Results overview: Found 6 records in 0.03 seconds.
Articles, 6 records found
Articles 6 records found  
1.
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 Biologia Molecular) ; Ariño Carmona, Joaquín (Universitat Autònoma de Barcelona. Departament de Bioquímica i 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  
2.
14 p, 23.8 MB Shining Light On An mGlu5 Photoswitchable NAM : A Theoretical Perspective / Dalton, James A.R. (Universitat Autònoma de Barcelona. Institut de Neurociències) ; Lans, Isaias (Universitat Autònoma de Barcelona. Institut de Neurociències) ; Rovira Algans, Xavier (Institut de Génomique Fonctionnelle) ; Malhaire, Fanny (Institut de Génomique Fonctionnelle) ; Gómez-Santacana, Xavier (Universitat Autònoma de Barcelona. Institut de Neurociències) ; Pittolo, Silvia (Institute for Bioengineering of Catalonia (IBEC)) ; Gorostiza, Pau (Institute for Bioengineering of Catalonia (IBEC)) ; Llebaria, Amadeu (Institut de Química Avançada de Catalunya) ; Goudet, Cyril (Institut de Génomique Fonctionnelle) ; Pin, Jean-Philippe (Institut de Génomique Fonctionnelle) ; Giraldo, Jesús (Universitat Autònoma de Barcelona. Institut de Neurociències)
Metabotropic glutamate receptors (mGluRs) are important drug targets because of their involvement in several neurological diseases. Among mGluRs, mGlu5 is a particularly high-profile target because its positive or negative allosteric modulation can potentially treat schizophrenia or anxiety and chronic pain, respectively. [...]
2016 - 10.2174/1570159X13666150407231417
Curr Neuropharmacol, Vol. 14, Num. 5 (2016) , p. 441-454  
3.
13 p, 2.6 MB The Impact of Extra-Domain Structures and PostTranslational Modifications in the Folding/Misfolding Behaviour of the Third PDZ Domain of MAGUK Neuronal Protein PSD-95 / Murciano Calles, Javier (Universidad de Granada. Departamento de Química Física) ; Marin Argany, Marta (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Cobos, Eva S. (Universidad de Granada. Departamento de Química Física) ; Villegas Hernández, Sandra (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Martínez, José C. (Universidad de Granada. Departamento de Química Física)
The modulation of binding affinities and specificities by post-translational modifications located out from the binding pocket of the third PDZ domain of PSD-95 (PDZ3) has been reported recently. It is achieved through an intra-domain electrostatic network involving some charged residues in the β2–β3 loop (were a succinimide modification occurs), the α3 helix (an extra-structural element that links the PDZ3 domain with the following SH3 domain in PSD-95, and contains the phosphorylation target Tyr397), and the ligand peptide. [...]
2014 - 10.1371/journal.pone.0098124
PLoS one, Vol. 9, Num. 5 (2014) , p. e98124  
4.
10 p, 1.2 MB Redefining the PF06864 Pfam Family Based on Burkholderia pseudomallei PilO2Bp S-SAD Crystal Structure / Lassaux, Patricia (Università di Milano. Department of Biosciences) ; Conchillo-Solé, Óscar (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Manjasetty, Babu A. (Grenoble Outstation. European Molecular Biology Laboratory) ; Yero Corona, Daniel (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ; Perletti, Lucia (Università di Milano. Department of Biosciences) ; Belrhali, Hassan (Grenoble Outstation. European Molecular Biology Laboratory) ; Daura i Ribera, Xavier (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Gourlay, Louise J. (Università di Milano. Department of Biosciences) ; Bolognesi, Martino (Università di Milano. Department of Biosciences)
Type IV pili are surface-exposed filaments and bacterial virulence factors, represented by the Tfpa and Tfpb types, which assemble via specific machineries. The Tfpb group is further divided into seven variants, linked to heterogeneity in the assembly machineries. [...]
2014 - 10.1371/journal.pone.0094981
PLoS one, Vol. 9 Issue 4 (April 2014) , p. e94981  
5.
5 p, 543.2 KB Genomic Instability in Newborn with Short Telomeres / Moreno-Palomo, Jennifer (Universitat Autònoma de Barcelona. Departament de Genètica i Microbiologia) ; Creus Capdevila, Amadeu (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ; Marcos Dauder, Ricardo (Universitat Autònoma de Barcelona. Departament de Genètica i Microbiologia) ; Hernández Bonilla, Alba (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia)
Telomere length is considered to be a risk factor in adults due to its proved association with cancer incidence and mortality. Since newborn present a wide interindividual variation in mean telomere length, it is relevant to demonstrate if these differences in length can act also as an early risk indicator. [...]
2014 - 10.1371/journal.pone.0091753
PLoS one, Vol. 9, Issue 3 (March 2014) , p.e91753  
6.
16 p, 1.6 MB Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases / Castillo Cano, Virginia (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Ventura i Zamora, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Protein aggregation underlies a wide range of human disorders. The polypeptides involved in these pathologies might be intrinsically unstructured or display a defined 3D-structure. Little is known about how globular proteins aggregate into toxic assemblies under physiological conditions, where they display an initially folded conformation. [...]
2009 - 10.1371/journal.pcbi.1000476
PLOS Computational Biology, Vol. 5, Issue 8 (August 2009) , p. e1000476  

Interested in being notified about new results for this query?
Set up a personal email alert or subscribe to the RSS feed.