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13 p, 1.1 MB |
Repositioning tolcapone as a potent inhibitor of transthyretin amyloidogenesis and associated cellular toxicity
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Sant'Anna, Ricardo (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Gallego Alonso, Pablo (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Robinson, Lei Z. (Scripps Research Institute) ;
Pereira-Henriques, Alda (Instituto de Ciências Biomédicas de Abel Salazar) ;
Ferreira, Nelson (Instituto de Ciências Biomédicas de Abel Salazar) ;
Pinheiro, Francisca (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Esperante, Sebastián (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Pallarès i Goitiz, Irantzu (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ;
Huertas, Oscar (SOM-Biotech) ;
Almeida, Maria Rosário (Instituto de Ciências Biomédicas de Abel Salazar) ;
Reixach, Natàlia (Scripps Research Institute) ;
Insa, Raul (SOM-Biotech) ;
Velazquez-Campoy, Adrián (Universidad de Zaragoza. Departamento de Bioquímica y Biología Celular y Molecular) ;
Reverter i Cendrós, David (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Reig, Núria (SOM-Biotech) ;
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Transthyretin (TTR) is a plasma homotetrameric protein implicated in fatal systemic amyloidoses. TTR tetramer dissociation precedes pathological TTR aggregation. Native state stabilizers are promising drugs to treat TTR amyloidoses. [...]
2016 -  10.1038/ncomms10787
Nature communications, Vol. 7 (2016) , art. 10787
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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, 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) ;
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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29 p, 862.1 KB |
Crystal structure and mechanism of human carboxypeptidase O : insights into its specific activity for acidic residues
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García Guerrero, María del Carmen (Universitat Autònoma de Barcelona. Departament de Bioquimica i Biologia Molecular) ;
Garcia-Pardo, Javier (Institut Català de Nanociència i Nanotecnologia) ;
Berenguer de la Cuesta, Esther (Universitat Autònoma de Barcelona. Departament de Bioquimica i Biologia Molecular) ;
Fernández Álvarez, Roberto (Universitat Autònoma de Barcelona. Departament de Bioquimica i Biologia Molecular) ;
Barfi, Gifty B. (Andrews University. Department of Biology) ;
Lyons, Peter J. (Andrews University. Department of Biology) ;
Avilés, Francesc X. (Francesc Xavier) (Universitat Autònoma de Barcelona. Departament de Bioquimica i Biologia Molecular) ;
Huber, Robert (Technische Universität München) ;
Lorenzo Rivera, Julia (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ;
Reverter i Cendrós, David (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Human metallocarboxypeptidase O (hCPO) is a recently discovered digestive enzyme localized to the apical membrane of intestinal epithelial cells. Unlike pancreatic metallocarboxypeptidases, hCPO is glycosylated and produced as an active enzyme with distinctive substrate specificity toward C-terminal (C-t) acidic residues. [...]
2018 - 10.1073/pnas.1803685115
Proceedings of the National Academy of Sciences of the United States of America, Vol. 115, Issue 17 (April 2018) , p. E3932-E3939
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14 p, 2.3 MB |
SUMO-2 and PIAS1 modulate insoluble mutant huntingtin protein accumulation
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O'Rourke, Jacqueline Gire (University of California) ;
Gareau, Jaclyn R. (Sloan-Kettering Institute) ;
Ochaba, Joseph (University of California) ;
Song, Wan (University of California) ;
Raskó, Tamás (Max-Delbrueck-Center for Molecular Medicine) ;
Reverter i Cendrós, David (Sloan-Kettering Institute) ;
Lee, John (University of Iowa) ;
Mas Monteys, Alexandre (University of Iowa) ;
Pallos, Judit (University of California) ;
Mee, Lisa (University of California) ;
Vashishtha, Malini (University of California) ;
Apostol, Barbara L. (University of California) ;
Nicholson, Thomas Peter (Enzo Life Sciences Ltd.) ;
Illes, Katalin (University of California) ;
Zhu, Ya-Zhen (University of California) ;
Dasso, Mary (National Institute of Child Health and Development) ;
Bates, Gillian P. (King's College London School of Medicine) ;
Difiglia, Marian (Massachusetts General Hospital and Harvard Medical School) ;
Davidson, Beverly (University of Iowa) ;
Wanker, Erich E. (Max-Delbrueck-Center for Molecular Medicine) ;
Marsh, J. Lawrence (University of California) ;
Lima, Christopher D. (Sloan-Kettering Institute) ;
Steffan, Joan S. (University of California) ;
Thompson, Leslie M. (University of California.)
A key feature in Huntington disease (HD) is the accumulation of mutant Huntingtin (HTT) protein, which may be regulated by posttranslational modifications. Here, we define the primary sites of SUMOmodification in the amino-terminal domain of HTT, show modification downstream of this domain, and demonstrate that HTT is modified by the stress-inducible SUMO-2. [...]
2013 - 10.1016/j.celrep.2013.06.034
Cell reports, Vol. 4, Issue 2 (July 2013) , p. 362-375
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2 p, 399.3 KB |
Mecanisme d'activació d'una proteïna termòfila
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Reverter i Cendrós, David (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Un equip de l'Institut de Biotecnologia i de Biomedicina (IBB), en col·laboració amb el sincrotró ALBA, ha estudiat el mecanisme d'activació per temperatura d'una esterasa termòfila, caracteritzant els canvis estructurals que sofreix la proteïna a diferents temperatures, directament relacionats amb la regulació de la seva activitat biològica. [...]
2018
UAB divulga, Abril 2018, p. 1-2
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