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Jose A. Gavira

Researcher at Spanish National Research Council

Publications -  129
Citations -  3421

Jose A. Gavira is an academic researcher from Spanish National Research Council. The author has contributed to research in topics: Crystallization & Protein crystallization. The author has an hindex of 28, co-authored 112 publications receiving 2841 citations. Previous affiliations of Jose A. Gavira include Tohoku University & University of Alabama in Huntsville.

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The Molecular Mechanism of Nitrate Chemotaxis via Direct Ligand Binding to the PilJ Domain of McpN.

TL;DR: It is shown that Pseudomonas aeruginosa PAO1 mediates nitrate chemotaxis on the basis of specific nitrate sensing by the periplasmic PilJ domain of the PA2788/McpN chemoreceptor.
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Is Agarose an Impurity or an Impurity Filter? In Situ Observation of the Joint Gel/Impurity Effect on Protein Crystal Growth Kinetics

TL;DR: In this paper, the joint effect of agarose gel and impurities on hen egg white lysozyme crystal growth kinetics was investigated in situ by comparing the two-dimensional (2D) nucleation rate and the step velocity of crystals growing from free and gelled (agarose) solutions having two different levels of purity: highly purified (99.99% pure) and commercial grade (98.5% pure).
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Effects of a Magnetic Field on Lysozyme Crystal Nucleation and Growth in a Diffusive Environment

TL;DR: In this article, Tetragonal hen egg white lysozyme crystals were grown in agarose gel under the influence of a 7 T homogeneous and static magnetic field, and the results showed that the effect of the magnetic field and the chemical effects due to the interaction between protein and agaroses was compromised.
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Enhanced vulnerability of human proteins towards disease-associated inactivation through divergent evolution.

TL;DR: The results support that recent divergence of consensus amino acids may have occurred with neutral effects on many functional and regulatory traits of wild-type human proteins, however, divergence at certain sites may have increased the propensity of some human proteins towards inactivation due to disease-associated mutations and polymorphisms.