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10 p, 3.5 MB |
Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium
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Aparicio Alarcón, David (Instituto de Biología Molecular de Barcelona) ;
Scheffer, Margot P. (Buchmann Institute for Molecular Life Sciences) ;
Marcos-Silva, Marina (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Vizarraga, David (Instituto de Biología Molecular de Barcelona) ;
Sprankel, Lasse (Buchmann Institute for Molecular Life Sciences) ;
Ratera, Mercè (Instituto de Biología Molecular de Barcelona) ;
Weber, Miriam S. (Buchmann Institute for Molecular Life Sciences) ;
Seybert, Anja (Buchmann Institute for Molecular Life Sciences) ;
Torres-Puig, Sergi (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Gonzalez-Gonzalez, Luis (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Reitz, Julian (Buchmann Institute for Molecular Life Sciences) ;
Querol, Enrique (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Piñol Ribas, Jaume (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Quijada Pich, Oscar (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Fita, Ignacio (Instituto de Biología Molecular de Barcelona) ;
Frangakis, Achilleas S. (Buchmann Institute for Molecular Life Sciences)
Mycoplasma genitalium is a human pathogen adhering to host target epithelial cells and causing urethritis, cervicitis and pelvic inflammatory disease. Essential for infectivity is a transmembrane adhesion complex called Nap comprising proteins P110 and P140. [...]
2020 -  10.1038/s41467-020-16511-2
Nature communications, Vol. 11 (June 2020) , art. 2877
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15 p, 3.9 MB |
Cavity filling mutations at the thyroxine-binding site dramatically increase transthyretin stability and prevent its aggregationres
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Sant'Anna, Ricardo (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Almedia, Maria Rosario (Instituto de Investigação e Inovação em Saúde da Universidade do Porto) ;
Varejao, Nathalia (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Gallego Alonso, Pablo (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Esperante, Sebastián (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Ferreira, Priscilla (Instituto de Bioquímica Médica Leopoldo de Meis) ;
Pereira-Henriques, Alda (Instituto de Investigação e Inovação em Saúde da Universidade do Porto) ;
Palhano, Fernando L. (Instituto de Bioquímica Médica Leopoldo de Meis) ;
De Carvalho, Mamede (Department Neurosciences. Hospital de Santa Maria. CHLN) ;
Foguel, Debora (Instituto de Bioquímica Médica Leopoldo de Meis) ;
Reverter i Cendrós, David (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Saraiva, Maria Joao (Instituto de Investigação e Inovação em Saúde da Universidade do Porto) ;
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
More than a hundred different Transthyretin (TTR) mutations are associated with fatal systemic amyloidoses. They destabilize the protein tetrameric structure and promote the extracellular deposition of TTR as pathological amyloid fibrils. [...]
2017 - 10.1038/srep44709
Scientific reports (Nature Publishing Group), Vol. 7 (2017) , art. 44709
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12 p, 1.7 MB |
Mechanistic basis of Nek7 activation through Nek9 binding and induced dimerization
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Haq, Tamanna (University of Leicester. Department of Biochemistry) ;
Richards, Mark W. (University of Leicester. Department of Biochemistry) ;
Burgess, Selena G. (University of Leicester. Department of Biochemistry) ;
Gallego Alonso, Pablo (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Yeoh, Sharon (University of Leicester. Department of Biochemistry) ;
O'Regan, Laura (University of Leicester. Department of Biochemistry) ;
Reverter i Cendrós, David (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Roig, Joan (Institut de Recerca Biomèdica de Lleida) ;
Fry, Andrew M. (University of Leicester. Department of Biochemistry) ;
Bayliss, Richard (Cancer Research UK Leicester Centre)
Mitotic spindle assembly requires the regulated activities of protein kinases such as Nek7 and Nek9. Nek7 is autoinhibited by the protrusion of Tyr97 into the active site and activated by the Nek9 non-catalytic C-terminal domain (CTD). [...]
2015 - 10.1038/ncomms9771
Nature communications, Vol. 6 (2015) , art. 8771
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13 p, 2.9 MB |
Efficacy of aldose reductase inhibitors is affected by oxidative stress induced under X-ray irradiation
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Castellví Toledo, Albert (ALBA Laboratori de Llum de Sincrotró) ;
Crespo, Isidro (ALBA Laboratori de Llum de Sincrotró) ;
Crosas, Eva (ALBA Laboratori de Llum de Sincrotró) ;
Cámara Artigas, Ana (Universidad de Almería) ;
Gavira, José A. (Universidad de Granada) ;
Aranda, Miguel A. G. (ALBA Laboratori de Llum de Sincrotró) ;
Parés i Casasampera, Xavier (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Farrés, Jaume (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Juanhuix, Judith (ALBA Laboratori de Llum de Sincrotró)
Human aldose reductase (hAR, AKR1B1) has been explored as drug target since the 1980s for its implication in diabetic complications. An activated form of hAR was found in cells from diabetic patients, showing a reduced sensitivity to inhibitors in clinical trials, which may prevent its pharmacological use. [...]
2019 - 10.1038/s41598-019-39722-0
Scientific reports (Nature Publishing Group), Vol. 9 (February 2019) , art. 3177
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14 p, 4.7 MB |
Efficient blue light emitting materials based on : M -carborane-anthracene dyads. Structure, photophysics and bioimaging studies
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Chaari, Mahdi (Institut de Ciència de Materials de Barcelona) ;
Kelemen, Zsolt (Institut de Ciència de Materials de Barcelona) ;
Choquesillo-Lazarte, Duane (Laboratorio de Estudios Cristalográficos) ;
Gaztelumendi, Nerea (Universitat Autònoma de Barcelona. Departament de Biologia Cel·lular, de Fisiologia i d'Immunologia) ;
Teixidor, Francesc (Institut de Ciència de Materials de Barcelona) ;
Viñas, Clara (Institut de Ciència de Materials de Barcelona) ;
Nogués, Carme (Universitat Autònoma de Barcelona. Departament de Biologia Cel·lular, de Fisiologia i d'Immunologia) ;
Núñez, Rosario (Institut de Ciència de Materials de Barcelona)
Efficient monosubstitution of the non-iodinated, mono-iodinated and di-iodinated m-carborane cluster at one C has led to the preparation of three single organic molecule-carborane dyads (4-6), which exhibited exceptional fluorescence properties with quantum yield values of 100% in solution, for all of them, with maxima around 415 nm, which correspond to the locally excited state (LE) emission. [...]
2019 - 10.1039/c9bm00903e
Biomaterials science, Vol. 7, Issue 12 (October 2019) , p. 5324-5337
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17 p, 4.3 MB |
Discovery of processive catalysis by an exo-hydrolase with a pocket-shaped active site
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Streltsov, Victor A. (Commonwealth Scientific and Industrial Research Organisation, Materials Science and Engineering) ;
Luang, Sukanya (University of Adelaide. School of Agriculture, Food and Wine) ;
Peisley, Alys (Commonwealth Scientific and Industrial Research Organisation, Materials Science and Engineering) ;
Varghese, Joseph N. (Commonwealth Scientific and Industrial Research Organisation. Materials Science and Engineering) ;
Ketudat Cairns, James R. (Suranaree University of Technology. School of Chemistry) ;
Fort, Sebastien (University Grenoble Alpes. Centre de Recherches sur les Macromolécules Végétales) ;
Hijnen, Marcel (GE Healthcare Life Sciences) ;
Tvaroška, Igor (Slovak Academy of Sciences. Institute of Chemistry) ;
Ardá, Ana (CIC bioGUNE) ;
Jiménez Barbero, Jesús (CIC bioGUNE) ;
Alfonso Prieto, Mercedes (Universitat de Barcelona. Departament de Química Inorgànica i Orgànica) ;
Rovira, Carme (Universitat de Barcelona. Departament de Química Inorgànica i Orgànica) ;
Mendoza, Fernanda (Universitat Autònoma de Barcelona. Departament de Química) ;
Tiessler Sala, Laura. (Universitat Autònoma de Barcelona. Departament de Química) ;
Sánchez-Aparicio, José-Emilio (Universitat Autònoma de Barcelona. Departament de Química) ;
Rodríguez-Guerra Pedregal, Jaime (Universitat Autònoma de Barcelona. Departament de Química) ;
Lluch López, Josep Maria (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Maréchal, Jean-Didier (Universitat Autònoma de Barcelona. Departament de Química) ;
Masgrau, Laura (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Hrmova, Maria (University of Adelaide. School of Agriculture, Food and Wine)
Substrates associate and products dissociate from enzyme catalytic sites rapidly, which hampers investigations of their trajectories. The high-resolution structure of the native Hordeum exo-hydrolase HvExoI isolated from seedlings reveals that non-covalently trapped glucose forms a stable enzyme-product complex. [...]
2019 - 10.1038/s41467-019-09691-z
Nature communications, Vol. 10 (2019) , p. 2222
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9 p, 7.2 MB |
Low-cost and portable UV holographic microscope for high-contrast protein crystal imaging
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Daloglu, Mustafa Ugur (University of California) ;
Ray, Aniruddha (University of California) ;
Collazo, Michael J. (University of California) ;
Brown, Calvin (University of California) ;
Tseng, Derek (University of California) ;
Chocarro Ruiz, Blanca (Institut Català de Nanociència i Nanotecnologia) ;
Lechuga, Laura (Institut Català de Nanociència i Nanotecnologia) ;
Cascio, Duilio (University of California) ;
Ozcan, Aydogan (University of California)
Imaging protein crystals and distinguishing them from salt crystals is an important task for protein crystallographers. The conventional tool used for this purpose is a dual-mode microscope composed of bright-field and ultraviolet (UV) induced fluorescence modes. [...]
2019 - 10.1063/1.5080158
APL Photonics, Vol. 4, Issue 3 (March 2019) , art. 30804
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