About: Erythrocyte membrane sidedness in lectin control of the Ca2+-A23187-mediated diskocyte goes to and comes from echinocyte conversion

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About: Erythrocyte membrane sidedness in lectin control of the Ca2+-A23187-mediated diskocyte goes to and comes from echinocyte conversion Goto Sponge NotDistinct Permalink

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scientific article published on 01 July 1981

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в липні 1981 (uk) article scientifique publié en 1981 (fr) im Juli 1981 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en xunetu de 1981 (ast) scientific article published on 01 July 1981 (en)
publication date	wds:Q71554197-9892A980-9766-4591-B1F3-ABB98F746485
publication date	1981-07-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q71554197-5F852309-5622-4258-B4B5-185249D71F73
language of work or name	English
exact match	wds:Q71554197-E06D2949-84D5-4F2A-AF6E-FD235230C6BE
exact match	https://scigraph.springernature.com/pub.10.1038/292158a0
cites work	wds:Q71554197-09674304-8DC2-4923-A27D-F032383C77E8 wds:Q71554197-15403A00-E138-4D7C-93C4-7C87D526342E wds:Q71554197-1891B78A-F6B4-4159-8DF2-294801048D69 wds:Q71554197-18D60E74-F161-4C8B-A706-001A9BE61440 wds:Q71554197-21B27394-87AE-491A-BD08-47E59C741440 wds:Q71554197-227CAC1F-2579-47F8-A5CD-A20A350D4C26 wds:Q71554197-23E6C0B7-3569-4386-9786-B99BD824EFD7 wds:Q71554197-27179F51-4EC8-4937-96AE-871D330E0CAC wds:Q71554197-28A64652-F00D-40E2-AFDE-A5AC446545A6 wds:Q71554197-3155886E-67B0-48B9-88A1-098A31DCB860 wds:Q71554197-3EE02084-0C16-4D9E-8D29-94CC67C05CA7 wds:Q71554197-4C03BA70-E95D-4D6A-9A57-1916E116009F wds:Q71554197-4FF14824-D688-43BF-B4DF-645537D62BB4 wds:Q71554197-5FBA0655-1AD6-4D2F-AD5D-6299C1FD0BFF wds:Q71554197-68B7E843-5572-4447-A2A9-F5517BD9B57F wds:Q71554197-7F6C8D91-B845-4123-B8B8-E23D3A706274 wds:Q71554197-83793136-D240-49AB-97EF-686E0211C4E4 wds:Q71554197-8B766ACD-E3F9-4943-B26F-B784DC713F97 wds:Q71554197-935990C4-1E3D-4134-8A8C-0F8C54717A97 wds:Q71554197-A16EDD84-CF40-4845-9F1D-3304A035717A wds:Q71554197-DB6A4E7E-4EBA-40BC-84F6-02CE084B16B2 wds:Q71554197-F1D436E9-F67B-4466-A543-FA3287C5F446 wds:Q71554197-FBC99B64-0DC4-49B1-B1FD-E3222746B2FC
cites work	The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes Metabolic dependence of red cell deformability Formation of γ-glutamyl-ε-lysine bridges between membrane proteins by a Ca2+-regulated enzyme in intact erythrocytes On the mechanism of ATP-induced shape changes in human erythrocyte membranes. I. The role of the spectrin complex Intramembrane particle aggregation in erythrocyte ghosts. I. The effects of protein removal Release of diacylglycerol-enriched vesicles from erythrocytes with increased intracellular [Ca2+] Stoichiometry of wheat germ agglutinin as a morphology controlling agent and as a morphology controlling agent and as a morphology protective agent for the human erythrocyte Calcium ion-dependent diacylglycerol accumulation in erythrocytes is associated with microvesiculation but not with efflux of potassium ions Purification of two spectrin-binding proteins: biochemical and electron microscopic evidence for site-specific reassociation between spectrin and bands 2.1 and 4.1 Crystallographic elucidation of the saccharide binding mode in wheat germ agglutinin and its biological significance Clustering and endocytosis of membrane receptors can be induced in mature erythrocytes of neonatal but not adult humans Band 3-glycophorin A association in erythrocyte membranes demonstrated by combining protein diffusion measurements with antibody-induced cross-linking On the mechanism of ATP-induced shape changes in the human erythrocyte membranes: the role of ATP Enzymic basis for the Ca2+ion-induced crosslinking of membrane proteins in intact human erythrocytes Polymerisation of red cell membrane protein contributes to spheroechinocyte shape irreversibility Control of interaction of spectrin and actin by phosphorylation Clarification of role of ATP in red-cell morphology and function The effect of calcium ionophore A23187 on the ATP level of human erythrocytes Use of ionophore A23187 to measure cytoplasmic Ca buffering and activation of the Ca pump by internal Ca The effects of ionophore A23187 on erythrocytes. Relationship of atp and 2,3-diphosphoglycerate to calcium-binding capacity Properties of the human erythrocyte membrane receptors for peanut and Dolichos biflorus lectins Phosphorylation and dephosphorylation reactions by erythrocyte plasma membrane enzymes Receptor distribution and the mechanism of enhanced erythrocyte agglutination by soybean agglutinin
author name string	wds:Q71554197-1864CBAC-D4CC-4633-9042-74BF1431F73F
author name string	R E Lovrien
rdfs:label	Erythrocyte membrane sidedness in lectin control of the Ca2+-A23187-mediated diskocyte goes to and comes from echinocyte conversion (en) Erythrocyte membrane sidedness in lectin control of the Ca2+-A23187-mediated diskocyte goes to and comes from echinocyte conversion (nl)
skos:prefLabel	Erythrocyte membrane sidedness in lectin control of the Ca2+-A23187-mediated diskocyte goes to and comes from echinocyte conversion (en) Erythrocyte membrane sidedness in lectin control of the Ca2+-A23187-mediated diskocyte goes to and comes from echinocyte conversion (nl)
name	Erythrocyte membrane sidedness in lectin control of the Ca2+-A23187-mediated diskocyte goes to and comes from echinocyte conversion (en) Erythrocyte membrane sidedness in lectin control of the Ca2+-A23187-mediated diskocyte goes to and comes from echinocyte conversion (nl)
author	wds:Q71554197-1128C79C-19F8-4FEE-8636-20298BD0F38D
author	Richard A. Anderson
title	wds:Q71554197-8E5CBFB8-3E66-454F-A907-F691431DF43F
title	Erythrocyte membrane sidedness in lectin control of the Ca2+-A23187-mediated diskocyte goes to and comes from echinocyte conversion (en)
page(s)	wds:Q71554197-BE62D778-9163-49A5-80A8-DFD8E0E8FC30
page(s)	158-161
instance of	wds:Q71554197-93F89BB3-E81C-4D8A-A1CB-754AFF76275F
instance of	scholarly article
main subject	wds:Q71554197-80B3002E-4C5D-4B9D-AC7E-808744E60D73
main subject	echinocyte
PubMed ID	wds:Q71554197-93EC1740-067B-4F93-9592-46208A932481
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/6787435
PubMed ID	6787435
published in	wds:Q71554197-51FAFB61-A12F-40AA-BCE5-12947B902270
published in	Nature
issue	wds:Q71554197-28FA2F56-46DC-4707-9598-83E4140029E6
volume	wds:Q71554197-5452746A-1137-4A8D-BD3E-CACA6E818DAA
issue	5819
volume	292
DOI	wds:Q71554197-2F94A2D6-01E6-4B05-B57B-7836E2CDE6C1
DOI	http://dx.doi.org/10.1038/292158A0
DOI	10.1038/292158A0
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q71554197
is cites work of	Effect of wheat germ agglutinin on the viscoelastic properties of erythrocyte membrane Regulation of the association of membrane skeletal protein 4.1 with glycophorin by a polyphosphoinositide Clinical disorders of the red cell membrane skeleton Erythrocyte membrane rigidity induced by glycophorin A-ligand interaction. Evidence for a ligand-induced association between glycophorin A and skeletal proteins Interactions between membrane skeleton proteins and the intrinsic domain of the erythrocyte membrane Control of erythrocyte shape by calmodulin Concanavalin A binding to human erythrocytes leads to alterations in properties of the membrane skeleton Concanavalin A-agglutinability of membrane-skeleton-free vesicles and aged cellular remnants derived from human erythrocytes. Is the membrane skeleton required for agglutination? Role of membrane integral proteins in the modulation of red cell shape by albumin, dinitrophenol and the glass effect A comparison of wheat germ agglutinin binding between normal and sickle red blood cells

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