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Associations of human erythrocyte band 4.2. Binding to ankyrin and to the cytoplasmic domain of band 3

The Journal of biological chemistry, 1988-07, Vol.263 (21), p.10212-10218

1988

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Epithelial shedding : restitution as a causative process in airway inflammation

Clinical and experimental allergy, 1996-07, Vol.26 (7), p.746-755

1996

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Human erythrocyte membrane protein band 4.2 (pallidin)

Seminars in hematology, 1993-04, Vol.30 (2), p.119-137

1993

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Control of band 3 lateral and rotational mobility by band 4.2 in intact erythrocytes: release of band 3 oligomers from low-affinity binding sites

Biophysical journal, 1996-03, Vol.70 (3), p.1534-1542

1996

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Organization of the Gene for Human Erythrocyte Membrane Protein 4.2: Structural Similarities with the Gene for the a Subunit of Factor XIII

Proceedings of the National Academy of Sciences - PNAS, 1991-06, Vol.88 (11), p.4840-4844

1991

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Complete Amino Acid Sequence and Homologies of Human Erythrocyte Membrane Protein Band 4.2

Proceedings of the National Academy of Sciences - PNAS, 1990-01, Vol.87 (2), p.613-617

1990

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Purification and properties of human erythrocyte band 4.2. Association with the cytoplasmic domain of band 3

The Journal of biological chemistry, 1986-04, Vol.261 (12), p.5536-5543

1986

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A point mutation in the protein 4.2 gene (allele 4.2 Tozeur) associated with hereditary haemolytic anaemia

British journal of haematology, 1995-04, Vol.89 (4), p.762-770

1995

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Mild spherocytosis and altered red cell ion transport in protein 4.2–null mice

The Journal of clinical investigation, 1999-06, Vol.103 (11), p.1527-1537

1999

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A New Spectrin, βIV, Has a Major Truncated Isoform That Associates with Promyelocytic Leukemia Protein Nuclear Bodies and the Nuclear Matrix

The Journal of biological chemistry, 2001-06, Vol.276 (26), p.23974-23985

2001

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Epithelial shedding-restitution as a causative process in airway inflammation

Clinical and experimental allergy, 1996, Vol.26 (7), p.746-755

1996

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The murine pallid mutation is a platelet storage pool disease associated with the protein 4.2 (pallidin) gene

Nature genetics, 1992-09, Vol.2 (1), p.80-83

1992

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Organization of the gene for human erythrocyte membrane protein 4. 2: Structural similarities with the gene for the a subunit of factor XIII

Proceedings of the National Academy of Sciences - PNAS, 1991-06, Vol.88:11

1991

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Role of N-myristylation in targeting of band 4.2 (pallidin) in nonerythroid cells

Experimental cell research, 1996-12, Vol.229 (2), p.421-431

1996

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cDNA Sequence, Gene Sequence, and Properties of Murine Pallidin (Band 4.2), the Protein Implicated in the Murine pallid Mutation

Genomics (San Diego, Calif.), 1994-06, Vol.21 (3), p.478-485

1994

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Human Erythrocyte Dematin and Protein 4.2 (Pallidin) Are ATP Binding Proteins

Biochemistry (Easton), 1996-03, Vol.35 (9), p.3001-3006

1996

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The Gene Encoding Protein 4.2 Is Distinct from the Mouse Platelet Storage Pool Deficiency Mutation Pallid

Genomics (San Diego, Calif.), 1997-06, Vol.42 (3), p.532-535

1997

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Mild spherocytosis and altered red cell ion transport in protein 4. 2-null mice

The Journal of clinical investigation, 1999-06, Vol.103 (11), p.1527

1999

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Human erythrocyte membrane protein band 4.2 (pallidin): Cellular and molecular biology of red blood cell membrane proteins in health and disease. III: Their genes and mutations (continued)

Seminars in hematology, 1993, Vol.30 (2), p.119-137

1993

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Functional associations of band 4.1 in the erythrocyte membrane skeleton and their role in inherited membrane skeletal abnormalities

Progress in clinical and biological research, 1984, Vol.159, p.13

1984

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Band 4.1 causes spectrin-actin gels to become thixiotropic

Biochemical and biophysical research communications, 1980-12, Vol.97 (4), p.1429-1435

1980

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A protein immunologically related to erythrocyte band 4.1 is found on stress fibres of non-erythroid cells

Nature (London), 1982-10, Vol.299 (5884), p.648-650

1982

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Complete amino acid sequence and homologies of human erythrocyte membrane protein band 4. 2

Proceedings of the National Academy of Sciences - PNAS, 1990-01, Vol.87:2

1990

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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

Blood, 1992-07, Vol.80 (2), p.523-529

1992

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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

Blood, 1992-07, Vol.80 (2), p.523-529

1992

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Associations of human erythrocyte band 4.2. Binding to ankyrin and to the cytoplasmic domain of band 3

Epithelial shedding : restitution as a causative process in airway inflammation

Human erythrocyte membrane protein band 4.2 (pallidin)

Control of band 3 lateral and rotational mobility by band 4.2 in intact erythrocytes: release of band 3 oligomers from low-affinity binding sites

Organization of the Gene for Human Erythrocyte Membrane Protein 4.2: Structural Similarities with the Gene for the a Subunit of Factor XIII

Complete Amino Acid Sequence and Homologies of Human Erythrocyte Membrane Protein Band 4.2

Purification and properties of human erythrocyte band 4.2. Association with the cytoplasmic domain of band 3

A point mutation in the protein 4.2 gene (allele 4.2 Tozeur) associated with hereditary haemolytic anaemia

Mild spherocytosis and altered red cell ion transport in protein 4.2–null mice

A New Spectrin, βIV, Has a Major Truncated Isoform That Associates with Promyelocytic Leukemia Protein Nuclear Bodies and the Nuclear Matrix

Epithelial shedding-restitution as a causative process in airway inflammation

The murine pallid mutation is a platelet storage pool disease associated with the protein 4.2 (pallidin) gene

Organization of the gene for human erythrocyte membrane protein 4. 2: Structural similarities with the gene for the a subunit of factor XIII

Role of N-myristylation in targeting of band 4.2 (pallidin) in nonerythroid cells

cDNA Sequence, Gene Sequence, and Properties of Murine Pallidin (Band 4.2), the Protein Implicated in the Murine pallid Mutation

Human Erythrocyte Dematin and Protein 4.2 (Pallidin) Are ATP Binding Proteins

The Gene Encoding Protein 4.2 Is Distinct from the Mouse Platelet Storage Pool Deficiency Mutation Pallid

Mild spherocytosis and altered red cell ion transport in protein 4. 2-null mice

Human erythrocyte membrane protein band 4.2 (pallidin): Cellular and molecular biology of red blood cell membrane proteins in health and disease. III: Their genes and mutations (continued)

Functional associations of band 4.1 in the erythrocyte membrane skeleton and their role in inherited membrane skeletal abnormalities

Band 4.1 causes spectrin-actin gels to become thixiotropic

A protein immunologically related to erythrocyte band 4.1 is found on stress fibres of non-erythroid cells

Complete amino acid sequence and homologies of human erythrocyte membrane protein band 4. 2

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

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

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