ncd Antibody

1. In vitro experiments using the drosophila kinesin-14, non-claret disjunctional (Ncd) show that the diffusive anchorage indeed impacts the force that kinesin-14 motors can generate between two microtubules and that modifications of the anchorage interfaces may act as a regulatory factor influencing the force generation by kinesin-14. PMID: 29880831
2. 14-3-3 translates a spatial cue provided by Aurora B to target Ncd selectively to the spindle within the large volume of oocytes. PMID: 28860275
3. Drosophila Ncd reveals an evolutionarily conserved powerstroke mechanism for homodimeric and heterodimeric kinesin-14s. PMID: 25941402
4. Mutation of an invariant residue in loop L7 of the central beta-sheet of the Drosophila kinesin-14 Ncd motor alters both nucleotide and microtubule binding, although the mutated residue is not present in either site. PMID: 23077560
5. Data suggest that the C-terminal residues of Ncd play an important role in modulating the interaction of the motor with the microtubule. PMID: 22449971
6. Ensemble averaging for each event category revealed that plus- and minus-directed strokes have different size and occur at different instants within the ncd-microtubules attachment sequence. PMID: 21156132
7. mutation of a single residue in the kinesin-14 Ncd causes the motor to release ADP and hydrolyze ATP faster than wild type PMID: 20602775
8. Stable neck-core interactions in ncd generate a binding geometry between motor & microtubule, placing motor ahead of cargo in the minus-end direction. After ATP uptake, the heads rearrange, promoting a swing of the neck in the minus-end direction. PMID: 12426369
9. results show that the nucleotide-binding site of kinesin-family motors closes when the motor.diphosphate complex binds to microtubules PMID: 12730601
10. Spindle assembly occurs in an ncd mutant, but interactions between microtubule-coated chromosomes are unstable; thus Ncd movement along microtubules is needed to stabilize interactions between chromosomes. PMID: 15797926
11. a bidirectional Drosophila Kinesin-14 motor that moves either to the microtubule plus or minus end in vitro unexpectedly causes only minor spindle defects in vivo PMID: 16190984
12. results show that the force-producing conformational change in Ncd occurs on ATP binding, as in other kinesins, but involves the swing of a lever-arm mechanical element similar to that described for myosins PMID: 16382238
13. These data demonstrate generation of sliding forces between adjacent microtubules by Ncd, and they confirm the proposed roles of kinesins-14 in the mitotic spindle morphogenesis. PMID: 17596520
14. Motility of a truncation series of Ncd and removal of the tubulin tail suggested that the Ncd tail serves as an electrostatic tether to microtubules. PMID: 18207739
15. The tail of ncd is essential for binding to spindles and centrosomes, but both the head and tail are needed for normal spindle assembly and function. PMID: 18957509
16. Results show that kinesin-14 causes sliding and expansion of anti-parallel microtubules by interactions through the motor domain on one side and the tail domain on the other, and that this accounts for the roles of kinesin-14 in spindle organization. PMID: 19430467

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KEGG: dme:Dmel_CG7831

STRING: 7227.FBpp0084900

UniGene: Dm.6668