Results overview: Found 15 records in 0.02 seconds.
Articles, 14 records found
Research literature, 1 records found
Articles 14 records found  1 - 10next  jump to record:
1.
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  
2.
3 p, 161.8 KB Editorial : protein solubility and aggregation in bacteria / Ventura, Salvador (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  
3.
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  
4.
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 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 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  
5.
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 (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  
6.
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, Jordi (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ventura, Salvador (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  
7.
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  
8.
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  
9.
17 p, 839.2 KB Molecular and Functional Bases of Selection against a Mutation Bias in an RNA Virus / de la Higuera, Ignacio (Centro de Biología Molecular "Severo Ochoa" (CSIC-UAM)) ; Ferrer-Orta, Cristina (Institut de Biologia Molecular de Barcelona (CSIC)) ; de Ávila, Ana I. (Centro de Biología Molecular "Severo Ochoa" (CSIC-UAM)) ; Perales, Celia (Hospital Universitari Vall d'Hebron. Institut de Recerca) ; Sierra, Macarena (Centro de Biología Molecular "Severo Ochoa" (CSIC-UAM)) ; Singh, Kamalendra (Christopher S. Bond Life Sciences Center, University of Missouri) ; Sarafianos, Stefan G. (Christopher S. Bond Life Sciences Center, University of Missouri) ; Dehouck, Yves (Machine Learning Group, Université Libre de Bruxelles (ULB)) ; Bastolla, Ugo (Centro de Biología Molecular "Severo Ochoa" (CSIC-UAM)) ; Verdaguer, Nuria (Institut de Biologia Molecular de Barcelona (CSIC)) ; Domingo, Esteban (Centro de Biología Molecular "Severo Ochoa" (CSIC-UAM)) ; Universitat Autònoma de Barcelona
The selective pressures acting on viruses that replicate under enhanced mutation rates are largely unknown. Here, we describe resistance of foot-and-mouth disease virus to the mutagen 5-fluorouracil (FU) through a single polymerase substitution that prevents an excess of A to G and U to C transitions evoked by FU on the wild-type foot-and-mouth disease virus, while maintaining the same level of mutant spectrum complexity. [...]
2017 - 10.1093/gbe/evx075
Genome biology and evolution, Vol. 9 (may 2017) , p. 1212-1228  
10.
2 p, 710.8 KB Protein misfolding diseases / Ventura, Salvador (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
2015 - 10.4155/fso.15.38
Future science OA, Vol. 1, issue 2 (Sep. 2015)  

Articles : 14 records found   1 - 10next  jump to record:
Research literature 1 records found  
1.
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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