About: A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses

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About: A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses Goto Sponge NotDistinct Permalink

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scientific journal article

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rdf:type	Item
description	artículu científicu espublizáu en 1989 (ast) vědecký článek publikovaný v roce 1989 (cs) 1989 թվականի մարտին հրատարակված գիտական հոդված (hy) наукова стаття, опублікована в березні 1989 (uk) 1989 թուականի Մարտին հրատարակուած գիտական յօդուած (hyw) article scientifique publié en 1989 (fr) scientific journal article (en) im März 1989 veröffentlichter wissenschaftlicher Artikel (de) vedecký článok (publikovaný 1989/03/10) (sk) مقالة علمية (نشرت في 10-3-1989) (ar) wetenschappelijk artikel (gepubliceerd op 1989/03/10) (nl)
publication date	wds:Q28633593-C459AFE6-C8E0-4858-A128-5FFD284F6530
publication date	1989-03-10 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28633593-0CE12BF8-E9FC-4287-BA83-2D453F6EB889
language of work or name	English
author name string	wds:Q28633593-1412F86C-40FC-4F09-BA0B-49054FDA906A wds:Q28633593-A595679F-495A-49EB-B4AF-5C344FF0DFF3 wds:Q28633593-B57058F8-FBE9-4FD5-A476-9E583351F97B
OpenCitations bibliographic resource ID	wds:Q28633593-30A61A74-892D-4F9D-B09D-1EE1FDC3ED47
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/1494522
author name string	J. T. Yang L. S. Goldstein R. A. Laymon
OpenCitations bibliographic resource ID	1494522
rdfs:label	A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses (en) A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses (nl) A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses (ast)
skos:prefLabel	A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses (en) A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses (nl) A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses (ast)
name	A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses (en) A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses (nl) A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses (ast)
title	wds:Q28633593-1E27EDFA-3D44-44DF-A96D-A124E147E303
title	A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses (en)
page(s)	wds:Q28633593-14E1AB3C-4BA4-4566-A235-A98E3DC79BFD
page(s)	879–889
instance of	wds:Q28633593-D7A1FEA4-0A5C-42BA-91EC-F66E9674C53D
instance of	scholarly article
main subject	wds:Q28633593-FEDF46DE-1D7D-4964-812C-64F67495FCE2
main subject	microtubule
PubMed ID	wds:Q28633593-83CF3182-7EC8-4529-9A87-97B4771F4CD3
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/2522352
PubMed ID	2522352
published in	wds:Q28633593-166653FB-950E-43C4-BEDC-1D97A6DA6F4C
published in	Cell
issue	wds:Q28633593-6DA61B50-C400-4969-900B-7E19A93496A9
volume	wds:Q28633593-1AF2B1CE-695B-47BD-82E3-52AE70D5924D
issue	5
volume	56
DOI	wds:Q28633593-EA16BB65-FF88-4218-8D9B-86CC34BB5374
DOI	http://dx.doi.org/10.1016/0092-8674(89)90692-2
DOI	10.1016/0092-8674(89)90692-2
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28633593
is cites work of	Three routes to suppression of the neurodegenerative phenotypes caused by kinesin heavy chain mutations Recombinant kinesin motor domain binds to beta-tubulin and decorates microtubules with a B surface lattice Kinesin heavy chain is essential for viability and neuromuscular functions in Drosophila, but mutants show no defects in mitosis Cell biology. Motoring in the spindle. Multiple kinesin motors coordinate cytoplasmic RNA transport on a subpopulation of microtubules in Xenopus oocytes Protrudin serves as an adaptor molecule that connects KIF5 and its cargoes in vesicular transport during process formation Patient mutations in doublecortin define a repeated tubulin-binding domain Molecular motors and their functions in plants Poleward microtubule flux mitotic spindles assembled in vitro The C. elegans unc-104 4 gene encodes a putative kinesin heavy chain-like protein Unstable kinetochore-microtubule capture and chromosomal instability following deletion of CENP-E Kinesin-like protein CHO1 is required for the formation of midbody matrix and the completion of cytokinesis in mammalian cells A new kinesin-like protein (Klp1) localized to a single microtubule of the Chlamydomonas flagellum Increased chromokinesin immunoreactivity in retinoblastoma cells Chromokinesin: a DNA-binding, kinesin-like nuclear protein Cytoplasmic microtubule-based motor proteins Identification of globular mechanochemical heads of kinesin. Dynein and kinesin share an overlapping microtubule-binding site β-COP, a 110 kd protein associated with non-clathrin-coated vesicles and the golgi complex, shows homology to β-adaptin Two activators of microtubule-based vesicle transport A cytoskeleton-related gene, uso1, is required for intracellular protein transport in Saccharomyces cerevisiae A plus-end-directed motor enzyme that moves antiparallel microtubules in vitro localizes to the interzone of mitotic spindles The neuron-specific kinesin superfamily protein KIF1A is a unique monomeric motor for anterograde axonal transport of synaptic vesicle precursors Cytoplasmic dynein is required for normal nuclear segregation in yeast KIF3A is a new microtubule-based anterograde motor in the nerve axon Direction of microtubule movement is an intrinsic property of the motor domains of kinesin heavy chain and Drosophila ncd protein Mediation of meiotic and early mitotic chromosome segregation in Drosophila by a protein related to kinesin Microtubule-based motor proteins Two kinesin light chain genes in mice. Identification and characterization of the encoded proteins Kinesin's processivity results from mechanical and chemical coordination between the ATP hydrolysis cycles of the two motor domains. The Kar3p kinesin-related protein forms a novel heterodimeric structure with its associated protein Cik1p Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins The Drosophila kinesin-like protein KLP3A is a midbody component required for central spindle assembly and initiation of cytokinesis Three-dimensional cryoelectron microscopy of dimeric kinesin and ncd motor domains on microtubules Primary structure of NuMA, an intranuclear protein that defines a novel pathway for segregation of proteins at mitosis Kinesin-related proteins required for assembly of the mitotic spindle Two Saccharomyces cerevisiae kinesin-related gene products required for mitotic spindle assembly Novel potential mitotic motor protein encoded by the fission yeast cut7+ gene Molecular structure and function of microtubule-associated proteins The primary structure of rat brain (cytoplasmic) dynein heavy chain, a cytoplasmic motor enzyme Drosophila cytoplasmic dynein, a microtubule motor that is asymmetrically localized in the oocyte Homer regulates the association of group 1 metabotropic glutamate receptors with multivalent complexes of homer-related, synaptic proteins CENP-E is a putative kinetochore motor that accumulates just before mitosis Cloning and localization of a conventional kinesin motor expressed exclusively in neurons Cloning and expression of a human kinesin heavy chain gene: interaction of the COOH-terminal domain with cytoplasmic microtubules in transfected CV-1 cells

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