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1.
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69 p, 3.2 MB |
Overexpression of budding yeast protein phosphatase Ppz1 impairs translation
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Calafí, Carlos (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
López-Malo, María (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Velázquez, Diego (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Zhang, Chunyi (Universitat Autònoma de Barcelona. 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 (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Casamayor Gracia, Antonio (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 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
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2.
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16 p, 2.9 MB |
Cyclophilins A and B oppositely regulate renal tubular epithelial cell phenotype
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Sarró, Eduard (Hospital Universitari Vall d'Hebron. Institut de Recerca) ;
Durán, Mónica (Hospital Universitari Vall d'Hebron. Institut de Recerca) ;
Rico, Ana (Hospital Universitari Vall d'Hebron. Institut de Recerca) ;
Bou-Teen, Diana (Cardiovascular Diseases Group) ;
Fernández-Majada, Vanesa (Biomimetic Systems for Cell Engineering Laboratory) ;
Croatt, Anthony J. (Division of Nephrology and Hypertension and Department of Medicine) ;
Nath, Karl A. (Division of Nephrology and Hypertension and Department of Medicine) ;
Salcedo, Maria Teresa (Hospital Universitari Vall d'Hebron. Institut de Recerca) ;
Gundelach, Justin H. (Department of Biochemistry and Molecular Biology) ;
Batlle, Daniel (Division of Nephrology and Hypertension) ;
Bram, Richard J. (Department of Immunology) ;
Meseguer Navarro, Anna (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Restoration of kidney tubular epithelium following sublethal injury sequentially involves partial epithelial-mesenchymal transition (pEMT), proliferation, and further redifferentiation into specialized tubule epithelial cells (TECs). [...]
2020 - 10.1093/jmcb/mjaa005
Journal of Molecular Cell Biology, Vol. 12 (march 2020) , p. 499-514
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3.
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14 p, 624.0 KB |
Classification and nomenclature of metacaspases and paracaspases : no more confusion with caspases
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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) ;
Casanova, Magali (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) ;
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 (Israel). Department of Plant and Environmental Sciences) ;
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
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4.
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20 p, 6.8 MB |
IKKα Kinase Regulates the DNA Damage Response and Drives Chemo-resistance in Cancer
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Colomer, Carlota (Institut Hospital del Mar d'Investigacions Mèdiques) ;
Margalef, Pol (Institut Hospital del Mar d'Investigacions Mèdiques) ;
Villanueva, Alberto (Institut d'Investigació Biomèdica de Bellvitge) ;
Vert, Anna (Institut Hospital del Mar d'Investigacions Mèdiques) ;
Pecharroman, Irene (Institut Hospital del Mar d'Investigacions Mèdiques) ;
Solé Font, Laura (Institut Hospital del Mar d'Investigacions Mèdiques) ;
Gonzàlez-Farré, Mònica (Institut Hospital del Mar d'Investigacions Mèdiques) ;
Alonso, Josune (Institut Hospital del Mar d'Investigacions Mèdiques) ;
Montagut, Clara (Institut Hospital del Mar d'Investigacions Mèdiques) ;
Martinez-Iniesta, Maria (Institut d'Investigació Biomèdica de Bellvitge) ;
Bertran, Joan (Universitat de Vic - Universitat Central de Catalunya) ;
Borràs, Eva (Centre de Regulació Genòmica) ;
Iglesias, Mar (Universitat Autònoma de Barcelona. Departament de Ciències Morfològiques) ;
Sabidó, Eduard (Centre de Regulació Genòmica) ;
Bigas Salvans, Anna (Institut Hospital del Mar d'Investigacions Mèdiques) ;
Boulton, Simon J. (The Francis Crick Institute) ;
Espinosa, Lluís (Institut Hospital del Mar d'Investigacions Mèdiques)
Phosphorylated IKKα(p45) is a nuclear active form of the IKKα kinase that is induced by the MAP kinases BRAF and TAK1 and promotes tumor growth independent of canonical NF-κB signaling. Insights into the sources of IKKα(p45) activation and its downstream substrates in the nucleus remain to be defined. [...]
2019 - 10.1016/j.molcel.2019.05.036
Molecular Cell, Vol. 75 (august 2019) , p. 669-682.e5
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5.
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9 p, 1.8 MB |
Heavy chain dimers stabilized by disulfide bonds are required to promote in vitro assembly of trastuzumab
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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
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6.
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7.
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10 p, 1.9 MB |
Down-regulation of the Wnt/β-catenin signaling pathway by Cacnb4
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Rima, Mohamad ;
Daghsni, Marwa ;
Lopez, Anaïs ;
Fajloun, Ziad ;
Lefrancois, Lydie ;
Dunach, Mireia (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Merle, Philippe ;
Brusés, Juan L. ;
De Waard, Michel ;
Ronjat, Michel
The cytoplasmic β-subunit of the voltage-gated calcium channels has been shown be involved in the regulation of gene transcription. This subunit interacts with the transcription factor TCF4 and inhibits the Wnt/β-catenin signaling pathway. [...]
2017 - 10.1091/mbc.E17-01-0076
Molecular biology of the cell, Vol. 28 (december 2017) , p. 3699-3708
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8.
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14 p, 3.3 MB |
Evidence for new C-terminally truncated variants of α- and β-tubulins
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Aillaud, Chrystelle (Université Grenoble Alpes. Grenoble Institut des Neurosciences) ;
Bosc, Christophe (Université Grenoble Alpes. Grenoble Institut des Neurosciences) ;
Saoudi, Yasmina (Université Grenoble Alpes. Grenoble Institut des Neurosciences) ;
Denarier, Eric (Université Grenoble Alpes. Grenoble Institut des Neurosciences) ;
Peris, Leticia (Université Grenoble Alpes. Grenoble Institut des Neurosciences) ;
Sago, Laila (Centre national de la recherche scientifique. Service d'Identification et de Caractérisation des Protéines par Spectrométrie de masse) ;
Taulet, Nicolas (Centre national de la recherche scientifique. Centre de Recherche de Biochimie Macromoléculaire) ;
Cieren, Adeline (Université Grenoble Alpes. Grenoble Institut des Neurosciences) ;
Tort, Olívia (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Magiera, Maria M. (Institut Curie) ;
Janke, Carsten (Institut Curie) ;
Redeker, Virginie (Paris-Saclay Institute of Neuroscience) ;
Andrieux, Annie (Université Grenoble Alpes. Grenoble Institut des Neurosciences) ;
Moutin, Marie-Jo (Université Grenoble Alpes. Grenoble Institut des Neurosciences)
New C-terminally truncated α- and β-tubulin variants, both ending with an -EEEG sequence, are identified in vivo: αΔ3-tubulin, which has a specific neuronal distribution pattern (distinct from that of αΔ2-tubulin) and seems to be related to dynamic microtubules, and βΔ4-tubulin, corresponding to β2A/B-tubulin modified by truncation of four C-terminal residues, which is ubiquitously present in cells and tissues. [...]
2016 - 10.1091/mbc.E15-03-0137
Molecular biology of the cell, Vol. 27, issue 4 (Feb. 2016) , p. 640-653
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9.
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14 p, 4.4 MB |
Diacylglycerol is required for the formation of COPI vesicles in the Golgi-to-ER transport pathway
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Fernández Ulibarri, Inés (Universitat de Barcelona. Departament de Biologia Cel·lular i Anatomia Patològica) ;
Vilella, Montserrat (Universitat de Barcelona. Departament de Biologia Cel·lular i Anatomia Patològica) ;
Lázaro Diéguez, Francisco (Universitat de Barcelona. Departament de Biologia Cel·lular i Anatomia Patològica) ;
Sarri Plans, Elisabet (Universitat de Barcelona. Departament de Biologia Cel·lular i Anatomia Patològica) ;
Martínez, Susana E. (Universitat de Barcelona. Departament de Biologia Cel·lular i Anatomia Patològica) ;
Jiménez, Nuria (Utrecht University) ;
Claro Izaguirre, Enrique (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Mérida, Isabel (Universidad Autónoma de Madrid. Departamento de Inmunología y Oncología) ;
Burger, Koert N. J. (Utrecht University) ;
Egea, Gustavo (Universitat de Barcelona. Departament de Biologia Cel·lular i Anatomia Patològica)
Diacylglycerol is necessary for trans-Golgi network (TGN) to cell surface transport, but its functional relevance in the early secretory pathway is unclear. Although depletion of diacylglycerol did not affect ER-to-Golgi transport, it led to a redistribution of the KDEL receptor to the Golgi, indicating that Golgi-to-ER transport was perturbed. [...]
2007 - 10.1091/mbc.E07-04-0334
Molecular biology of the cell, Vol. 18, Num. 9 (2007) , p. 3250-3263
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10.
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24 p, 7.3 MB |
The cytosolic carboxypeptidases CCP2 and CCP3 catalyze posttranslational removal of acidic amino acids
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Tort Regàs, Olívia (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") ;
Rocha, Cecilia (Institut Curie) ;
Bièche, Ivan (Institut Curie) ;
Seixas, Cecilia (Universidade Nova de Lisboa. Centro de Estudos de Doenças Crónicas) ;
Bosc, Christophe (Université de Grenoble. Institut des neurosciences) ;
Andrieux, Annie (Université de Grenoble. Institut des neurosciences) ;
Moutin, Marie-Jo (Université de Grenoble. Institut des neurosciences) ;
Avilés, Francesc X. (Francesc Xavier) (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Lorenzo Rivera, Julia (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Janke, Carsten (Institut Curie)
The posttranslational modification of carboxy-terminal tails of tubulin plays an important role in the regulation of the microtubule cytoskeleton. Enzymes responsible for deglutamylating tubulin have been discovered within a novel family of mammalian cytosolic carboxypeptidases. [...]
2014 - 10.1091/mbc.E14-06-1072
Molecular biology of the cell, Vol. 25, No. 19 (Oct. 2014) , p. 3017-27
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