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Jonathan T. Henry

Researcher at University of Chicago

Publications -  7
Citations -  794

Jonathan T. Henry is an academic researcher from University of Chicago. The author has contributed to research in topics: Caulobacter crescentus & Ligand (biochemistry). The author has an hindex of 6, co-authored 7 publications receiving 688 citations.

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Ligand-Binding PAS Domains in a Genomic, Cellular, and Structural Context

TL;DR: The current state of knowledge of the structural foundations and evolution of ligand recognition and binding by Per-Arnt-Sim domains is synthesized.
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Scaling laws governing stochastic growth and division of single bacterial cells

TL;DR: The experimental and theoretical analysis reveals a simple physical principle governing these complex biological processes: a single temperature-dependent scale of cellular time governs the stochastic dynamics of growth and division in balanced growth conditions.
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ppGpp and Polyphosphate Modulate Cell Cycle Progression in Caulobacter crescentus

TL;DR: Two cell cycle regulatory signals, ppGpp and polyphosphate (polyP), are identified that inhibit the swarmer-to-stalked transition in both complex and glucose-exhausted media, thereby increasing the proportion ofSwarmer cells in mixed culture and providing evidence that ppGopp and polyP are cell-type-specific developmental regulators.
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Identification of the PhoB Regulon and Role of PhoU in the Phosphate Starvation Response of Caulobacter crescentus

TL;DR: Using chromatin immunoprecipitation-DNA sequencing (ChIP-Seq) and genome-wide expression profiling, this work demonstrates that PhoB is induced to regulate nearly 50 genes under phosphate-starved conditions and favors a model in which PhoU affects intracellular phosphate accumulation, possibly through the high-affinity phosphate transporter.
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The Positive Allosteric Modulator Morantel Binds at Noncanonical Subunit Interfaces of Neuronal Nicotinic Acetylcholine Receptors

TL;DR: Seven cysteine-substituted subunits are created by site-directed mutagenesis, choosing residues in the putative morantel binding site with the aid of structural homology models and it is concluded that the four residues showing MTS effects contribute to the morantels binding site.