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Molecular cloning of bovine actin-like protein, actin2
Biochemical and Biophysical Research Communications, 1992Actins are major cytoskeletal components and highly conserved in evolution. In mammals, there are six actin isoforms, a pair of which shows at least 93% identity in the amino acid sequence. We have cloned cDNA for a bovine protein that is distantly related to members of the mammalian actin isotypes. The predicted amino acid sequence (418 residues long,
T, Tanaka +7 more
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Bacterial DNA segregation by the actin-like MreB protein
Trends in Cell Biology, 2005Faithful chromosome segregation is vital to all organisms. Eukaryotic cells use the tubulin-based cytoskeleton to segregate their chromosomes during mitosis. A handful of papers have provided convincing evidence that, in bacteria, this task is accomplished by the actin homolog MreB. In particular, a recent study by Gitai et al.
Kruse T, Gerdes K
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Occurrence of actin-like protein in extracellular matrix vesicles
Calcified Tissue International, 1982Preliminary indications of the occurrence of actin and myosin in crude matrix vesicle preparations have been reported previously. In the present study extracellular matrix vesicles from rat alveolar bone were isolated. They were further purified by a sucrose density gradient.
A, Muhlrad +3 more
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Regulation of actin polymerization by non-polymerizable actin-like proteins
Nature, 1984Three functionally distinct actin-capping proteins from the slime mould Physarum are structurally closely related to actin itself. In Physarum, actin polymerization is regulated by a set of non-polymerizable actin-like proteins. It remains to be established whether these proteins and actin are each encoded by separate genes.
H, Maruta +3 more
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Actin-like Properties of Colchicine Binding Protein isolated from Brain
Nature, 1970THE isolation from mammalian brain of a protein with properties similar to those of muscle actomyosin was recently reported1 and it was suggested that the protein was composed of actin-like and myosin-like subunits. There have also been references2 to the possibility that colchicine binding protein isolated from the microtubules of sea urchin sperm ...
S, Puszkin, S, Berl
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Actin-like and tubulin-like proteins in synaptic junctional complexes
Canadian Journal of Biochemistry, 1978Synaptic junctional complexes (SJCs), isolated by a procedure which preserves presynaptic dense projections (PDPs) contain as their major component a polypeptide (P55) which comigrates with tubulin on sodium dodecyl sulfate - polyacrylamide gels and another major polypeptide (P45) which comigrates with muscle actin. We report here the characterization
W E, Mushynski, S, Glen, H M, Thérien
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Arthrin: A new actin-like protein in insect flight muscle
Journal of Molecular Biology, 1985There are one or more proteins of 50,000 to 60,000 Mr in the thin filaments of insect flight muscle. A protein of 55,000 Mr has been isolated from insect fibrillar flight muscle and called arthrin. Despite its higher molecular weight, arthrin is in many ways like actin. The amino acid composition of arthrin was similar to that of actin.
B, Bullard +3 more
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Myosin-Like Protein and Actin-Like Protein from Escherichia coli K12 C600
The Journal of Biochemistry, 1978Myosin-like protein was obtained from E. coli by extraction with a sucrose solution and by precipitation with rabbit skeletal actin. The preparation of E. coli myosin-like protein looked very similar, in the sodium dodecyl sulfate-gel electrophoretic pattern, to that of rabbit skeletal myosin.
K, Nakamura, S, Watanabe
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Actin-like protein associated with plasma membranes fromEuglena gracilis
Protoplasma, 1998Microtubules are characteristic components of the membrane skeleton ofEuglena gracilis, but whether microfilaments are present has been controversial. We here present evidence that an actin-like protein may indeed be associated with the plasma membrane (PM) ofE. gracilis.
Silja K. Petersen-Mahrt +2 more
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Actin-like protein in normal and neoplastic tissue
2021This thesis was scanned from the print manuscript for digital preservation and is copyright the author. Researchers can access this thesis by asking their local university, institution or public library to make a request on their behalf. Monash staff and postgraduate students can use the link in the References field.
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