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0037177814
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Functional overlap between retinitis pigmentosa 2 protein and the tubulin-specific chaperone cofactor C
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Bartolini F., Bhamidipati A., Thomas S., Schwahn U., Lewis S.A., and Cowan N.J. Functional overlap between retinitis pigmentosa 2 protein and the tubulin-specific chaperone cofactor C J. Biol. Chem. 277 2002 14629 14634
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Lewis, S.A.5
Cowan, N.J.6
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2
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0034729382
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ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin
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Bhamidipati A., Lewis S.A., and Cowan N.J. ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin J. Cell Biol. 149 2000 1087 1096
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Bhamidipati, A.1
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18344391605
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A comprehensive mutation analysis of RP2 and RPGR in a North American cohort of families with X-linked retinitis pigmentosa
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Breuer D.K., Yashar B.M., Filippova E., Hiriyanna S., Lyons R.H., Mears A.J., Asaye B., Acar C., Vervoort R., Wright A.F., Musarella M.A., Wheeler P., MacDonald I., Iannaccone A., Birch D., Hoffman D.R., Fishman G.A., Heckenlively J.R., Jacobson S.G., Sieving P.A., and Swaroop A. A comprehensive mutation analysis of RP2 and RPGR in a North American cohort of families with X-linked retinitis pigmentosa Am. J. Hum. Genet. 70 2002 1545 1554
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Mears, A.J.6
Asaye, B.7
Acar, C.8
Vervoort, R.9
Wright, A.F.10
Musarella, M.A.11
Wheeler, P.12
MacDonald, I.13
Iannaccone, A.14
Birch, D.15
Hoffman, D.R.16
Fishman, G.A.17
Heckenlively, J.R.18
Jacobson, S.G.19
Sieving, P.A.20
Swaroop, A.21
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4
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0034641595
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Mutations in the N-terminus of the X-linked retinitis pigmentosa protein RP2 interfere with the normal targeting of the protein to the plasma membrane
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Chapple J.P., Hardcastle A.J., Grayson C., Spackman L.A., Willison K.R., and Cheetham M.E. Mutations in the N-terminus of the X-linked retinitis pigmentosa protein RP2 interfere with the normal targeting of the protein to the plasma membrane Hum. Mol. Genet. 9 2000 1919 1926
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Chapple, J.P.1
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Grayson, C.3
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Willison, K.R.5
Cheetham, M.E.6
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5
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0036276367
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Delineation of the plasma membrane targeting domain of the X-linked retinitis pigmentosa protein RP2
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Chapple J.P., Hardcastle A.J., Grayson C., Willison K.R., and Cheetham M.E. Delineation of the plasma membrane targeting domain of the X-linked retinitis pigmentosa protein RP2 Invest. Ophthalmol. Vis. Sci. 43 2002 2015 2020
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Chapple, J.P.1
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Grayson, C.3
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Cheetham, M.E.5
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6
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0038000559
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Organization on the plasma membrane of the retinitis pigmentosa protein RP2: Investigation of association with detergent-resistant membranes and polarized sorting
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Chapple J.P., Grayson C., Hardcastle A.J., Bailey T.A., Matter K., Adamson P., Graham C.H., Willison K.R., and Cheetham M.E. Organization on the plasma membrane of the retinitis pigmentosa protein RP2: Investigation of association with detergent-resistant membranes and polarized sorting Biochem. J. 372 2003 427 433
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Chapple, J.P.1
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Adamson, P.6
Graham, C.H.7
Willison, K.R.8
Cheetham, M.E.9
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7
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0034084213
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LdARL-3A, a Leishmania promastigote-specific ADP-ribosylation factor-like protein, is essential for flagellum integrity
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Cuvillier A., Redon F., Antoine J.C., Chardin P., DeVos T., and Merlin G. LdARL-3A, a Leishmania promastigote-specific ADP-ribosylation factor-like protein, is essential for flagellum integrity J. Cell Sci. 113 2000 2065 2074
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Cuvillier, A.1
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12144291356
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An atypical phenotype of macular and peripapillary retinal atrophy caused by a mutation in the RP2 gene
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Dandekar S.S., Ebenezer N.D., Grayson C., Chapple J.P., Egan C.A., Holder G.E., Jenkins S.A., Fitzke F.W., Cheetham M.E., Webster A.R., and Hardcastle A.J. An atypical phenotype of macular and peripapillary retinal atrophy caused by a mutation in the RP2 gene Br. J. Ophthalmol. 88 2004 528 532
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Dandekar, S.S.1
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Holder, G.E.6
Jenkins, S.A.7
Fitzke, F.W.8
Cheetham, M.E.9
Webster, A.R.10
Hardcastle, A.J.11
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9
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1842869139
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Localization in the human retina of the X-linked retinitis pigmentosa protein RP2, its homologue cofactor C and the RP2 interacting protein Arl3
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Grayson C., Bartolini F., Chapple J.P., Willison K.R., Bhamidipati A., Lewis S.A., Luthert P.J., Hardcastle A.J., Cowan N.J., and Cheetham M.E. Localization in the human retina of the X-linked retinitis pigmentosa protein RP2, its homologue cofactor C and the RP2 interacting protein Arl3 Hum. Mol. Genet. 11 2002 3065 3074
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Luthert, P.J.7
Hardcastle, A.J.8
Cowan, N.J.9
Cheetham, M.E.10
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10
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0033361920
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Mutations in the RP2 gene cause disease in 10% of families with familial X-linked retinitis pigmentosa assessed in this study
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Hardcastle A.J., Thiselton D.L., Van Maldergem L., Saha B.K., Jay M., Plant C., Taylor R., Bird A.C., and Bhattacharya S. Mutations in the RP2 gene cause disease in 10% of families with familial X-linked retinitis pigmentosa assessed in this study Am. J. Hum. Genet. 64 1999 1210 1215
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Jay, M.5
Plant, C.6
Taylor, R.7
Bird, A.C.8
Bhattacharya, S.9
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11
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0033573083
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Functionally different GPI proteins are organized in different domains on the neuronal surface
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Madore N., Smith K.L., Graham C.H., Jen A., Brady K., Hall S., and Morris R. Functionally different GPI proteins are organized in different domains on the neuronal surface EMBO J. 18 1999 6917 6926
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Genotype-phenotype correlation in X-linked retinitis pigmentosa 2 (RP2)
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Rosenberg T., Schwahn U., Feil S., and Berger W. Genotype-phenotype correlation in X-linked retinitis pigmentosa 2 (RP2) Ophthalmic Genet. 20 1999 161 172
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Positional cloning of the gene for X-linked retinitis pigmentosa 2
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Schwahn U., Lenzner S., Dong J., Feil S., Hinzmann B., van Duijnhoven G., Kirschner R., Hemberger M., Bergen A.A., Rosenberg T., Pinckers A.J., Fundele R., Rosenthal A., Cremers F.P., Ropers H.H., and Berger W. Positional cloning of the gene for X-linked retinitis pigmentosa 2 Nature Genet. 19 1998 327 332
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Kirschner, R.7
Hemberger, M.8
Bergen, A.A.9
Rosenberg, T.10
Pinckers, A.J.11
Fundele, R.12
Rosenthal, A.13
Cremers, F.P.14
Ropers, H.H.15
Berger, W.16
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14
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0035872885
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Mutations in the X-linked RP2 gene cause intracellular misrouting and loss of the protein
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Schwahn U., Paland N., Techritz S., Lenzner S., and Berger W. Mutations in the X-linked RP2 gene cause intracellular misrouting and loss of the protein Hum. Mol. Genet. 10 2001 1177 1183
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Schwahn, U.1
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15
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0142039933
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Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A
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Shern J.F., Sharer J.D., Pallas D.C., Bartolini F., Cowan N.J., Reed M.S., Pohl J., and Kahn R.A. Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A J. Biol. Chem. 278 2003 40829 40836
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Kahn, R.A.8
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16
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Pathway leading to correctly folded beta-tubulin
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Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors
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Tian G., Lewis S.A., Feierbach B., Stearns T., Rommelaere H., Ampe C., and Cowan N.J. Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors J. Cell Biol. 138 1997 821 832
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0033588020
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Tubulin folding cofactors as GTPase-activating proteins: GTP hydrolysis and the assembly of the alpha/beta-tubulin heterodimer
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Tian G., Bhamidipati A., Cowan N.J., and Lewis S.A. Tubulin folding cofactors as GTPase-activating proteins: GTP hydrolysis and the assembly of the alpha/beta-tubulin heterodimer J. Biol. Chem. 274 1999 24054 24058
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