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Human erythrocyte protein 4.1 is a phosphatidylserine binding protein.
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/jcb.240190209openalex-snapshot
Transbilayer movement of various phosphatidylcholine species in intact human erythrocytes
inferredcites →https://doi.org/10.1006/abio.1976.9999openalex-snapshot
A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding
inferredcites →https://doi.org/10.1016/0003-2697(76)90528-5openalex-snapshot
Preparation of cytochrome c2 from Rhodospirillum rubrum
inferredcites →https://doi.org/10.1016/0003-9861(63)90042-0openalex-snapshot
The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes
inferredcites →https://doi.org/10.1016/0005-2736(76)90199-1openalex-snapshot
Possible relationship between membrane proteins and phospholipid asymmetry in the human erythrocyte membrane
inferredcites →https://doi.org/10.1016/0005-2736(78)90004-4openalex-snapshot
Spectrin as a stabilizer of the phospholipid asymmetry in the human erythrocyte membrane
inferredcites →https://doi.org/10.1016/0005-2736(79)90085-3openalex-snapshot
Preparation of liposomes of defined size distribution by extrusion through polycarbonate membranes
inferredcites →https://doi.org/10.1016/0005-2736(80)90390-9openalex-snapshot
Spectrin-phospholipid interaction
inferredcites →https://doi.org/10.1016/0005-2736(80)90558-1openalex-snapshot
Preparation of unilamellar liposomes of intermediate size (0.1–0.2 μm) by a combination of reverse phase evaporation and extrusion through polycarbonate membranes
inferredcites →https://doi.org/10.1016/0005-2736(89)90005-9openalex-snapshot
The interaction of spectrin-actin and synthetic phospholipids. II. The interaction with phosphatidylserine
inferredcites →https://doi.org/10.1016/0014-5793(85)80644-xopenalex-snapshot
The phospholipid organisation in the membranes of McLeod and Leach phenotype erythrocytes
inferredcites →https://doi.org/10.1016/0076-6879(74)31019-1openalex-snapshot
[16] Preparation of impermeable ghosts and inside-out vesicles from human erythrocyte membranes
inferredcites →https://doi.org/10.1016/0092-8674(82)90277-xopenalex-snapshot
Involvement of spectrin in the maintenance of phase-state asymmetry in the erythrocyte membrane
inferredcites →https://doi.org/10.1016/0304-4157(82)90001-6openalex-snapshot
Interactions between membrane skeleton proteins and the intrinsic domain of the erythrocyte membrane
inferredcites →https://doi.org/10.1016/s0021-9258(18)43680-0openalex-snapshot
Associations of erythrocyte membrane proteins. Binding of purified bands 2.1 and 4.1 to spectrin.
inferredcites →https://doi.org/10.1016/s0021-9258(18)43756-8openalex-snapshot
Association between ankyrin and the cytoplasmic domain of band 3 isolated from the human erythrocyte membrane.
inferredcites →https://doi.org/10.1016/s0021-9258(18)61794-6openalex-snapshot
Glycoproteins of Cell Surfaces
inferredcites →https://doi.org/10.1016/s0021-9258(18)70226-3openalex-snapshot
Phosphorus Assay in Column Chromatography
inferredcites →https://doi.org/10.1016/s0021-9258(19)83676-1openalex-snapshot
Interactions between protein 4.1 and band 3. An alternative binding site for an element of the membrane skeleton.
inferredcites →https://doi.org/10.1016/s0021-9258(20)82083-3openalex-snapshot
Accelerated transbilayer movement of phosphatidylcholine in sickled erythrocytes. A reversible process.
inferredcites →https://doi.org/10.1016/s0022-2275(20)39314-7openalex-snapshot
Improved procedure for the extraction of lipids from human erythrocytes
inferredcites →https://doi.org/10.1021/bi00320a029openalex-snapshot
Biochemical characterization of complex formation by human erythrocyte spectrin, protein 4.1, and actin
inferredcites →https://doi.org/10.1021/bi00341a019openalex-snapshot
Incorporation and translocation of aminophospholipids in human erythrocytes
inferredcites →https://doi.org/10.1021/bi00567a011openalex-snapshot
Studies on the mechanism of membrane fusion: kinetics of calcium ion induced fusion of phosphatidylserine vesicles followed by a new assay for mixing of aqueous vesicle contents
inferredcites →https://doi.org/10.1038/227680a0openalex-snapshot
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
inferredcites →https://doi.org/10.1038/307655a0openalex-snapshot
Glycophorin is linked by band 4.1 protein to the human erythrocyte membrane skeleton
inferredcites →https://doi.org/10.1042/bj1330529openalex-snapshot
The labelling of proteins to high specific radioactivities by conjugation to a 125I-containing acylating agent. Application to the radioimmunoassay
inferredcites →https://doi.org/10.1042/bj2180615openalex-snapshot
Two individuals with elliptocytic red cells apparently lack three minor erythrocyte membrane sialoglycoproteins
inferredcites →https://doi.org/10.1042/bj2240285openalex-snapshot
Lipid organization in erythrocyte membrane microvesicles
inferredcites →https://doi.org/10.1073/pnas.75.9.4194openalex-snapshot
Procedure for preparation of liposomes with large internal aqueous space and high capture by reverse-phase evaporation.
inferredcites →https://doi.org/10.1073/pnas.76.9.4350openalex-snapshot
Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.
inferredcites →https://doi.org/10.1073/pnas.81.12.3751openalex-snapshot
ATP-dependent asymmetric distribution of spin-labeled phospholipids in the erythrocyte membrane: relation to shape changes.
inferredcites →https://doi.org/10.1073/pnas.81.14.4404openalex-snapshot
Protein 4.1: its association with the human erythrocyte membrane.
inferredcites →https://doi.org/10.1083/jcb.62.1.1openalex-snapshot
THE ORGANIZATION OF PROTEINS IN THE HUMAN RED BLOOD CELL MEMBRANE
inferredcites →https://doi.org/10.1111/j.1432-1033.1983.tb07111.xopenalex-snapshot
Interaction of a Peripheral Protein of the Erythrocyte Membrane, Band 4.1, with Phosphatidylserine‐Containing Liposomes and Erythrocyte Inside‐Out Vesicles
inferredcites →https://doi.org/10.1146/annurev.bi.48.070179.000403openalex-snapshot
Lipid Asymmetry in Membranes
inferredcites →https://doi.org/10.1159/000350087openalex-snapshot
Short-Term Effects of Nose-Only Cigarette Smoke Exposure on Glutathione Redox Homeostasis, Cytochrome P450 1A1/2 and Respiratory Enzyme Activities in Mice Tissues
inferredcites →https://doi.org/10.1172/jci110200openalex-snapshot
Abnormalities in membrane phospholipid organization in sickled erythrocytes.
inferredcites →https://doi.org/10.1182/blood.v69.2.618.618openalex-snapshot
Structural polymorphism of glycophorins demonstrated by immunoblotting techniques
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.5281/zenodo.886948openalex-extracted
Calmodulin-Protein 4.1R Rendez-Vous: Chaperon-Like Function For Calmodulin And Protein 4.1R In Erythrocytes
inferred← citeshttps://doi.org/10.1002/ajh.2830290404openalex-snapshot
Impaired echinocytic transformation of ankyrin‐ and spectrin‐deficient erythrocytes in mice
inferred← citeshttps://doi.org/10.1002/ajh.2830340306openalex-snapshot
Excess of red cell membrane proteins in hereditary high‐phosphatidylcholine hemolytic anemia
inferred← citeshttps://doi.org/10.1002/med.10009openalex-snapshot
Chemical control of phospholipid distribution across bilayer membranes
inferred← citeshttps://doi.org/10.1006/bcmd.2002.0562openalex-snapshot
Alterations in Skeletal Protein, Distribution of PKCα, and Level of Phospholipids in Erythrocyte Membranes of Women with Primary Breast Cancer
inferred← citeshttps://doi.org/10.1007/978-1-4612-3230-8_5openalex-snapshot
The Role of Oxidation in Diseases of the Human Erythrocyte
inferred← citeshttps://doi.org/10.1007/978-1-4757-9528-8_15openalex-snapshot
Erythrocyte Membrane Damage in Hemolytic Anemias
inferred← citeshttps://doi.org/10.1007/978-3-642-61126-1_29openalex-snapshot
Phospholipid Flippases: Neither Exclusively, Nor Only Involved In Maintaining Membrane Phospholipid Asymmetry
inferred← citeshttps://doi.org/10.1007/978-3-642-74415-0_7openalex-snapshot
Changes in the Structure and Function of the Red Cell Membrane Skeleton and Hemolytic Anemias
inferred← citeshttps://doi.org/10.1007/978-3-642-85789-8_4openalex-snapshot
Membrane Processes in Human Red Cell Aging
inferred← citeshttps://doi.org/10.1007/978-3-662-02922-0_18openalex-snapshot
Anti-Phosphatidylserine Monoclonal Antibody: Structural Template for Studying Lipid-Protein Interactions and for Identificationo of Phosphatidylserine Binding Proteins
inferred← citeshttps://doi.org/10.1007/bf01774032openalex-snapshot
Actin binding proteins — lipid interactions
inferred← citeshttps://doi.org/10.1007/bf02535574openalex-snapshot
Zinc deficiency in the rat alters the lipid composition of the erythrocyte membrane triton shell
inferred← citeshttps://doi.org/10.1007/s10237-020-01302-xopenalex-snapshot
Vital erythrocyte phenomena: what can theory, modeling, and simulation offer?
inferred← citeshttps://doi.org/10.1016/0003-9861(89)90168-9openalex-snapshot
Effect of oxidative stress on membrane phospholipid and protein organization in human erythrocytes
inferred← citeshttps://doi.org/10.1016/0003-9861(91)90352-jopenalex-snapshot
Effect of 2,3-diphosphoglycerate on the phosphorylation of protein 4.1 by protein kinase C
inferred← citeshttps://doi.org/10.1016/0005-2736(89)90093-xopenalex-snapshot
Involvement of ATP-dependent aminophospholipid translocation in maintaining phospholipid asymmetry in diamide-treated human erythrocytes
inferred← citeshttps://doi.org/10.1016/0005-2736(89)90121-1openalex-snapshot
Aminophospholipid translocase in the plasma membrane of Friend erythroleukemic cells can induce an asymmetric topology for phosphatidylserine but not for phosphatidylethanolamine
inferred← citeshttps://doi.org/10.1016/0005-2736(89)90236-8openalex-snapshot
Interaction between phosphatidylserine and the isolated cytoskeleton of human blood platelets
inferred← citeshttps://doi.org/10.1016/0005-2736(90)90010-lopenalex-snapshot
Membrane skeleton-bilayer interaction is not the major determinant of membrane phospholipid asymmetry in human erythrocytes
inferred← citeshttps://doi.org/10.1016/0005-2736(90)90058-vopenalex-snapshot
Loss of membrane phospholipid asymmetry in platelets and red cells may be associated with calcium-induced shedding of plasma membrane and inhibition of aminophospholipid translocase
inferred← citeshttps://doi.org/10.1016/0005-2736(90)90303-6openalex-snapshot
Heat-induced alterations in monkey erythrocyte membrane phospholipid organization and skeletal protein structure and interactions
inferred← citeshttps://doi.org/10.1016/0005-2736(92)90100-zopenalex-snapshot
Phospholipid asymmetry during erythrocyte deformation: maintenance of the unit membrane
inferred← citeshttps://doi.org/10.1016/0005-2736(93)90308-mopenalex-snapshot
Release of protein 4.1-rich vesicles from diamide-treated erythrocytes under hydrostatic pressure
inferred← citeshttps://doi.org/10.1016/0005-2736(94)90257-7openalex-snapshot
Effects of chemical modification of membrane thiol groups on hemolysis of human erythrocytes under hydrostatic pressure
inferred← citeshttps://doi.org/10.1016/0005-2736(94)90268-2openalex-snapshot
Calcium-induced transbilayer scrambling of fluorescent phospholipid analogs in platelets and erythrocytes
inferred← citeshttps://doi.org/10.1016/0006-2952(92)90370-xopenalex-snapshot
Effects of snake venom phospholipase A2 toxins (β-bungarotoxin, notexin) and enzymes (Naja naja atra, Naja nigricollis) on aminophospholipid asymmetry in rat cerebrocortical synaptosomes
inferred← citeshttps://doi.org/10.1016/0047-6374(91)90050-aopenalex-snapshot
Evidence for membrane protein oxidation during in vivo aging of human erythrocytes
inferred← citeshttps://doi.org/10.1016/0098-2997(90)90001-iopenalex-snapshot
The red cell skeleton and its genetic disorders
inferred← citeshttps://doi.org/10.1016/0268-960x(91)90031-7openalex-snapshot
Platelet procoagulant activity: physiological significance and mechanisms of exposure
inferred← citeshttps://doi.org/10.1016/0304-4157(89)90006-3openalex-snapshot
The spectrin-actin junction of erythrocyte membrane skeletons
inferred← citeshttps://doi.org/10.1016/0304-4157(91)90019-sopenalex-snapshot
Transbilayer movement of phospholipids in red cell and platelet membranes
inferred← citeshttps://doi.org/10.1016/b978-1-4557-5414-4.00015-2openalex-snapshot
10.1016/b978-1-4557-5414-4.00015-2
inferred← citeshttps://doi.org/10.1016/s0006-3495(97)78229-8openalex-snapshot
Cytoskeletal protein binding kinetics at planar phospholipid membranes
inferred← citeshttps://doi.org/10.1016/s0021-9258(18)98452-8openalex-snapshot
Erythropoietin enhances the assembly of alpha,beta spectrin heterodimers on the murine erythroblast membranes by increasing beta spectrin synthesis
inferred← citeshttps://doi.org/10.1016/s0021-9258(18)99068-xopenalex-snapshot
Distance between skeletal protein 4.1 and the erythrocyte membrane bilayer measured by resonance energy transfer
inferred← citeshttps://doi.org/10.1016/s0070-2161(08)60975-2openalex-snapshot
Plasma Membrane Phospholipid Asymmetry and Its Maintenance: The Human Erythrocyte as a Model
inferred← citeshttps://doi.org/10.1016/s0070-2161(08)60976-4openalex-snapshot
Protein-Mediated Phospholipid Movement in Red Blood Cells
inferred← citeshttps://doi.org/10.1016/s0301-0082(03)00114-xopenalex-snapshot
Patterned Purkinje cell death in the cerebellum
inferred← citeshttps://doi.org/10.1016/s0301-4622(99)00114-3openalex-snapshot
Fluorescence correlation spectroscopy analysis of the hydrophobic interactions of protein 4.1 with phosphatidyl serine liposomes
inferred← citeshttps://doi.org/10.1016/s1383-8121(06)80010-2openalex-snapshot
Cell Membranes and the Cytoskeleton
inferred← citeshttps://doi.org/10.1016/s1388-1981(00)00052-4openalex-snapshot
Identification and purification of aminophospholipid flippases
inferred← citeshttps://doi.org/10.1021/bi00094a031openalex-snapshot
Human erythrocyte membrane lipid asymmetry: Transbilayer distribution of rapidly diffusing phosphatidylserines
inferred← citeshttps://doi.org/10.1021/bi00245a012openalex-snapshot
Bilayer/cytoskeleton interactions in lipid-symmetric erythrocytes assessed by a photoactivable phospholipid analog
inferred← citeshttps://doi.org/10.1021/bi00432a007openalex-snapshot
Exposure of endogenous phosphatidylserine at the outer surface of stimulated platelets is reversed by restoration of aminophospholipid translocase activity
inferred← citeshttps://doi.org/10.1021/bi00443a025openalex-snapshot
A photoactivable phospholipid analog that specifically labels membrane cytoskeletal proteins of intact erythrocytes
inferred← citeshttps://doi.org/10.1021/bi00453a005openalex-snapshot
Aminophospholipid translocation in erythrocytes: evidence for the involvement of a specific transporter and an endofacial protein
inferred← citeshttps://doi.org/10.1021/bi0256330openalex-snapshot
Functional Characterization of Spectrin-Actin-Binding Domains in 4.1 Family of Proteins
inferred← citeshttps://doi.org/10.1021/bi200154gopenalex-snapshot
Phosphorylation-Dependent Perturbations of the 4.1R-Associated Multiprotein Complex of the Erythrocyte Membrane
inferred← citeshttps://doi.org/10.1038/bjc.1998.516openalex-snapshot
The biochemical modification of the erythrocyte membranes from women with ovarian cancer
inferred← citeshttps://doi.org/10.1042/bj2560689openalex-snapshot
Role of the phosphorylation of red blood cell membrane proteins
inferred← citeshttps://doi.org/10.1042/bj2820075openalex-snapshot
Fluorescence quenching of spectrin and other red cell membrane cytoskeletal proteins. Relation to hydrophobic binding sites
inferred← citeshttps://doi.org/10.1053/j.seminhematol.2004.01.003openalex-snapshot
Hereditary elliptocytosis: spectrin and protein 4.1R
inferred← citeshttps://doi.org/10.1055/s-0037-1616224openalex-snapshot
Unraveling the Mysteries of Phospholipid Scrambling
inferred← citeshttps://doi.org/10.1074/jbc.272.5.2977openalex-snapshot
Identification of ä-Spectrin Domains Susceptible to Ubiquitination
inferred← citeshttps://doi.org/10.1074/jbc.273.11.6171openalex-snapshot
Biochemical Analysis of Potential Sites for Protein 4.1-mediated Anchoring of the Spectrin-Actin Skeleton to the Erythrocyte Membrane
inferred← citeshttps://doi.org/10.1074/jbc.m101364200openalex-snapshot
Structural and Functional Characterization of Protein 4.1R-Phosphatidylserine Interaction
inferred← citeshttps://doi.org/10.1074/jbc.m107855200openalex-snapshot
Analysis of Integral Membrane Protein Contributions to the Deformability and Stability of the Human Erythrocyte Membrane
inferred← citeshttps://doi.org/10.1111/1523-1747.ep12371695openalex-snapshot
Localization of Adducin in Epidermis
inferred← citeshttps://doi.org/10.1111/j.1365-2141.1995.tb03380.xopenalex-snapshot
Enhanced Mg2+‐ATPase activity in ghosts from HS erythrocytes and in normal ghosts stripped of membrane skeletal proteins may reflect enhanced aminophospholipid translocase activity
inferred← citeshttps://doi.org/10.1111/j.1365-2141.2008.07091.xopenalex-snapshot
Disorders of red cell membrane
inferred← citeshttps://doi.org/10.1111/j.1432-1033.1989.tb14883.xopenalex-snapshot
Composition of the ternary protein complex of the red cell membrane cytoskeleton
inferred← citeshttps://doi.org/10.1111/j.1471-4159.1992.tb08472.xopenalex-snapshot
Monoclonal Antibody Analysis of Phosphatidylserine and Protein Kinase C Localizations in Developing Rat Cerebellum
inferred← citeshttps://doi.org/10.1111/j.1537-2995.2010.02861.xopenalex-snapshot
Red blood cell microparticles show altered inflammatory chemokine binding and release ligand upon interaction with platelets
inferred← citeshttps://doi.org/10.1111/j.1600-0609.1991.tb00554.xopenalex-snapshot
Congenital haemolytic anaemia in a low birth weight infant due to congenital stomatocytosis
inferred← citeshttps://doi.org/10.1134/s1990747815020129openalex-snapshot
Protein spectrum of the erythrocyte membrane and its changes in pathology
inferred← citeshttps://doi.org/10.1177/096120339400300406openalex-snapshot
Physiology of Membrane Lipid Asymmetry
inferred← citeshttps://doi.org/10.1182/blood-2008-07-161166openalex-snapshot
Red cell membrane: past, present, and future
inferred← citeshttps://doi.org/10.1182/blood.v76.1.198.198openalex-snapshot
Alteration of the erythrocyte membrane skeletal ultrastructure in hereditary spherocytosis, hereditary elliptocytosis, and pyropoikilocytosis
inferred← citeshttps://doi.org/10.1182/blood.v77.2.214.bloodjournal772214openalex-snapshot
Beyond hemoglobin polymerization: the red blood cell membrane and sickle disease pathophysiology
inferred← citeshttps://doi.org/10.1182/blood.v80.2.523.523openalex-snapshot
Band 3 Tuscaloosa: Pro327----Arg327 substitution in the cytoplasmic domain of erythrocyte band 3 protein associated with spherocytic hemolytic anemia and partial deficiency of protein 4.2
inferred← citeshttps://doi.org/10.1182/blood.v81.4.1051.1051openalex-snapshot
The distribution of erythrocyte phospholipids in hereditary spherocytosis demonstrates a minimal role for erythrocyte spectrin on phospholipid diffusion and asymmetry
inferred← citeshttps://doi.org/10.1182/blood.v82.11.3482.3482openalex-snapshot
Membrane attachment sites for the membrane cytoskeletal protein 4.1 of the red blood cell [see comments]
inferred← citeshttps://doi.org/10.1182/blood.v83.6.1668.1668openalex-snapshot
Quantitation of the number of molecules of glycophorins C and D on normal red blood cells using radioiodinated Fab fragments of monoclonal antibodies
inferred← citeshttps://doi.org/10.1182/blood.v91.8.3044.3044_3044_3051openalex-snapshot
Membrane Phospholipid Asymmetry in Human Thalassemia
inferred← citeshttps://doi.org/10.18388/abp.2000_3979openalex-snapshot
Interaction of membrane skeletal proteins with membrane lipid domain.
inferred← citeshttps://doi.org/10.32657/10356/47450openalex-snapshot
Invasion pathway switching of plasmodium falciparum reveals post-transcriptional regulation of merozoite proteins
inferred← citeshttps://doi.org/10.70675/d5d836a7z9626z4a70z9038ze3b12cea9400openalex-snapshot
Role of nucleotide metabolite transporters in erythropoiesis and red blood cell functions
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