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Isolation, purification and characterization of byosin B from myxomycete plasmodium.
Biochim Biophys Acta. 1968 Apr 9;154(3):507-19
PMID: 4231303
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Protein measurement with the Folin phenol reagent.
J Biol Chem. 1951 Nov;193(1):265-75
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Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
Nature. 1970 Aug 15;227(5259):680-5
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The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin.
J Biol Chem. 1971 Aug 10;246(15):4866-71
PMID: 4254541
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Properties of Physarum myosin purified by a potassium iodide procedure.
J Cell Biol. 1974 Jul;62(1):54-65
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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.
J Biol Chem. 1975 Jul 25;250(14):5706-12
PMID: 124735
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Filamin, a new high-molecular-weight protein found in smooth muscle and non-muscle cells.
Proc Natl Acad Sci U S A. 1975 Nov;72(11):4483-6
PMID: 53835
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Filamin, a new high-molecular-weight protein found in smooth muscle and nonmuscle cells. Purification and properties of chicken gizzard filamin.
Biochemistry. 1977 May 3;16(9):1857-65
PMID: 139917
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Interactions of actin, myosin, and a new actin-binding protein of rabbit pulmonary macrophages. II. Role in cytoplasmic movement and phagocytosis.
J Cell Biol. 1976 Mar;68(3):602-19
PMID: 1035911
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Self-association of human spectrin. A thermodynamic and kinetic study.
Eur J Biochem. 1978 Aug 1;88(2):379-85
PMID: 689023
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The gelation of actin by actin-binding protein.
J Biol Chem. 1978 Dec 25;253(24):8988-93
PMID: 721823
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Spectrin-actin interaction. Phosphorylated and dephosphorylated spectrin tetramer cross-link F-actin.
J Biol Chem. 1979 Sep 10;254(17):8620-7
PMID: 468843
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The molecular structure of human erythrocyte spectrin. Biophysical and electron microscopic studies.
J Mol Biol. 1979 Jun 25;131(2):303-29
PMID: 490648
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Isolation of a high molecular weight actin-binding protein from baby hamster kidney (BHK-21) cells.
Proc Natl Acad Sci U S A. 1979 Sep;76(9):4484-8
PMID: 291980
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Viscometric analysis of the gelation of Acanthamoeba extracts and purification of two gelation factors.
J Cell Biol. 1980 May;85(2):414-28
PMID: 6892818
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Structural comparison of several actin-binding macromolecules.
J Cell Biol. 1980 May;85(2):489-95
PMID: 6768755
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Interaction of cytoskeletal proteins on the human erythrocyte membrane.
Cell. 1981 Apr;24(1):24-32
PMID: 6453651
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Structure of macrophage actin-binding protein molecules in solution and interacting with actin filaments.
J Mol Biol. 1981 Jan 25;145(3):563-81
PMID: 6894945
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Fodrin: axonally transported polypeptides associated with the internal periphery of many cells.
J Cell Biol. 1981 Sep;90(3):631-42
PMID: 6169732
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Isolation and characterization of actin and actin-binding protein from human platelets.
J Cell Biol. 1981 Oct;91(1):201-11
PMID: 7197680
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An F-actin- and calmodulin-binding protein from isolated intestinal brush borders has a morphology related to spectrin.
Cell. 1982 Apr;28(4):843-54
PMID: 7201352
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Actin gelation and structure of cortical cytoplasm.
Cold Spring Harb Symp Quant Biol. 1982;46 Pt 2:569-78
PMID: 6286216
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Brain spectrin, a membrane-associated protein related in structure and function to erythrocyte spectrin.
Nature. 1982 Sep 9;299(5879):126-31
PMID: 7110333
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Erythroid spectrin, brain fodrin, and intestinal brush border proteins (TW-260/240) are related molecules containing a common calmodulin-binding subunit bound to a variant cell type-specific subunit.
Proc Natl Acad Sci U S A. 1982 Jul;79(13):4002-5
PMID: 6955786
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Nonerythrocyte spectrins: actin-membrane attachment proteins occurring in many cell types.
J Cell Biol. 1982 Nov;95(2 Pt 1):478-86
PMID: 6183274
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Purification of a HeLa cell high molecular weight action binding protein and its identification in HeLa cell plasma membrane ghosts and intact HeLa cells.
Biochemistry. 1983 Apr 12;22(8):1839-47
PMID: 6342667
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Physical and chemical properties of a protein isolated from red cell membranes.
Biochemistry. 1970 Jan 6;9(1):50-7
PMID: 4983452