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Dan L. Sackett

Researcher at National Institutes of Health

Publications -  175
Citations -  8900

Dan L. Sackett is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Tubulin & Microtubule. The author has an hindex of 46, co-authored 163 publications receiving 8280 citations. Previous affiliations of Dan L. Sackett include University of California, San Diego & University of Minnesota.

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Paclitaxel-resistant Human Ovarian Cancer Cells Have Mutant β-Tubulins That Exhibit Impaired Paclitaxel-driven Polymerization

TL;DR: Results identify residues β270 and β364 as important modulators of paclitaxel’s interaction with tubulin as well as acquired mutations in the M40 isotype at nucleotide 810 (T → G; Phe270 → Val) in 1A9PTX10 cells and nucleotide 1092 (G → A; Ala364 → Thr) in1A 9PTX22 cells.
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Nile red as a polarity-sensitive fluorescent probe of hydrophobic protein surfaces.

TL;DR: The dye Nile red detects the exposure or formation of new hydrophobic surfaces induced by ligand binding to calmodulin, oligomerization of melittin, or unfolding of ovalbumin during early thermal denaturation.
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A common pharmacophore for epothilone and taxanes: Molecular basis for drug resistance conferred by tubulin mutations in human cancer cells

TL;DR: The unification of taxane, epothilone, and sarcodictyin chemistries in a single pharmacophore provides a framework to study drug-tubulin interactions that should assist in the rational design of agents targeting tubulin.
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p53 is associated with cellular microtubules and is transported to the nucleus by dynein.

TL;DR: It is proposed that functional microtubules and the dynein motor protein participate in transport of p53 and facilitate its accumulation in the nucleus after DNA damage.
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Tubulin binding blocks mitochondrial voltage-dependent anion channel and regulates respiration

TL;DR: A previously unknown mechanism of regulation of mitochondrial energetics, governed by VDAC and tubulin at the mitochondria–cytosol interface is suggested, which requires tubulin anionic C-terminal tail (CTT) peptides and may reflect the evolutionary conservation of length and anionic charge in CTT throughout eukaryotes, despite wide changes in the exact sequence.