Matches in UGent Biblio for { <https://biblio.ugent.be/publication/509692#aggregation> ?p ?o. }
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- aggregation classification "A1".
- aggregation creator B170118.
- aggregation creator B170119.
- aggregation creator B170120.
- aggregation creator B170121.
- aggregation creator B170122.
- aggregation creator B170123.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2008".
- aggregation format "application/pdf".
- aggregation hasFormat 509692.bibtex.
- aggregation hasFormat 509692.csv.
- aggregation hasFormat 509692.dc.
- aggregation hasFormat 509692.didl.
- aggregation hasFormat 509692.doc.
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- aggregation isPartOf urn:issn:1059-1524.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Two microtubule-associated proteins of Arabidopsis MAP65s promote antiparallel microtubule bundling".
- aggregation abstract "The Arabidopsis MAP65s are a protein family with similarity to the microtubule-associated proteins PRC1/Ase1p that accumulate in the spindle midzone during late anaphase in mammals and yeast, respectively. Here we investigate the molecular and functional properties of AtMAP65-5 and improve our understanding of AtMAP65-1 properties. We demonstrate that, in vitro, both proteins promote the formation of a planar network of antiparallel microtubules. In vivo, we show that AtMAP65-5 selectively binds the preprophase band and the prophase spindle microtubule during prophase, whereas AtMAP65-1-GFP selectively binds the preprophase band but does not accumulate at the prophase spindle microtubules that coexists within the same cell. At later stages of mitosis, AtMAP65-1 and AtMAP65-5 differentially label the late spindle and phragmoplast. We present evidence for a mode of action for both proteins that involves the binding of monomeric units to microtubules that "zipper up" antiparallel arranged microtubules through the homodimerization of the N-terminal halves when adjacent microtubules encounter.".
- aggregation authorList BK419209.
- aggregation endPage "4544".
- aggregation issue "10".
- aggregation startPage "4534".
- aggregation volume "19".
- aggregation aggregates 3067062.
- aggregation isDescribedBy 509692.
- aggregation similarTo mbc.E08-04-0341.
- aggregation similarTo LU-509692.