.X. Gomis-Rüth * (2014). The pCri system: a vector collection for recombinant protein expression and purification. PLoS ONE, 9, e112643
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