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1
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MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties.
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J Cell Biol
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1987
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4.78
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2
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Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins.
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Nature
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1990
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4.30
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3
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Motor proteins of cytoplasmic microtubules.
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Annu Rev Biochem
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1990
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2.45
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4
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Identification of an early endosomal protein regulated by phosphatidylinositol 3-kinase.
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Proc Natl Acad Sci U S A
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1997
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2.39
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5
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Microtubule-associated protein 1C from brain is a two-headed cytosolic dynein.
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Nature
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1988
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2.26
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6
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Microtubules and Src homology 3 domains stimulate the dynamin GTPase via its C-terminal domain.
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Proc Natl Acad Sci U S A
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1993
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1.88
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7
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Purification of brain cytoplasmic dynein and characterization of its in vitro properties.
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Methods Enzymol
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1991
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1.15
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8
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Cell confluence-dependent remodeling of endothelial membranes mediated by cholesterol.
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J Biol Chem
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2000
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0.93
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9
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The role of dynein in retrograde axonal transport.
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Trends Neurosci
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1989
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0.92
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10
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The role of dynein and other microtubule-activated ATPases in mitosis.
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1989
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0.90
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11
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Potential roles of microtubule-associated motor molecules in cell division.
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1990
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0.87
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12
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Dynamin, a GTPase involved in the initial stages of endocytosis.
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Ciba Found Symp
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1993
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0.85
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13
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Cell biology. Dynamin in synaptic dynamics.
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Nature
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1993
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0.85
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14
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Purification and characterization of dynamin.
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1991
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0.84
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15
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Dynamin: a microtubule-associated GTP-binding protein.
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J Cell Sci Suppl
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1991
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0.75
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