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Artículos, Encontrados 12 registros
Artículos Encontrados 12 registros  1 - 10siguiente  ir al registro:
1.
13 p, 973.0 KB Structural determination of Bi-doped magnetite multifunctional nanoparticles for contrast imaging / Laguna-Marco, María Angeles (Instituto de Ciencia de Materiales de Aragón) ; Piquer, Cristina (Instituto de Ciencia de Materiales de Aragón) ; Gómez Roca, Alejandro. (Institut Català de Nanociència i Nanotecnologia) ; Boada, Roberto (Instituto de Ciencia de Materiales de Aragón) ; Andrés-Vergés, Manuel (Universidad de Extremadura. Departamento de Química Orgánica e Inorgánica) ; Veintemillas-Verdaguer, Sabino (Instituto de Ciencia de Materiales de Madrid) ; Serna, C. J. (Instituto de Ciencia de Materiales de Madrid) ; Iadecola, A. (Elettra Sincrotrone Trieste) ; Chaboy, J. (Instituto de Ciencia de Materiales de Aragón)
To determine with precision how Bi atoms are distributed in Bi-doped iron oxide nanoparticles their structural characterization has been carried out by X-ray absorption spectroscopy (XAS) recorded at the K edge of Fe and at the L edge of Bi. [...]
2014 - 10.1039/c4cp01392a
Physical chemistry chemical physics, Vol. 16, issue 34 (Sep. 2014) , p. 18301-18310  
2.
16 p, 3.9 MB Plasticity in the Oxidative Folding Pathway of the High Affinity Nerita Versicolor Carboxypeptidase Inhibitor (NvCI) / Esperante, Sebastián (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Bronsoms, Sílvia (Universitat Autònoma de Barcelona. Servei de Proteòmica i Biologia Estructural) ; Covaleda Cortés, Giovanni (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Trejo, Sebastián A. (Universitat Autònoma de Barcelona. Servei de Proteòmica i Biologia Estructural) ; Avilés, Francesc X. (Francesc Xavier) (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Nerita Versicolor carboxypeptidase inhibitor (NvCI) is the strongest inhibitor reported so far for the M14A subfamily of carboxypeptidases. It comprises 53 residues and a protein fold composed of a two-stranded antiparallel β sheet connected by three loops and stabilized by three disulfide bridges. [...]
2017 - 10.1038/s41598-017-05657-7
Scientific reports, Vol. 7 (2017) , art. 5457  
3.
15 p, 3.9 MB Cavity filling mutations at the thyroxine-binding site dramatically increase transthyretin stability and prevent its aggregationres / Sant'Anna, Ricardo (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Almedia, Maria Rosario (Instituto de Investigação e Inovação em Saúde da Universidade do Porto) ; Varejao, Nathalia (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Gallego Alonso, Pablo (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Esperante, Sebastián (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ferreira, Priscilla (Instituto de Bioquímica Médica Leopoldo de Meis) ; Pereira-Henriques, Alda (Instituto de Investigação e Inovação em Saúde da Universidade do Porto) ; Palhano, Fernando L. (Instituto de Bioquímica Médica Leopoldo de Meis) ; De Carvalho, Mamede (Department Neurosciences. Hospital de Santa Maria. CHLN) ; Foguel, Debora (Instituto de Bioquímica Médica Leopoldo de Meis) ; Reverter i Cendrós, David (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Saraiva, Maria Joao (Instituto de Investigação e Inovação em Saúde da Universidade do Porto) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
More than a hundred different Transthyretin (TTR) mutations are associated with fatal systemic amyloidoses. They destabilize the protein tetrameric structure and promote the extracellular deposition of TTR as pathological amyloid fibrils. [...]
2017 - 10.1038/srep44709
Scientific reports, Vol. 7 (2017) , art. 44709  
4.
11 p, 3.5 MB Mycoplasma genitalium adhesin P110 binds sialic-acid human receptors / Aparicio Alarcón, David (Institut de Biologia Molecular de Barcelona) ; Torres Puig, Sergi (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ratera, Mercè (Institut de Biologia Molecular de Barcelona) ; Querol Murillo, Enrique (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Piñol Ribas, Jaume (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Quijada Pich, Oscar (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Fita Rodríguez, Ignasi (Institut de Biologia Molecular de Barcelona)
Adhesion of pathogenic bacteria to target cells is a prerequisite for colonization and further infection. The main adhesins of the emerging sexually transmitted pathogen Mycoplasma genitalium, P140 and P110, interact to form a Nap complex anchored to the cell membrane. [...]
2018 - 10.1038/s41467-018-06963-y
Nature communications, Vol. 9 (2018) , art. 4471  
5.
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  
6.
16 p, 3.8 MB Disulfide driven folding for a conditionally disordered protein / Fraga, Hugo (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pujols Pujol, Jordi (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Gil-Garcia, Marcos (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Roque Córdova, Alicia (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Bernardo-Seisdedos, Ganeko (CIC BioGUNE) ; Santambrogio, Carlo (University of Milano-Bicocca. Dipartimento di Biotecnologie e Bioscienze) ; Bech-Serra, Joan-Josep (Vall d'Hebron Institut d'Oncologia) ; Canals, Francesc (Vall d'Hebron Institut d'Oncologia) ; Bernadó, Pau (Centre de biochimie Structurale (Montpellier)) ; Grandori, Rita (University of Milano-Bicocca. Dipartimento di Biotecnologie e Bioscienze) ; Millet, Oscar (CIC BioGUNE) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Conditionally disordered proteins are either ordered or disordered depending on the environmental context. The substrates of the mitochondrial intermembrane space (IMS) oxidoreductase Mia40 are synthesized on cytosolic ribosomes and diffuse as intrinsically disordered proteins to the IMS, where they fold into their functional conformations; behaving thus as conditionally disordered proteins. [...]
2017 - 10.1038/s41598-017-17259-4
Scientific reports, Vol. 7 (2017) , art. 16994  
7.
17 p, 1.7 MB Intradomain confinement of disulfides in the folding of two consecutive modules of the LDL receptor / Martínez-Oliván, Juan (Universidad de Zaragoza. Departamento de Bioquímica y Biología Molecular y Celular) ; Fraga, Hugo (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Arias-Moreno, Xabier (Universidad de Zaragoza. Departamento de Bioquímica y Biología Molecular y Celular) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Sancho, Javier (Universidad de Zaragoza. Departamento de Bioquímica y Biología Molecular y Celular)
The LDL receptor internalizes circulating LDL and VLDL particles for degradation. Its extracellular binding domain contains ten (seven LA and three EGF) cysteine-rich modules, each bearing three disulfide bonds. [...]
2015 - 10.1371/journal.pone.0132141
PloS one, Vol. 10, issue 7 (2015) , art. e0132141  
8.
15 p, 1.8 MB A model of protein association based on their hydrophobic and electric interactions / Mozo-Villarias, Angel (Institut de Recerca Biomèdica de Lleida) ; Cedano Rodríguez, Juan Antonio (Universidad de la República (Uruguai).Laboratorio de Inmunología) ; Querol Murillo, Enrique (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
The propensity of many proteins to oligomerize and associate to form complex structures from their constituent monomers, is analyzed in terms of their hydrophobic (H), and electric pseudo-dipole (D) moment vectors. [...]
2014 - 10.1371/journal.pone.0110352
PloS one, Vol. 9 issue 10 (2014) , art. e110352  
9.
19 p, 2.2 MB A protein self-assembly model guided by electrostatic and hydrophobic dipole moments / Mozo-Villarias, Angel (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Querol Murillo, Enrique (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Protein self-assembling is studied under the light of the Biological Membrane model. To this purpose we define a simplified formulation of hydrophobic interaction energy in analogy with electrostatic energy stored in an electric dipole. [...]
2019 - 10.1371/journal.pone.0216253
PloS one, Vol. 14, issue 4 (April 2019) , art. e0216253  
10.
16 p, 2.6 MB Reduced level of docosahexaenoic acid shifts GPCR neuroreceptors to less ordered membrane regions / Javanainen, Matti (Czech Academy of Sciences. Institute of Organic Chemistry and Biochemistry) ; Enkavi, Giray (Department of Physics. University of Helsinki) ; Guixà González, Ramon (Universitat Autònoma de Barcelona. Laboratori de Medicina Computacional) ; Kulig, Waldemar (Department of Physics. University of Helsinki) ; Martinez-Seara, Hector (Czech Academy of Sciences. Institute of Organic Chemistry and Biochemistry) ; Levental, Ilya (Department of Integrated Biology and Pharmacology. McGovern Medical School. University of Texas Health Science Center at Houston) ; Vattulainen, Ilpo (MEMPHYS - Center for Biomembrane Physics)
G protein-coupled receptors (GPCRs) control cellular signaling and responses. Many of these GPCRs are modulated by cholesterol and polyunsaturated fatty acids (PUFAs) which have been shown to co-exist with saturated lipids in ordered membrane domains. [...]
2019 - 10.1371/journal.pcbi.1007033
PLoS computational biology, Vol. 15 Núm. 5 (may 2019) , p. e1007033  

Artículos : Encontrados 12 registros   1 - 10siguiente  ir al registro:
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