Search Results - "Mateo, Pedro L."

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  1. 1

    Thermodynamic Analysis of the Binding of 2F5 (Fab and Immunoglobulin G Forms) to Its gp41 Epitope Reveals a Strong Influence of the Immunoglobulin Fc Region on Affinity by Crespillo, Sara, Casares, Salvador, Mateo, Pedro L., Conejero-Lara, Francisco

    Published in The Journal of biological chemistry (10-01-2014)
    “…Immunotherapies and vaccines based on the induction of broadly neutralizing monoclonal antibodies (bNAbs) have become outstanding strategies against HIV-1…”
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    Molecular and Physicochemical Factors Governing Solubility of the HIV gp41 Ectodomain by Manssour-Triedo, Fadia, Crespillo, Sara, Morel, Bertrand, Casares, Salvador, Mateo, Pedro L., Notka, Frank, Roger, Marie G., Mouz, Nicolas, El-Habib, Raphaelle, Conejero-Lara, Francisco

    Published in Biophysical journal (23-08-2016)
    “…The HIV gp41 ectodomain (e-gp41) is an attractive target for the development of vaccines and drugs against HIV because of its crucial role in viral fusion to…”
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  4. 4

    An Oligomeric Equilibrium Intermediate as the Precursory Nucleus of Globular and Fibrillar Supramacromolecular Assemblies in a PDZ Domain by Murciano-Calles, Javier, Cobos, Eva S., Mateo, Pedro L., Camara-Artigas, Ana, Martinez, Jose C.

    Published in Biophysical journal (07-07-2010)
    “…The equilibrium unfolding at neutral pH of the third PDZ domain of PSD95, as followed by DSC, is characterized by the presence of an equilibrium intermediate…”
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  5. 5

    A comparative analysis of the folding and misfolding pathways of the third PDZ domain of PSD95 investigated under different pH conditions by Murciano-Calles, Javier, Cobos, Eva S., Mateo, Pedro L., Camara-Artigas, Ana, Martinez, Jose C.

    Published in Biophysical chemistry (01-10-2011)
    “…Equilibrium unfolding at neutral pH of the third PDZ domain of PSD95 is well described by the presence of a partly unfolded intermediate that presents…”
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    The denaturation of circular enterocin AS-48 by urea and guanidinium hydrochloride by Cobos, Eva S, Filimonov, Vladimir V, Gálvez, Antonio, Valdivia, Eva, Maqueda, Mercedes, Martı́nez, Jose C, Mateo, Pedro L

    Published in Biochimica et biophysica acta (29-07-2002)
    “…The unfolding thermodynamics of the circular enterocin protein AS-48, produced by Enterococcus faecalis, has been studied. The native structure of the…”
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    Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin by Sanchez-Ruiz, Jose M, Lopez-Lacomba, Jose L, Cortijo, Manuel, Mateo, Pedro L

    Published in Biochemistry (Easton) (08-03-1988)
    “…A differential scanning calorimetry study of the thermal denaturation of Bacillus thermoproteolyticus rokko thermolysin was carried out. The calorimetric…”
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    Thermodynamic Characterization of the Folding Equilibrium of the Human Nedd4-WW4 Domain: At the Frontiers of Cooperative Folding by Cobos, Eva S, Iglesias-Bexiga, Manuel, Ruiz-Sanz, Javier, Mateo, Pedro L, Luque, Irene, Martinez, Jose C

    Published in Biochemistry (Easton) (15-09-2009)
    “…WW domains are the smallest naturally independent β-sheet protein structures available to date and constitute attractive model systems for investigating the…”
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  10. 10

    Unfolding and aggregation during the thermal denaturation of streptokinase by Azuaga, Ana I., Dobson, Christopher M., Mateo, Pedro L., Conejero‐Lara, Francisco

    Published in European journal of biochemistry (01-08-2002)
    “…The thermal denaturation of streptokinase from Streptococcus equisimilis (SK) together with that of a set of fragments encompassing each of its three domains…”
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    Presence of a Slow Dimerization Equilibrium on the Thermal Unfolding of the 205−316 Thermolysin Fragment at Neutral pH by Conejero-Lara, Francisco, Mateo, Pedro L

    Published in Biochemistry (Easton) (19-03-1996)
    “…Differential scanning calorimetry and size-exclusion chromatography have been used to characterize the dimerization and unfolding of the 205−316 C-terminal…”
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  12. 12

    Thermodynamic dissection of the binding energetics of proline-rich peptides to the Abl-SH3 domain: implications for rational ligand design by Palencia, Andrés, Cobos, Eva S, Mateo, Pedro L, Martínez, Jose C, Luque, Irene

    Published in Journal of molecular biology (13-02-2004)
    “…The inhibition of the interactions between SH3 domains and their targets is emerging as a promising therapeutic strategy. To date, rational design of potent…”
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  13. 13

    Thermodynamic analysis of the chemotactic protein from Escherichia coli, CheY by Filimonov, Vladimir V, Prieto, Jesus, Martinez, Jose C, Bruix, Marta, Mateo, Pedro L, Serrano, Luis

    Published in Biochemistry (Easton) (01-11-1993)
    “…CheY, the 129 amino acid chemotactic protein from Escherichia coli, is a good model for studies of folding of parallel alpha/beta proteins. We report here the…”
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    Crystallographic structure of the SH3 domain of the human c-Yes tyrosine kinase: Loop flexibility and amyloid aggregation by Martín-García, José M., Luque, Irene, Mateo, Pedro L., Ruiz-Sanz, Javier, Cámara-Artigas, Ana

    Published in FEBS letters (01-05-2007)
    “…SH3 domains from the Src family of tyrosine kinases represent an interesting example of the delicate balance between promiscuity and specificity characteristic…”
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    The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase by van den Berg, Bert, Chung, Evonne W., Robinson, Carol V., Mateo, Pedro L., Dobson, Christopher M.

    Published in The EMBO journal (01-09-1999)
    “…The oxidative refolding of hen lysozyme has been studied by a variety of time‐resolved biophysical methods in conjunction with analysis of folding…”
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    Structure of human TSG101 UEV domain by Mateo, Pedro L., Palencia, Andres, Martinez, Jose C., Luque, Irene, Camara-Artigas, Ana

    “…The UEV domain of the TSG101 protein functions in the vacuolar protein‐sorting pathway and in the budding process of HIV‐1 and other retroviruses by…”
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    Structural and thermodynamic studies of Bergerac-SH3 chimeras by Gushchina, Liubov' V., Gabdulkhakov, Azat G., Nikonov, Stanislav V., Mateo, Pedro L., Filimonov, Vladimir V.

    Published in Biophysical chemistry (01-02-2009)
    “…Bergerac-type chimeras of spectrin SH3 were designed by extending a β-hairpin by eight amino acids so that the extension protruded from the domain body like a…”
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    NMR Solution Structure of the 205−316 C-Terminal Fragment of Thermolysin. An Example of Dimerization Coupled to Partial Unfolding by Conejero-Lara, Francisco, González, Carlos, Jiménez, M. Angeles, Padmanabhan, S, Mateo, Pedro L, Rico, Manuel

    Published in Biochemistry (Easton) (30-09-1997)
    “…The solution structure of the C-terminal fragment 205−316 of thermolysin has been determined by 1H-NMR methods. The fragment forms a dimer in which each…”
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    A Thermodynamic and Kinetic Analysis of the Folding Pathway of an SH3 Domain Entropically Stabilised by a Redesigned Hydrophobic Core by Cobos, Eva S, Filimonov, Vladimir V, Vega, Maria Cristina, Mateo, Pedro L, Serrano, Luis, Martı́nez, Jose C

    Published in Journal of molecular biology (18-04-2003)
    “…The folding thermodynamics and kinetics of the α-spectrin SH3 domain with a redesigned hydrophobic core have been studied. The introduction of five…”
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    Thermodynamic Analysis of α-spectrin SH3 and Two of Its Circular Permutants with Different Loop Lengths:  Discerning the Reasons for Rapid Folding in Proteins by Martínez, Jose C, Viguera, Ana R, Berisio, Rita, Wilmanns, Matthias, Mateo, Pedro L, Filimonov, Vladimir V, Serrano, Luis

    Published in Biochemistry (Easton) (12-01-1999)
    “…The temperature dependences of the unfolding−refolding reaction of a shorter version of the α-spectrin SH3 domain (PWT) used as a reference and of two circular…”
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