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Christopher P. Arthur

Researcher at Genentech

Publications -  33
Citations -  1463

Christopher P. Arthur is an academic researcher from Genentech. The author has contributed to research in topics: Biology & Medicine. The author has an hindex of 13, co-authored 27 publications receiving 1063 citations. Previous affiliations of Christopher P. Arthur include Scripps Research Institute & FEI Company.

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Insights into antiparallel microtubule crosslinking by PRC1, a conserved nonmotor microtubule binding protein.

TL;DR: The data show how MAP65s, by combining structural flexibility and rigidity, tune microtubule associations to establish crosslinks that selectively "mark" antiparallel overlap in dynamic cytoskeletal networks.
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An Unbiased Screen for Human Cytomegalovirus Identifies Neuropilin-2 as a Central Viral Receptor.

TL;DR: A library consisting of most single transmembrane human receptors is built and a workflow for unbiased and high-sensitivity detection of receptor-ligand interactions is implemented to elucidate the long-sought receptor of human cytomegalovirus (HCMV), the leading viral cause of congenital birth defects.
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Structural basis of α-scorpion toxin action on Nav channels

TL;DR: Structures reveal how activation of voltage-gated sodium channels causes conformational changes in a voltage-sensor domain, leading to fast inactivation, and pharmacological trapping of VSD4 reveals state-dependent interactions of gating charges from the S4 helix and S4-S5 linker.
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Autapses and networks of hippocampal neurons exhibit distinct synaptic transmission phenotypes in the absence of synaptotagmin I.

TL;DR: Comparing synaptic transmission in two different hippocampal neuron preparations found that aspects of synaptic transmission differ between autaptic and dissociated cultures, and the synaptic transmission phenotype, resulting from loss of syt-I, is dictated by the connectivity of neurons.
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Structural Basis of Nav1.7 Inhibition by a Gating-Modifier Spider Toxin.

TL;DR: ProTx2 from the Peruvian green velvet tarantula is an inhibitor cystine-knot peptide and selective antagonist of the human Nav1.7 channel, providing a structural framework for activation gating in voltage-gated ion channels.