-
2
-
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15144351296
-
Conservation with the myosin motor domain: Implications for structure and function
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of special interest. A comprehensive review bringing together the structural data available for the myosin II motor domain with a comparative analysis of the motor domain sequences for all known classes of myosins. The authors highlight functionally important conserved sequences.
-
Cope MJTV, Whisstock J, Rayment I, Kendrick-Jones JK. Conservation with the myosin motor domain: implications for structure and function. of special interest Structure. 4:1996;969-987 A comprehensive review bringing together the structural data available for the myosin II motor domain with a comparative analysis of the motor domain sequences for all known classes of myosins. The authors highlight functionally important conserved sequences.
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(1996)
Structure
, vol.4
, pp. 969-987
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Cope, M.J.T.V.1
Whisstock, J.2
Rayment, I.3
Kendrick-Jones, J.K.4
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3
-
-
0028803112
-
The mouse Snell's waltzer deafness gene encodes an unconventional myosin required for structural integrity of inner ear hair cells
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Avraham KB, Hasson T, Steel KP, Kingsley DM, Russel LB, Mooseker MS, Copeland NG, Jenkins NA. The mouse Snell's waltzer deafness gene encodes an unconventional myosin required for structural integrity of inner ear hair cells. Nat Genet. 11:1995;369-375.
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(1995)
Nat Genet
, vol.11
, pp. 369-375
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-
Avraham, K.B.1
Hasson, T.2
Steel, K.P.3
Kingsley, D.M.4
Russel, L.B.5
Mooseker, M.S.6
Copeland, N.G.7
Jenkins, N.A.8
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4
-
-
0030973305
-
Unconventional myosins in innerear sensory epithelia
-
of outstanding interest. A beautiful study on the expression and localization of myosins Iβ, V, VI, and VII in the ear. The authors correlate the distribution of each myosin with different actin-rich structures in the ear of several different vertebrates and draw conclusions regarding the specialized function of each type of myosin. A 'must read' for anyone interested in myosins!
-
Hasson T, Gillespie PG, Garcia JA, MacDonald RB, Zhao Y, Yee AG, Mooseker MS, Corey DP. Unconventional myosins in innerear sensory epithelia. of outstanding interest J Cell Biol. 137:1997;1287-1307 A beautiful study on the expression and localization of myosins Iβ, V, VI, and VII in the ear. The authors correlate the distribution of each myosin with different actin-rich structures in the ear of several different vertebrates and draw conclusions regarding the specialized function of each type of myosin. A 'must read' for anyone interested in myosins!
-
(1997)
J Cell Biol
, vol.137
, pp. 1287-1307
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-
Hasson, T.1
Gillespie, P.G.2
Garcia, J.A.3
MacDonald, R.B.4
Zhao, Y.5
Yee, A.G.6
Mooseker, M.S.7
Corey, D.P.8
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5
-
-
0030951102
-
The autosomal recessive deafness, DFNB2, and the Usher 1B syndrome are allelic defects of the myosin-VIIA gene
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Weil D, Küssel P, Blanchard S, Lévy G, Levi-Acobas F, Drira M, Ayadi H, Petit C. The autosomal recessive deafness, DFNB2, and the Usher 1B syndrome are allelic defects of the myosin-VIIA gene. Nat Genet. 16:1997;191-193.
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(1997)
Nat Genet
, vol.16
, pp. 191-193
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-
Weil, D.1
Küssel, P.2
Blanchard, S.3
Lévy, G.4
Levi-Acobas, F.5
Drira, M.6
Ayadi, H.7
Petit, C.8
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6
-
-
0030811605
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Myosin VIIa, the product of the Usher 1B syndrome gene, is concentrated in the connecting cilia of photoreceptor cells
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Liu X, Vansant G, Udovichenko IP, Wolfrum U, Williams DS. Myosin VIIa, the product of the Usher 1B syndrome gene, is concentrated in the connecting cilia of photoreceptor cells. Cell Motil Cytoskeleton. 37:1997;240-252.
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(1997)
Cell Motil Cytoskeleton
, vol.37
, pp. 240-252
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Liu, X.1
Vansant, G.2
Udovichenko, I.P.3
Wolfrum, U.4
Williams, D.S.5
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7
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0027439124
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Identification of a 120 kd hair-bundle myosin located near sterocilliary tips
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Gillespie PC, Wagner MC, Hudspeth AJ. Identification of a 120 kd hair-bundle myosin located near sterocilliary tips. Neuron. 11:1993;581-594.
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(1993)
Neuron
, vol.11
, pp. 581-594
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Gillespie, P.C.1
Wagner, M.C.2
Hudspeth, A.J.3
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8
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0027960895
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Molecular cloning of a myosin Iβ isozyme that may mediate adaptation by hair cells of the bullfrog's internal ear
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Metcalf AB, Chelliah Y, Hudspeth AJ. Molecular cloning of a myosin Iβ isozyme that may mediate adaptation by hair cells of the bullfrog's internal ear. Proc Natl Acad Sci USA. 91:1994;1182-11825.
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(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 1182-11825
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Metcalf, A.B.1
Chelliah, Y.2
Hudspeth, A.J.3
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9
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0003154314
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Molecular cloning of myosins from the bullfrog saccular macula: A candidate for the hair cell adaptation
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Solc CK, Derfler BH, Duyk GM, Corey DP. Molecular cloning of myosins from the bullfrog saccular macula: a candidate for the hair cell adaptation. Aud Neurosci. 1:1994;63-75.
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(1994)
Aud Neurosci
, vol.1
, pp. 63-75
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Solc, C.K.1
Derfler, B.H.2
Duyk, G.M.3
Corey, D.P.4
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10
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0031038446
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ATPase activity of myosin in hair bundles of the bullfrog's sacculus
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Burlacu S, Tap WD, Lumpkin EA, Hudspeth AJ. ATPase activity of myosin in hair bundles of the bullfrog's sacculus. Biophys J. 72:1997;263-271.
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(1997)
Biophys J
, vol.72
, pp. 263-271
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Burlacu, S.1
Tap, W.D.2
Lumpkin, E.A.3
Hudspeth, A.J.4
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11
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0030587438
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Mapping of unconventional myosins in mouse and human
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Hasson T, Skowron JF, Gilbert DJ, Avraham KB, Perry WL, Bement WM, Anderson BL, Sherr EM, Chen ZY, Greene LA, et al. Mapping of unconventional myosins in mouse and human. Genomics. 36:1996;431-439.
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(1996)
Genomics
, vol.36
, pp. 431-439
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Hasson, T.1
Skowron, J.F.2
Gilbert, D.J.3
Avraham, K.B.4
Perry, W.L.5
Bement, W.M.6
Anderson, B.L.7
Sherr, E.M.8
Chen, Z.Y.9
Greene, L.A.10
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12
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0029794058
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Human Usher 1B/shaker-1: The retinal phenotype discrepancy explained by the presence/absence of myosin VIIA in the photoreceptor cells
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El-Amraoui A, Sahly I, Picaud S, Sahel J, Abitbol M, Petit C. Human Usher 1B/shaker-1: the retinal phenotype discrepancy explained by the presence/absence of myosin VIIA in the photoreceptor cells. Hum Mol Genet. 5:1996;1171-1178.
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(1996)
Hum Mol Genet
, vol.5
, pp. 1171-1178
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El-Amraoui, A.1
Sahly, I.2
Picaud, S.3
Sahel, J.4
Abitbol, M.5
Petit, C.6
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13
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0028787263
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Expression in the cochlea and retina of myosin VIIa, the gene product defective in Usher syndrome type 1B
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Hasson T, Heintzelman MB, Santos-Sacchi J, Corey DP, Mooseker MS. Expression in the cochlea and retina of myosin VIIa, the gene product defective in Usher syndrome type 1B. Proc Natl Acad Sci USA. 92:1995;9815-9819.
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(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 9815-9819
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Hasson, T.1
Heintzelman, M.B.2
Santos-Sacchi, J.3
Corey, D.P.4
Mooseker, M.S.5
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14
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0030869710
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Mutation profile of all 49 exons of the human myosin VIIA gene, and haplotype analysis, in Usher 1B families from diverse origins
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Adato A, Weil D, Kalinski H, Pel-Or Y, Ayadi H, Petit C, Korostishevsky M, Bonne-Tamir B. Mutation profile of all 49 exons of the human myosin VIIA gene, and haplotype analysis, in Usher 1B families from diverse origins. Am J Hum Genet. 61:1997;813-821.
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(1997)
Am J Hum Genet
, vol.61
, pp. 813-821
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Adato, A.1
Weil, D.2
Kalinski, H.3
Pel-Or, Y.4
Ayadi, H.5
Petit, C.6
Korostishevsky, M.7
Bonne-Tamir, B.8
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15
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0030965704
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Effects of shaker-1 mutations on mysoin-VIIa protein and mRNA expression
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Hasson T, Walsh J, Cable J, Mooseker MS, Brown SDM, Steel KP. Effects of shaker-1 mutations on mysoin-VIIa protein and mRNA expression. Cell Motil Cytoskeleton. 37:1997;127-138.
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(1997)
Cell Motil Cytoskeleton
, vol.37
, pp. 127-138
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Hasson, T.1
Walsh, J.2
Cable, J.3
Mooseker, M.S.4
Brown, S.D.M.5
Steel, K.P.6
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16
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0030450156
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Myosin V in the retina: Localization in the rod photoreceptor synapse
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Schlamp CL, Williams DL. Myosin V in the retina: localization in the rod photoreceptor synapse. Exp Eye Res. 63:1996;613-619.
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(1996)
Exp Eye Res
, vol.63
, pp. 613-619
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Schlamp, C.L.1
Williams, D.L.2
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17
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84966140454
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A lethal allele of dilute in the house mouse
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Searle AG. A lethal allele of dilute in the house mouse. Heredity. 6:1952;395-401.
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(1952)
Heredity
, vol.6
, pp. 395-401
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Searle, A.G.1
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18
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0029955902
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Cultured melanocytes from dilute mutant mice exhibit dendritic morphology and altered melanosome distribution
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of outstanding interest. Early investigators postulated that the mouse dilute phenotype was due to the improper outgrowth of dendritic melanocyte spines. The authors of this paper isolated dilute melanocytes and showed that they were still dendritic, but that the melanosomes failed to migrate into the arbors.
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Provance DW Jr, Wei M, Ipe V, Mercer JA. Cultured melanocytes from dilute mutant mice exhibit dendritic morphology and altered melanosome distribution. of outstanding interest Proc Natl Acad Sci USA. 93:1996;14554-14558 Early investigators postulated that the mouse dilute phenotype was due to the improper outgrowth of dendritic melanocyte spines. The authors of this paper isolated dilute melanocytes and showed that they were still dendritic, but that the melanosomes failed to migrate into the arbors.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 14554-14558
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Provance D.W., Jr.1
Wei, M.2
Ipe, V.3
Mercer, J.A.4
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19
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0030964893
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Myosin V associates with melanosomes in mouse melanocytes: Evidence that myosin V is an organelle motor
-
of outstanding interest. Immunofluorescent and immunoelectron microscopy were utilized to explore the in vivo association of myosin V with melanosomes. The results of this paper point to both actin- and microtubule-dependent motility of these organelles. The acto-myosin driven segment appears to be in the dendritic endings alone.
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Wu X, Bowers B, Wei Q, Kocher B, Hammer JA III. Myosin V associates with melanosomes in mouse melanocytes: evidence that myosin V is an organelle motor. of outstanding interest J Cell Sci. 110:1997;847-859 Immunofluorescent and immunoelectron microscopy were utilized to explore the in vivo association of myosin V with melanosomes. The results of this paper point to both actin- and microtubule-dependent motility of these organelles. The acto-myosin driven segment appears to be in the dendritic endings alone.
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(1997)
J Cell Sci
, vol.110
, pp. 847-859
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Wu, X.1
Bowers, B.2
Wei, Q.3
Kocher, B.4
Hammer J.A. III5
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20
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0030803342
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The predominant defect in dilute melanocytes is in melanosome distribution and not cell shape, supporting a role for myosin V in melanosome transport
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of special interest. These authors also explore the morphology of mouse dilute melanocytes and demonstrate that these cells are still dendritic, but the melanosomes fail to migrate into the arbors both in vitro and in situ.
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Wei Q, Wu X, Hammer JA III. The predominant defect in dilute melanocytes is in melanosome distribution and not cell shape, supporting a role for myosin V in melanosome transport. of special interest J Mus Res Cell Motil. 18:1997;517-527 These authors also explore the morphology of mouse dilute melanocytes and demonstrate that these cells are still dendritic, but the melanosomes fail to migrate into the arbors both in vitro and in situ.
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(1997)
J Mus Res Cell Motil
, vol.18
, pp. 517-527
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Wei, Q.1
Wu, X.2
Hammer J.A. III3
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21
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0031049775
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Subcellular localization of myosin V in nerve growth cones and outgrowth from dilute-lethal neurons
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of outstanding interest. A beautiful study of myosin V localization in superior cervical ganglion neurons. Myosin V is enriched in organelle-rich zones of the extended growth cone and associated with a distinct subset of small organelles which are themselves associated with both actin and microtubules. The authors also explore the hypothesis that structural abnormalities in the mouse dilute neurons could account for neurological dysfunction. The morphology of the dilute-lethal neurons appears to be normal. These results are somewhat in conflict with earlier analyses that suggested that myosin V was required for neuronal extension; however, they might be reconciled with earlier studies if a different myosin V compensates for the loss of the dilute protein during neuronal growth and development.
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Evans LL, Hammer J, Bridgman PC. Subcellular localization of myosin V in nerve growth cones and outgrowth from dilute-lethal neurons. of outstanding interest J Cell Sci. 110:1997;439-449 A beautiful study of myosin V localization in superior cervical ganglion neurons. Myosin V is enriched in organelle-rich zones of the extended growth cone and associated with a distinct subset of small organelles which are themselves associated with both actin and microtubules. The authors also explore the hypothesis that structural abnormalities in the mouse dilute neurons could account for neurological dysfunction. The morphology of the dilute-lethal neurons appears to be normal. These results are somewhat in conflict with earlier analyses that suggested that myosin V was required for neuronal extension; however, they might be reconciled with earlier studies if a different myosin V compensates for the loss of the dilute protein during neuronal growth and development.
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(1997)
J Cell Sci
, vol.110
, pp. 439-449
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Evans, L.L.1
Hammer, J.2
Bridgman, P.C.3
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22
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0030822624
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Subcellular localization of myosin-V in the B16 melanoma cells, a wild-type cell line for the dilute gene
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of outstanding interest. A study examining the association of myosin V with organelles in the cultured melanocyte. Immunolocalization results demonstrate that myosin V colocalizes with melanosomes as well as other membrane-bound organelles. Subcellular fractionation experiments reveal that myosin V cofractionates with melanosomes. Treatment of cells with serotonin to stimulate melanin synthesis (and production of melanosomes) results in increased levels of myosin V present in the cell.
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Nascimento AAC, Amaral RG, Bizario JCS, Larson RE, Espreafico EM. Subcellular localization of myosin-V in the B16 melanoma cells, a wild-type cell line for the dilute gene. of outstanding interest Mol Biol Cell. 8:1997;1971-1988 A study examining the association of myosin V with organelles in the cultured melanocyte. Immunolocalization results demonstrate that myosin V colocalizes with melanosomes as well as other membrane-bound organelles. Subcellular fractionation experiments reveal that myosin V cofractionates with melanosomes. Treatment of cells with serotonin to stimulate melanin synthesis (and production of melanosomes) results in increased levels of myosin V present in the cell.
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(1997)
Mol Biol Cell
, vol.8
, pp. 1971-1988
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Nascimento, A.A.C.1
Amaral, R.G.2
Bizario, J.C.S.3
Larson, R.E.4
Espreafico, E.M.5
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23
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0030921711
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2+-dependent interaction with the snaptobrevin-synaptophysin complex
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of outstanding interest. The authors present biochemical data demonstrating a functional association of myosin V with synaptic vesicles. They also show that myosin V is associated with the synaptobrevin/synaptophysin complex. They suggest that myosin V may play an important role in the transport of synaptobrevin/synaptophysin-containing vesicles in nerve terminals.
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2+-dependent interaction with the snaptobrevin-synaptophysin complex. of outstanding interest J Cell Biol. 137:1997;1589-1601 The authors present biochemical data demonstrating a functional association of myosin V with synaptic vesicles. They also show that myosin V is associated with the synaptobrevin/synaptophysin complex. They suggest that myosin V may play an important role in the transport of synaptobrevin/synaptophysin-containing vesicles in nerve terminals.
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(1997)
J Cell Biol
, vol.137
, pp. 1589-1601
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Prekeris, R.1
Terrian, D.M.2
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24
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85047677416
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2+ store in the dendritic spine of Purkinje cells in mice
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of special interest. The origin of the neurological disorders in dilute mice is unknown. The brains appear normal at the gross level. These authors carried out a morphological analysis of the brains of dilute-lethal mice and found that the smooth endoplasmic reticulum of dilute mice was incorrectly localized and did not extend into the dendritic spines of Purkinje cells. The mislocation of the smooth ER may contribute to neurological dysfunction in these mice.
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2+ store in the dendritic spine of Purkinje cells in mice. of special interest Neurosci Lett. 215:1996;169-172 The origin of the neurological disorders in dilute mice is unknown. The brains appear normal at the gross level. These authors carried out a morphological analysis of the brains of dilute-lethal mice and found that the smooth endoplasmic reticulum of dilute mice was incorrectly localized and did not extend into the dendritic spines of Purkinje cells. The mislocation of the smooth ER may contribute to neurological dysfunction in these mice.
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(1996)
Neurosci Lett
, vol.215
, pp. 169-172
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-
Takagishi, Y.1
Oda, S.2
Hayasaka, S.3
Dekker-Ohno, K.4
Shikata, T.5
Inouye, M.6
Yamamura, H.7
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25
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0025801365
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The Saccharomyces cerevisiae MYO gene encodes an essential myosin for vectorial transport of vesicles
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Johnston GC, Prendergast JA, Singer RA. The Saccharomyces cerevisiae MYO gene encodes an essential myosin for vectorial transport of vesicles. J Cell Biol. 113:1991;530-551.
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(1991)
J Cell Biol
, vol.113
, pp. 530-551
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Johnston, G.C.1
Prendergast, J.A.2
Singer, R.A.3
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26
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0028902506
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The role of Myo2, a yeast class V myosin, in vesicular transport
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Govindan B, Bowser R, Novick P. The role of Myo2, a yeast class V myosin, in vesicular transport. J Cell Biol. 128:1995;1055-1068.
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(1995)
J Cell Biol
, vol.128
, pp. 1055-1068
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Govindan, B.1
Bowser, R.2
Novick, P.3
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27
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0030470182
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Actin and myosin function in directed vacuole movement during cell division in Saccharomyces cerevisiae
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of special interest. Myosin V is thought to act in trafficking of membrane-bound organelles. Further support for this hypothesis is provided by this analysis of the inheritance of the yeast vacuole. The yeast myo2 mutants were shown to fail to efficiently move the vacuole into their daughter cells. The authors find that Myop is localized to the vacuole and the tip of the growing bud (where the vacuole is anchored in wild type cells).
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Hill KL, Catlett NL, Weisman LS. Actin and myosin function in directed vacuole movement during cell division in Saccharomyces cerevisiae. of special interest J Cell Biol. 135:1996;1535-1549 Myosin V is thought to act in trafficking of membrane-bound organelles. Further support for this hypothesis is provided by this analysis of the inheritance of the yeast vacuole. The yeast myo2 mutants were shown to fail to efficiently move the vacuole into their daughter cells. The authors find that Myop is localized to the vacuole and the tip of the growing bud (where the vacuole is anchored in wild type cells).
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(1996)
J Cell Biol
, vol.135
, pp. 1535-1549
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Hill, K.L.1
Catlett, N.L.2
Weisman, L.S.3
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28
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0031013414
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Targeting of chitin synthase 3 to polarized growth sites in yeast requires Chs5p and Myo2p
-
of special interest. Yet another interesting function for myosin V in yeast. This time for the first myosin V identified, myo2. This paper presents data showing that myosin V mutants fail to properly localize a chitin synthase in cells about to divide. This chitin synthase is crucial for determining the position of the daughter cell bud.
-
Santos B, Snyder M. Targeting of chitin synthase 3 to polarized growth sites in yeast requires Chs5p and Myo2p. of special interest J Cell Biol. 136:1997;95-110 Yet another interesting function for myosin V in yeast. This time for the first myosin V identified, myo2. This paper presents data showing that myosin V mutants fail to properly localize a chitin synthase in cells about to divide. This chitin synthase is crucial for determining the position of the daughter cell bud.
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(1997)
J Cell Biol
, vol.136
, pp. 95-110
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Santos, B.1
Snyder, M.2
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29
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0029981258
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Mother cell-specific HO expression in-budding yeast depends on the unconventional myosin Myo4p and other cytoplasmic proteins
-
of special interest. The authors devised a clever screen to identify genes required for the suppression of mating type switching in the yeast daughter cell. They identified several genes essential for this process, one of which encodes the second yeast myosin V, Myo4p.
-
Jansen RP, Dowzer C, Michaelis C, Galova M, Nasmyth K. Mother cell-specific HO expression in-budding yeast depends on the unconventional myosin Myo4p and other cytoplasmic proteins. of special interest Cell. 84:1996;687-697 The authors devised a clever screen to identify genes required for the suppression of mating type switching in the yeast daughter cell. They identified several genes essential for this process, one of which encodes the second yeast myosin V, Myo4p.
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(1996)
Cell
, vol.84
, pp. 687-697
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Jansen, R.P.1
Dowzer, C.2
Michaelis, C.3
Galova, M.4
Nasmyth, K.5
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30
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0029914986
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Asymmetric accumulation of Ash1p in post-anaphase nuclei depends on a myosin and restricts yeast mating-type switching to mother cells
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Bobola N, Jansen RP, Shin TH, Nasmyth K. Asymmetric accumulation of Ash1p in post-anaphase nuclei depends on a myosin and restricts yeast mating-type switching to mother cells. Cell. 84:1996;699-709.
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(1996)
Cell
, vol.84
, pp. 699-709
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Bobola, N.1
Jansen, R.P.2
Shin, T.H.3
Nasmyth, K.4
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31
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0030930836
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Actin-dependent localization of an RNA encoding a cell-fate determinant in yeast
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of outstanding interest. There is a more interesting twist to the Myo4p story than originally thought. myo4 mutants fail to properly localize the Ash1 mRNA to the tip of the growing bud. A similar erffect is observed upon isruption of the actin cytoskeleton.
-
Takizawa PA, Sil A, Swedlow JR, Herzkowitz I, Vale RD. Actin-dependent localization of an RNA encoding a cell-fate determinant in yeast. of outstanding interest Nature. 389:1997;90-93 There is a more interesting twist to the Myo4p story than originally thought. myo4 mutants fail to properly localize the Ash1 mRNA to the tip of the growing bud. A similar erffect is observed upon isruption of the actin cytoskeleton.
-
(1997)
Nature
, vol.389
, pp. 90-93
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-
Takizawa, P.A.1
Sil, A.2
Swedlow, J.R.3
Herzkowitz, I.4
Vale, R.D.5
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32
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0030875775
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Mating type switching in yeast controlled by asymmetric localization of ash1 mrna
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of outstanding interest. These authors also show that myo4 mutants fail to properly localize the Ash1 message to the daughter cell. This suggests that myosin V may not simply act as an organelle motor but may participate in the localization of mRNAs as well.
-
Long RM, Singer RH, Meng XH, Gonzalez I, Nasmyth K, Jansen RP. Mating type switching in yeast controlled by asymmetric localization of ash1 mrna. of outstanding interest Science. 277:1997;383-387 These authors also show that myo4 mutants fail to properly localize the Ash1 message to the daughter cell. This suggests that myosin V may not simply act as an organelle motor but may participate in the localization of mRNAs as well.
-
(1997)
Science
, vol.277
, pp. 383-387
-
-
Long, R.M.1
Singer, R.H.2
Meng, X.H.3
Gonzalez, I.4
Nasmyth, K.5
Jansen, R.P.6
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33
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0024284814
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Identification of genes required for cytoplasmic localization in early C. elegans embryos
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Kemphues KJ, Priess JR, Morton DG, Cheng NS. Identification of genes required for cytoplasmic localization in early C. elegans embryos. Cell. 52:1988;311-320.
-
(1988)
Cell
, vol.52
, pp. 311-320
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Kemphues, K.J.1
Priess, J.R.2
Morton, D.G.3
Cheng, N.S.4
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34
-
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0029836212
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A non-muscle myosin required for embryonic polarity in Caenorhabditis elegans
-
of outstanding interest. A surprising result from this lab showed a non-muscle myosin II to be involved in correct asymmetric partitioning in Caenorhabditis elegans. It was found that this protein is coprecipitated with another protein involved in this process, Par-1.
-
Guo S, Kemphues KJ. A non-muscle myosin required for embryonic polarity in Caenorhabditis elegans. of outstanding interest Nature. 382:1996;455-458 A surprising result from this lab showed a non-muscle myosin II to be involved in correct asymmetric partitioning in Caenorhabditis elegans. It was found that this protein is coprecipitated with another protein involved in this process, Par-1.
-
(1996)
Nature
, vol.382
, pp. 455-458
-
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Guo, S.1
Kemphues, K.J.2
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35
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0029586647
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A Dictyostelium myosin I plays a crucial role in regulating the frequency of pseudopods formed on the substratum
-
of special interest. The original data on myosin I in Dictyostelium showed that deletion of these genes reduced the instantaneous velocity of these cells. This paper shows that this is probably due to excess turning which is the result of too many pseudopods being produced adjacent to the substratum. This points to a role for this class in suppression of membrane extensions.
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Wessels D, Titus MA, Soll DR. A Dictyostelium myosin I plays a crucial role in regulating the frequency of pseudopods formed on the substratum. of special interest Cell Motil Cytoskeleton. 33:1996;64-79 The original data on myosin I in Dictyostelium showed that deletion of these genes reduced the instantaneous velocity of these cells. This paper shows that this is probably due to excess turning which is the result of too many pseudopods being produced adjacent to the substratum. This points to a role for this class in suppression of membrane extensions.
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(1996)
Cell Motil Cytoskeleton
, vol.33
, pp. 64-79
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Wessels, D.1
Titus, M.A.2
Soll, D.R.3
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36
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0029750192
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Function of myosin-V in filopodial extension of neuronal growth cones
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of special interest. A novel method of studying myosin function using microCALI. These authors attach a light sensitive probe to a specific antibody. When this probe is irradiated, it becomes toxic to proteins attached to the antibody. This allows study in small areas and short time scales. The authors use this to inhibit both myosin I and myosin V in growth cones.
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Wang FS, Wolenski JS, Cheney RE, Mooseker MS, Jay DG. Function of myosin-V in filopodial extension of neuronal growth cones. of special interest Science. 273:1996;660-663 A novel method of studying myosin function using microCALI. These authors attach a light sensitive probe to a specific antibody. When this probe is irradiated, it becomes toxic to proteins attached to the antibody. This allows study in small areas and short time scales. The authors use this to inhibit both myosin I and myosin V in growth cones.
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(1996)
Science
, vol.273
, pp. 660-663
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Wang, F.S.1
Wolenski, J.S.2
Cheney, R.E.3
Mooseker, M.S.4
Jay, D.G.5
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37
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0028838302
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Dictyostelium myosin I double mutants exhibit conditional defects in pinocytosis
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Novak KD, Peterson MD, Reedy MC, Titus MA. Dictyostelium myosin I double mutants exhibit conditional defects in pinocytosis. J Cell Biol. 131:1995;1205-1221.
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(1995)
J Cell Biol
, vol.131
, pp. 1205-1221
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Novak, K.D.1
Peterson, M.D.2
Reedy, M.C.3
Titus, M.A.4
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38
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0029925627
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Dictyostelium mutants lacking multiple classic myosin I isoforms reveal combinations of shared and distinct functions
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Jung G, Wu X, Hammer JA III. Dictyostelium mutants lacking multiple classic myosin I isoforms reveal combinations of shared and distinct functions. J Cell Biol. 133:1996;305-323.
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(1996)
J Cell Biol
, vol.133
, pp. 305-323
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Jung, G.1
Wu, X.2
Hammer J.A. III3
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39
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0031046060
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Fluid-phase uptake by macropinocytosis in Dictyostelium
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Hacker U, Albrecht R, Maniak M. Fluid-phase uptake by macropinocytosis in Dictyostelium. J Cell Sci. 110:1997;105-112.
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(1997)
J Cell Sci
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Hacker, U.1
Albrecht, R.2
Maniak, M.3
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40
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0031045035
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Myosin I overexpression impairs cell migration
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Novak KD, Titus MA. Myosin I overexpression impairs cell migration. J Cell Biol. 136:1997;633-648.
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(1997)
J Cell Biol
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Novak, K.D.1
Titus, M.A.2
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41
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0029923034
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Role of type I myosins in receptor-mediated endocytosis in yeast
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Geli MI, Riezman H. Role of type I myosins in receptor-mediated endocytosis in yeast. Science. 272:1996;533-535.
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Science
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Geli, M.I.1
Riezman, H.2
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42
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0029984773
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Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): Myosin I proteins are required for polarization of the actin cytoskeleton
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Goodson HV, Anderson BL, Warrick HM, Pon LA, Spudich JA. Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): myosin I proteins are required for polarization of the actin cytoskeleton. J Cell Biol. 133:1996;1277-1291.
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(1996)
J Cell Biol
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Goodson, H.V.1
Anderson, B.L.2
Warrick, H.M.3
Pon, L.A.4
Spudich, J.A.5
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43
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0031977198
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Human myosin IXb is a mechanochemically active motor and GAP for rho
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of special interest. The first demonstration that myosin IX is a functional actin-based motor. These authors enrich for myosin IX by immunoaffinity precipitation of the native protein from tissue culture cells. They show that the entire protein has the same GAP activity as the expressed version. Even more importantly, they show that this motor is capable of moving along actin filaments
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Post PL, Bokoch GM, Mooseker MS. Human myosin IXb is a mechanochemically active motor and GAP for rho. of special interest J Cell Sci. 1998; The first demonstration that myosin IX is a functional actin-based motor. These authors enrich for myosin IX by immunoaffinity precipitation of the native protein from tissue culture cells. They show that the entire protein has the same GAP activity as the expressed version. Even more importantly, they show that this motor is capable of moving along actin filaments.
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(1998)
J Cell Sci
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Post, P.L.1
Bokoch, G.M.2
Mooseker, M.S.3
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44
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0039521743
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The rat myosin myr5 is a GTPase activating protein for rho in vivo: Essential role of arginine 1695
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of special interest. This paper presents the result of functional tests on the GAP domain in the myosin IX tail. They express the GAP domain alone and show that it specifically activates the GTPase activity of the RHO subfamily. Overexpression of this domain in either insect tissue or cultured rat kidney cells alters the actin distribution.
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Müller RT, Honnert U, Reinhard J, Bähler M. The rat myosin myr5 is a GTPase activating protein for rho in vivo: essential role of arginine 1695. of special interest Mol Biol Cell. 8:1997;2039-2053 This paper presents the result of functional tests on the GAP domain in the myosin IX tail. They express the GAP domain alone and show that it specifically activates the GTPase activity of the RHO subfamily. Overexpression of this domain in either insect tissue or cultured rat kidney cells alters the actin distribution.
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(1997)
Mol Biol Cell
, vol.8
, pp. 2039-2053
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Müller, R.T.1
Honnert, U.2
Reinhard, J.3
Bähler, M.4
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45
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0031551570
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A family of unconventional myosins from the nematode Caenorhabditis elegans
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Baker JP, Titus MA. A family of unconventional myosins from the nematode Caenorhabditis elegans. J Mol Biol. 272:1997;523-535.
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(1997)
J Mol Biol
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Baker, J.P.1
Titus, M.A.2
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46
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0030587490
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Molecular cloning and domain structure of human myosin-VIIa, the gene product defective in Usher syndrome
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Chen ZY, Hasson T, Kelley PM, Schwender BJ, Schwartz MF, Ramakrishnan M, Kimberling WJ, Mooseker MS, Corey DP. Molecular cloning and domain structure of human myosin-VIIa, the gene product defective in Usher syndrome. Genomics. 36:1996;440-448.
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(1996)
Genomics
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Chen, Z.Y.1
Hasson, T.2
Kelley, P.M.3
Schwender, B.J.4
Schwartz, M.F.5
Ramakrishnan, M.6
Kimberling, W.J.7
Mooseker, M.S.8
Corey, D.P.9
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47
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9244233852
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Human myosin VIIA responsible for Usher 1B syndrome: A predicted membrane-associated motor protein expressed in developing sensory epithelia
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Weil D, Lévy G, sahly I, Lévi-Acobas F, Blanchard S, El-Amraoui A, Crozet F, Phillipe H, Abitbol M, Petit C. Human myosin VIIA responsible for Usher 1B syndrome: a predicted membrane-associated motor protein expressed in developing sensory epithelia. Proc Natl Acad Sci USA. 93:1996;3232-3237.
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(1996)
Proc Natl Acad Sci USA
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, pp. 3232-3237
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Weil, D.1
Lévy, G.2
Sahly, I.3
Lévi-Acobas, F.4
Blanchard, S.5
El-Amraoui, A.6
Crozet, F.7
Phillipe, H.8
Abitbol, M.9
Petit, C.10
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48
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0031559564
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A novel class of unconventional myosins from Toxoplasma gondii
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Heintzelman MB, Schwartzman JD. A novel class of unconventional myosins from Toxoplasma gondii. J Mol Biol. 271:1997;139-146.
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J Mol Biol
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Heintzelman, M.B.1
Schwartzman, J.D.2
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50
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0030174870
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The chsD and chsE genes of Aspergillus nidulans and their roles in chitin synthesis
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Specht CA, Liu Y, Robbins PW, Bulawa CE, Iartchouk N, Winter KR, Riggle PJ, Rhodes JC, Dodge CL, Culp DW, et al. The chsD and chsE genes of Aspergillus nidulans and their roles in chitin synthesis. Fungal Genet Biol. 20:1996;153-167.
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(1996)
Fungal Genet Biol
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Specht, C.A.1
Liu, Y.2
Robbins, P.W.3
Bulawa, C.E.4
Iartchouk, N.5
Winter, K.R.6
Riggle, P.J.7
Rhodes, J.C.8
Dodge, C.L.9
Culp, D.W.10
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51
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0028860302
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A type VII myosin encoded by the mouse deafness gene shaker-1
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Gibson F, Walsh J, Mburu P, Varela A, Brown KA, Antonio M, Beisel KW, Steel KP, Brown SDM. A type VII myosin encoded by the mouse deafness gene shaker-1. Nature. 374:1995;62-64.
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(1995)
Nature
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Gibson, F.1
Walsh, J.2
Mburu, P.3
Varela, A.4
Brown, K.A.5
Antonio, M.6
Beisel, K.W.7
Steel, K.P.8
Brown, S.D.M.9
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52
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0028815440
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Defective myosin VIIa gene responsible for Usher syndrome type 1B
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Weil D, Blanchard S, Kaplan J, Guliford P, Gibson F, Walsh J, Mburu P, Varela A, Levilliers J, Weston MD, et al. Defective myosin VIIa gene responsible for Usher syndrome type 1B. Nature. 374:1995;60-61.
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(1995)
Nature
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Weil, D.1
Blanchard, S.2
Kaplan, J.3
Guliford, P.4
Gibson, F.5
Walsh, J.6
Mburu, P.7
Varela, A.8
Levilliers, J.9
Weston, M.D.10
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