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Literature DB >> 6768755

Structural comparison of several actin-binding macromolecules.

Abstract

The cytoskeletal components, macrophage actin-binding protein and filamin, were dried from glycerol and examined by low-angle rotary shadowing electron microscopy. Both are elongate, flexible molecules whose general morphologi is similar to that of erythrocyte spectrin. Neither actin-binding protein nor filamin binds to spectrin-depleted erythrocyte membranes.

Entities: Chemical

Mesh：

Substances：

Year: 1980 PMID： 6768755 PMCID： PMC2110609 DOI： 10.1083/jcb.85.2.489

Source DB: PubMed Journal: J Cell Biol ISSN： 0021-9525 Impact factor: 10.539

19 in total

1. Purification of two spectrin-binding proteins: biochemical and electron microscopic evidence for site-specific reassociation between spectrin and bands 2.1 and 4.1.

Authors: J M Tyler; W R Hargreaves; D Branton
Journal: Proc Natl Acad Sci U S A Date: 1979-10 Impact factor: 11.205

2. Spectrin-actin interaction. Phosphorylated and dephosphorylated spectrin tetramer cross-link F-actin.

Authors: S L Brenner; E D Korn
Journal: J Biol Chem Date: 1979-09-10 Impact factor: 5.157

3. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane.

Authors: G Fairbanks; T L Steck; D F Wallach
Journal: Biochemistry Date: 1971-06-22 Impact factor: 3.162

4. Proteolytic fragmentation of spectrin:effect of removal of terminal phosphopeptides on spectrin binding to human erythrocyte membranes.

Authors: J M Anderson; J M Tyler
Journal: Prog Clin Biol Res Date: 1979

5. Selective solubilization of a protein component of the red cell membrane.

Authors: V T Marchesi; E Steers
Journal: Science Date: 1968-01-12 Impact factor: 47.728

6. State of spectrin phosphorylation does not affect erythrocyte shape or spectrin binding to erythrocyte membranes.

Authors: J M Anderson; J M Tyler
Journal: J Biol Chem Date: 1980-02-25 Impact factor: 5.157

7. The molecular structure of human erythrocyte spectrin. Biophysical and electron microscopic studies.

Authors: D M Shotton; B E Burke; D Branton
Journal: J Mol Biol Date: 1979-06-25 Impact factor: 5.469

8. Interactions between actin, myosin, and an actin-binding protein from rabbit alveolar macrophages. Alveolar macrophage myosin Mg-2+-adenosine triphosphatase requires a cofactor for activation by actin.

Authors: T P Stossel; J H Hartwig
Journal: J Biol Chem Date: 1975-07-25 Impact factor: 5.157

9. The labelling of proteins to high specific radioactivities by conjugation to a 125I-containing acylating agent.

Authors: A E Bolton; W M Hunter
Journal: Biochem J Date: 1973-07 Impact factor: 3.857

10. Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin.

Authors: F Thoma; T Koller; A Klug
Journal: J Cell Biol Date: 1979-11 Impact factor: 10.539

23 in total

Review 8. Filamin structure, function and mechanics: are altered filamin-mediated force responses associated with human disease?

Authors: Andrew J Sutherland-Smith
Journal: Biophys Rev Date: 2011-01-27

9. Titin is an extraordinarily long, flexible, and slender myofibrillar protein.

Authors: K Wang; R Ramirez-Mitchell; D Palter
Journal: Proc Natl Acad Sci U S A Date: 1984-06 Impact factor: 11.205

Review 10. The thin filaments of smooth muscles.

Authors: S B Marston; C W Smith
Journal: J Muscle Res Cell Motil Date: 1985-12 Impact factor: 2.698

Structural comparison of several actin-binding macromolecules.

1. Purification of two spectrin-binding proteins: biochemical and electron microscopic evidence for site-specific reassociation between spectrin and bands 2.1 and 4.1.

2. Spectrin-actin interaction. Phosphorylated and dephosphorylated spectrin tetramer cross-link F-actin.

3. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane.

4. Proteolytic fragmentation of spectrin:effect of removal of terminal phosphopeptides on spectrin binding to human erythrocyte membranes.

5. Selective solubilization of a protein component of the red cell membrane.

6. State of spectrin phosphorylation does not affect erythrocyte shape or spectrin binding to erythrocyte membranes.

7. The molecular structure of human erythrocyte spectrin. Biophysical and electron microscopic studies.

8. Interactions between actin, myosin, and an actin-binding protein from rabbit alveolar macrophages. Alveolar macrophage myosin Mg-2+-adenosine triphosphatase requires a cofactor for activation by actin.

9. The labelling of proteins to high specific radioactivities by conjugation to a 125I-containing acylating agent.

10. Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin.

Review 1. Creation of functional micro/nano systems through top-down and bottom-up approaches.

Review 2. The origins and evolution of freeze-etch electron microscopy.

3. The human erythrocyte membrane skeleton may be an ionic gel. I. Membrane mechanochemical properties.

4. A novel protein accumulated during maturation of the pods of the plant Impatiens balsamina.

5. Electron-microscopical approach to a structural model of intima collagen.

6. Structure of filamin and the F-actin-heavy merofilamin complex.

Review 7. The red cell membrane and its cytoskeleton.

Review 8. Filamin structure, function and mechanics: are altered filamin-mediated force responses associated with human disease?

9. Titin is an extraordinarily long, flexible, and slender myofibrillar protein.

Review 10. The thin filaments of smooth muscles.