About: The influence of electrochemical gradients of Na+ and K+ upon the membrane binding and pore forming activity of the terminal complement proteins

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: The influence of electrochemical gradients of Na+ and K+ upon the membrane binding and pore forming activity of the terminal complement proteins Goto Sponge NotDistinct Permalink

An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

scientific article published on 01 January 1984

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в січні 1984 (uk) im Januar 1984 veröffentlichter wissenschaftlicher Artikel (de) artikull shkencor i botuar më 01 janar 1984 (sq) scientific article published on 01 January 1984 (en) artículu científicu espublizáu en xineru de 1984 (ast)
publication date	wds:Q71330255-79B864D9-CF19-4F70-AB87-14C0BE91CAB5
publication date	1984-01-01 00:00:00Z (xsd:dateTime)
exact match	wds:Q71330255-88C2E53F-BC84-4030-AEA9-0CE54A3CDDDA
exact match	https://scigraph.springernature.com/pub.10.1007/bf01869204
cites work	wds:Q71330255-04F39D08-4C0C-4230-A298-1498815BCA96 wds:Q71330255-06DF9024-2745-46E1-A1CE-C5AFA606CE68 wds:Q71330255-286C4EC8-872E-4F1F-99FB-12674554798D wds:Q71330255-3E938BF5-6CB8-4624-99B0-95372F48D4AD wds:Q71330255-467474A7-7035-4367-86AE-B84CF1921061 wds:Q71330255-4F0EC4AC-1DC0-441E-987D-F96CFEE0762D wds:Q71330255-550882D0-655A-4855-98D9-D541DFB65E9A wds:Q71330255-662F3EC8-9F4E-4D18-BDE6-ECFA1E525FCD wds:Q71330255-6E9BE3A5-8B84-494A-BBB2-8F9235A5258F wds:Q71330255-6EFFD914-5C8E-45A1-AC2E-6BE14BE5CAF4 wds:Q71330255-76ED74E8-9F45-47A9-8278-620C86E203FB wds:Q71330255-776F0B1F-9155-4368-9E0B-1F17EF2B7D87 wds:Q71330255-7C1F9E3B-089B-4311-9F8B-C525491270F4 wds:Q71330255-8D18C904-3D42-43C8-8E4A-1DA47CCF51E1 wds:Q71330255-914AA461-DE74-478E-9AEE-E72DB2AC1D88 wds:Q71330255-999D38E6-40D1-494D-BCB7-DA82E309C145 wds:Q71330255-9C69B4EB-3EDB-4A11-B4C6-A67564147D6A wds:Q71330255-A0233AD3-E03F-491E-B93A-C9BA4886C317 wds:Q71330255-A327DD84-9379-441D-9771-E52FD151264F wds:Q71330255-A70C32EA-0204-4AB6-B706-6A0114C3DC94 wds:Q71330255-B720B852-CE04-4D6D-A35D-1269C6147FD9 wds:Q71330255-B9FC3A37-B017-4891-9CC0-69E6611B942A wds:Q71330255-BD11D218-B6D2-479D-92E8-E7F4E29F9AC9 wds:Q71330255-D0533B98-5934-4CFA-97C4-5959FD438AE4 wds:Q71330255-D1D8EF88-ED45-41A8-B6CE-7545D3BFF559 wds:Q71330255-E0C3FF38-16CA-4ED8-9A34-67E4964AACEE wds:Q71330255-E6E872AE-D7C0-4315-B548-D3E311B11430 wds:Q71330255-E7F0AFF2-CC53-42BB-8B72-924CFA124168 wds:Q71330255-E940D721-F185-48D0-B47C-D1C02419B246 wds:Q71330255-EFA8EDF5-9F53-4731-BA84-17027EBEB561 wds:Q71330255-F9692258-19F7-40A7-9303-8068FE140EBA wds:Q71330255-FC5B2746-CF1B-4C69-B54F-338CEEB823B1
cites work	Chloride transport in human erythrocytes and ghosts: a quantitative comparison Determination of membrane potentials in human and Amphiuma red blood cells by means of fluorescent probe Formation of transmembrane tubules by spontaneous polymerization of the hydrophilic complement protein C9 POTENTIAL, IMPEDANCE, AND RECTIFICATION IN MEMBRANES Molecular organization of C9 within the membrane attack complex of complement. Induction of circular C9 polymerization by the C5b-8 assembly Studies on the mechanism by which cyanine dyes measure membrane potential in red blood cells and phosphatidylcholine vesicles. Immunological and physiological characteristics of the rapid immune hemolysis of neuraminidase-treated sheep red cells produced by fresh guinea pig serum The modifications of the final stages of the complement reaction by alkali metal cations Role of intracellular and extracellular cationic composition in immune lysis of mammalian erythrocytes Effect of the cationic environment on immune haemolysis of high potassium and low potassium sheep erythrocytes Increased ion permeability of planar lipid bilayer membranes after treatment with the C5b-9 cytolytic attack mechanism of complement Molecular reorganization of lipid bilayers by complement: a possible mechanism for membranolysis Mechanism of cytolysis by complement Studies on the cation permeability of human red cell ghosts. Characterization and biological significance of two membrane sites with high affinities for Ca A quantitative estimate of the non-exchange-restricted chloride permeability of the human red cell Permeability characteristics of complement-damaged membranes: evaluation of the membrane leak generated by the complement proteins C5b-9. Assembly of the functional membrane attack complex of human complement: formation of disulfide-linked C9 dimers Analysis of the colloid osmotic step of complement-mediated immune hemolysis. Mode of action of human C9: adsorption of multiple C9 molecules to cell-bound C8 Analysis of solute diffusion across the C5b-9 membrane lesion of complement: evidence that individual C5b-9 complexes do not function as discrete, uniform pores. Preparation and properties of human erythrocyte ghosts Studies on the terminal stages of immune hemolysis. V. Evidence that not all complement-produced transmembrane channels are equal The action of antibody and complement on mammalian cells Mechanism of complement-induced cell lysis. Demonstration of a three-step mechanism of EAC1-8 cell lysis by C9 and of a non-osmotic swelling of erythrocytes Transmembrane channel formation by complement: functional analysis of the number of C5b6, C7, C8, and C9 molecules required for a single channel Immune hemolysis. I. Differing susceptibility of three genetic types of sheep red cells Steady-state analysis of tracer exchange across the C5b-9 complement lesion in a biological membrane Lesions of different functional size produced by human and guinea pig complement in sheep red cell membranes. Complement pores in erythrocyte membranes. Analysis of C8/C9 binding required for functional membrane damage Unmasking of a potassium leak in resealed human red blood cell ghosts Erythrocyte surface antigens and cation transport Determination of the number of lytic sites in biconcave and spheroid erythrocyte ghosts after complement lysis
author name string	wds:Q71330255-281B6C8F-F197-4A61-A2A3-21F501F6BBC5 wds:Q71330255-8AEB9186-33D8-4D7B-B1D5-5CFCD308C984
author name string	P J Sims T Wiedmer
rdfs:label	The influence of electrochemical gradients of Na+ and K+ upon the membrane binding and pore forming activity of the terminal complement proteins (en) The influence of electrochemical gradients of Na+ and K+ upon the membrane binding and pore forming activity of the terminal complement proteins (nl)
skos:prefLabel	The influence of electrochemical gradients of Na+ and K+ upon the membrane binding and pore forming activity of the terminal complement proteins (en) The influence of electrochemical gradients of Na+ and K+ upon the membrane binding and pore forming activity of the terminal complement proteins (nl)
name	The influence of electrochemical gradients of Na+ and K+ upon the membrane binding and pore forming activity of the terminal complement proteins (en) The influence of electrochemical gradients of Na+ and K+ upon the membrane binding and pore forming activity of the terminal complement proteins (nl)
title	wds:Q71330255-B02F90C7-971D-4C11-99A8-0A2900BFEF00
title	The influence of electrochemical gradients of Na+ and K+ upon the membrane binding and pore forming activity of the terminal complement proteins (en)
page(s)	wds:Q71330255-6F9A58DF-9303-433A-BEAE-0E972E333972
page(s)	169-176
instance of	wds:Q71330255-E76205E5-C2D0-462C-BD70-3DA076D7F4AB
instance of	scholarly article
PubMed ID	wds:Q71330255-3C616968-3572-44F0-929B-30ADA2475A03
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/6716452
PubMed ID	6716452
published in	wds:Q71330255-F75F6373-1FCE-4D3A-8821-35CF4BB6F7EF
published in	Journal of Membrane Biology
issue	wds:Q71330255-F4FA8389-EBE0-4C40-8FC8-05558138E7CD
volume	wds:Q71330255-4909F870-783F-4B42-9F2C-9B847023B339
issue	2
volume	78

Faceted Search & Find service v1.16.117 as of May 05 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3239 as of May 5 2024, on Linux (x86_64-centos_6-linux-gnu), Single-Server Edition (378 GB total memory, 194 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software