Search Results - "Mateo, Pedro L."
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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
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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2
Single-chain protein mimetics of the N-terminal heptad-repeat region of gp41 with potential as anti–HIV-1 drugs
Published in Proceedings of the National Academy of Sciences - PNAS (23-12-2014)“…During HIV-1 fusion to the host cell membrane, the N-terminal heptad repeat (NHR) and the C-terminal heptad repeat (CHR) of the envelope subunit gp41 become…”
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3
Molecular and Physicochemical Factors Governing Solubility of the HIV gp41 Ectodomain
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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An Oligomeric Equilibrium Intermediate as the Precursory Nucleus of Globular and Fibrillar Supramacromolecular Assemblies in a PDZ Domain
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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A comparative analysis of the folding and misfolding pathways of the third PDZ domain of PSD95 investigated under different pH conditions
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
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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Sublingual Priming with a HIV gp41-Based Subunit Vaccine Elicits Mucosal Antibodies and Persistent B Memory Responses in Non-Human Primates
Published in Frontiers in immunology (01-02-2017)“…Persistent B cell responses in mucosal tissues are crucial to control infection against sexually transmitted pathogens like human immunodeficiency virus 1…”
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8
Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin
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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9
Thermodynamic Characterization of the Folding Equilibrium of the Human Nedd4-WW4 Domain: At the Frontiers of Cooperative Folding
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
Unfolding and aggregation during the thermal denaturation of streptokinase
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
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
Thermodynamic dissection of the binding energetics of proline-rich peptides to the Abl-SH3 domain: implications for rational ligand design
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
Thermodynamic analysis of the chemotactic protein from Escherichia coli, CheY
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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14
Crystallographic structure of the SH3 domain of the human c-Yes tyrosine kinase: Loop flexibility and amyloid aggregation
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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15
The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase
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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16
Structure of human TSG101 UEV domain
Published in Acta crystallographica. Section D, Biological crystallography. (01-04-2006)“…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
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
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
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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20
Thermodynamic Analysis of α-spectrin SH3 and Two of Its Circular Permutants with Different Loop Lengths: Discerning the Reasons for Rapid Folding in Proteins
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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