F
Francisco Conejero-Lara
Researcher at University of Granada
Publications - 64
Citations - 1287
Francisco Conejero-Lara is an academic researcher from University of Granada. The author has contributed to research in topics: Protein folding & Heptad repeat. The author has an hindex of 19, co-authored 60 publications receiving 1128 citations. Previous affiliations of Francisco Conejero-Lara include Spanish National Research Council & University of Oxford.
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Environmental Conditions Affect the Kinetics of Nucleation of Amyloid Fibrils and Determine Their Morphology
TL;DR: The results suggest that the influence of environmental variables on protein solvation is crucial in determining the nucleation kinetics, the pathway of assembly, and the final fibril morphology.
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Identification of a Chemoreceptor for Tricarboxylic Acid Cycle Intermediates: DIFFERENTIAL CHEMOTACTIC RESPONSE TOWARDS RECEPTOR LIGANDS*
Jesús Lacal,Carlos Alfonso,Xianxian Liu,Rebecca E. Parales,Bertrand Morel,Francisco Conejero-Lara,Germán Rivas,Estrella Duque,Juan L. Ramos,Tino Krell +9 more
TL;DR: Equilibrium sedimentation studies show that malate, the chemoattractant that causes the strongest chemotactic response, stabilizes the dimeric state of McpS-LBD, the only chemoreceptor of TCA cycle intermediates in the strain under study.
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The native state conformational ensemble of the SH3 domain from alpha-spectrin.
Mourad Sadqi,Salvador Casares,María A. Abril,Obdulio López-Mayorga,Francisco Conejero-Lara,Ernesto Freire +5 more
TL;DR: The results demonstrate that under native conditions the SH3 domain needs to be considered as an ensemble of conformations and that the hydrogen exchange data obtained under those conditions cannot be interpreted by a two-state equilibrium.
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The thermodynamic stability of amyloid fibrils studied by differential scanning calorimetry.
TL;DR: This work analyzed the thermal melting of the amyloid fibrils of the N47A mutant of the alpha-spectrin SH3 domain by differential scanning calorimetry (DSC) and found that with the use of appropriate models of analysis DSC has an extraordinary potential to analyze the thermodynamic determinants of amyloids fibril stability.
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Unfolding and aggregation during the thermal denaturation of streptokinase.
TL;DR: Results indicate that each structural domain of SK behaves as a single cooperative unfolding unit under equilibrium conditions, and that in the aggregates the N-terminal segment 1-63 and the whole of SK domain C are at least partially structured, while domain B is highly unstructured.