Results overview: Found 10 records in 0.02 seconds.
Articles, 8 records found
Research literature, 1 records found
Course materials, 1 records found
Articles 8 records found  
1.
17 p, 3.4 MB Protein environment : A crucial triggering factor in josephin domain aggregation: The role of 2,2,2-trifluoroethanol / Visentin, Cristina (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Navarro, Susanna (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Grasso, Gianvito (Università della Svizzera italiana. Istituto Dalle Molle di Studi sull'Intelligenza Artificiale (IDSIA)) ; Regonesi, Maria Elena (Università di Milano-Bicocca. Dipartimento di Biotecnologie e Bioscienze) ; Deriu, Marco Agostino (Università della Svizzera italiana. Istituto Dalle Molle di Studi sull'Intelligenza Artificiale (IDSIA)) ; Tortora, Paolo (Università di Milano-Bicocca. Dipartimento di Biotecnologie e Bioscienze) ; Ventura i Zamora, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
The protein ataxin-3 contains a polyglutamine stretch that triggers amyloid aggregation when it is expanded beyond a critical threshold. This results in the onset of the spinocerebellar ataxia type 3. [...]
2018 - 10.3390/ijms19082151
International Journal of Molecular Sciences, Vol. 19, Núm. 8 (August 2018) , art. 2151  
2.
10 p, 1.2 MB A single cysteine post-translational oxidation suffices to compromise globular proteins kinetic stability and promote amyloid formation / Marinelli, Patrizia (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Navarro, Susanna (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Graña Montes, Ricardo (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Bañó-Polo, Manuel (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Fernández Gallegos, Ma. Rosario (María Rosario) (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Papaleo, Elena (Kræftens Bekæmpelse) ; Ventura i Zamora, Salvador (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Oxidatively modified forms of proteins accumulate during aging. Oxidized protein conformers might act as intermediates in the formation of amyloids in age-related disorders. However, it is not known whether this amyloidogenic conversion requires an extensive protein oxidative damage or it can be promoted just by a discrete, localized post-translational modification of certain residues. [...]
2017 - 10.1016/j.redox.2017.10.022
Redox Biology, Vol. 14 (April 2018) , p. 566-575  
3.
13 p, 1.1 MB Protein aggregation into insoluble deposits protects from oxidative stress / Carija, Anita (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Navarro, Susanna (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biomedicina Molecular) ; Sánchez de Groot, Natalia (Centre de Regulació Genòmica) ; Ventura i Zamora, Salvador (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Protein misfolding and aggregation have been associated with the onset of neurodegenerative disorders. Recent studies demonstrate that the aggregation process can result in a high diversity of protein conformational states, however the identity of the specific species responsible for the cellular damage is still unclear. [...]
2017 - 10.1016/j.redox.2017.03.027
Redox Biology, Vol. 12 (Aug. 2017) , p. 699-711  
4.
12 p, 12.3 MB High-throughput screening methodology to identify alpha-synuclein aggregation inhibitors / Pujols, Jordi (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Peña Díaz, Samuel (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Conde-Giménez, María (Universidad de Zaragoza. Instituto Universitario de Investigación de Biocomputación y Física de Sistemas Complejos) ; Pinheiro, Francisca (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Navarro, Susanna (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Sancho, Javier (Universidad de Zaragoza. Instituto Universitario de Investigación de Biocomputación y Física de Sistemas Complejos) ; Ventura i Zamora, Salvador (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
An increasing number of neurodegenerative diseases are being found to be associated with the abnormal accumulation of aggregated proteins in the brain. In Parkinson's disease, this process involves the aggregation of alpha-synuclein (α-syn) into intraneuronal inclusions. [...]
2017 - 10.3390/ijms18030478
International journal of molecular sciences, Vol. 18 (March 2017) , art. 478  
5.
15 p, 4.8 MB The effects of the novel A53E alpha-synuclein mutation on its oligomerization and aggregation / Lázaro, Diana F. (Universitätsmedizin Göttingen) ; Dias, Mariana Castro (Universitätsmedizin Göttingen) ; Carija, Anita (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Navarro, Susanna (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biomedicina Molecular) ; Madaleno, Carolina Silva (Universidade Nova de Lisboa. Centro de Estudos de Doenças Crónicas) ; Tenreiro, Sandra (Universidade Nova de Lisboa. Centro de Estudos de Doenças Crónicas) ; Ventura i Zamora, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Outeiro, Tiago F. (Max-Planck-Gesellschaft)
α-synuclein (aSyn) is associated with both sporadic and familial forms of Parkinson’s disease (PD), the second most common neurodegenerative disorder after Alzheimer’s disease. In particular, multiplications and point mutations in the gene encoding for aSyn cause familial forms of PD. [...]
2016 - 10.1186/s40478-016-0402-8
Acta neuropathologica communications, Vol. 4 (2016) , art. 128  
6.
16 p, 722.5 KB Exploring the mechanisms of action of human secretory RNase 3 and RNase 7 against Candida albicans. / Salazar, Vivian A. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Arranz-Trullén, Javier (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Navarro, Susanna (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Blanco, Jose A. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Sánchez, Daniel (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Moussaoui, Mohammed (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Boix, Ester (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Human antimicrobial RNases, which belong to the vertebrate RNase A superfamily and are secreted upon infection, display a wide spectrum of antipathogen activities. In this work, we examined the antifungal activity of the eosinophil RNase 3 and the skin-derived RNase 7, two proteins expressed by innate cell types that are directly involved in the host defense against fungal infection. [...]
2016 - 10.1002/mbo3.373
MicrobiologyOpen, 2016  
7.
12 p, 2.1 MB Benzbromarone, Quercetin, and Folic Acid Inhibit Amylin Aggregation / López Rodríguez, Laura Catalina (Universidad de Zaragoza. Departamento de Bioquímica y Biología Molecular y Celular) ; Varea, Olga (Universidad de Zaragoza. Departamento de Bioquímica y Biología Molecular y Celular) ; Navarro Cantero, Susanna (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Carrodeguas Villar, José Alberto (Universidad de Zaragoza. Departamento de Bioquímica y Biología Molecular y Celular) ; Sánchez de Groot, Natalia (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Ventura Zamora, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Sancho Sanz, Javier (Universidad de Zaragoza. Departamento de Bioquímica y Biología Molecular y Celular)
Human Amylin, or islet amyloid polypeptide (hIAPP), is a small hormone secreted by pancreatic-cells that forms aggregates under insulin deficiency metabolic conditions, and it constitutes a pathological hallmark of type II diabetes mellitus. [...]
2016 - 10.3390/ijms17060964
International Journal of Molecular Sciences, Vol. 17 Núm. 6 (june 2016)  
8.
12 p, 919.1 KB A human ribonuclease induces apoptosis associated with p21WAF1/CIP1 induction and JNK inactivation / Castro, Jessica (Universitat de Girona. Departament de Biologia) ; Ribó i Panosa, Marc (Universitat de Girona. Departament de Biologia) ; Navarro Cantero, Susanna (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Nogués i Bara, M. Victòria (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Vilanova i Brugués, Maria (Universitat de Girona. Departament de Biologia) ; Benito i Mundet, Antoni (Universitat de Girona. Departament de Biologia)
Background: Ribonucleases are promising agents for use in anticancer therapy. Among the different ribonucleases described to be cytotoxic, a paradigmatic example is onconase which manifests cytotoxic and cytostatic effects, presents synergism with several kinds of anticancer drugs and is currently in phase II/III of its clinical trial as an anticancer drug against different types of cancer. [...]
2011 - 10.1186/1471-2407-11-9
BMC Cancer, Vol. 11, N. 9 (January 2011) , p. 1-12  

Research literature 1 records found  
1.
215 p, 7.5 MB From sequence to structure : determinants of functional and non-functional protein aggregation / Marinelli, Patrizia ; Ventura i Zamora, Salvador, dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Navarro Cantero, Susanna, dir (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular
El estudio de la agregación proteica representa un campo de investigación desafiante que abarca tanto el área biomédica como la biotecnológica. El creciente número de enfermedades humanas asociadas a la acumulación de agregados amiloides, así como la formación de depósitos intracelulares durante la producción recombinante de proteínas terapéuticas en modelos celulares ha impulsado la investigación para comprender y desarrollar estrategias contra la agregación de proteínas. [...]
The study of protein aggregation represents a challenging research field which embraces from biomedical to biotechnological areas. The growing number of human diseases associated to the deposition of amyloid aggregates as well as the formation of intracellular protein deposits during the recombinant production of therapeutic proteins in cell factories has pushed the research to understand and develop strategies against protein aggregation. [...]

Bellaterra : Universitat Autònoma de Barcelona, 2015  

Course materials 1 records found  
1.
4 p, 28.4 KB Bioquímica dels teixits [20166] / Arús i Caraltó, Carles ; Navarro Cantero, Susanna ; Universitat Autònoma de Barcelona. Facultat de Biociències
2007-08
Llicenciat en Bioquímica [477]  

See also: similar author names
1 Navarro, S
3 Navarro, S.
2 Navarro, Salud
1 Navarro, Salut
1 Navarro, Salvador
2 Navarro, Susana
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