Modulation of erythrocyte membrane material properties by Ca2+ and calmodulin. Implications for their role in regulation of skeletal protein interactions.
about
Ca(2+)-dependent and Ca(2+)-independent calmodulin binding sites in erythrocyte protein 4.1. Implications for regulation of protein 4.1 interactions with transmembrane proteinsA new function for adducin. Calcium/calmodulin-regulated capping of the barbed ends of actin filamentsMultiple protein 4.1 isoforms produced by alternative splicing in human erythroid cellsFunction, expression and localization of annexin A7 in platelets and red blood cells: insights derived from an annexin A7 mutant mouseSpin-labeling studies of the conformation of the Ca(2+)-regulatory protein calmodulin in solution and bound to the membrane skeleton in erythrocyte ghosts: implications to transmembrane signaling.Identification of a functional role for lipid asymmetry in biological membranes: Phosphatidylserine-skeletal protein interactions modulate membrane stabilityIn vivo shear flow and erythrocyte membrane fluidity in hypertensive patients.Characterization of cytoskeletal protein 4.1R interaction with NHE1 (Na(+)/H(+) exchanger isoform 1).Identification of signalling cascades involved in red blood cell shrinkage and vesiculation.Role of C-Peptide in the regulation of microvascular blood flow.The influence of membrane physical properties on microvesicle release in human erythrocytes.Phosphatidylserine externalization and procoagulant activation of erythrocytes induced by Pseudomonas aeruginosa virulence factor pyocyanin.Cytoskeletal and membrane remodelling during malaria parasite invasion of the human erythrocyte.Computational Biomechanics of Human Red Blood Cells in Hematological Disorders.Shedding of phosphatidylserine from developing erythroid cells involves microtubule depolymerization and affects membrane lipid composition.Curling and local shape changes of red blood cell membranes driven by cytoskeletal reorganization.Structural stabilization of protein 4.1R FERM domain upon binding to apo-calmodulin: novel insights into the biological significance of the calcium-independent binding of calmodulin to protein 4.1R.Oxidative stress and rheologic properties of stored red blood cells before and after transfusion to surgical patients.Effect of anandamide on erythrocyte survival.Epoetin beta pegol for treatment of anemia ameliorates deterioration of erythrocyte quality associated with chronic kidney disease.P. falciparum RH5-Basigin interaction induces changes in the cytoskeleton of the host RBC.The osmotic resistance, and zeta potential responses of human erythrocytes to transmembrane modification of Ca2+ fluxes in the presence of the imposed low rate radiation field of 90Sr.The degree of resistance of erythrocyte membrane cytoskeletal proteins to supra-physiologic concentrations of calcium: an in vitro study.
P2860
Q22253239-C4DED2D7-2CA7-475F-A1D5-488C14E524C8Q24309448-C830639A-5408-4672-BF9F-429935249B00Q24644272-2B8B2157-A22F-4C31-80B8-EB8F95C2C3E4Q24799802-9D081FB8-3576-47F3-AB95-302DBFBC6CE6Q30333800-E3397C02-71F7-4503-93A7-E1F17A31A8F2Q34011716-454E8830-43E1-43A2-B4DF-370D688D0649Q34345641-4CF358D6-9D0E-487B-844F-E2978414899FQ35114547-E45E37A4-2DCB-40F3-B254-BAF46639FB41Q35574674-B718705F-C81C-4325-B6A8-929DBE07E2D2Q37231760-BCC84CF9-6DE1-4F09-B82B-4421B6635559Q37337742-0551F8CC-4F4A-41E1-B9AB-41A3EADD2482Q37446009-76503B11-56F8-418C-9C7F-B7BC215E08A2Q37896123-23A34FA7-63E6-4817-81C3-4CBD681A06A9Q38998761-D4322A8E-1D6F-4162-9B60-FFAC10A09454Q39309339-9767273A-91DB-4921-8B31-FA0596E2E7B0Q41985271-8F8140C6-1CFA-4763-98DA-1F00ED615B5EQ46269790-1F8A88B3-4EEE-4E26-85F6-7DAB859257EEQ46603024-255B9137-D0BC-4AAA-8A99-B2600B051E12Q46920562-3F095AF5-E100-424E-8754-7EF6550A76C0Q48157066-282DDF65-5A38-4C21-B1FA-709CC4C70D79Q48274383-50A968E3-905B-4D36-832B-FD5607F8791FQ50463786-C0303963-BA44-4084-B734-D5FDDB67F5E2Q52651096-D2218675-72EF-4E2A-9745-32A23CE0B990
P2860
Modulation of erythrocyte membrane material properties by Ca2+ and calmodulin. Implications for their role in regulation of skeletal protein interactions.
description
1988 nî lūn-bûn
@nan
1988 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
name
Modulation of erythrocyte memb ...... skeletal protein interactions.
@ast
Modulation of erythrocyte memb ...... skeletal protein interactions.
@en
Modulation of erythrocyte memb ...... skeletal protein interactions.
@nl
type
label
Modulation of erythrocyte memb ...... skeletal protein interactions.
@ast
Modulation of erythrocyte memb ...... skeletal protein interactions.
@en
Modulation of erythrocyte memb ...... skeletal protein interactions.
@nl
prefLabel
Modulation of erythrocyte memb ...... skeletal protein interactions.
@ast
Modulation of erythrocyte memb ...... skeletal protein interactions.
@en
Modulation of erythrocyte memb ...... skeletal protein interactions.
@nl
P2860
P356
P1476
Modulation of erythrocyte memb ...... skeletal protein interactions.
@en
P2093
N Mohandas
Y Takakuwa
P2860
P304
P356
10.1172/JCI113611
P407
P577
1988-08-01T00:00:00Z