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2 p, 169.5 KB |
Nou mecanisme molecular en la reparació de DNA
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Reverter i Cendrós, David (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Un estudi liderat per un equip de recerca de l'IBB i del Departament de Bioquímica i Biologia Molecular de la UAB, ha revelat el funcionament d'un complex enzimàtic format per un conjunt de proteïnes: -una E3 lligasa unida a una E2 i a dos SUMO, i ha identificat els punts clau per al funcionament correcte d'aquesta E3 lligasa, que participa en la reparació de dany a l'ADN a través de modificacions post-traduccionals per SUMO.
Un estudio liderado por un equipo de investigación del IBB y del Departamento de Bioquímica y Biología Molecular de la UAB ha revelado el funcionamiento de un complejo enzimático formado por un conjunto de proteínas: una E3 ligasa, unida a una E2 y a dos SUMO, y ha identificado los puntos clave para el correcto funcionamiento de esta E3 ligasa, que participa en la reparación de daño en el ADN a través de modificaciones post-traduccionales por SUMO.
A study led by a researcher teams from the IBB and the Department of Biochemistry and Molecular Biology of the UAB has revealed the functioning of an enzyme complex formed by a set of proetines -an E3 ligase, linked to an E2 and two SUMOs, identifying the key points for the correct function of this E3 ligase that participates in the repair of DNA damage through post-translational modifications by SUMO.
2022
UAB divulga, Gener 2022
3 documentos
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14 p, 2.5 MB |
Disease-associated mutations impacting BC-loop flexibility trigger long-range transthyretin tetramer destabilization and aggregation
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Esperante, Sebastián A. (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Varejāo, Nathalia (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Pinheiro, Francisca (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Sant'Anna, Ricardo (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Luque-Ortega, Juan Román (Centro de Investigaciones Biológicas Margarita Salas) ;
Alfonso, Carlos (Centro de Investigaciones Biológicas Margarita Salas) ;
Sora, Valentina (Technical University of Denmark. Cancer Systems Biology, Health and Technology Department) ;
Papaleo, Elena (Technical University of Denmark. Cancer Systems Biology, Health and Technology Department) ;
Rivas, Germán (Centro de Investigaciones Biológicas Margarita Salas) ;
Reverter i Cendrós, David (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Hereditary transthyretin amyloidosis (ATTR) is an autosomal dominant disease characterized by the extracellular deposition of the transport protein transthyretin (TTR) as amyloid fibrils. Despite the progress achieved in recent years, understanding why different TTR residue substitutions lead to different clinical manifestations remains elusive. [...]
2021 -  10.1016/j.jbc.2021.101039
Journal of biological chemistry, Vol. 297, Issue 3 (September 2021) , art. 101039
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20 p, 10.5 MB |
Binding site profiles and N-terminal minor groove interactions of the master quorum-sensing regulator LuxR enable flexible control of gene activation and repression
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Zhang, Jun (East China University of Science and Technology. State Key Laboratory of Bioreactor Engineering (China)) ;
Liu, Bing (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Gu, Dan (Yangzhou University. Jiangsu Co-Innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonoses (China)) ;
Hao, Yuan (East China University of Science and Technology. State Key Laboratory of Bioreactor Engineering (China)) ;
Chen, Mo (East China University of Science and Technology. State Key Laboratory of Bioreactor Engineering (China)) ;
Ma, Yue (East China University of Science and Technology. State Key Laboratory of Bioreactor Engineering (China)) ;
Zhou, Xiaohui (University of Connecticut. Department of Pathobiology and Veterinary Science (USA)) ;
Reverter i Cendrós, David (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Zhang, Yuanxing (Southern Marine Science and Engineering Guangdong Laboratory (China)) ;
Wang, Qiyao (East China University of Science and Technology. State Key Laboratory of Bioreactor Engineering (China)) ;
Universitat Autònoma de Barcelona.
Departament de Bioquímica i de Biologia Molecular
LuxR is a TetR family master quorum sensing (QS) regulator activating or repressing expression of hundreds of genes that control collective behaviors in Vibrios with underlying mechanism unknown. To illuminate how this regulator controls expression of various target genes, we applied ChIP-seq and DNase I-seq technologies. [...]
2021 - 10.1093/nar/gkab150
Nucleic acids research, Vol. 49, Issue 6 (April 2021) , p. 3274-3293
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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 (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") ;
Robinson, Lei Z. (Scripps Research Institute) ;
Pereira-Henriques, Alda (Instituto de Ciências Biomédicas de Abel Salazar (Porto, Portugal)) ;
Ferreira, Nelson (Instituto de Ciências Biomédicas de Abel Salazar (Porto, Portugal)) ;
Pinheiro, Francisca (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") ;
Pallarès i Goitiz, Irantzu (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Huertas, Oscar (SOM-Biotech) ;
Almeida, Maria Rosário (Instituto de Ciências Biomédicas de Abel Salazar (Porto, Portugal)) ;
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 (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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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 Bioquímica i de Biologia Molecular) ;
Garcia-Pardo, Javier (Institut Català de Nanociència i Nanotecnologia) ;
Berenguer de la Cuesta, Esther (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Fernandez-Alvarez, Roberto (Universitat Autònoma de Barcelona. Departament de Bioquímica i de 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 Bioquímica i de Biologia Molecular) ;
Huber, Robert (Technische Universität München) ;
Lorenzo Rivera, Julia (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Reverter i Cendrós, David (Universitat Autònoma de Barcelona. Departament de Bioquímica i de 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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