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Brian R. Crane

Researcher at Cornell University

Publications -  183
Citations -  11342

Brian R. Crane is an academic researcher from Cornell University. The author has contributed to research in topics: Histidine kinase & Heme. The author has an hindex of 58, co-authored 171 publications receiving 10403 citations. Previous affiliations of Brian R. Crane include Albert Einstein College of Medicine & Cleveland Clinic.

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Structure of nitric oxide synthase oxygenase dimer with pterin and substrate.

TL;DR: 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 how dimerization, cofactor tetrahydrobiopterin, and L-Arg binding complete the catalytic center for synthesis of the essential biological signal and cytotoxin nitricoxide.
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Structure of CheA, a Signal-Transducing Histidine Kinase

TL;DR: A resolution crystal structure of Thermotoga maritima CheA reveals a dimer where the functions of dimerization, ATP binding, and regulation are segregated into domains, suggesting that relative domain motions link receptor response to kinase activity.
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Tryptophan-Accelerated Electron Flow Through Proteins

TL;DR: In this paper, transient optical and infrared spectroscopic experiments were conducted to quantify the extent to which an intervening tryptophan residue can facilitate electron transfer between distant metal redox centers in a mutant Pseudomonas aeruginosa azurin.
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The structure of nitric oxide synthase oxygenase domain and inhibitor complexes.

TL;DR: Juxtaposed hydrophobic O2- and polar L-arginine-binding sites occupied by imidazole and aminoguanidine, respectively, provide a template for designing dual-function inhibitors and imply substrate-assisted catalysis.
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Conformational switching in the fungal light sensor Vivid.

TL;DR: The Neurospora crassa photoreceptor Vivid tunes blue-light responses and modulates gating of the circadian clock and key elements of this activation mechanism are conserved by other photosensors such as White Collar-1, ZEITLUPE, ENVOY, and flavin-binding, kelch repeat, F-BOX 1.