D
David W. Ehrhardt
Researcher at Carnegie Institution for Science
Publications - 92
Citations - 12830
David W. Ehrhardt is an academic researcher from Carnegie Institution for Science. The author has contributed to research in topics: Microtubule & Cortical microtubule. The author has an hindex of 52, co-authored 89 publications receiving 11666 citations. Previous affiliations of David W. Ehrhardt include Stanford University & Howard Hughes Medical Institute.
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Journal ArticleDOI
Visualization of Cellulose Synthase Demonstrates Functional Association with Microtubules
Alexander R. Paredez,Alexander R. Paredez,Chris Somerville,Chris Somerville,David W. Ehrhardt +4 more
TL;DR: Inhibition of microtubule polymerization changed the fine-scale distribution and pattern of moving CESA complexes in the membrane, indicating a relatively direct mechanism for guidance of cellulose deposition by the cytoskeleton.
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Random GFP∷cDNA fusions enable visualization of subcellular structures in cells of Arabidopsis at a high frequency
TL;DR: The results indicate that screening GFP-fusion protein libraries is a useful approach for identifying and visualizing components of subcellular structures and their associated dynamics in higher plant cells.
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Calcium Spiking in Plant Root Hairs Responding to Rhizobium Nodulation Signals
TL;DR: A nonnodulating alfalfa mutant is defective in calcium spiking, consistent with the possibility that this mutant is blocked in an early stage of nodulation signal perception.
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Arabidopsis cortical microtubules position cellulose synthase delivery to the plasma membrane and interact with cellulose synthase trafficking compartments
Ryan Gutierrez,Jelmer J. Lindeboom,Alexander R. Paredez,Anne Mie C. Emons,Anne Mie C. Emons,David W. Ehrhardt,David W. Ehrhardt +6 more
TL;DR: Evidence is provided that cortical microtubules also position the delivery of CESA complexes to the plasma membrane and interact with small CESA-containing compartments by a mechanism that permits motility driven by microtubule depolymerization.
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Colocalization of cell division proteins FtsZ and FtsA to cytoskeletal structures in living Escherichia coli cells by using green fluorescent protein
TL;DR: FtsZ and FtsA proteins tagged with green fluorescent protein (GEP) colocalize to division-site ring-like structures in living bacterial cells in a visible space between the segregated nucleoids, suggesting a degree of interspecies functional conservation.