Depósito Digital de Documentos de la UAB Encontrados 117 registros  1 - 10siguientefinal  ir al registro: La búsqueda tardó 0.02 segundos. 
1.
13 p, 1.0 MB A pRb-responsive, RGD-modified, and hyaluronidase-armed canine oncolytic adenovirus for application in veterinary oncology / Laborda Jambrina, Eduardo (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Puig-Saus, Cristina (Institut Català d'Oncologia) ; Rodriguez-García, Alba (Institut Català d'Oncologia) ; Moreno, Rafael (Institut Català d'Oncologia) ; Cascalló, Manel (VCN Biosciences) ; Pastor Milán, Josep (Universitat Autònoma de Barcelona. Departament de Medicina i Cirurgia Animals) ; Alemany Bonastre, Ramon (Institut Català d'Oncologia)
Human and canine cancer share similarities such as genetic and molecular aspects, biological complexity, tumor epidemiology, and targeted therapeutic treatment. Lack of good animal models for human adenovirotherapy has spurred the use of canine adenovirus 2-based oncolytic viruses. [...]
2014
The American Society of Gene & Cell Therapy, Vol. 22 Núm. 5 (Maig 2014) , p. 986-998  
2.
Overexpression of budding yeast protein phosphatase Ppz1 impairs translation / Calafí, Carlos (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; López-Malo, María (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Velázquez, Diego (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Zhang, Chunyi (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Fernández-Fernández, José (Universidad de Sevilla. Departamento de Genética) ; Rodríguez-Galán, Olga (Universidad de Sevilla. Departamento de Genética) ; de la Cruz, Jesús (Universidad de Sevilla. Departamento de Genética) ; Ariño Carmona, Joaquín (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Casamayor Gracia, Antonio (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
The Ser/Thr protein phosphatase Ppz1 from Saccharomyces cerevisiae is the best characterized member of a family of enzymes only found in fungi. Ppz1 is regulated in vivo by two inhibitory subunits, Hal3 and Vhs3, which are moonlighting proteins also involved in the decarboxylation of the 4-phosphopantothenoylcysteine (PPC) intermediate required for coenzyme A biosynthesis. [...]
2020 - 10.1016/j.bbamcr.2020.118727
Biochimica et Biophysica Acta - Molecular Cell Research, Vol. 1867, Issue 8 (August 2020) , art. 118727  
3.
14 p, 624.0 KB Classification and nomenclature of metacaspases and paracaspases: no more confusion with caspases / Minina, Elena A. (Swedish University of Agricultural Sciences and Linnean Center for Plant Biology. Department of Molecular Sciences (Sweden)) ; Staal, Jens (Ghent University. Department of Biomedical Molecular Biology (Belgium)) ; Alvarez, Vanina E. (Universidad Nacional de San Martin. Instituto de Investigaciones Biotecnológicas (Argentina)) ; Berges, John A. (University of Wisconsin-Milwaukee. Department of Biological Sciences and School of Freshwater Sciences (USA)) ; Berman-Frank, Ilana (University of Haifa. Department of Marine Biology (Israel)) ; Beyaert, Rudi (Heidelberg University. COS (Germany)) ; Bidle, Kay D. (Rutgers University. Department of Marine and Coastal Sciences (USA)) ; Bornancin, Frédéric (Novartis Institutes for BioMedical Research (Switzerland)) ; Casanova, Magali (Aix-Marseille Université. Centre National de la Recherche Scientifique. Institut de Microbiologie de la Méditerranée (France)) ; Cazzulo, Juan J. (Universidad Nacional de San Martin. Instituto de Investigaciones Biotecnológicas (Argentina)) ; Choi, Chang Jae (The University of Texas at Austin. Marine Science Institute (USA)) ; Sánchez Coll, Núria (Centre de Recerca en Agrigenòmica) ; Dixit, Vishva M. (Genentech. Department of Physiological Chemistry (USA)) ; Dolinar, Marko (University of Ljubljana. Faculty of Chemistry and Chemical Technology (Slovenia)) ; Fasel, Nicolas (University of Lausanne. Department of Biochemistry (Switzerland)) ; Funk, Christiane (Umeå University. Department of Chemistry (Sweden)) ; Gallois, Patrick (University of Manchester. Faculty of Biology, Medicine and Health (UK)) ; Gevaert, Kris (Ghent University. Department of Biomolecular Medicine (Belgium)) ; Gutierrez-Beltran, Emilio (Universidad de Sevilla. Instituto de Bioquímica Vegetal y Fotosíntesis) ; Hailfinger, Stephan (Eberhard Karls University. Interfaculty Institute for Biochemistry (Germany)) ; Klemenčič, Marina (University of Ljubljana. Faculty of Chemistry and Chemical Technology (Slovenia)) ; Koonin, Eugene V. (National Library of Medicine. National Center for Biotechnology Information (USA)) ; Krappmann, Daniel (Helmholtz Zentrum München - German Research Center for Environmental Health. Research Unit Cellular Signal Integration (Germany)) ; Linusson, Anna (Umeå University. Department of Chemistry (Sweden)) ; Machado, Maurício F. M. (University of Mogi das Cruzes. Interdisciplinary Center for Biochemical Research (Brazil)) ; Madeo, Frank (University of Graz. NAWI Graz. Institute of Molecular Biosciences (Austria)) ; Megeney, Lynn A. (University of Ottawa. Ottawa Hospital Research Institute. Sprott Centre for Stem Cell Research (Canada)) ; Moschou, Panagiotis N. (University of Crete. Department of Biology (Greece)) ; Mottram, Jeremy C. (University of York. York Biomedical Research Institute. Department of Biology (UK)) ; Nyström, Thomas (University of Gothenburg. Centre for Ageing and Health - AgeCap. Institute for Biomedicine (Sweden)) ; Osiewacz, Heinz D. (Goethe University. Institute for Molecular Biosciences (Germany)) ; Overall, Christopher M. (University of British Columbia. Life Sciences Institute. Departments of Oral Biological and Medical Sciences / and Biochemistry and Molecular Biology (Canada)) ; Pandey, Kailash C. (Indian Council of Medical Research. National Institute of Malaria Research (India)) ; Ruland, Jürgen (German Cancer Consortium (Germany)) ; Salvesen, Guy S. (Sanford Burnham Prebys Medical Discovery Institute (USA)) ; Shi, Yigong (Westlake University. School of Life Sciences (China)) ; Smertenko, Andrei (Washington State University. Institute of Biological Chemistry (USA)) ; Stael, Simon (Ghent University. Department of Plant Biotechnology and Bioinformatics (Belgium)) ; Ståhlberg, Jerry (Swedish University of Agricultural Sciences and Linnean Center for Plant Biology. Department of Molecular Sciences (Sweden)) ; Suárez, María Fernanda (Universidad de Málaga. Departamento de Biologia Molecular y Bioquimica) ; Thome, Margot (University of Lausanne. Department of Biochemistry (Switzerland)) ; Tuominen, Hannele (Umeå University. Umeå Plant Science Centre. Department of Plant Physiology (Sweden)) ; Van Breusegem, Frank (Ghent University. Department of Plant Biotechnology and Bioinformatics (Belgium)) ; Van der Hoorn, Renier A. L. (University of Oxford. Department of Plant Sciences (UK)) ; Vardi, Assaf (Weizmann Institute of Science. Department of Plant and Environmental Sciences (Israel)) ; Zhivotovsky, Boris (MV Lomonosov Moscow State University. Faculty of Fundamental Medicine (Russia)) ; Lam, Eric (Rutgers the State University of New Jersey. Department of Plant Biology (USA)) ; Bozhkov, Peter V. (Swedish University of Agricultural Sciences and Linnean Center for Plant Biology. Department of Molecular Sciences (Sweden))
Metacaspases and paracaspases are proteases that were first identified as containing a caspase-like structural fold (Uren et al. , 2000). Like caspases, meta- and paracaspases are multifunctional proteins regulating diverse biological phenomena, such as aging, immunity, proteostasis and programmed cell death. [...]
2020 - 10.1016/j.molcel.2019.12.020
Molecular Cell, Vol. 77, Issue 5 (March 2020) , p. 927-929  
4.
19 p, 5.0 MB SIVA-1 regulates apoptosis and synaptic function by modulating XIAP interaction with the death receptor antagonist FAIM-L / Coccia, Elena (Universitat Autònoma de Barcelona. Institut de Neurociències) ; Planells-Ferrer, Laura (Universitat Autònoma de Barcelona. Institut de Neurociències) ; Badillos-Rodríguez, Raquel (Universitat Autònoma de Barcelona. Institut de Neurociències) ; Pascual, Marta (Institut de Neurociències, Universitat de Barcelona. Department of Cell Biology, Physiology and Immunology) ; Segura, Miguel F. (Hospital Universitari Vall d'Hebron. Institut de Recerca) ; Fernández-Hernández, Rita (Universitat de Lleida. Cell Cycle Laboratory, Institut de Recerca Biomèdica de Lleida (IRBLleida), and Departament de Ciències Mèdiques Bàsiques; Facultat de Medicina) ; López-Soriano, Joaquin (Universitat Autònoma de Barcelona. Institut de Neurociències) ; Garí, Eloi (Universitat de Lleida. Cell Cycle Laboratory, Institut de Recerca Biomèdica de Lleida (IRBLleida), and Departament de Ciències Mèdiques Bàsiques; Facultat de Medicina) ; Soriano, Eduardo (ICREA Academia) ; Barneda-Zahonero, Bruna (Universitat Autònoma de Barcelona. Institut de Neurociències) ; Moubarak, Rana S. (NYU Langone Health. Present Address: Department of Pathology) ; Pérez-García, M. Jose (Universitat Autònoma de Barcelona. Institut de Neurociències) ; Comella, Joan X. (Universitat Autònoma de Barcelona. Institut de Neurociències)
The long isoform of Fas apoptosis inhibitory molecule (FAIM-L) is a neuron-specific death receptor antagonist that modulates apoptotic cell death and mechanisms of neuronal plasticity. FAIM-L exerts its antiapoptotic action by binding to X-linked inhibitor of apoptosis protein (XIAP), an inhibitor of caspases, which are the main effectors of apoptosis. [...]
2020 - 10.1038/s41419-020-2282-x
Cell death and disease, Vol. 11 (february 2020)  
5.
18 p, 3.6 MB hnRNPDL phase separation is regulated by alternative splicing and disease-causing mutations accelerate its aggregation / Batlle Carreras, Cristina (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Yang, Peiguo (St. Jude Children's Research Hospital. Department of Cell and Molecular Biology) ; Coughlin, Maura (St. Jude Children's Research Hospital. Department of Cell and Molecular Biology) ; Messing, James (Howard Hughes Medical Institute) ; Pesarrodona Roches, Mireia (Institut de Recerca Biomèdica) ; Szulc, Elzbieta (Institut de Recerca Biomèdica) ; Salvatella, Xavier (Institut de Recerca Biomèdica) ; Kim, Hong Joo (St. Jude Children's Research Hospital. Department of Cell and Molecular Biology) ; Taylor, J. Paul (Howard Hughes Medical Institute) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Prion-like proteins form multivalent assemblies and phase separate into membraneless organelles. Heterogeneous ribonucleoprotein D-like (hnRNPDL) is a RNA-processing prion-like protein with three alternative splicing (AS) isoforms, which lack none, one, or both of its two disordered domains. [...]
2020 - 10.1016/j.celrep.2019.12.080
Cell reports, Vol. 30, issue 4 (Jan. 2020) , p. 1117-1128  
6.
16 p, 12.4 MB H2AFX and MDC1 promote maintenance of genomic integrity in male germ cells / Testa, Erika. (Università degli Studi di Roma "Tor Vergata". Dipartimento di Biomedicina e Prevenzione) ; Nardozi, Daniela (Università degli Studi di Roma "Tor Vergata". Dipartimento di Biomedicina e Prevenzione) ; Antinozzi, Cristina (Università degli Studi di Roma "Tor Vergata". Dipartimento di Biomedicina e Prevenzione) ; Faieta, Monica (Università degli Studi di Roma "Tor Vergata". Dipartimento di Biomedicina e Prevenzione) ; Di Cecca, Stefano (Università degli Studi di Roma "Tor Vergata". Dipartimento di Biomedicina e Prevenzione) ; Caggiano, Cinzia (Università degli Studi di Roma "Tor Vergata". Dipartimento di Biomedicina e Prevenzione) ; Fukuda, Tomoyuki (Niigata University Graduate School of Medical and Dental Sciences. Department of Cellular Physiology) ; Bonanno, Elena (Università degli Studi di Roma "Tor Vergata". Unità di Anatomia patologica) ; Zhenkun, Lou (Mayo Clinic. Department of Oncology.) ; Maldonado Linares, Andros (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Roig, I. (Ignasi) (Universitat Autònoma de Barcelona. Departament de Biologia Cel·lular, de Fisiologia i d'Immunologia) ; Di Giacomo, Monica (European Molecular Biology Laboratory) ; Barchi, Marco (Università degli Studi di Roma "Tor Vergata". Dipartimento di Biomedicina e Prevenzione)
In somatic cells, H2afx and Mdc1 are close functional partners in DNA repair and damage response. However, it is not known whether they are also involved in the maintenance of genome integrity in meiosis. [...]
2018 - 10.1242/jcs.214411
Journal of Cell Science, Vol. 131, issue 6 (2018) , p. jcs214411  
7.
12 p, 3.2 MB Structural and functional features of self-assembling protein nanoparticles produced in endotoxin-free Escherichia coli / Rueda, Fabian (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Céspedes, Maria Virtudes (Institut d'Investigació Biomèdica Sant Pau) ; Sánchez Chardi, Alejandro (Universitat Autònoma de Barcelona. Servei de Microscòpia) ; Seras-Franzoso, Joaquín (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pesarrodona Roches, Mireia (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ferrer Miralles, Neus (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ; Vázquez Gómez, Esther (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ; Rinas, Ursula (Helmholtz Centre for Infection Research) ; Unzueta Elorza, Ugutz (Institut d'Investigació Biomèdica Sant Pau) ; Mamat, Uwe (Airway Research Center North) ; Mangues, Ramon (Institut d'Investigació Biomèdica Sant Pau) ; García Fruitós, Elena (Institut de Recerca i Tecnologia Agroalimentàries) ; Villaverde Corrales, Antonio (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ; Universitat Autònoma de Barcelona
Background: production of recombinant drugs in process-friendly endotoxin-free bacterial factories targets to a lessened complexity of the purification process combined with minimized biological hazards during product application. [...]
2016 - 10.1186/s12934-016-0457-z
Microbial cell factories, Vol. 15 (2016) , art. 59  
8.
12 p, 1.7 MB Functional inclusion bodies produced in the yeast Pichia pastoris / Rueda, Fabián (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Gasser, Brigitte (Austrian Centre of Industrial Biotechnology) ; Sánchez Chardi, Alejandro (Universitat Autònoma de Barcelona. Servei de Microscòpia) ; Roldán, Mónica (Universitat Autònoma de Barcelona. Servei de Microscòpia) ; Villegas Hernández, Sandra (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Puxbaum, Verena (Austrian Centre of Industrial Biotechnology (ACIB)) ; Ferrer Miralles, Neus (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Unzueta Elorza, Ugutz (Institut d'Investigació Biomèdica Sant Pau) ; Vázquez Gómez, Esther (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; García Fruitós, Elena (Institut de Recerca i Tecnologia Agroalimentàries) ; Mattanovich, Diethard (Austrian Centre of Industrial Biotechnology) ; Villaverde Corrales, Antonio (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ; Universitat Autònoma de Barcelona
Background: Bacterial inclusion bodies (IBs) are non-toxic protein aggregates commonly produced in recombinant bacteria. They are formed by a mixture of highly stable amyloid-like fibrils and releasable protein species with a significant extent of secondary structure, and are often functional. [...]
2016 - 10.1186/s12934-016-0565-9
Microbial cell factories, Vol. 15 (2016) , art. 166  
9.
16 p, 3.8 MB Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria / Macedo, Bruno (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Sant'Anna, Ricardo (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Navarro Cantero, Susanna (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.
3 p, 133.1 KB Modeling amyloids in bacteria / Villar Piqué, Anna (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Ventura, Salvador (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
An increasing number of proteins are being shown to assemble into amyloid structures, self-seeding fibrillar aggregates that may lead to pathological states or play essential biological functions in organisms. [...]
2012 - 10.1186/1475-2859-11-166
Microbial cell factories, Vol. 11 (2012) , art. 166  

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