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Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase.
Single-site mutants in the Cu,Zn superoxide dismutase (SOD) gene (SOD1) occur in patients with the fatal neurodegenerative disorder familial amyotrophic lateral sclerosis (FALS). Complete screening
Structure of the fibre-forming protein pilin at 2.6 Å resolution
The crystallographic structure of Neisseria gonorrhoeae pilin reveals an α–β roll fold with a striking 85 Å α-helical spine and an 0-linked disaccharide to stabilize interactions that allow sequence hypervariability, responsible for pilin's celebrated antigenic variation, within disulphide region β-strands and connections.
The structural biochemistry of the superoxide dismutases.
Structural Mechanism of Abscisic Acid Binding and Signaling by Dimeric PYR1
Structures of pyrabactin resistance 1 (PYR1), a prototypical PYR/PYP1-like (PYL)/regulatory component of ABA receptor (RCAR) protein that functions in early ABA signaling are reported.
Early abscisic acid signal transduction mechanisms: newly discovered components and newly emerging questions.
An emerging PYR/RCAR-PP2C-SnRK2 model of ABA signal transduction provides researchers with a framework through which early ABA signaling can be understood, and allow novel questions about the hormone response pathway and possible applications in stress resistance engineering of plants to be addressed.
Plant UVR8 Photoreceptor Senses UV-B by Tryptophan-Mediated Disruption of Cross-Dimer Salt Bridges
Donuts Dissociate In Arabidopsis, the UVR8 protein responds to ultraviolet-B (UV-B) light by dissociating into monomers, which are then available to interact with downstream factors that enact the
Structure of nitric oxide synthase oxygenase dimer with pterin and substrate.
Crystal structures of the murine cytokine-inducible nitric oxide synthase oxygenase dimer with active-center water molecules, the substrate L-arginine (L-Arg), or product analog thiocitrulline reveal
1.4 A structure of photoactive yellow protein, a cytosolic photoreceptor: unusual fold, active site, and chromophore.
The high-resolution structure of photoactive yellow protein supports a mechanism whereby electrostatic interactions create an active site poised for photon-induced rearrangements and efficient protein-mediated signal transduction.
Structure of a Protein Photocycle Intermediate by Millisecond Time-Resolved Crystallography
The atomic structure of the bleached signaling intermediate in the light cycle of PYP was determined by millisecond time-resolved, multiwavelength Laue crystallography and simultaneous optical spectroscopy to suggest a general framework for the interpretation of protein photocycles.