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Resultados globales: 8 registros encontrados en 0.02 segundos.
Artículos, Encontrados 7 registros
Documentos de investigación, Encontrados 1 registros
Artículos Encontrados 7 registros  
1.
17 p, 3.5 MB The N-Terminal Region of Yeast Protein Phosphatase Ppz1 Is a Determinant for Its Toxicity / Calafi Pascual, Carlos Alberto (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; López-Malo, María (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Albacar, Marcel (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") ; Ariño Carmona, Joaquín (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
The Ppz enzymes are Ser/Thr protein phosphatases present only in fungi that are characterized by a highly conserved C-terminal catalytic region, related to PP1c phosphatases, and a more divergent N-terminal extension. [...]
2020 - 10.3390/ijms21207733
International journal of molecular sciences, Vol. 21, Núm. 20 (October 2020) , art. 7733  
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2.
10 p, 6.7 MB Structural analysis and evolution of specificity of the SUMO UFD E1-E2 interactions / Liu, Bing (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Lois, L. Maria (Centre de Recerca en Agrigenòmica) ; Reverter i Cendrós, David (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
SUMO belongs to the ubiquitin-like family (UbL) of protein modifiers. SUMO is conserved among eukaryotes and is essential for the regulation of processes such as DNA damage repair, transcription, DNA replication and mitosis. [...]
2017 - 10.1038/srep41998
Scientific reports, Vol. 7 (February 2017) , art. 41998  
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3.
12 p, 2.4 MB Mutations at the hydrophobic core affect Hal3 trimer stability, reducing its Ppz1 inhibitory capacity but not its PPCDC moonlighting function / Santolaria Bello, Carlos (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") ; Strauss, Erick (Stellenbosch University. Department of Biochemistry) ; Ariño Carmona, Joaquín (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
S. cerevisiae Hal3 (ScHal3) is a moonlighting protein that, is in its monomeric state, regulates the Ser/Thr protein phosphatase Ppz1, but also joins ScCab3 (and in some instances the Hal3 paralog Vhs3) to form an unusual heterotrimeric phosphopantothenoylcysteine decarboxylase (PPCDC) enzyme. [...]
2018 - 10.1038/s41598-018-32979-x
Scientific reports, Vol. 8 (2018) , art. 14701  
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4.
17 p, 1.6 MB Complex stability and dynamic subunit interchange modulates the disparate activities of the yeast moonlighting proteins Hal3 and Vhs3 / Abrie, J. Albert (Stellenbosch University. Department of Biochemistry) ; Molero Merinero, Cristina (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Ariño Carmona, Joaquín (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Strauss, Erick (Stellenbosch University. Department of Biochemistry) ; Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí"
Saccharomyces cerevisiae Hal3 and Vhs3 are moonlighting proteins, acting both as inhibitors of the serine/threonine protein phosphatase Ppz1 and as subunits (together with Cab3) of the unique heterotrimeric phosphopantothenoylcysteine decarboxylase (PPCDC) enzyme of Hemiascomycetous yeast. [...]
2015 - 10.1038/srep15774
Scientific reports, Vol. 5 (October 2015) , art. 15774  
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5.
20 p, 1.8 MB Regulation of the Na+/K+-ATPase Ena1 expression by calcineurin/Crz1 under high pH stress : a quantitative study / Petrezsélyová, Silvia (Institute of Molecular Genetics (Vestec, República Txeca)) ; López-Malo, María (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Canadell, David (Universitat Pompeu Fabra. Departament de Ciències Experimentals i de la Salut) ; Roque Córdova, Alicia (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Serra Cardona, Albert (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Marqués, M. Carmen (Instituto de Biologia Molecular y Celular de Plantas (València, Espanya)) ; Vilaprinyó, Ester (Universitat de Lleida) ; Alves, Rui (Universitat de Lleida) ; Yenush, Lynne (Instituto de Biologia Molecular y Celular de Plantas (València, Espanya)) ; Ariño Carmona, Joaquín (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Regulated expression of the Ena1 Na+-ATPase is a crucial event for adaptation to high salt and/or alkaline pH stress in the budding yeast Saccharomyces cerevisiae. ENA1 expression is under the control of diverse signaling pathways, including that mediated by the calcium-regulatable protein phosphatase calcineurin and its downstream transcription factor Crz1. [...]
2016 - 10.1371/journal.pone.0158424
PloS one, Vol. 11 Num. 6 (June 2016) , p. 1-20  
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6.
24 p, 1.7 MB Integration and Validation of the GenomeScale Metabolic Models of Pichia pastoris : a Comprehensive Update of Protein Glycosylation Pathways, Lipid and Energy Metabolism / Tomàs Gamisans, Màrius (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental) ; Ferrer, Pau (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental) ; Albiol i Sala, Joan (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental)
Motivation: Genome-scale metabolic models (GEMs) are tools that allow predicting a phenotype from a genotype under certain environmental conditions. GEMs have been developed in the last ten years for a broad range of organisms, and are used for multiple purposes such as discovering new properties of metabolic networks, predicting new targets for metabolic engineering, as well as optimizing the cultivation conditions for biochemicals or recombinant protein production. [...]
2016 - 10.1371/journal.pone.0148031
PloS one, Vol. 11 Núm. 1 (January 2016) , p. 1-24  
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7.
16 p, 2.3 MB Analysis of Two Putative Candida albicans Phosphopantothenoylcysteine Decarboxylase / Protein Phosphatase Z Regulatory Subunits Reveals an Unexpected Distribution of Functional Roles / Petrényi, Katalin (University of Debrecen. Department of Medical Chemistry) ; Molero Merinero, Cristina (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Kónya, Zoltán (University of Debrecen. Department of Medical Chemistry) ; Erdődi, Ferenc (University of Debrecen. Department of Medical Chemistry) ; Ariño Carmona, Joaquín (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Dombrádi, Viktor (University of Debrecen. Department of Medical Chemistry)
Protein phosphatase Z (Ppz) is a fungus specific enzyme that regulates cell wall integrity, cation homeostasis and oxidative stress response. Work on Saccharomyces cerevisiae has shown that the enzyme is inhibited by Hal3/Vhs3 moonlighting proteins that together with Cab3 constitute the essential phosphopantothenoylcysteine decarboxylase (PPCDC) enzyme. [...]
2016 - 10.1371/journal.pone.0160965
PloS one, Vol. 11 Núm. 8 (August 2016) , p. 1-16  
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Documentos de investigación Encontrados 1 registros  
1.
1 p, 850.5 KB Bioprocess design for human hemoglobin production in Saccharomyces cerevisiae : Part III, project analysis / Dorrego Rivas, Ana ; Durá Esteve, Irene ; López Gil, Carlos ; Solà i Ferrando, Carles, 1945-, dir. (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental) ; Universitat Autònoma de Barcelona. Facultat de Biociències
2015
Grau en Biotecnologia [815]  
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