Results overview: Found 8 records in 0.01 seconds.
Articles, 6 records found
Research literature, 2 records found
Articles 6 records found  
1.
21 p, 2.6 MB Proximity Mapping of CCP6 Reveals Its Association with Centrosome Organization and Cilium Assembly / Rodriguez-Calado, Sergi (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Van Damme, Petra (Ghent University) ; Avilés, Francesc X. (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Candiota Silveira, Ana Paula (Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina) ; Tanco, Sebastián Martín (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Lorenzo Rivera, Julia (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
The cytosolic carboxypeptidase 6 (CCP6) catalyzes the deglutamylation of polyglutamate side chains, a post-translational modification that affects proteins such as tubulins or nucleosome assembly proteins. [...]
2023 - 10.3390/ijms24021273
International journal of molecular sciences, Vol. 24, Issue 2 (January 2023) , art. 1273  
2.
14 p, 2.0 MB Enhanced Production of ECM Proteins for Pharmaceutical Applications Using Mammalian Cells and Sodium Heparin Supplementation / Garcia-Pardo, Javier (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Montané, Sergi (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Avilés, Francesc X. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Tanco, Sebastián Martín (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Lorenzo Rivera, Julia (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
The yields of soluble ECM proteins recombinantly produced with mammalian cells can be significantly enhanced by exploiting the stabilizing properties of heparin. Here, we propose a simple and straightforward scalable protocol for the mammalian cell production of ECM proteins with affinity for heparin, using heparin as a supplement. [...]
2022 - 10.3390/pharmaceutics14102138
Pharmaceutics, Vol. 14, Núm. 10 (October 2022) , art. 2138  
3.
24 p, 3.9 MB Substrate specificity and structural modeling of human Carboxypeptidase Z : a unique protease with a Frizzled-like domain / Garcia-Pardo, Javier (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Tanco, Sebastián Martín (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; García Guerrero, María del Carmen (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Dasgupta, Sayani (Albert Einstein College of Medicine. Department of Molecular Pharmacology) ; Avilés, Francesc X. (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Lorenzo Rivera, Julia (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Fricker, Lloyd D. (Albert Einstein College of Medicine. Department of Molecular Pharmacology)
Metallocarboxypeptidase Z (CPZ) is a secreted enzyme that is distinguished from all other members of the M14 metallocarboxypeptidase family by the presence of an N-terminal cysteine-rich Frizzled-like (Fz) domain that binds Wnt proteins. [...]
2020 - 10.3390/ijms21228687
International journal of molecular sciences, Vol. 21, Issue 22 (November 2020) , art. 8687  
4.
29 p, 9.5 MB Substrate specificity of human metallocarboxypeptidase D : comparison of the two active carboxypeptidase domains / Garcia-Pardo, Javier (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") ; Díaz, Lucía (Barcelona Supercomputing Center) ; Dasgupta, Sayani (Albert Einstein College of Medicine. Department of Molecular Pharmacology) ; Fernández-Recio, Juan (Barcelona Supercomputing Center) ; Lorenzo Rivera, Julia (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Avilés, Francesc X. (Francesc Xavier) (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Fricker, Lloyd D. (Albert Einstein College of Medicine. Department of Molecular Pharmacology)
Metallocarboxypeptidase D (CPD) is a membrane-bound component of the trans-Golgi network that cycles to the cell surface through exocytic and endocytic pathways. Unlike other members of the metallocarboxypeptidase family, CPD is a multicatalytic enzyme with three carboxypeptidase-like domains, although only the first two domains are predicted to be enzymatically active. [...]
2017 - 10.1371/journal.pone.0187778
PloS one, Vol. 12 issue 11 (2017) , art. e0187778  
5.
19 p, 3.2 MB Biochemical and MALDI-TOF mass spectrometric characterization of a novel native and recombinant cystine knot miniprotein from Solanum tuberosum subsp. andigenum cv. Churqueña / Cotabarren, Juliana (Universidad Nacional de La Plata. Centro de Investigación de Proteínas Vegetales (CIPROVE). Departamento de Ciencias Biológicas) ; Tellechea, Mariana Edith (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") ; Lorenzo Rivera, Julia (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Garcia-Pardo, Javier (Institut Català de Nanociència i Nanotecnologia) ; Avilés, Francesc X. (Francesc Xavier) (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Obregón, Walter David (Universidad Nacional de La Plata. Centro de Investigación de Proteínas Vegetales (CIPROVE). Departamento de Ciencias Biológicas)
Cystine-knot miniproteins (CKMPs) are an intriguing group of cysteine-rich molecules that combine the characteristics of proteins and peptides. Typically, CKMPs are fewer than 50 residues in length and share a characteristic knotted scaffold characterized by the presence of three intramolecular disulfide bonds that form the singular knotted structure. [...]
2018 - 10.3390/ijms19030678
International journal of molecular sciences, Vol. 19, Núm. 3 (February 2018) , art. 678  
6.
24 p, 7.3 MB The cytosolic carboxypeptidases CCP2 and CCP3 catalyze posttranslational removal of acidic amino acids / 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  

Research literature 2 records found  
1.
175 p, 2.6 MB Structural modeling and functional characterization of mammalian cytosolic carboxypeptidases 2 and 3 / Tort Regàs, Olívia ; Avilés, Francesc X., (Francesc Xavier), dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Lorenzo Rivera, Julia, dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Tanco, Sebastián Martín, dir. ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
Aquesta tesis s'emmarca en el camp de les carboxipeptidases citosòliques de mamífers, centrant-­-se particularment en els membres 2 i 3 d'aquesta subfamília de metalocarboxipeptidases. Aquest treball constitueix el primer estudi sobre la funció d'aquests enzims a través d'aproximacions in silico, in vitro i in vivo. [...]
This thesis is situated in the field of the mammalian cytosolic carboxypeptidases, particularly focusing in members 2 and 3 from this subfamily of metallocarboxypeptidases. This work gives insight for the first time into the role of those enzymes by in silico, in vitro and in vivo approaches. [...]

[Barcelona] : Universitat Autònoma de Barcelona, 2014  
2.
222 p, 3.0 MB Insights into the specificity and function of M14 metallocarboxypeptidases from structural and degradomic studies / Tanco, Sebastián Martín ; Lorenzo Rivera, Julia, dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Avilés, Francesc X. (Francesc Xavier) (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí"
Las proteasas son enzimas que escinden proteínas catalizando la hidrólisis del enlace peptídico. Todas las proteínas sufren proteólisis en algún momento u otro de su ciclo de vida y de este modo las proteasas regulan casi todos los procesos biológicos. [...]
Proteases are enzymes that irreversibly cleave proteins by the catalysis of peptide-bond hydrolysis. With all proteins undergoing proteolysis at any point of their life cycle, proteases regulate virtually every biological process. [...]

[Barcelona] : Universitat Autònoma de Barcelona, 2013  

See also: similar author names
1 Tanco, Sara
1 Tanco, Sebastián
1 Tanco, Sebastián Martín,
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