About: Binding of myosin I to membrane lipids

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scientific article published in Nature

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rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) bài báo khoa học (vi) article publié dans la revue scientifique Nature (fr) scientific article published in Nature (en) im August 1989 veröffentlichter wissenschaftlicher Artikel (de) наукова стаття, опублікована в Nature в серпні 1989 (uk)
publication date	wds:Q59087389-4BB89FDE-A8E4-418D-92DF-A4009BDF0521
publication date	1989-08-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q59087389-7B05665A-C5D5-46F0-8707-1A23894A88EC
language of work or name	English
exact match	wds:Q59087389-9B8F0F67-D2DA-47F9-8E38-513CB0FD6074
exact match	https://scigraph.springernature.com/pub.10.1038/340565a0
cites work	wds:Q59087389-2C1156F4-7445-4618-B5BF-137937224644 wds:Q59087389-3F467082-3B87-4175-A71F-A7B5C0F1E5FA wds:Q59087389-548DBD81-DE17-4464-A80F-CE61D579A146 wds:Q59087389-57793B5A-6F1A-45DB-A22B-657A76DE72AB wds:Q59087389-5DB080DB-3159-4E38-B03E-6E818C0D512C wds:Q59087389-673C67FC-A548-42E4-BBFC-6ABD6DF06DC2 wds:Q59087389-67A3ED1A-A116-4AA9-B713-94B6BF938F86 wds:Q59087389-6DBCECE9-D40A-4CDF-8960-5FB14F7F8644 wds:Q59087389-8CEC02C3-98E8-44E9-83EF-19C3E1C626DB wds:Q59087389-946B8394-3EEB-481B-9016-078CABC360A2 wds:Q59087389-9C21CD95-D4F8-4257-98BF-681BF9C5260A wds:Q59087389-C0CD21EC-D119-4126-AF5A-C5F0218412BA wds:Q59087389-C43CBC87-5794-43E8-9D69-4220241BDAA2 wds:Q59087389-C73D26A8-E617-4A6A-86B9-DA6D49A07717 wds:Q59087389-CF8BC1AA-D240-4329-BBA6-983FD86D7406 wds:Q59087389-D10BD1C5-92D9-4B02-AF4A-8EC8444F4B2A wds:Q59087389-D342B054-4FD1-4DC0-A98C-38C4C60A1E1F wds:Q59087389-D3EB0663-AE9A-4F56-86D4-5179E56EFAD5 wds:Q59087389-D573D4EA-6BD4-4F48-98E7-E96F7B8BCB50 wds:Q59087389-E40356AA-F4F4-41EC-BA34-474E92AA1E6E wds:Q59087389-E6F2B951-EEF1-470A-B1B7-59554AA1C3D8 wds:Q59087389-FB30D9B7-7F5A-4AF8-9DED-FCE1C695175B
cites work	Cytoskeletal dynamics and nerve growth The heavy chain of Acanthamoeba myosin IB is a fusion of myosin-like and non-myosin-like sequences Modulation of cellular morphology and locomotory activity by antibodies against myosin 7 Preparation of myosin and its subfragments from rabbit skeletal muscle Structural and immunological characterization of the myosin-like 110-kD subunit of the intestinal microvillar 110K-calmodulin complex: evidence for discrete myosin head and calmodulin-binding domains Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 Organization of an actin filament-membrane complex. Filament polarity and membrane attachment in the microvilli of intestinal epithelial cells Antisense RNA inactivation of myosin heavy chain gene expression in Dictyostelium discoideum Disruption of the Dictyostelium myosin heavy chain gene by homologous recombination. Characterization of monoclonal antibodies to Acanthamoeba myosin-I that cross-react with both myosin-II and low molecular mass nuclear proteins A specific sorting signal is not required for the polarized secretion of newly synthesized proteins from cultured intestinal epithelial cells Purification of plasma membrane from Acanthamoeba castellanii Evidence for differential intracellular localization of the Acanthamoeba myosin isoenzymes A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding The labelling of proteins to high specific radioactivities by conjugation to a 125I-containing acylating agent. Application to the radioimmunoassay Neuronal cytomechanics: the actin-based motility of growth cones Propulsion of organelles isolated from Acanthamoeba along actin filaments by myosin-I. Selective solubilization of proteins from red blood cell membranes by protein perturbants. Myosins of nonmuscle cells Microinjection into Acanthamoeba castellanii of monoclonal antibodies to myosin-II slows but does not stop cell locomotion Plasma and phagosome membranes of Acanthamoeba castellanii. A membrane cytoskeleton from Dictyostelium discoideum. I. Identification and partial characterization of an actin-binding activity
author name string	wds:Q59087389-12D72FAD-43BD-4A83-89D0-CAA874F1D7E9
author name string	Adams RJ
rdfs:label	Binding of myosin I to membrane lipids (en) Binding of myosin I to membrane lipids (nl)
skos:prefLabel	Binding of myosin I to membrane lipids (en) Binding of myosin I to membrane lipids (nl)
name	Binding of myosin I to membrane lipids (en) Binding of myosin I to membrane lipids (nl)
author	wds:Q59087389-A76F0E02-A5E7-419C-9BED-EFD39277262B
author	Thomas D. Pollard
title	wds:Q59087389-B3C0AAB4-6929-4B08-86FA-971A5F644A25
title	Binding of myosin I to membrane lipids (en)
page(s)	wds:Q59087389-27FB134A-8276-4332-ABD2-C70B86C08C2C
page(s)	565-568
instance of	wds:Q59087389-19163AB6-BC81-4E47-B53E-3951F914EE80
instance of	scholarly article
main subject	wds:Q59087389-CC116C7D-5BEB-4C88-8EC0-2EECD71F8935
main subject	lipid
PubMed ID	wds:Q59087389-4EAB9C01-7005-45A3-BB43-277888CC3129
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/2770861
PubMed ID	2770861
published in	wds:Q59087389-CDF35398-67F1-4A8F-B326-91F562028BD3
published in	Nature
issue	wds:Q59087389-93426314-57E6-4A79-90AC-9261FC4D923D
volume	wds:Q59087389-A24FC0FA-6D17-4C53-A598-20F547643EE8
issue	6234
volume	340
DOI	wds:Q59087389-091F8D07-F410-475C-ABD4-452815D7B4DC
DOI	http://dx.doi.org/10.1038/340565A0
DOI	10.1038/340565A0
Dimensions Publication ID	wds:Q59087389-A7F513C1-F531-4B8B-BD5B-080629606195
Dimensions Publication ID	1015187510
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q59087389
is cites work of	The clutch hypothesis revisited: ascribing the roles of actin-associated proteins in filopodial protrusion in the nerve growth cone Casein kinase I is regulated by phosphatidylinositol 4,5-bisphosphate in native membranes Auxins and Cytokinins as Antipodal Modulators of Elasticity within the Actin Network of Plant Cells Phosphoinositide-binding peptides derived from the sequences of gelsolin and villin A Pleckstrin Homology Domain Specific for Phosphatidylinositol 4,5-Bisphosphate (PtdIns-4,5-P2) and Fused to Green Fluorescent Protein Identifies Plasma Membrane PtdIns-4,5-P2as Being Important in Exocytosis Actin and myosin I in the nucleus: what next? Relative distribution of actin, myosin I, and myosin II during the wound healing response of fibroblasts. Myosin I is located at the leading edges of locomoting Dictyostelium amoebae Myr 8, a novel unconventional myosin expressed during brain development associates with the protein phosphatase catalytic subunits 1alpha and 1gamma1

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