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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 (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 (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Gallego Alonso, Pablo (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Esperante, Sebastián (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 (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) ;
García Aranda, Miguel Ángel (ALBA Laboratori de Llum de Sincrotró) ;
Parés i Casasampera, Xavier (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Farrés i Vicén, 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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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, J.E (Universitat Autònoma de Barcelona. Departament de Química) ;
Rodríguez-Guerra Pedregal, Jaime (Universitat Autònoma de Barcelona. Departament de Química) ;
Lluch López, Josep Maria (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Maréchal, Jean-Didier (Universitat Autònoma de Barcelona. Departament de Química) ;
Masgrau, Laura (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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48 p, 8.9 MB |
The first crystal structure of human RNase6 reveals a novel substrate binding and cleavage site arrangement
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Prats, Guillem, 1942- (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Arranz Trullén, Javier (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Blanco, JA. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Pulido, Daniel. (Imperial College London) ;
Nogués, MV. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Moussaoui, Mohammed. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Boix i Borràs, Esther (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Human RNase 6 is a cationic secreted protein that belongs to the RNase A superfamily. Its expression is induced in neutrophils and monocytes upon bacterial infection, suggesting a role in host defence. [...]
2016 - 10.1042/BCJ20160245
The Biochemical journal, 2016
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3 p, 215.1 KB |
[1,9-Bis(3,5-dimethylpyrazol-1-yl-κN2)-3,7-dithianonane-κ2S,S']palladium(II) bis(tetrafluoroborate)
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García-Antón Aviñó, Jordi (Universitat Autònoma de Barcelona. Departament de Química) ;
Pons Picart, Josefina (Universitat Autònoma de Barcelona. Departament de Química) ;
Ros i Badosa, Josep (Universitat Autònoma de Barcelona. Departament de Química) ;
Solans, Xavier, 1949-2007 (Universitat de Barcelona. Departament de Cristal·lografia, Mineralogia i Dipòsits Minerals) ;
Font Bardia, Ma. Mercedes (Universitat de Barcelona. Departament de Cristal·lografia, Mineralogia i Dipòsits Minerals)
In the crystal structure of the title compound, [Pd(C17H28N4S2)](BF4)2, the PdII atom is coordinated by one N atom from each of the pyrazolyl groups and the two thio¬ether S atoms in a slightly distorted square-planar geometry.
2004 - 10.1107/S1600536804016022
Acta crystallographica. Section E : Structure reports online, Vol. 60, Issue 8 (August 2004) , p. 1087-1089
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