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FRET imaging of hemoglobin concentration in Plasmodium falciparum-infected red cellsTemperature transition of human hemoglobin at body temperature: effects of calcium.PfCHA is a mitochondrial divalent cation/H+ antiporter in Plasmodium falciparumEffects of deoxygenation on active and passive Ca2+ transport and on the cytoplasmic Ca2+ levels of sickle cell anemia red cells.Changes of intracellular Ca++ as measured by arsenazo III in relation to the K permeability of human erythrocyte ghostsEnergized endocytosis in human erythrocyte ghosts.The erythrocyte membrane abnormality of hereditary spherocytosis.Calcium in human red blood cells.Ion transport pathology in the mechanism of sickle cell dehydration.Spectrin plus band 4.1 cross-link actin. Regulation by micromolar calcium.EDTA aggregates induce SYPRO orange-based fluorescence in thermal shift assay.The erythrocyte ghost is a perfect osmometer.Passive Ca transport in human red blood cell ghosts measured with entrapped arsenazo III.Studies on the active transport of calcium in human red cells.Imaging ion flux and ion homeostasis in blood stage malaria parasites.Platelet-activating factor stimulates metabolism of phosphoinositides in horse platelets: possible relationship to Ca2+ mobilization during stimulation.The binding of calcium ions by erythrocytes and 'ghost' -cell membranes.The binding of calcium ions by human erythrocytes.Phenomenon of hot-cold hemolysis: chelator-induced lysis of sphingomyelinase-treated erythrocytes.Cross-linking of membrane proteins of metabolically-depleted and calcium-loaded erythrocytes.The use of ionophores of rapid loading of human red cells with radioactive cations for cation-pump studies.Red cell membrane injury in sickle cell anaemia.Activation of membrane-bound high-affinity calcium ion-sensitive adenosine triphosphatase of human erythrocytes by bivalent metal ions.Calcium and magnesium ATPases of the spectrin fraction of human erythrocytes.Studies on calcium transport and calcium-dependent adenosine triphosphatase activity of erythrocyte membranes in hereditary spherocytosis.Altered sodium permeability, calcium binding and Na-K-ATPase activity in the red blood cell membrane in essential hypertension.(Ca2++Mg2+)-ATPase activity of sickle cell membranes: decreased activation by red blood cell cytoplasmic activator.Red cell membrane protein phosphorylation in hemolytic anemias and muscular dystrophies.Selective loss of calcium permeability on maturation of reticulocytes.Sickle red cell calcium metabolism: studies on Ca2+-Mg2+ATPase and Ca-binding properties of sickle red cell membranes.Calcium, cell shrinkage, and prolytic state of human red blood cells.Erythrocyte calcium metabolism. Calcium exchange in normal and sickle-cell-anaemia erythrocytesThe kinetics of resealing of washed erythrocyte ghosts.The influx of calcium ions into human erythrocytes during cold storage. The influences of extracellular pH, intracellular adenosine triphosphate and efflux of univalent cationsThe influx of calcium ions into human erythrocytes during cold storage.Calcium binding by human erythrocyte membranes.Calcium ion-dependent p-nitrophenyl phosphate phosphatase activity and calcium ion-dependent adenosine triphosphatase activity from human erythrocyte membranesFunctional significance of the intermediate conductance Ca2+-activated K+ channel for the short-term survival of injured erythrocytes.Reconstitution of the Ca2+-transport system of human erythrocytes.Agglutinins from fish ova defining blood groups B and P.
P2860
Q21092165-9B83878C-D073-4BCF-B376-E4512446B363Q28365701-42E36F4F-7E2A-4A74-BE73-87ED3851C0CAQ30049303-BF36984B-ED28-4E1C-B15F-9D209EA7467FQ33908772-76950610-572F-4BF5-9636-FFA0B278236BQ34656607-F58183DD-CD86-488A-8E2F-1A2E4BC3BD53Q35193944-03D7C959-97B2-4143-B3F9-58E2DFE1F466Q35598649-A68852E0-0CD9-413D-9691-6A85F31A8C0DQ35811804-E0B5C0A9-AAA6-4895-9BA7-4AB0A897C244Q35993299-71BEBAD8-6370-436C-B01F-3561E7D38F08Q36201388-AF558FB1-12D6-4E4E-9CF7-A1032F5A185DQ36363131-DDDDC0C9-228F-40F3-B70D-70A6D92C3D6CQ36387381-8E34333E-D29D-46B9-BE6E-36E6A9140B82Q36408876-DCC30AE5-5B22-43D1-8F18-7177163773DFQ36428233-354414A2-3F82-4065-8515-8FFB5EB77456Q37511936-F56CC175-BA6D-4909-9C98-F90533226004Q37603754-0BBF6784-5171-46EA-B0FD-1DC18273A10DQ38362660-8E163FFC-09B0-4680-B41F-CA8C242A7EFAQ38362783-673FBD4D-2D69-4D61-9759-F6827F6E076DQ39063961-36D0AEE7-18F4-47D0-A8BD-9D96E53BFBF6Q39279967-98490016-11E3-4B53-8523-469A2E1A687FQ39387032-045506DB-DC07-4634-BC7B-A2C9294F3B01Q39620503-C7E90BF2-423E-47E2-83EE-7D71B469EE44Q39745511-88AD3D52-E7A2-42B7-A8B4-402D23CF7D2BQ39754856-806473D3-638C-4524-93ED-9B9CD22C2400Q39791509-D7938280-AA71-4787-9124-CAC83E44D6EFQ39842221-1E9E16E1-3B32-4E3F-88A3-2BDE823B35E9Q39911645-8662C2B2-ACB8-4B0F-9234-D67E278E9798Q40120027-73DD56EB-0A99-4914-87A6-4A4F3A31CEE0Q40690873-6BDE8039-9971-456E-B3CD-01FA8412F3AFQ41574285-93AA612A-B215-43EA-8843-0D48488B49E4Q41828630-0F18EB66-50BF-4A88-9E44-04788BC8A8C8Q41846079-704FC674-EE7A-4022-A167-D053647FB1D9Q41947346-5515E639-9E93-4CF9-B11F-73CB0EC9A18EQ42013295-02EEFFB7-A778-4950-89EF-747E58DEAA8EQ42146850-56E7577A-E022-48AD-A3D1-81B0667F3E13Q42273443-C0FAE4D5-1DF4-4E59-A9C7-5D040A7F92C1Q42558728-8051311F-620E-4AB7-BAF6-A0BD620CEED0Q42881600-7302EE95-4494-4B8F-A251-D26D66582025Q42882481-818A2E19-7681-4CD8-958E-FAF67D2C90ABQ43759091-2588B56A-96E3-4C00-971D-6BA32DB3AFB8
P2860
description
1968 nî lūn-bûn
@nan
1968年の論文
@ja
1968年学术文章
@wuu
1968年学术文章
@zh-cn
1968年学术文章
@zh-hans
1968年学术文章
@zh-my
1968年学术文章
@zh-sg
1968年學術文章
@yue
1968年學術文章
@zh
1968年學術文章
@zh-hant
name
The calcium content of human erythrocytes.
@en
The calcium content of human erythrocytes.
@nl
type
label
The calcium content of human erythrocytes.
@en
The calcium content of human erythrocytes.
@nl
prefLabel
The calcium content of human erythrocytes.
@en
The calcium content of human erythrocytes.
@nl
P1476
The calcium content of human erythrocytes.
@en
P2093
P304
P356
10.1113/JPHYSIOL.1968.SP008658
P407
P577
1968-12-01T00:00:00Z