Resultados globales: 10 registros encontrados en 0.04 segundos.
Artículos, Encontrados 10 registros
Artículos Encontrados 10 registros  
1.
14 p, 4.5 MB Ultrafast action chemistry in slow motion : atomistic description of the excitation and fluorescence processes in an archetypal fluorescent protein / Armengol Torrella, Pau (Universitat Autònoma de Barcelona. Departament de Química) ; Spörkel, Lasse (Max-Planck-Institut für Kohlenforschung) ; Gelabert Peiri, Ricard (Universitat Autònoma de Barcelona. Departament de Química) ; Moreno Ferrer, Miquel (Universitat Autònoma de Barcelona. Departament de Química) ; Thiel, Walter (Max-Planck-Institut für Kohlenforschung) ; Lluch López, Josep Maria (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
We report quantum mechanical/molecular mechanical non-adiabatic molecular dynamics simulations on the electronically excited state of green fluorescent protein mutant S65T/H148D. We examine the driving force of the ultrafast (τ < 50 fs) excited-state proton transfer unleashed by absorption in the A band at 415 nm and propose an atomistic description of the two dynamical regimes experimentally observed [Stoner Ma et al. [...]
2018 - 10.1039/c8cp00371h
Physical chemistry chemical physics, Vol. 20, issue 16 (2018) , p. 11067-11080  
2.
16 p, 3.9 MB Plasticity in the Oxidative Folding Pathway of the High Affinity Nerita Versicolor Carboxypeptidase Inhibitor (NvCI) / Esperante, Sebastián (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Bronsoms i Fabrellas, Sílvia (Universitat Autònoma de Barcelona. Servei de Proteòmica i Biologia Estructural) ; Covaleda Cortés, Giovanni (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 Biologia Molecular) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i 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 (Nature Publishing Group), Vol. 7 (2017) , art. 5457  
3.
10 p, 6.7 MB Structural analysis and evolution of specificity of the SUMO UFD E1-E2 interactions / Liu, Bing (Institut de Biotecnologia i de Biomedicina) ; Lois, L. Maria (Centre de Recerca en Agrigenòmica) ; Reverter i Cendrós, David (Institut de Biotecnologia i de Biomedicina) ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
SUMO belongs to the ubiquitin-like family (UbL) of protein modifiers. SUMO is conserved among eukaryotes and is essential for the regulation of processes such as DNA damage repair, transcription, DNA replication and mitosis. [...]
2017 - 10.1038/srep41998
Scientific reports (Nature Publishing Group), Vol. 7 (February 2017) , art. 41998  
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 (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  
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 (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 Biologia Molecular) ; Piñol Ribas, Jaume (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Quijada Pich, Oscar (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  
6.
16 p, 3.8 MB Disulfide driven folding for a conditionally disordered protein / Fraga, Hugo (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pujols, Jordi (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Gil-Garcia, Marcos (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Roque Córdova, Alicia (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Bernardo-Seisdedos, Ganeko (CIC BioGUNE) ; Santambrogio, Carlo (University of Milano-Bicocca. Dipartimento di Biotecnologie e Bioscienze) ; Bech-Serra, Joan-Josep (Vall d'Hebron Institute d'Oncologia) ; Canals, Francesc (Vall d'Hebron Institute d'Oncologia) ; Bernadó, Pau (Centre de biochimie Structurale (Montpellier)) ; Grandori, Rita (University of Milano-Bicocca. Dipartimento di Biotecnologie e Bioscienze) ; Millet, Oscar (CIC BioGUNE) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Conditionally disordered proteins are either ordered or disordered depending on the environmental context. The substrates of the mitochondrial intermembrane space (IMS) oxidoreductase Mia40 are synthesized on cytosolic ribosomes and diffuse as intrinsically disordered proteins to the IMS, where they fold into their functional conformations; behaving thus as conditionally disordered proteins. [...]
2017 - 10.1038/s41598-017-17259-4
Scientific reports (Nature Publishing Group), Vol. 7 (2017) , art. 16994  
7.
16 p, 3.8 MB Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria / Macedo, Bruno (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Sant'Anna, Ricardo (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Navarro Cantero, Susanna (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Cordeiro, Yraima (Universidade Federal do Rio de Janeiro. Faculdade de Farmácia) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Background: An increasing number of proteins are being shown to assemble into amyloid structures that lead to pathological states. Among them, mammalian prions outstand due to their ability to transmit the pathogenic conformation, becoming thus infectious. [...]
2015 - 10.1186/s12934-015-0361-y
Microbial cell factories, Vol. 14 (2015) , art. 174  
8.
15 p, 1.8 MB A model of protein association based on their hydrophobic and electric interactions / Mozo Villarías, Angel (Institut de Recerca Biomèdica de Lleida) ; Cedano, Juan (Universidad de la República (Uruguai).Laboratorio de Inmunología) ; Querol Murillo, Enrique (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
The propensity of many proteins to oligomerize and associate to form complex structures from their constituent monomers, is analyzed in terms of their hydrophobic (H), and electric pseudo-dipole (D) moment vectors. [...]
2014 - 10.1371/journal.pone.0110352
PloS one, Vol. 9 issue 10 (2014) , art. e110352  
9.
7 p, 899.7 KB Common features in the unfolding and misfolding of PDZ domains and beyond : the modulatory effect of domain swapping and extra-elements / Murciano Calles, Javier (Universidad de Granada. Departamento de Química Física) ; Güell Bosch, Jofre (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Villegas Hernández, Sandra (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Martínez, José C. (Universidad de Granada. Departamento de Química Física)
PDZ domains are protein-protein interaction modules sharing the same structural arrangement. To discern whether they display common features in their unfolding/misfolding behaviour we have analyzed in this work the unfolding thermodynamics, together with the misfolding kinetics, of the PDZ fold using three archetypical examples: the second and third PDZ domains of the PSD95 protein and the Erbin PDZ domain. [...]
2016 - 10.1038/srep19242
Scientific reports (Nature Publishing Group), Vol. 6 (January 2016) , art. 19242  
10.
21 p, 6.7 MB Identification and characterization of new isoforms of human fas apoptotic inhibitory molecule (FAIM) / Coccia, Elena (Universitat Autònoma de Barcelona. Institut de Neurociències. Departament de Bioquímica i Biologia Molecular) ; Calleja Yagüe, Isabel (Universitat Autònoma de Barcelona. Institut de Neurociències. Departament de Bioquímica i Biologia Molecular) ; Planells Ferrer, Laura (Universitat Autònoma de Barcelona. Institut de Neurociències. Departament de Bioquímica i Biologia Molecular) ; Sanuy, Blanca (Universitat Autònoma de Barcelona. Institut de Neurociències. Departament de Bioquímica i Biologia Molecular) ; Sanz, Belen (Cell Division and Cancer Group. Spanish National Cancer Research Centre (CNIO)) ; López Soriano, Joaquin (Universitat Autònoma de Barcelona. Institut de Neurociències. Departament de Bioquímica i Biologia Molecular) ; Moubarak, Rana S. (Department of Pathology. NYU Langone Medical Center) ; Munell Casadesus, Francina (Vall d'Hebron Institut de Recerca(VHIR)) ; Barneda Zahonero, Bruna (Universitat Autònoma de Barcelona. Institut de Neurociències. Departament de Bioquímica i Biologia Molecular) ; Comella i Carnicé, Joan Xavier 1963- (Universitat Autònoma de Barcelona. Institut de Neurociències. Departament de Bioquímica i Biologia Molecular) ; Pérez García, María José (Universitat Autònoma de Barcelona. Institut de Neurociències. Departament de Bioquímica i Biologia Molecular)
Fas Apoptosis Inhibitory Molecule (FAIM) is an evolutionarily highly conserved death receptor antagonist, widely expressed and known to participate in physiological and pathological processes. Two FAIM transcript variants have been characterized to date, namely FAIM short (FAIM-S) and FAIM long (FAIM-L). [...]
2017 - 10.1371/journal.pone.0185327
PloS one, Vol. 12 Núm. 10 (october 2017) , p. e0185327  

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