Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.4.4 (kinesin)
 5,033 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Biomolecular motor-powered active transport represents an alternate means for analyte processing in nanoscale biosensors and bioanalytical devices. For example, a prototype "smart dust" biosensor has recently been reported in which the motor protein kinesin processes antibody-functionalized microtubules (MTs) to capture and separate optically tagged protein analytes. A potential limitation of this technology, however, involves the inhibition of transport function by interfering compounds that may be present in raw samples. Here we characterized the response of kinesin-MT transport to a range of potential interferents including solvents, acids, oxidizers, and environmental contaminants. The results of kinesin motility assays suggest that, among the tested interferents, only acetic acid and sodium hypochlorite adversely affected MT transport, primarily due to depolymerization of MT filaments. While negative effects were not observed for the remaining compounds tested, enhancement in motility was observed in the presence of acetone, antifreeze, and organic matter. Overall, the data suggest that kinesin-MT transport is resilient against a variety of common interferents, but primarily susceptible to failure due to significant changes in pH or the presence of an oxidizer.
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PMID:Effects of potential environmental interferents on kinesin-powered molecular shuttles. 2258 42

Aucsia is a green plant gene family encoding 44-54 amino acids long miniproteins. The sequenced genomes of most land plants contain two Aucsia genes. RNA interference of both tomato (Solanum lycopersicum) Aucsia genes (SlAucsia-1 and SlAucsia-2) altered auxin sensitivity, auxin transport and distribution; it caused parthenocarpic development of the fruit and other auxin-related morphological changes. Here we present data showing that the Aucsia-1 gene of Arabidopsis thaliana alters, by itself, root auxin biology and that the AtAUCSIA-1 miniprotein physically interacts with a kinesin-related protein. The AtAucsia-1 gene is ubiquitously expressed, although its expression is higher in roots and inflorescences in comparison to stems and leaves. Two allelic mutants for AtAucsia-1 gene did not display visible root morphological alterations; however both basipetal and acropetal indole-3-acetic acid (IAA) root transport was reduced as compared with wild-type plants. The transcript steady state levels of the auxin efflux transporters ATP BINDING CASSETTE subfamily B (ABCB) ABCB1, ABCB4 and ABCB19 were reduced in ataucsia-1 plants. In ataucsia-1 mutant, lateral root growth showed an altered response to i) exogenous auxin, ii) an inhibitor of polar auxin transport and iii) ethylene. Overexpression of AtAucsia-1 inhibited primary root growth. In vitro and in vivo protein-protein interaction experiments showed that AtAUCSIA-1 interacts with a 185 amino acids long fragment belonging to a 2712 amino acids long protein of unknown function (At4g31570). Bioinformatics analysis indicates that the AtAUCSIA-1 interacting protein (AtAUCSIA-1IP) clusters with a group of CENP-E kinesin-related proteins. Gene ontology predictions for the two proteins are consistent with the hypothesis that the AtAUCSIA-1/AtAUCSIA-1IP complex is involved in the regulation of the cytoskeleton dynamics underlying auxin biology.
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PMID:Arabidopsis thaliana AUCSIA-1 regulates auxin biology and physically interacts with a kinesin-related protein. 2291 80

Here, we report a covalently functionalized graphene oxide with Tris-(nitrilo Tris-acetic acid) (TGO), which can reconstitute kinesin mediated intracellular cargo transport, and deliver multiple proteins and therapeutic antimitotic dodecapeptide peptides into the cancer cell.
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PMID:Single functionalized graphene oxide reconstitutes kinesin mediated intracellular cargo transport and delivers multiple cytoskeleton proteins and therapeutic molecules into the cell. 2514 Sep 14