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Resultados globales: 8 registros encontrados en 0.03 segundos.
Artículos, Encontrados 8 registros
Artículos Encontrados 8 registros  
1.
17 p, 4.4 MB Exploring the RNase A scaffold to combine catalytic and antimicrobial activities. Structural characterization of RNase 3/1 chimeras / Fernández-Millán, Pablo (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) ; Prats-Ejarque, Guillem (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Vázquez-Monteagudo, Sergi (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Design of novel antibiotics to fight antimicrobial resistance is one of the first global health priorities. Novel protein-based strategies come out as alternative therapies. Based on the structure-function knowledge of the RNase A superfamily we have engineered a chimera that combines RNase 1 highest catalytic activity with RNase 3 unique antipathogen properties. [...]
2022 - 10.3389/fmolb.2022.964717
Frontiers in Molecular Biosciences, Vol. 9 (September 2022) , art. 964717  
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2.
43 p, 2.5 MB Validation and Applications of Protein-Ligand Docking Approaches Improved for Metalloligands with Multiple Vacant Sites / Sciortino, Giuseppe (Universitat Autònoma de Barcelona. Departament de Química) ; Garribba, Eugenio (Università di Sassari. Dipartimento di Chimica e Farmacia) ; Maréchal, Jean-Didier (Universitat Autònoma de Barcelona. Departament de Química)
Decoding the interaction between coordination compounds and proteins is of fundamental importance in biology, pharmacy, and medicine. In this context, protein-ligand docking represents a particularly interesting asset to predict how small compounds could interact with biomolecules, but to date, very little information is available to adapt these methodologies to metal-containing ligands. [...]
2019 - 10.1021/acs.inorgchem.8b02374
Inorganic chemistry, Vol. 58, Issue 1 (January 2019) , p. 294-306  
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3.
16 p, 3.9 MB Plasticity in the Oxidative Folding Pathway of the High Affinity Nerita Versicolor Carboxypeptidase Inhibitor (NvCI) / Esperante, Sebastián (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Bronsoms, Sílvia (Universitat Autònoma de Barcelona. Servei de Proteòmica i Biologia Estructural) ; Covaleda Cortés, Giovanni (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Trejo, Sebastián A. (Universitat Autònoma de Barcelona. Servei de Proteòmica i Biologia Estructural) ; Avilés, Francesc X. (Francesc Xavier) (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Nerita Versicolor carboxypeptidase inhibitor (NvCI) is the strongest inhibitor reported so far for the M14A subfamily of carboxypeptidases. It comprises 53 residues and a protein fold composed of a two-stranded antiparallel β sheet connected by three loops and stabilized by three disulfide bridges. [...]
2017 - 10.1038/s41598-017-05657-7
Scientific reports, Vol. 7 (2017) , art. 5457  
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4.
15 p, 3.9 MB Cavity filling mutations at the thyroxine-binding site dramatically increase transthyretin stability and prevent its aggregationres / 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, Vol. 7 (2017) , art. 44709  
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5.
11 p, 3.5 MB Mycoplasma genitalium adhesin P110 binds sialic-acid human receptors / Aparicio Alarcón, David (Institut de Biologia Molecular de Barcelona) ; Torres Puig, Sergi (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ratera, Mercè (Institut de Biologia Molecular de Barcelona) ; Querol Murillo, Enrique (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Piñol Ribas, Jaume (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Quijada Pich, Oscar (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Fita Rodríguez, Ignasi (Institut de Biologia Molecular de Barcelona)
Adhesion of pathogenic bacteria to target cells is a prerequisite for colonization and further infection. The main adhesins of the emerging sexually transmitted pathogen Mycoplasma genitalium, P140 and P110, interact to form a Nap complex anchored to the cell membrane. [...]
2018 - 10.1038/s41467-018-06963-y
Nature communications, Vol. 9 (2018) , art. 4471  
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6.
19 p, 5.2 MB Computational insight into the catalytic implication of head/tail-first orientation of arachidonic acid in human 5-lipoxygenase : consequences for the positional specificity of oxygenation / Saura Martínez, Patricia (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") ; Lluch López, Josep Maria (Universitat Autònoma de Barcelona. Departament de Química) ; González-Lafont, Àngels (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
In the present work we have combined homology modeling, protein-ligand dockings, quantum mechanics/molecular mechanics calculations and molecular dynamics simulations to generate human 5-lipoxygenase (5-LOX):arachidonic acid (AA) complexes consistent with the 5-lipoxygenating activity (which implies hydrogen abstraction at the C position). [...]
2016 - 10.1039/c6cp03973a
Physical chemistry chemical physics, Vol. 18, issue 33 (2016) , p. 23017-23035  
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7.
17 p, 1.7 MB Intradomain confinement of disulfides in the folding of two consecutive modules of the LDL receptor / Martínez-Oliván, Juan (Universidad de Zaragoza. Departamento de Bioquímica y Biología Molecular y Celular) ; Fraga, Hugo (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Arias-Moreno, Xabier (Universidad de Zaragoza. Departamento de Bioquímica y Biología Molecular y Celular) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Sancho, Javier (Universidad de Zaragoza. Departamento de Bioquímica y Biología Molecular y Celular)
The LDL receptor internalizes circulating LDL and VLDL particles for degradation. Its extracellular binding domain contains ten (seven LA and three EGF) cysteine-rich modules, each bearing three disulfide bonds. [...]
2015 - 10.1371/journal.pone.0132141
PloS one, Vol. 10, issue 7 (2015) , art. e0132141  
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8.
12 p, 1.7 MB Mechanistic basis of Nek7 activation through Nek9 binding and induced dimerization / 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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