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Articles, 13 registres trobats
Articles 13 registres trobats  1 - 10següent  anar al registre:
1.
14 p, 2.8 MB Critical assessment of protein intrinsic disorder prediction / Necci, Marco (University of Padua. Department of Biomedical Sciences) ; Piovesan, Damiano (University of Padua. Department of Biomedical Sciences) ; Hoque, M. T. (University of New Orleans. Computer Science) ; Walsh, Ian (Agency for Science, Technology and Research. Bioprocessing Technology Institute) ; Iqbal, Sumaiya (Broad Institute of MIT and Harvard. Center for Psychiatric Research) ; Vendruscolo, Michele (University of Cambridge. Centre for Misfolding Diseases. Department of Chemistry) ; Sormanni, Pietro (University of Cambridge. Centre for Misfolding Diseases. Department of Chemistry) ; Wang, Chen (Columbia University. Department of Medicine) ; Raimondi, Daniele (ESAT-STADIUS. KU Leuven) ; Sharma, Ronesh (Fiji National University) ; Zhou, Yaoqi (Griffith University. Institute for Glycomics and School of Information and Communication Technology) ; Litfin, Thomas (Griffith University. Institute for Glycomics and School of Information and Communication Technology) ; Galzitskaya, Oxxana Valerianovna (Russian Academy of Sciences. Institute of Theoretical and Experimental Biophysics) ; Lobanov, Michail Yu (Russian Academy of Sciences. Institute of Protein Research) ; Vranken, Wim (Vrije Universiteit Brussel. Interuniversity Institute of Bioinformatics in Brussels) ; Wallner, Björn (Linköping University. Department of Physics, Chemistry and Biology) ; Mirabello, Claudio (Linköping University. Department of Physics, Chemistry and Biology) ; Malhis, Nawar (University of British Columbia. Michael Smith Laboratories) ; Dosztányi, Zsuzsanna (Eötvös Loránd University. Department of Biochemistry) ; Erdős, Gábor (Eötvös Loránd University. Department of Biochemistry) ; Mészáros, Bálint (European Molecular Biology Laboratory. Structural and Computational Biology Unit) ; Gao, Jianzhao (Nankai University. School of Mathematical Sciences and LPMC) ; Wang, Kui (Nankai University. School of Mathematical Sciences and LPMC) ; Hu, Gang (Nankai University. School of Statistics and Data Science) ; Wu, Zhonghua (Nankai University. School of Mathematical Sciences and LPMC) ; Sharma, Alok (University of the South Pacific. School of Engineering and Physics) ; Hanson, Jack (Griffith University. School of Engineering and Built Environment. Signal Processing Laboratory Griffith University. School of Engineering and Built Environment. Signal Processing Laboratory Signal Processing Laboratory. School of Engineering and Built Environment. Griffith University) ; Callebaut, Isabelle (Sorbonne Université. Institut de Minéralogie, de Physique des Matériaux et de Cosmochimie. Muséum National d'Histoire Naturelle) ; Bitard-Feildel, Tristan (Sorbonne Université. Institut de Minéralogie, de Physique des Matériaux et de Cosmochimie. Muséum National d'Histoire Naturelle) ; Orlando, Gabriele (VIB-KU Leuven. Switch Laboratorium.) ; Peng, Zhenling (Tianjin University. Center for Applied Mathematics) ; Xu, Jinbo (Toyota Technological Institute at Chicago) ; Wang, Sheng (Toyota Technological Institute at Chicago) ; Jones, David T. (University College London) ; Cozzetto, Domenico (University College London) ; Meng, Fanchi (University of Alberta. Department of Electrical and Computer Engineering) ; Yan, Jing (University of Alberta. Department of Electrical and Computer Engineering) ; Gsponer, Jörg (University of British Columbia. Michael Smith Laboratories) ; Cheng, Jianlin (University of Missouri. Department of Electrical Engineering and Computer Science) ; Wu, Tianqi (University of Missouri. Department of Electrical Engineering and Computer Science) ; Kurgan, Lukasz (Virginia Commonwealth University. Department of Computer Science) ; Promponas, Vasilis J. (University of Cyprus. Department of Biological Sciences. Bioinformatics Research Laboratory) ; Tamana, Stella (University of Cyprus. Department of Biological Sciences. Bioinformatics Research Laboratory) ; Marino-Buslje, Cristina (Fundación Instituto Leloir (Buenos Aires, Argentina)) ; Martínez-Pérez, Elisabeth (Fundación Instituto Leloir (Buenos Aires, Argentina)) ; Chasapi, Anastasia (Centre for Research & Technology Hellas. Chemical Process & Energy Resources Institute) ; Ouzounis, Christos (Centre for Research & Technology Hellas. Chemical Process & Energy Resources Institute) ; Dunker, A. Keith (Indiana University School of Medicine. Center for Computational Biology and Bioinformatics) ; Kajava, Andrey V (University of Montpellier. Centre de Recherche en Biologie cellulaire de Montpellier) ; Leclercq, Jeremy Y. (University of Montpellier. Centre de Recherche en Biologie cellulaire de Montpellier) ; Aykac-Fas, Burcu (Danish Cancer Society Research Center) ; Lambrughi, Matteo (Danish Cancer Society Research Center) ; Maiani, Emiliano (Danish Cancer Society Research Center) ; Papaleo, Elena (Danish Cancer Society Research Center) ; Chemes, Lucía Beatriz (Universidad Nacional de San Martín. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Biotecnológicas) ; Álvarez, Lucía (Universidad Nacional de San Martín. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Biotecnológicas) ; González-Foutel, Nicolás S. (Universidad Nacional de San Martín. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Biotecnológicas) ; Iglesias, Valentin (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Pujols Pujol, Jordi (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Palopoli, Nicolas (Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología) ; Benítez, Guillermo I (Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología) ; Parisi, Gustavo (Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología) ; Bassot, Claudio (Stockholm University. Department of Biochemistry and Biophysics and Science for Life Laboratory) ; Elofsson, Arne (Stockholm University. Department of Biochemistry and Biophysics and Science for Life Laboratory) ; Govindarajan, Sudha (Stockholm University. Department of Biochemistry and Biophysics and Science for Life Laboratory) ; Lamb, John (Stockholm University. Department of Biochemistry and Biophysics and Science for Life Laboratory) ; Salvatore, Marco (Copenhagen University. Department of Biology) ; Hatos, András (Università di Padova. Dipartimento di Scienze Biomediche) ; Monzon, Alexander Miguel (Università di Padova. Dipartimento di Scienze Biomediche) ; Bevilacqua, Martina (Università di Padova. Dipartimento di Scienze Biomediche) ; Mičetić, Ivan (Università di Padova. Dipartimento di Scienze Biomediche) ; Minervini, Giovanni (Università di Padova. Dipartimento di Scienze Biomediche) ; Paladin, Lisanna (Università di Padova. Dipartimento di Scienze Biomediche) ; Quaglia, Federica (Università di Padova. Dipartimento di Scienze Biomediche) ; Leonardi, Emanuela (Università di Padova) ; Davey, Norman E. (The Institute of Cancer Research. Chelsea) ; Horvath, Tamas (Research Centre for Natural Sciences. Institute of Enzymology) ; Kovacs, Orsolya Panna (Research Centre for Natural Sciences. Institute of Enzymology) ; Murvai, Nikoletta (Research Centre for Natural Sciences. Institute of Enzymology) ; Pancsa, Rita (Research Centre for Natural Sciences. Institute of Enzymology) ; Schad, Eva (Research Centre for Natural Sciences. Institute of Enzymology) ; Szabo, Beata (Research Centre for Natural Sciences. Institute of Enzymology) ; Tantos, Agnes (Research Centre for Natural Sciences. Institute of Enzymology) ; Macedo-Ribeiro, Sandra (Universidade do Porto. Instituto de Biologia Molecular e Celular and Instituto de Investigação e Inovação em Saúde) ; Manso, Jose Antonio (Universidade do Porto. Instituto de Biologia Molecular e Celular and Instituto de Investigação e Inovação em Saúde) ; Barbosa Pereira, Pedro José (Universidade do Porto. Instituto de Biologia Molecular e Celular and Instituto de Investigação e Inovação em Saúde) ; Davidović, Radoslav (University of Belgrade. Vinča Institute of Nuclear Sciences - National Institute of thе Republic of Serbia.) ; Veljkovic, Nevena (University of Belgrade. Vinča Institute of Nuclear Sciences - National Institute of thе Republic of Serbia.) ; Hajdu-Soltész, Borbála (Eötvös Loránd University. Department of Biochemistry) ; Pajkos, Mátyás (Eötvös Loránd University. Department of Biochemistry) ; Szaniszló, Tamás (Eötvös Loránd University. Department of Biochemistry) ; Guharoy, Mainak (Vrije Universiteit Brussel. Structural Biology Brussels) ; Lazar, Tamas (Vrije Universiteit Brussel. Structural Biology Brussels) ; Macossay-Castillo, Mauricio (Vrije Universiteit Brussel. Structural Biology Brussels) ; Tompa, Peter (Vrije Universiteit Brussel. Structural Biology Brussels) ; Tosatto, Silvio (University of Padua. Department of Biomedical Sciences)
Intrinsically disordered proteins, defying the traditional protein structure-function paradigm, are a challenge to study experimentally. Because a large part of our knowledge rests on computational predictions, it is crucial that their accuracy is high. [...]
2021 - 10.1038/s41592-021-01117-3
Nature Methods, Vol. 18 (May 2021) , p. 472-481  
2.
29 p, 849.9 KB Conformational conversion during controlled oligomerization into nonamylogenic protein nanoparticles / Sanchez, Julieta M. (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Sánchez-García, Laura (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ; Pesarrodona Roches, Mireia (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Serna, Naroa (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Sánchez Chardi, Alejandro (Universitat Autònoma de Barcelona. Servei de Microscòpia) ; Unzueta Elorza, Ugutz (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Mangues, Ramon 1957- (Institut Germans Trias i Pujol. Institut de Recerca contra la Leucèmia Josep Carreras) ; Vázquez Gómez, Esther (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ; Villaverde Corrales, Antonio (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Protein materials are rapidly gaining interest in materials sciences and nanomedicine because of their intrinsic biocompatibility and full biodegradability. The controlled construction of supramolecular entities relies on the controlled oligomerization of individual polypeptides, achievable through different strategies. [...]
2018 - 10.1021/acs.biomac.8b00924
Biomacromolecules, Vol. 19, issue 9 (Sep. 2018) , p. 3788-3797  
3.
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 (Universitat Autònoma de Barcelona. 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  
4.
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  
5.
10 p, 6.7 MB Structural analysis and evolution of specificity of the SUMO UFD E1-E2 interactions / Liu, Bing (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Lois, L. Maria (Centre de Recerca en Agrigenòmica) ; Reverter i Cendrós, David (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; 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, Vol. 7 (February 2017) , art. 41998  
6.
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  
7.
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  
8.
16 p, 3.8 MB Disulfide driven folding for a conditionally disordered protein / Fraga, Hugo (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pujols Pujol, Jordi (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Gil-Garcia, Marcos (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Roque Córdova, Alicia (Universitat Autònoma de Barcelona. Departament de Bioquímica i de 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 Institut d'Oncologia) ; Canals, Francesc (Vall d'Hebron Institut 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 de 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, Vol. 7 (2017) , art. 16994  
9.
16 p, 3.8 MB Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria / Macedo, Bruno (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Sant'Anna, Ricardo (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Navarro, Susanna (Universitat Autònoma de Barcelona. 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  
10.
15 p, 1.8 MB A model of protein association based on their hydrophobic and electric interactions / Mozo-Villarias, Angel (Institut de Recerca Biomèdica de Lleida) ; Cedano Rodríguez, Juan Antonio (Universidad de la República (Uruguai).Laboratorio de Inmunología) ; Querol Murillo, Enrique (Universitat Autònoma de Barcelona. 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  

Articles : 13 registres trobats   1 - 10següent  anar al registre:
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