Depósito Digital de Documentos de la UAB Encontrados 13 registros  1 - 10siguiente  ir al registro: La búsqueda tardó 0.04 segundos. 
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.
11 p, 2.4 MB Amino acid substitutions at sugar-recognizing codons confer ABO blood group system-related α1,3 Gal(NAc) transferases with differential enzymatic activity / Cid, Emili (Institut Germans Trias i Pujol. Institut de Recerca contra la Leucèmia Josep Carreras) ; Yamamoto, Miyako (Institut Germans Trias i Pujol. Institut de Recerca contra la Leucèmia Josep Carreras) ; Yamamoto, Fumiichiro (Institut Germans Trias i Pujol. Institut de Recerca contra la Leucèmia Josep Carreras) ; Universitat Autònoma de Barcelona
Functional paralogous ABO, GBGT1, A3GALT2, and GGTA1 genes encode blood group A and B transferases (AT and BT), Forssman glycolipid synthase (FS), isoglobotriaosylceramide synthase (iGb3S), and α1,3-galactosyltransferase (GT), respectively. [...]
2019 - 10.1038/s41598-018-37515-5
Scientific reports, Vol. 9 Núm. 1 (january 2019) , p. 846  
3.
16 p, 9.5 MB Characterization of Soft Amyloid Cores in Human Prion-Like Proteins / Batlle Carreras, Cristina (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Sánchez de Groot, Natalia (Centre de Regulació Genòmica) ; Iglesias, Valentin (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") ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Prion-like behaviour is attracting much attention due to the growing evidences that amyloid-like self-assembly may reach beyond neurodegeneration and be a conserved functional mechanism. The best characterized functional prions correspond to a subset of yeast proteins involved in translation or transcription. [...]
2017 - 10.1038/s41598-017-09714-z
Scientific reports, Vol. 7 (2017) , art. 12134  
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.
29 p, 9.5 MB Substrate specificity of human metallocarboxypeptidase D : comparison of the two active carboxypeptidase domains / Garcia-Pardo, Javier (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Tanco, Sebastián Martín (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Díaz, Lucía (Barcelona Supercomputing Center) ; Dasgupta, Sayani (Albert Einstein College of Medicine. Department of Molecular Pharmacology) ; Fernández-Recio, Juan (Barcelona Supercomputing Center) ; Lorenzo Rivera, Julia (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Avilés, Francesc X. (Francesc Xavier) (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Fricker, Lloyd D. (Albert Einstein College of Medicine. Department of Molecular Pharmacology)
Metallocarboxypeptidase D (CPD) is a membrane-bound component of the trans-Golgi network that cycles to the cell surface through exocytic and endocytic pathways. Unlike other members of the metallocarboxypeptidase family, CPD is a multicatalytic enzyme with three carboxypeptidase-like domains, although only the first two domains are predicted to be enzymatically active. [...]
2017 - 10.1371/journal.pone.0187778
PloS one, Vol. 12 issue 11 (2017) , art. e0187778  
6.
13 p, 2.3 MB A quaternary tetramer assembly inhibits the deubiquitinating activity of USP25 / Liu, Bing (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Sureda-Gómez, Marta (Institut d'Investigacions Biomèdiques August Pi i Sunyer) ; Zhen, Yang (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Amador, Virginia (Institut d'Investigacions Biomèdiques August Pi i Sunyer) ; Reverter i Cendrós, David (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
USP25 deubiquitinating enzyme is a key member of the ubiquitin system, which acts as a positive regulator of the Wnt/β-catenin signaling by promoting the deubiquitination and stabilization of tankyrases. [...]
2018 - 10.1038/s41467-018-07510-5
Nature communications, Vol. 9 (2018) , art. 4973  
7.
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  
8.
13 p, 4.4 MB Dissecting the contribution of Staphylococcus aureus α-phenol-soluble modulins to biofilm amyloid structure / Marinelli, Patrizia (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) ; Navarro, Susanna (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)
The opportunistic pathogen Staphylococcus aureus is recognized as one of the most frequent causes of biofilm-associated infections. The recently discovered phenol soluble modulins (PSMs) are small α-helical amphipathic peptides that act as the main molecular effectors of staphylococcal biofilm maturation, promoting the formation of an extracellular fibril structure with amyloid-like properties. [...]
2016 - 10.1038/srep34552
Scientific reports, Vol. 6 (2016) , art. 34552  
9.
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  
10.
36 p, 10.5 MB Defective AMH signaling disrupts GnRH neuron development and function and contributes to hypogonadotropic hypogonadism / Malone, Samuel Andrew (Jean-Pierre Aubert Research Center) ; Papadakis, Georgios E. (Lausanne University Hospital) ; Messina, Andrea (Lausanne University Hospital) ; Mimouni, Nour El Houda (Jean-Pierre Aubert Research Center) ; Trova, Sara (Jean-Pierre Aubert Research Center) ; Imbernon, Monica (Jean-Pierre Aubert Research Center) ; Allet, Cecile (Jean-Pierre Aubert Research Center) ; Cimino, Irene (Jean-Pierre Aubert Research Center) ; Acierno, James (Lausanne University Hospital) ; Cassatella, Daniele (Lausanne University Hospital) ; Xu, Cheng (Lausanne University Hospital) ; Quinton, Richard (University of Newcastle-upon-Tyne. Institute of Genetic Medicine) ; Szinnai, Gabor (University Children's Hospital Basel (Basilea, Suïssa)) ; Pigny, Pascal (Centre de Biologie Pathologie Génétique. Service Hormonologie Métabolisme Nutrition Oncologie) ; Alonso-Cotchico, Lur (Universitat Autònoma de Barcelona. Departament de Química) ; Masgrau, Laura (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Maréchal, Jean-Didier (Universitat Autònoma de Barcelona. Departament de Química) ; Prevot, V. (Jean-Pierre Aubert Research Center) ; Pitteloud, Nelly (Lausanne University Hospital) ; Giacobini, Polo (Jean-Pierre Aubert Research Center)
Congenital hypogonadotropic hypogonadism (CHH) is a condition characterized by absent puberty and infertility due to gonadotropin releasing hormone (GnRH) deficiency, which is often associated with anosmia (Kallmann syndrome, KS). [...]
2019 - 10.7554/eLife.47198
eLife, Vol. 8 (2019) , art. e47198  

Depósito Digital de Documentos de la UAB : Encontrados 13 registros   1 - 10siguiente  ir al registro:
¿Le interesa recibir alertas sobre nuevos resultados de esta búsqueda?
Defina una alerta personal vía correo electrónico o subscríbase al canal RSS.