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Articles, 17 registres trobats
Documents de recerca, 2 registres trobats
Articles 17 registres trobats  1 - 10següent  anar al registre:
1.
20 p, 3.7 MB A Review of Fifteen Years Developing Computational Tools to Study Protein Aggregation / Pintado-Grima, Carlos (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Bárcenas, Oriol (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Bartolomé-Nafría, Andrea (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Fornt-Suñé, Marc (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Iglesias, Valentin (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Garcia-Pardo, Javier (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") ; Universitat Autònoma de Barcelona
The presence of insoluble protein deposits in tissues and organs is a hallmark of many human pathologies. In addition, the formation of protein aggregates is considered one of the main bottlenecks to producing protein-based therapeutics. [...]
2023 - 10.3390/biophysica3010001
Biophysica, Vol. 3 Núm. 1 (January 2023)  
2.
3 p, 125.0 KB Editorial : Protein Aggregation and Solubility in Microorganisms (Archaea, Bacteria and Unicellular Eukaryotes): Implications and Applications / Skretas, Georgios (National Hellenic Research Foundation. Institute of Chemical Biology) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
2020 - 10.3389/fmicb.2020.620239
Frontiers in microbiology, Vol. 11 (November 2020) , art. 620939  
3.
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  
4.
9 p, 1.8 MB Heavy chain dimers stabilized by disulfide bonds are required to promote in vitro assembly of trastuzumab / Farràs, Mercè (Department of Biotechnology. Farmhispania SA) ; Román, Ramón (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental) ; Camps, Marc (Department of Biotechnology. Farmhispania SA) ; Miret, Joan (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental) ; Martínez, Óscar (Department of Biotechnology. Farmhispania SA) ; Pujol, Xavier (Department of Biotechnology. Farmhispania SA) ; Casablancas, Antoni (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental) ; Cairó i Badillo, Jordi Joan (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental)
Monoclonal antibodies (mAbs) and their derivatives have become one of the most important classes of therapeutic drugs. Their multiple applications increased the interest for understanding their complex structure. [...]
2020 - 10.1186/s12860-019-0244-x
BMC Molecular and Cell Biology, Vol. 21 (January 2020) , art. 2  
5.
3 p, 161.8 KB Editorial : protein solubility and aggregation in bacteria / Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
The Editorial on the research topic protein solubility and aggregation in bacteria.
2016 - 10.3389/fmicb.2016.01178
Frontiers in microbiology, Vol. 7 (July 2016) , art. 1178  
6.
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  
7.
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  
8.
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  
9.
15 p, 1.8 MB C-mannosylation supports folding and enhances stability of thrombospondin repeats / Shcherbakova, Aleksandra (Medizinische Hochschule Hannover. Institut für Klinische Biochemie) ; Preller, Matthias (Medizinische Hochschule Hannover. Institut für Biophysikalische Chemie) ; Taft, Manuel H. (Medizinische Hochschule Hannover. Institut für Biophysikalische Chemie) ; 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") ; Tiemann, Birgit (Medizinische Hochschule Hannover. Institut für Klinische Biochemie) ; Buettner, Falk F. R. (Medizinische Hochschule Hannover. Institut für Klinische Biochemie) ; Bakker, Hans (Medizinische Hochschule Hannover. Institut für Klinische Biochemie)
Previous studies demonstrated importance of C-mannosylation for efficient protein secretion. To study its impact on protein folding and stability, we analyzed both C-mannosylated and non-C-mannosylated thrombospondin type 1 repeats (TSRs) of netrin receptor UNC-5. [...]
2019 - 10.7554/eLife.52978
eLife, Vol. 8 (Dec. 2019) , art. e52978  
10.
10 p, 342.2 KB New set of 2D/3D thermodynamic indices for proteins. A formalism based on "Molten Globule" theory / Ruiz Blanco, Yasser B. (Central University of Las Villas. Unit of Computer-Aided Molecular Biosilico Discovery and Bioinformatic Research (Cuba)) ; García, Yamila (Centre d'Investigació en Nanociència i Nanotecnologia) ; Sotomayor Torres, Clivia M. (Centre d'Investigació en Nanociència i Nanotecnologia) ; Marrero Ponce, Yovani (Central University of Las Villas. Unit of Computer-Aided Molecular Biosilico Discovery and Bioinformatic Research (Cuba))
We define eight new macromolecular indices, and several related descriptors for proteins. The coarse grained methodology used for its deduction ensures its fast execution and becomes a powerful potential tool to explore large databases of protein structures. [...]
2010 - 10.1016/j.phpro.2010.10.013
Physics Procedia, Vol. 8 (March 2010) , p. 63-72  

Articles : 17 registres trobats   1 - 10següent  anar al registre:
Documents de recerca 2 registres trobats  
1.
285 p, 10.3 MB Connection between protein disorder, folding and aggregation : Physiological and Pathological implications / Pujols Pujol, Jordi ; Avilés, Francesc X, dir. ; Ventura Zamora, Salvador, dir.
Les Proteïnes o Regions Intrínsecament Desordenades (IDPs, IDRs) son una classe de polipèptids que són incapaços d'adoptar una estructura tridimensional definida en el seu estat natiu. La seva funció depèn de la flexibilitat estructural i de la fluctuació entre un conjunt de conformacions diferents. [...]
Las proteínas o Regiones Intrínsecamente Desordenadas (IDPs, IDRs) son una clase de polipéptidos incapaces de adoptar una estructura tridimensional definida en su estado nativo. Su función depende de la flexibilidad estructural y de la fluctuación entre un conjunto de diferentes conformaciones. [...]
Intrinsically Disordered Proteins (IDPs) and Regions (IDRs) are a class of polypeptides that lack defined three-dimensional structures. Instead, they populate a dynamic ensemble of flexible conformers that endorse them with unique properties to interact with multiple partners and mediate in signal transduction. [...]

2021  
2.
171 p, 3.7 MB Analysis of different evolutionary strategies to prevent protein aggregation / Graña Montes, Ricardo ; Ventura, Salvador, dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
En els darrers 15 anys, l'estudi de l'agregació de proteïnes ha evolucionat de ser una part de la química de proteïnes que tradicionalment generava poc interès, a convertir-se en una àrea d'investigació dinàmica que ha ampliat el seu abast a diferents camps de recerca incloenthi la bioquímica, la biotecnologia, la nanotecnologia y la biomedicina. [...]
In the last 15 years, the study of protein aggregation has evolved from a mostly neglected topic of protein chemistry to a highly dynamic research area which has expanded its implications through different fields including biochemistry, biotechnology, nanotechnology and biomedicine. [...]

[Barcelona] : Universitat Autònoma de Barcelona, 2014  

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