Depósito Digital de Documentos de la UAB Encontrados 6 registros  La búsqueda tardó 0.02 segundos. 
1.
14 p, 3.5 MB Crystal structure of c5321 : a protective antigen present in uropathogenic Escherichia coli strains displaying an SLR fold / Urosev, Dunja (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ferrer Navarro, Mario (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pastorello, Ilaria (Novartis Vaccines and Diagnostics (Siena, Itàlia)) ; Cartocci, Elena (Novartis Vaccines and Diagnostics (Siena, Itàlia)) ; Costenaro, Lionel (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Zhulenkovs, Dmitrijs (ASLA Biotech (Riga, Letònia)) ; Maréchal, Jean-Didier (Universitat Autònoma de Barcelona. Departament de Química) ; Leonchiks, Ainars (ASLA Biotech (Riga, Letònia)) ; Reverter i Cendrós, David (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Serino, Laura (Novartis Vaccines and Diagnostics (Siena, Itàlia)) ; Soriani, Marco (Novartis Vaccines and Diagnostics (Siena, Itàlia)) ; Daura i Ribera, Xavier (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Background: Increasing rates of antimicrobial resistance among uropathogens led, among other efforts, to the application of subtractive reverse vaccinology for the identification of antigens present in extraintestinal pathogenic E. [...]
2013 - 10.1186/1472-6807-13-19
BMC Structural biology, Vol. 13, Núm. 19 (October 2013) , p. 1-14  
2.
11 p, 1.8 MB DockAnalyse : an application for the analysis of protein-protein interactions / Amela Abellán, Isaac (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Delicado, Pedro (Universitat Politècnica de Catalunya. Departament d'Estadística i Investigació Operativa) ; Gómez, Antonio (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Bonàs, Sílvia (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Querol Murillo, Enrique (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Cedano Rodríguez, Juan Antonio (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Background: Is it possible to identify what the best solution of a docking program is? The usual answer to this question is the highest score solution, but interactions between proteins are dynamic processes, and many times the interaction regions are wide enough to permit protein-protein interactions with different orientations and/or interaction energies. [...]
2010 - 10.1186/1472-6807-10-37
BMC Structural biology, Vol. 10, N. 37 (October 2010) , p.
2 documentos
3.
11 p, 2.4 MB The role of Cysteine 6.47 in class A GPCRs / Olivella, Mireia (Universitat de Vic. Departament de Biologia de Sistemes) ; Caltabiano, Gianluigi 1978- (Universitat Autònoma de Barcelona. Laboratori de Medicina Computacional) ; Cordomí Montoya, Arnau (Universitat Autònoma de Barcelona. Laboratori de Medicina Computacional)
Background: The CWxP motif of transmembrane helix 6 (x: any residue) is highly conserved in class A GPCRs. Within this motif, W6. 48 is a big star in the theory of the global "toggle switch" because of its key role in the activation mechanism of GPCRs upon ligand binding. [...]
2013 - 10.1186/1472-6807-13-3
BMC Structural biology, Vol. 13, Núm. 3 (March 2013) , p. 1-10
2 documentos
4.
11 p, 596.8 KB Self-assembly of human latexin into amyloid-like oilgomers / Pallarès i Goitiz, Irantzu (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Berenguer, Clara (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Avilés, Francesc X. (Francesc Xavier) (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Vendrell i Roca, Josep (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Background: In conformational disorders, it is not evident which amyloid aggregates affect specific molecular mechanisms or cellular pathways, which cause disease because of their quantity and mechanical features and which states in aggregate formation are pathogenic. [...]
2007 - 10.1186/1472-6807-7-75
BMC Structural biology, Vol. 7, N. 75 (November 2007) , p. 1-11  
5.
15 p, 658.6 KB Prediction of "hot spots" of aggregation in disease-linked polypeptides / Sánchez de Groot, Natalia (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Pallarès i Goitiz, Irantzu (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Avilés, Francesc X. (Francesc Xavier) (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Vendrell i Roca, Josep (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Background: The polypeptides involved in amyloidogenesis may be globular proteins with a defined 3D-structure or natively unfolded proteins. The first class includes polypeptides such as β2-microglobulin, lysozyme, transthyretin or the prion protein, whereas β-amyloid peptide, amylin or α-synuclein all belong to the second class. [...]
2005 - 10.1186/1472-6807-5-18
BMC Structural biology, Vol. 5, N. 18 (September 2005) , p. 1-15  
6.
14 p, 1.9 MB Assessing the structural conservation of protein pockets to study functional and allosteric sites: implications for drug discovery / Panjkovich, Alejandro (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Daura i Ribera, Xavier (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Background: With the classical, active-site oriented drug-development approach reaching its limits, protein ligand-binding sites in general and allosteric sites in particular are increasingly attracting the interest of medicinal chemists in the search for new types of targets and strategies to drug development. [...]
2010 - 10.1186/1472-6807-10-9
BMC Structural biology, Vol. 10, Núm. 9 (March 2010) , p. 9-9  

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