메뉴 건너뛰기




Volumn 71, Issue 3, 2014, Pages 517-538

The nucleotide-binding proteins Nubp1 and Nubp2 are negative regulators of ciliogenesis

Author keywords

CCT TRiC complex; Ciliogenesis; Molecular chaperones; Motor proteins; Primary cilium

Indexed keywords

AURORA A KINASE; CENEXIN; CHAPERONE; CHIBBY PROTEIN; MEMBRANE PROTEIN; NUCLEOTIDE BINDING PROTEIN; PROTEIN CEP290; PROTEIN CP110; PROTEIN NUBP1; PROTEIN NUBP2; PROTEIN RAB8; UNCLASSIFIED DRUG;

EID: 84892802478     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-013-1401-6     Document Type: Article
Times cited : (22)

References (103)
  • 1
    • 33846785192 scopus 로고    scopus 로고
    • Centriole/basal body morphogenesis and migration during ciliogenesis in animal cells
    • DOI 10.1242/jcs.03305
    • Dawe HR, Farr H, Gull K (2007) Centriole/basal body morphogenesis and migration during ciliogenesis in animal cells. J Cell Sci 120(Pt 1):7-15 (Pubitemid 46206644)
    • (2007) Journal of Cell Science , vol.120 , Issue.1 , pp. 7-15
    • Dawe, H.R.1    Farr, H.2    Gull, K.3
  • 3
    • 63049116544 scopus 로고    scopus 로고
    • The vertebrate primary cilium in development, homeostasis, and disease
    • 1:CAS:528:DC%2BD1MXls1Srsr0%3D 3016012 19345185 10.1016/j.cell.2009.03. 023
    • Gerdes JM, Davis EE, Katsanis N (2009) The vertebrate primary cilium in development, homeostasis, and disease. Cell 137(1):32-45
    • (2009) Cell , vol.137 , Issue.1 , pp. 32-45
    • Gerdes, J.M.1    Davis, E.E.2    Katsanis, N.3
  • 4
    • 76649096673 scopus 로고    scopus 로고
    • The primary cilium at a glance
    • 1:CAS:528:DC%2BC3cXjs1Kkurs%3D 20144997 10.1242/jcs.050377
    • Satir P, Pedersen LB, Christensen ST (2010) The primary cilium at a glance. J Cell Sci 123(Pt 4):499-503
    • (2010) J Cell Sci , vol.123 , Issue.PART 4 , pp. 499-503
    • Satir, P.1    Pedersen, L.B.2    Christensen, S.T.3
  • 5
    • 76649103368 scopus 로고    scopus 로고
    • The perennial organelle: Assembly and disassembly of the primary cilium
    • 1:CAS:528:DC%2BC3cXjs1Kkurk%3D 20144999 10.1242/jcs.061093
    • Seeley ES, Nachury MV (2010) The perennial organelle: assembly and disassembly of the primary cilium. J Cell Sci 123(Pt 4):511-518
    • (2010) J Cell Sci , vol.123 , Issue.PART 4 , pp. 511-518
    • Seeley, E.S.1    Nachury, M.V.2
  • 6
    • 33846211025 scopus 로고    scopus 로고
    • Sensory Cilia and integration of signal transduction in human health and disease
    • DOI 10.1111/j.1600-0854.2006.00516.x
    • Christensen ST, Pedersen LB, Schneider L, Satir P (2007) Sensory cilia and integration of signal transduction in human health and disease. Traffic 8(2):97-109 (Pubitemid 46099997)
    • (2007) Traffic , vol.8 , Issue.2 , pp. 97-109
    • Christensen, S.T.1    Pedersen, L.B.2    Schneider, L.3    Satir, P.4
  • 8
    • 77951101203 scopus 로고    scopus 로고
    • The primary cilium: A signalling centre during vertebrate development
    • 1:CAS:528:DC%2BC3cXkvVSqs74%3D 3121168 20395968 10.1038/nrg2774
    • Goetz SC, Anderson KV (2010) The primary cilium: a signalling centre during vertebrate development. Nat Rev Genet 11(5):331-344
    • (2010) Nat Rev Genet , vol.11 , Issue.5 , pp. 331-344
    • Goetz, S.C.1    Anderson, K.V.2
  • 9
    • 79551587194 scopus 로고    scopus 로고
    • Strange as it may seem: The many links between Wnt signaling, planar cell polarity, and cilia
    • 1:CAS:528:DC%2BC3MXisVehsbo%3D 21289065 10.1101/gad.2008011
    • Wallingford JB, Mitchell B (2011) Strange as it may seem: the many links between Wnt signaling, planar cell polarity, and cilia. Genes Dev 25(3):201-213
    • (2011) Genes Dev , vol.25 , Issue.3 , pp. 201-213
    • Wallingford, J.B.1    Mitchell, B.2
  • 10
    • 77249159842 scopus 로고    scopus 로고
    • Centriole maturation and transformation to basal body
    • 19595783 10.1016/j.semcdb.2009.07.002
    • Hoyer-Fender S (2010) Centriole maturation and transformation to basal body. Semin Cell Dev Biol 21(2):142-147
    • (2010) Semin Cell Dev Biol , vol.21 , Issue.2 , pp. 142-147
    • Hoyer-Fender, S.1
  • 12
    • 0015385636 scopus 로고
    • The three-dimensional structure of the basal body from the rhesus monkey oviduct
    • 1:STN:280:DyaE383isleisA%3D%3D 5064817 10.1083/jcb.54.2.246
    • Anderson RG (1972) The three-dimensional structure of the basal body from the rhesus monkey oviduct. J Cell Biol 54(2):246-265
    • (1972) J Cell Biol , vol.54 , Issue.2 , pp. 246-265
    • Anderson, R.G.1
  • 13
    • 0035899865 scopus 로고    scopus 로고
    • Localization of intraflagellar transport protein IFT52 identifies basal body transitional fibers as the docking site for IFT particles
    • DOI 10.1016/S0960-9822(01)00484-5
    • Deane JA, Cole DG, Seeley ES, Diener DR, Rosenbaum JL (2001) Localization of intraflagellar transport protein IFT52 identifies basal body transitional fibers as the docking site for IFT particles. Curr Biol 11(20):1586-1590 (Pubitemid 32978523)
    • (2001) Current Biology , vol.11 , Issue.20 , pp. 1586-1590
    • Deane, J.A.1    Cole, D.G.2    Seeley E.Scott3    Diener, D.R.4    Rosenbaum, J.L.5
  • 14
    • 77954841928 scopus 로고    scopus 로고
    • A septin diffusion barrier at the base of the primary cilium maintains ciliary membrane protein distribution
    • 1:CAS:528:DC%2BC3cXptVWgtr4%3D 3092790 20558667 10.1126/science.1191054
    • Hu Q, Milenkovic L, Jin H, Scott MP, Nachury MV, Spiliotis ET, Nelson WJ (2010) A septin diffusion barrier at the base of the primary cilium maintains ciliary membrane protein distribution. Science 329(5990):436-439
    • (2010) Science , vol.329 , Issue.5990 , pp. 436-439
    • Hu, Q.1    Milenkovic, L.2    Jin, H.3    Scott, M.P.4    Nachury, M.V.5    Spiliotis, E.T.6    Nelson, W.J.7
  • 16
    • 34547939469 scopus 로고    scopus 로고
    • Cep97 and CP110 Suppress a Cilia Assembly Program
    • DOI 10.1016/j.cell.2007.06.027, PII S0092867407007945
    • Spektor A, Tsang WY, Khoo D, Dynlacht BD (2007) Cep97 and CP110 suppress a cilia assembly program. Cell 130(4):678-690 (Pubitemid 47268052)
    • (2007) Cell , vol.130 , Issue.4 , pp. 678-690
    • Spektor, A.1    Tsang, W.Y.2    Khoo, D.3    Dynlacht, B.D.4
  • 17
    • 48549102438 scopus 로고    scopus 로고
    • CP110 suppresses primary cilia formation through its interaction with CEP290, a protein deficient in human ciliary disease
    • 1:CAS:528:DC%2BD1cXhtVehtL7F 18694559 10.1016/j.devcel.2008.07.004
    • Tsang WY, Bossard C, Khanna H, Peranen J, Swaroop A, Malhotra V, Dynlacht BD (2008) CP110 suppresses primary cilia formation through its interaction with CEP290, a protein deficient in human ciliary disease. Dev Cell 15(2):187-197
    • (2008) Dev Cell , vol.15 , Issue.2 , pp. 187-197
    • Tsang, W.Y.1    Bossard, C.2    Khanna, H.3    Peranen, J.4    Swaroop, A.5    Malhotra, V.6    Dynlacht, B.D.7
  • 18
    • 56049117628 scopus 로고    scopus 로고
    • CEP290 interacts with the centriolar satellite component PCM-1 and is required for Rab8 localization to the primary cilium
    • 1:CAS:528:DC%2BD1cXhtlGis7%2FI 18772192 10.1093/hmg/ddn277
    • Kim J, Krishnaswami SR, Gleeson JG (2008) CEP290 interacts with the centriolar satellite component PCM-1 and is required for Rab8 localization to the primary cilium. Hum Mol Genet 17(23):3796-3805
    • (2008) Hum Mol Genet , vol.17 , Issue.23 , pp. 3796-3805
    • Kim, J.1    Krishnaswami, S.R.2    Gleeson, J.G.3
  • 19
    • 34250758641 scopus 로고    scopus 로고
    • HEF1-Dependent Aurora A Activation Induces Disassembly of the Primary Cilium
    • DOI 10.1016/j.cell.2007.04.035, PII S0092867407005466
    • Pugacheva EN, Jablonski SA, Hartman TR, Henske EP, Golemis EA (2007) HEF1-dependent Aurora A activation induces disassembly of the primary cilium. Cell 129(7):1351-1363 (Pubitemid 46962087)
    • (2007) Cell , vol.129 , Issue.7 , pp. 1351-1363
    • Pugacheva, E.N.1    Jablonski, S.A.2    Hartman, T.R.3    Henske, E.P.4    Golemis, E.A.5
  • 20
    • 84865803552 scopus 로고    scopus 로고
    • The BBSome controls IFT assembly and turnaround in cilia
    • 3434251 22922713 10.1038/ncb2560
    • Wei Q, Zhang Y, Li Y, Zhang Q, Ling K, Hu J (2012) The BBSome controls IFT assembly and turnaround in cilia. Nat Cell Biol 14(9):950-957
    • (2012) Nat Cell Biol , vol.14 , Issue.9 , pp. 950-957
    • Wei, Q.1    Zhang, Y.2    Li, Y.3    Zhang, Q.4    Ling, K.5    Hu, J.6
  • 21
    • 23144445446 scopus 로고    scopus 로고
    • Functional coordination of intraflagellar transport motors
    • DOI 10.1038/nature03818
    • Ou G, Blacque OE, Snow JJ, Leroux MR, Scholey JM (2005) Functional coordination of intraflagellar transport motors. Nature 436(7050):583-587 (Pubitemid 41112934)
    • (2005) Nature , vol.436 , Issue.7050 , pp. 583-587
    • Ou, G.1    Blacque, O.E.2    Snow, J.J.3    Leroux, M.R.4    Scholey, J.M.5
  • 22
    • 33646164168 scopus 로고    scopus 로고
    • Intraflagellar transport and cilium-based signaling
    • 1:CAS:528:DC%2BD28XkslCjtL8%3D 16678091 10.1016/j.cell.2006.04.013
    • Scholey JM, Anderson KV (2006) Intraflagellar transport and cilium-based signaling. Cell 125(3):439-442
    • (2006) Cell , vol.125 , Issue.3 , pp. 439-442
    • Scholey, J.M.1    Anderson, K.V.2
  • 23
    • 58149326846 scopus 로고    scopus 로고
    • Intraflagellar transport (IFT) role in ciliary assembly, resorption and signalling
    • 1:CAS:528:DC%2BD1MXpsVensLY%3D 19147001
    • Pedersen LB, Rosenbaum JL (2008) Intraflagellar transport (IFT) role in ciliary assembly, resorption and signalling. Curr Top Dev Biol 85:23-61
    • (2008) Curr Top Dev Biol , vol.85 , pp. 23-61
    • Pedersen, L.B.1    Rosenbaum, J.L.2
  • 24
    • 67649635952 scopus 로고    scopus 로고
    • Intraflagellar transport and the generation of dynamic, structurally and functionally diverse cilia
    • 1:CAS:528:DC%2BD1MXosVGjtr4%3D 19560357 10.1016/j.tcb.2009.04.002
    • Silverman MA, Leroux MR (2009) Intraflagellar transport and the generation of dynamic, structurally and functionally diverse cilia. Trends Cell Biol 19(7):306-316
    • (2009) Trends Cell Biol , vol.19 , Issue.7 , pp. 306-316
    • Silverman, M.A.1    Leroux, M.R.2
  • 25
    • 0035913964 scopus 로고    scopus 로고
    • Cell cycle: The mitotic spindle: A self-made machine
    • DOI 10.1126/science.1063488
    • Karsenti E, Vernos I (2001) The mitotic spindle: a self-made machine. Science 294(5542):543-547 (Pubitemid 32999544)
    • (2001) Science , vol.294 , Issue.5542 , pp. 543-547
    • Karsenti, E.1    Vernos, I.2
  • 26
    • 0027098030 scopus 로고
    • Polarity of flagellar assembly in Chlamydomonas
    • DOI 10.1083/jcb.119.6.1605
    • Johnson KA, Rosenbaum JL (1992) Polarity of flagellar assembly in Chlamydomonas. J Cell Biol 119(6):1605-1611 (Pubitemid 23006557)
    • (1992) Journal of Cell Biology , vol.119 , Issue.6 , pp. 1605-1612
    • Johnson, K.A.1    Rosenbaum, J.L.2
  • 27
    • 0035851915 scopus 로고    scopus 로고
    • Intraflagellar transport balances continuous turnover of outer doublet microtubules: Implications for flagellar length control
    • Marshall WF, Rosenbaum JL (2001) Intraflagellar transport balances continuous turnover of outer doublet microtubules: implications for flagellar length control. J Cell Biol 155(3):405-414 (Pubitemid 34289331)
    • (2001) Journal of Cell Biology , vol.155 , Issue.4 , pp. 405-414
    • Marshall, W.F.1    Rosenbaum, J.L.2
  • 28
    • 41149156427 scopus 로고    scopus 로고
    • Tracking the ends: A dynamic protein network controls the fate of microtubule tips
    • DOI 10.1038/nrm2369, PII NRM2369
    • Akhmanova A, Steinmetz MO (2008) Tracking the ends: a dynamic protein network controls the fate of microtubule tips. Nat Rev Mol Cell Biol 9(4):309-322 (Pubitemid 351430849)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.4 , pp. 309-322
    • Akhmanova, A.1    Steinmetz, M.O.2
  • 29
    • 0035906940 scopus 로고    scopus 로고
    • Microtubule "plus-end-tracking proteins": The end is just the beginning
    • DOI 10.1016/S0092-8674(01)00364-6
    • Schuyler SC, Pellman D (2001) Microtubule "plus-end-tracking proteins": the end is just the beginning. Cell 105(4):421-424 (Pubitemid 32520848)
    • (2001) Cell , vol.105 , Issue.4 , pp. 421-424
    • Schuyler, S.C.1    Pellman, D.2
  • 30
    • 27544464474 scopus 로고    scopus 로고
    • TIP maker and TIP marker; EB1 as a master controller of microtubule plus ends
    • DOI 10.1083/jcb.200509150
    • Vaughan KT (2005) TIP maker and TIP marker; EB1 as a master controller of microtubule plus ends. J Cell Biol 171(2):197-200 (Pubitemid 41540012)
    • (2005) Journal of Cell Biology , vol.171 , Issue.2 , pp. 197-200
    • Vaughan, K.T.1
  • 31
    • 34347211354 scopus 로고    scopus 로고
    • EB1 Is Required for Primary Cilia Assembly in Fibroblasts
    • DOI 10.1016/j.cub.2007.05.055, PII S0960982207014790
    • Schrøder JM, Schneider L, Christensen ST, Pedersen LB (2007) EB1 is required for primary cilia assembly in fibroblasts. Curr Biol 17(13):1134-1139 (Pubitemid 46992829)
    • (2007) Current Biology , vol.17 , Issue.13 , pp. 1134-1139
    • Schroder, J.M.1    Schneider, L.2    Christensen, S.T.3    Pedersen, L.B.4
  • 33
    • 36949033246 scopus 로고    scopus 로고
    • Two families of chaperonin: Physiology and mechanism
    • 1:CAS:528:DC%2BD2sXhtlartrzE 17489689 10.1146/annurev.cellbio.23.090506. 123555
    • Horwich AL, Fenton WA, Chapman E, Farr GW (2007) Two families of chaperonin: physiology and mechanism. Annu Rev Cell Dev Biol 23:115-145
    • (2007) Annu Rev Cell Dev Biol , vol.23 , pp. 115-145
    • Horwich, A.L.1    Fenton, W.A.2    Chapman, E.3    Farr, G.W.4
  • 35
    • 0026650749 scopus 로고
    • TCP1 complex is a molecular chaperone in tubulin biogenesis
    • 1:CAS:528:DyaK38XlsVGnt7s%3D 1630491 10.1038/358245a0
    • Yaffe MB, Farr GW, Miklos D, Horwich AL, Sternlicht ML, Sternlicht H (1992) TCP1 complex is a molecular chaperone in tubulin biogenesis. Nature 358(6383):245-248
    • (1992) Nature , vol.358 , Issue.6383 , pp. 245-248
    • Yaffe, M.B.1    Farr, G.W.2    Miklos, D.3    Horwich, A.L.4    Sternlicht, M.L.5    Sternlicht, H.6
  • 36
    • 0026776331 scopus 로고
    • A cytoplasmic chaperonin that catalyzes beta-actin folding
    • 1:CAS:528:DyaK38XksVejtrc%3D 1351421 10.1016/0092-8674(92)90622-J
    • Gao Y, Thomas JO, Chow RL, Lee GH, Cowan NJ (1992) A cytoplasmic chaperonin that catalyzes beta-actin folding. Cell 69(6):1043-1050
    • (1992) Cell , vol.69 , Issue.6 , pp. 1043-1050
    • Gao, Y.1    Thomas, J.O.2    Chow, R.L.3    Lee, G.H.4    Cowan, N.J.5
  • 37
    • 0027293897 scopus 로고
    • Chaperonin-mediated folding of vertebrate actin-related protein and γ- tubulin
    • Melki R, Vainberg IE, Chow RL, Cowan NJ (1993) Chaperonin-mediated folding of vertebrate actin-related protein and gamma-tubulin. J Cell Biol 122(6):1301-1310 (Pubitemid 23277299)
    • (1993) Journal of Cell Biology , vol.122 , Issue.6 , pp. 1301-1310
    • Melki, R.1    Vainberg, I.E.2    Chow, R.L.3    Cowan, N.J.4
  • 38
    • 0028867374 scopus 로고
    • Identification of a molecular chaperone in the eukaryotic flagellum and its localization to the site of microtubule assembly
    • 1:CAS:528:DyaK2MXptlKrsrg%3D 8586665
    • Bloch MA, Johnson KA (1995) Identification of a molecular chaperone in the eukaryotic flagellum and its localization to the site of microtubule assembly. J Cell Sci 108(Pt 11):3541-3545
    • (1995) J Cell Sci , vol.108 , Issue.PART 11 , pp. 3541-3545
    • Bloch, M.A.1    Johnson, K.A.2
  • 41
    • 77956273128 scopus 로고    scopus 로고
    • CCTalpha and CCTdelta chaperonin subunits are essential and required for cilia assembly and maintenance in Tetrahymena
    • 2872681 20502701 10.1371/journal.pone.0010704
    • Seixas C, Cruto T, Tavares A, Gaertig J, Soares H (2010) CCTalpha and CCTdelta chaperonin subunits are essential and required for cilia assembly and maintenance in Tetrahymena. PLoS One 5(5):e10704
    • (2010) PLoS One , vol.5 , Issue.5 , pp. 10704
    • Seixas, C.1    Cruto, T.2    Tavares, A.3    Gaertig, J.4    Soares, H.5
  • 42
    • 76549121983 scopus 로고    scopus 로고
    • BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly
    • 1:CAS:528:DC%2BC3cXhslOrsro%3D 20080638 10.1073/pnas.0910268107
    • Seo S, Baye LM, Schulz NP, Beck JS, Zhang Q, Slusarski DC, Sheffield VC (2010) BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly. Proc Natl Acad Sci USA 107(4):1488-1493
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.4 , pp. 1488-1493
    • Seo, S.1    Baye, L.M.2    Schulz, N.P.3    Beck, J.S.4    Zhang, Q.5    Slusarski, D.C.6    Sheffield, V.C.7
  • 43
    • 42049111410 scopus 로고    scopus 로고
    • Cell cycle-dependent ciliogenesis and cancer
    • DOI 10.1158/0008-5472.CAN-07-5838
    • Plotnikova OV, Golemis EA, Pugacheva EN (2008) Cell cycle-dependent ciliogenesis and cancer. Cancer Res 68(7):2058-2061 (Pubitemid 351521774)
    • (2008) Cancer Research , vol.68 , Issue.7 , pp. 2058-2061
    • Plotnikova, O.V.1    Golemis, E.A.2    Pugacheva, E.N.3
  • 44
    • 68549096165 scopus 로고    scopus 로고
    • Centrosomes and cancer: How cancer cells divide with too many centrosomes
    • 10.1007/s10555-008-9163-6 1:CAS:528:DC%2BD1MXjsVWntr0%3D 19156503 10.1007/s10555-008-9163-6
    • Godinho SA, Kwon M, Pellman D (2009) Centrosomes and cancer: how cancer cells divide with too many centrosomes. Cancer Metastasis Rev 28(1-2):85-98. doi: 10.1007/s10555-008-9163-6
    • (2009) Cancer Metastasis Rev , vol.28 , Issue.1-2 , pp. 85-98
    • Godinho, S.A.1    Kwon, M.2    Pellman, D.3
  • 45
    • 80052411567 scopus 로고    scopus 로고
    • The life cycle of centrioles
    • 1:CAS:528:DC%2BC38XnsVOjtbY%3D 21502410 10.1101/sqb.2010.75.054
    • Hatch E, Stearns T (2010) The life cycle of centrioles. Cold Spring Harb Symp Quant Biol 75:425-431
    • (2010) Cold Spring Harb Symp Quant Biol , vol.75 , pp. 425-431
    • Hatch, E.1    Stearns, T.2
  • 46
    • 84866169462 scopus 로고    scopus 로고
    • Supernumerary centrosomes nucleate extra cilia and compromise primary cilium signaling
    • 1:CAS:528:DC%2BC38XhtFahsr3M 22840514 10.1016/j.cub.2012.06.057
    • Mahjoub MR, Stearns T (2012) Supernumerary centrosomes nucleate extra cilia and compromise primary cilium signaling. Curr Biol 22(17):1628-1634
    • (2012) Curr Biol , vol.22 , Issue.17 , pp. 1628-1634
    • Mahjoub, M.R.1    Stearns, T.2
  • 47
    • 0028145299 scopus 로고
    • Cloning of a human cDNA encoding a putative nucleotide-binding protein related to Escherichia coli MinD
    • DOI 10.1016/0378-1119(94)90082-5
    • Shahrestanifar M, Saha DP, Scala LA, Basu A, Howells RD (1994) Cloning of a human cDNA encoding a putative nucleotide-binding protein related to Escherichia coli MinD. Gene 147(2):281-285 (Pubitemid 24306346)
    • (1994) Gene , vol.147 , Issue.2 , pp. 281-285
    • Shahrestanifar, M.1    Saha, D.P.2    Scala, L.A.3    Basu, A.4    Howells, R.D.5
  • 48
    • 0033199354 scopus 로고    scopus 로고
    • Two novel mouse genes - Nubp2, mapped to the t-complex on chromosome 17, and Nubp1, mapped to chromosome 16 - Establish a new gene family of nucleotide-binding proteins in eukaryotes
    • DOI 10.1006/geno.1999.5898
    • Nakashima H, Grahovac MJ, Mazzarella R, Fujiwara H, Kitchen JR, Threat TA, Ko MS (1999) Two novel mouse genes-Nubp2, mapped to the t-complex on chromosome 17, and Nubp1, mapped to chromosome 16-establish a new gene family of nucleotide-binding proteins in eukaryotes. Genomics 60(2):152-160 (Pubitemid 29463673)
    • (1999) Genomics , vol.60 , Issue.2 , pp. 152-160
    • Nakashima, H.1    Grahovac, M.J.2    Mazzarella, R.3    Fujiwara, H.4    Kitchen, J.R.5    Threat, T.A.6    Ko, M.S.H.7
  • 49
    • 33745208485 scopus 로고    scopus 로고
    • Motor protein KIFC5A interacts with Nubp1 and Nubp2, and is implicated in the regulation of cetrosome duplication
    • DOI 10.1242/jcs.02922
    • Christodoulou A, Lederer CW, Surrey T, Vernos I, Santama N (2006) Motor protein KIFC5A interacts with Nubp1 and Nubp2, and is implicated in the regulation of centrosome duplication. J Cell Sci 119(Pt 10):2035-2047 (Pubitemid 43904958)
    • (2006) Journal of Cell Science , vol.119 , Issue.10 , pp. 2035-2047
    • Christodoulou, A.1    Lederer, C.W.2    Surrey, T.3    Vernos, I.4    Santama, N.5
  • 50
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • DOI 10.1006/jmbi.2001.5378
    • Leipe DD, Wolf YI, Koonin EV, Aravind L (2002) Classification and evolution of P-loop GTPases and related ATPases. J Mol Biol 317(1):41-72 (Pubitemid 34722199)
    • (2002) Journal of Molecular Biology , vol.317 , Issue.1 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 51
    • 0030608375 scopus 로고    scopus 로고
    • NBP35 encodes an essential and evolutionary conserved protein in Saccharomyces cerevisiae with homology to a superfamily of bacterial ATPases
    • DOI 10.1016/0378-1119(96)00341-1, PII S0378111996003411
    • Vitale G, Fabre E, Hurt EC (1996) NBP35 encodes an essential and evolutionary conserved protein in Saccharomyces cerevisiae with homology to a superfamily of bacterial ATPases. Gene 178(1-2):97-106 (Pubitemid 26377135)
    • (1996) Gene , vol.178 , Issue.1-2 , pp. 97-106
    • Vitale, G.1    Fabre, E.2    Hurt, E.C.3
  • 53
    • 34247247617 scopus 로고    scopus 로고
    • The Cfd1-Nbp35 complex acts as a scaffold for iron-sulfur protein assembly in the yeast cytosol
    • DOI 10.1038/nchembio872, PII NCHEMBIO872
    • Netz DJ, Pierik AJ, Stumpfig M, Muhlenhoff U, Lill R (2007) The Cfd1-Nbp35 complex acts as a scaffold for iron-sulfur protein assembly in the yeast cytosol. Nat Chem Biol 3(5):278-286 (Pubitemid 46625831)
    • (2007) Nature Chemical Biology , vol.3 , Issue.5 , pp. 278-286
    • Netz, D.J.A.1    Pierik, A.J.2    Stumpfig, M.3    Muhlenhoff, U.4    Lill, R.5
  • 54
    • 50249156530 scopus 로고    scopus 로고
    • Human Nbp35 is essential for both cytosolic iron-sulfur protein assembly and iron homeostasis
    • 1:CAS:528:DC%2BD1cXhtVersLjN 2519719 18573874 10.1128/MCB.00545-08
    • Stehling O, Netz DJ, Niggemeyer B, Rosser R, Eisenstein RS, Puccio H, Pierik AJ, Lill R (2008) Human Nbp35 is essential for both cytosolic iron-sulfur protein assembly and iron homeostasis. Mol Cell Biol 28(17):5517-5528
    • (2008) Mol Cell Biol , vol.28 , Issue.17 , pp. 5517-5528
    • Stehling, O.1    Netz, D.J.2    Niggemeyer, B.3    Rosser, R.4    Eisenstein, R.S.5    Puccio, H.6    Pierik, A.J.7    Lill, R.8
  • 55
    • 84859492661 scopus 로고    scopus 로고
    • A bridging [4Fe-4S] cluster and nucleotide binding are essential for function of the Cfd1-Nbp35 complex as a scaffold in iron-sulfur protein maturation
    • 1:CAS:528:DC%2BC38XltVyku7o%3D 22362766 10.1074/jbc.M111.328914
    • Netz DJ, Pierik AJ, Stumpfig M, Bill E, Sharma AK, Pallesen LJ, Walden WE, Lill R (2012) A bridging [4Fe-4S] cluster and nucleotide binding are essential for function of the Cfd1-Nbp35 complex as a scaffold in iron-sulfur protein maturation. J Biol Chem 287(15):12365-12378
    • (2012) J Biol Chem , vol.287 , Issue.15 , pp. 12365-12378
    • Netz, D.J.1    Pierik, A.J.2    Stumpfig, M.3    Bill, E.4    Sharma, A.K.5    Pallesen, L.J.6    Walden, W.E.7    Lill, R.8
  • 56
    • 0242625186 scopus 로고    scopus 로고
    • The Microtubule Plus End-Tracking Protein EB1 Is Localized to the Flagellar Tip and Basal Bodies in Chlamydomonas reinhardtii
    • DOI 10.1016/j.cub.2003.10.058
    • Pedersen LB, Geimer S, Sloboda RD, Rosenbaum JL (2003) The microtubule plus end-tracking protein EB1 is localized to the flagellar tip and basal bodies in Chlamydomonas reinhardtii. Curr Biol 13(22):1969-1974 (Pubitemid 37425206)
    • (2003) Current Biology , vol.13 , Issue.22 , pp. 1969-1974
    • Pedersen, L.B.1    Geimer, S.2    Sloboda, R.D.3    Rosenbaum, J.L.4
  • 57
    • 34047177462 scopus 로고    scopus 로고
    • The lissencephaly protein Lis1 is present in motile mammalian cilia and requires outer arm dynein for targeting to Chlamydomonas flagella
    • DOI 10.1242/jcs.03374
    • Pedersen LB, Rompolas P, Christensen ST, Rosenbaum JL, King SM (2007) The lissencephaly protein Lis1 is present in motile mammalian cilia and requires outer arm dynein for targeting to Chlamydomonas flagella. J Cell Sci 120(Pt 5):858-867 (Pubitemid 46523487)
    • (2007) Journal of Cell Science , vol.120 , Issue.5 , pp. 858-867
    • Pedersen, L.B.1    Rompolas, P.2    Christensen, S.T.3    Rosenbaum, J.L.4    King, S.M.5
  • 58
    • 77954240714 scopus 로고    scopus 로고
    • SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity through CP110 degradation
    • 2946399 20596027 10.1038/nature09140
    • D'Angiolella V, Donato V, Vijayakumar S, Saraf A, Florens L, Washburn MP, Dynlacht B, Pagano M (2010) SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity through CP110 degradation. Nature 466(7302):138-142
    • (2010) Nature , vol.466 , Issue.7302 , pp. 138-142
    • D'Angiolella, V.1    Donato, V.2    Vijayakumar, S.3    Saraf, A.4    Florens, L.5    Washburn, M.P.6    Dynlacht, B.7    Pagano, M.8
  • 59
    • 70349241932 scopus 로고    scopus 로고
    • Transgenesis in Caenorhabditis elegans
    • 1:CAS:528:DC%2BC3cXhvVKgtLc%3D 19504062 10.1007/978-1-60327-019-9-2
    • Rieckher M, Kourtis N, Pasparaki A, Tavernarakis N (2009) Transgenesis in Caenorhabditis elegans. Methods Mol Biol 561:21-39
    • (2009) Methods Mol Biol , vol.561 , pp. 21-39
    • Rieckher, M.1    Kourtis, N.2    Pasparaki, A.3    Tavernarakis, N.4
  • 60
    • 0030669834 scopus 로고    scopus 로고
    • Reprogramming chemotaxis responses: Sensory neurons define olfactory preferences in C. Elegans
    • DOI 10.1016/S0092-8674(00)80399-2
    • Troemel ER, Kimmel BE, Bargmann CI (1997) Reprogramming chemotaxis responses: sensory neurons define olfactory preferences in C. elegans. Cell 91(2):161-169 (Pubitemid 27456384)
    • (1997) Cell , vol.91 , Issue.2 , pp. 161-169
    • Troemel, E.R.1    Kimmel, B.E.2    Bargmann, C.I.3
  • 61
    • 0035229245 scopus 로고    scopus 로고
    • Effectiveness of specific RNA-mediated interference through ingested double-stranded RNA in Caenorhabditis elegans
    • Kamath RS, Martinez-Campos M, Zipperlen P, Fraser AG, Ahringer J (2001) Effectiveness of specific RNA-mediated interference through ingested double-stranded RNA in Caenorhabditis elegans. Genome Biol 2 (1):RESEARCH0002
    • (2001) Genome Biol , vol.2 , Issue.1
    • Kamath, R.S.1    Martinez-Campos, M.2    Zipperlen, P.3    Fraser, A.G.4    Ahringer, J.5
  • 62
    • 0013832925 scopus 로고
    • Cytochrome f and plastocyanin: Their sequence in the photosynthetic electron transport chain of Chlamydomonas reinhardi
    • 1:CAS:528:DyaF28XmtFGjtw%3D%3D 4379719 10.1073/pnas.54.6.1665
    • Gorman DS, Levine RP (1965) Cytochrome f and plastocyanin: their sequence in the photosynthetic electron transport chain of Chlamydomonas reinhardi. Proc Natl Acad Sci USA 54(6):1665-1669
    • (1965) Proc Natl Acad Sci USA , vol.54 , Issue.6 , pp. 1665-1669
    • Gorman, D.S.1    Levine, R.P.2
  • 63
    • 0031750484 scopus 로고    scopus 로고
    • Chlamydomonas kinesin-II-dependent intraflagellar transport (IFT): IFT particles contain proteins required for ciliary assembly in Caenorhabditis elegans sensory neurons
    • DOI 10.1083/jcb.141.4.993
    • Cole DG, Diener DR, Himelblau AL, Beech PL, Fuster JC, Rosenbaum JL (1998) Chlamydomonas kinesin-II-dependent intraflagellar transport (IFT): IFT particles contain proteins required for ciliary assembly in Caenorhabditis elegans sensory neurons. J Cell Biol 141(4):993-1008 (Pubitemid 28243966)
    • (1998) Journal of Cell Biology , vol.141 , Issue.4 , pp. 993-1008
    • Cole, D.G.1    Diener, D.R.2    Himelblau, A.L.3    Beech, P.L.4    Fuster, J.C.5    Rosenbaum, J.L.6
  • 64
    • 55949094005 scopus 로고    scopus 로고
    • ODA16 aids axonemal outer row dynein assembly through an interaction with the intraflagellar transport machinery
    • 1:CAS:528:DC%2BD1cXht12hsLnK 18852297 10.1083/jcb.200802025
    • Ahmed NT, Gao C, Lucker BF, Cole DG, Mitchell DR (2008) ODA16 aids axonemal outer row dynein assembly through an interaction with the intraflagellar transport machinery. J Cell Biol 183(2):313-322
    • (2008) J Cell Biol , vol.183 , Issue.2 , pp. 313-322
    • Ahmed, N.T.1    Gao, C.2    Lucker, B.F.3    Cole, D.G.4    Mitchell, D.R.5
  • 65
    • 33644779653 scopus 로고    scopus 로고
    • Dissecting the molecular mechanisms of intraflagellar transport in Chlamydomonas
    • DOI 10.1016/j.cub.2006.02.020, PII S0960982206011389
    • Pedersen LB, Geimer S, Rosenbaum JL (2006) Dissecting the molecular mechanisms of intraflagellar transport in Chlamydomonas. Curr Biol 16(5):450-459. doi: 10.1016/j.cub.2006.02.020 (Pubitemid 43343705)
    • (2006) Current Biology , vol.16 , Issue.5 , pp. 450-459
    • Pedersen, L.B.1    Geimer, S.2    Rosenbaum, J.L.3
  • 68
    • 33748297500 scopus 로고    scopus 로고
    • A kinesin-like calmodulin-binding protein in Chlamydomonas: Evidence for a role in cell division and flagellar functions
    • DOI 10.1242/jcs.03028
    • Dymek EE, Goduti D, Kramer T, Smith EF (2006) A kinesin-like calmodulin-binding protein in Chlamydomonas: evidence for a role in cell division and flagellar functions. J Cell Sci 119(Pt 15):3107-3116 (Pubitemid 44322125)
    • (2006) Journal of Cell Science , vol.119 , Issue.15 , pp. 3107-3116
    • Dymek, E.E.1    Goduti, D.2    Kramer, T.3    Smith, E.F.4
  • 69
    • 0000569744 scopus 로고    scopus 로고
    • Riddle DL, Blumenthal T, Meyer BJ, Priess JR (eds) C. elegans II, 2nd edn, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Bargmann CI, Mori I (1997) Chemotaxis and thermotaxis. In: Riddle DL, Blumenthal T, Meyer BJ, Priess JR (eds) C. elegans II, 2nd edn. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (1997) Chemotaxis and Thermotaxis
    • Bargmann, C.I.1    Mori, I.2
  • 70
    • 0002451348 scopus 로고    scopus 로고
    • Riddle DL, Blumenthal T, Meyer BJ, Priess JR (eds) C. elegans II, 2nd edn. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Driscoll M, Kaplan J (1997) Mechanotransduction. In: Riddle DL, Blumenthal T, Meyer BJ, Priess JR (eds) C. elegans II, 2nd edn. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (1997) Mechanotransduction
    • Driscoll, M.1    Kaplan, J.2
  • 71
    • 0004082546 scopus 로고    scopus 로고
    • Riddle DL, Blumenthal T, Meyer BJ, Priess JR (eds) C. elegans II, 2nd edn. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Riddle DL, Albert PS (1997) Genetic and environmental regulation of dauer larva development. In: Riddle DL, Blumenthal T, Meyer BJ, Priess JR (eds) C. elegans II, 2nd edn. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (1997) Genetic and Environmental Regulation of Dauer Larva Development
    • Riddle, D.L.1    Albert, P.S.2
  • 72
    • 0037197871 scopus 로고    scopus 로고
    • C. Elegans responds to chemical repellents by integrating sensory inputs from the head and the tail
    • DOI 10.1016/S0960-9822(02)00813-8, PII S0960982202008138
    • Hilliard MA, Bargmann CI, Bazzicalupo P (2002) C. elegans responds to chemical repellents by integrating sensory inputs from the head and the tail. Curr Biol 12(9):730-734 (Pubitemid 34455426)
    • (2002) Current Biology , vol.12 , Issue.9 , pp. 730-734
    • Hilliard, M.A.1    Bargmann, C.I.2    Bazzicalupo, P.3
  • 73
    • 0242515751 scopus 로고    scopus 로고
    • Chibby, a nuclear β-catenin-associated antagonist of the Wnt/Wingless pathway
    • DOI 10.1038/nature01570
    • Takemaru K, Yamaguchi S, Lee YS, Zhang Y, Carthew RW, Moon RT (2003) Chibby, a nuclear beta-catenin-associated antagonist of the Wnt/Wingless pathway. Nature 422(6934):905-909 (Pubitemid 36520044)
    • (2003) Nature , vol.422 , Issue.6934 , pp. 905-909
    • Takemaru, K.-I.1    Yamaguchi, S.2    Sik Lee, Y.3    Zhang, Y.4    Carthew, R.W.5    Moon, R.T.6
  • 74
    • 84864084441 scopus 로고    scopus 로고
    • A Wnt/beta-catenin pathway antagonist Chibby binds cenexin at the distal end of mother centrioles and functions in primary cilia formation
    • 1:CAS:528:DC%2BC38XhtFSkt7rM 3401179 22911743 10.1371/journal.pone. 0041077
    • Steere N, Chae V, Burke M, Li FQ, Takemaru K, Kuriyama R (2012) A Wnt/beta-catenin pathway antagonist Chibby binds cenexin at the distal end of mother centrioles and functions in primary cilia formation. PLoS One 7(7):e41077
    • (2012) PLoS One , vol.7 , Issue.7 , pp. 41077
    • Steere, N.1    Chae, V.2    Burke, M.3    Li, F.Q.4    Takemaru, K.5    Kuriyama, R.6
  • 75
    • 0036745763 scopus 로고    scopus 로고
    • CP110, a cell cycle-dependent CDK substrate, regulates centrosome duplication in human cells
    • 1:CAS:528:DC%2BD38XntlCqtro%3D 12361598 10.1016/S1534-5807(02)00258-7
    • Chen Z, Indjeian VB, McManus M, Wang L, Dynlacht BD (2002) CP110, a cell cycle-dependent CDK substrate, regulates centrosome duplication in human cells. Dev Cell 3(3):339-350
    • (2002) Dev Cell , vol.3 , Issue.3 , pp. 339-350
    • Chen, Z.1    Indjeian, V.B.2    McManus, M.3    Wang, L.4    Dynlacht, B.D.5
  • 78
    • 34547590810 scopus 로고    scopus 로고
    • Functional dissection of Rab GTPases involved in primary cilium formation
    • DOI 10.1083/jcb.200703047
    • Yoshimura S, Egerer J, Fuchs E, Haas AK, Barr FA (2007) Functional dissection of Rab GTPases involved in primary cilium formation. J Cell Biol 178(3):363-369 (Pubitemid 47196146)
    • (2007) Journal of Cell Biology , vol.178 , Issue.3 , pp. 363-369
    • Yoshimura, S.-I.1    Egerer, J.2    Fuchs, E.3    Haas, A.K.4    Barr, F.A.5
  • 79
    • 80054759802 scopus 로고    scopus 로고
    • Rab8 GTPase as a regulator of cell shape
    • 10.1002/cm.20529
    • Peränen J (2011) Rab8 GTPase as a regulator of cell shape. Cytoskeleton (Hoboken) 68(10):527-539
    • (2011) Cytoskeleton (Hoboken) , vol.68 , Issue.10 , pp. 527-539
    • Peränen, J.1
  • 80
    • 0037031146 scopus 로고    scopus 로고
    • Centrin-2 is required for centriole duplication in mammalian cells
    • DOI 10.1016/S0960-9822(02)01019-9, PII S0960982202010199
    • Salisbury JL, Suino KM, Busby R, Springett M (2002) Centrin-2 is required for centriole duplication in mammalian cells. Curr Biol 12(15):1287-1292 (Pubitemid 34869878)
    • (2002) Current Biology , vol.12 , Issue.15 , pp. 1287-1292
    • Salisbury, J.L.1    Suino, K.M.2    Busby, R.3    Springett, M.4
  • 81
    • 0029062216 scopus 로고
    • The chaperonin containing t-complex polypeptide 1 (TCP-1). Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol
    • 1:CAS:528:DyaK2MXlvFalsLc%3D 7601114 10.1111/j.1432-1033.1995.tb20527.x
    • Kubota H, Hynes G, Willison K (1995) The chaperonin containing t-complex polypeptide 1 (TCP-1). Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol. Eur J Biochem 230(1):3-16
    • (1995) Eur J Biochem , vol.230 , Issue.1 , pp. 3-16
    • Kubota, H.1    Hynes, G.2    Willison, K.3
  • 83
    • 0035783192 scopus 로고    scopus 로고
    • Review: Cellular substrates of the eukaryotic chaperonin TRiC/CCT
    • 1:CAS:528:DC%2BD3MXntFKqur8%3D 11580267 10.1006/jsbi.2001.4380
    • Dunn AY, Melville MW, Frydman J (2001) Review: cellular substrates of the eukaryotic chaperonin TRiC/CCT. J Struct Biol 135(2):176-184
    • (2001) J Struct Biol , vol.135 , Issue.2 , pp. 176-184
    • Dunn, A.Y.1    Melville, M.W.2    Frydman, J.3
  • 84
    • 7444231693 scopus 로고    scopus 로고
    • Mechanism of the eukaryotic chaperonin: Protein folding in the chamber of secrets
    • DOI 10.1016/j.tcb.2004.09.015, PII S0962892404002661
    • Spiess C, Meyer AS, Reissmann S, Frydman J (2004) Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets. Trends Cell Biol 14(11):598-604 (Pubitemid 39440608)
    • (2004) Trends in Cell Biology , vol.14 , Issue.11 , pp. 598-604
    • Spiess, C.1    Meyer, A.S.2    Reissmann, S.3    Frydman, J.4
  • 86
    • 0041669463 scopus 로고    scopus 로고
    • The CCT chaperonin promotes activation of the anaphase-promoting complex through the generation of functional Cdc20
    • DOI 10.1016/S1097-2765(03)00244-2
    • Camasses A, Bogdanova A, Shevchenko A, Zachariae W (2003) The CCT chaperonin promotes activation of the anaphase-promoting complex through the generation of functional Cdc20. Mol Cell 12(1):87-100 (Pubitemid 36945038)
    • (2003) Molecular Cell , vol.12 , Issue.1 , pp. 87-100
    • Camasses, A.1    Bogdanova, A.2    Shevchenko, A.3    Zachariae, W.4
  • 87
    • 76149101303 scopus 로고    scopus 로고
    • The Chlamydomonas reinhardtii BBSome is an IFT cargo required for export of specific signaling proteins from flagella
    • 1:CAS:528:DC%2BC3cXhs1Kktg%3D%3D 20038682 10.1083/jcb.200909183
    • Lechtreck KF, Johnson EC, Sakai T, Cochran D, Ballif BA, Rush J, Pazour GJ, Ikebe M, Witman GB (2009) The Chlamydomonas reinhardtii BBSome is an IFT cargo required for export of specific signaling proteins from flagella. J Cell Biol 187(7):1117-1132
    • (2009) J Cell Biol , vol.187 , Issue.7 , pp. 1117-1132
    • Lechtreck, K.F.1    Johnson, E.C.2    Sakai, T.3    Cochran, D.4    Ballif, B.A.5    Rush, J.6    Pazour, G.J.7    Ikebe, M.8    Witman, G.B.9
  • 88
    • 84862004139 scopus 로고    scopus 로고
    • Intrinsic protein-protein interaction-mediated and chaperonin-assisted sequential assembly of stable Bardet-Biedl syndrome protein complex, the BBSome
    • 1:CAS:528:DC%2BC38Xot1Kju7Y%3D 22500027 10.1074/jbc.M112.341487
    • Zhang Q, Yu D, Seo S, Stone EM, Sheffield VC (2012) Intrinsic protein-protein interaction-mediated and chaperonin-assisted sequential assembly of stable Bardet-Biedl syndrome protein complex, the BBSome. J Biol Chem 287(24):20625-20635
    • (2012) J Biol Chem , vol.287 , Issue.24 , pp. 20625-20635
    • Zhang, Q.1    Yu, D.2    Seo, S.3    Stone, E.M.4    Sheffield, V.C.5
  • 89
    • 77951906324 scopus 로고    scopus 로고
    • Comparison of intracellular localization of Nubp1 and Nubp2 using GFP fusion proteins
    • 1:CAS:528:DC%2BC3cXhtlWqtLs%3D 19263241 10.1007/s11033-009-9477-7
    • Okuno T, Yamabayashi H, Kogure K (2010) Comparison of intracellular localization of Nubp1 and Nubp2 using GFP fusion proteins. Mol Biol Rep 37(3):1165-1168
    • (2010) Mol Biol Rep , vol.37 , Issue.3 , pp. 1165-1168
    • Okuno, T.1    Yamabayashi, H.2    Kogure, K.3
  • 90
    • 0033521588 scopus 로고    scopus 로고
    • In vivo newly translated polypeptides are sequestered in a protected folding environment
    • DOI 10.1093/emboj/18.1.85
    • Thulasiraman V, Yang CF, Frydman J (1999) In vivo newly translated polypeptides are sequestered in a protected folding environment. EMBO J 18(1):85-95 (Pubitemid 29005026)
    • (1999) EMBO Journal , vol.18 , Issue.1 , pp. 85-95
    • Thulasiraman, V.1    Yang, C.-F.2    Frydman, J.3
  • 91
    • 0028196813 scopus 로고
    • Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates
    • 1:CAS:528:DyaK2cXkslKms7w%3D 358657 7909354
    • Melki R, Cowan NJ (1994) Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates. Mol Cell Biol 14(5):2895-2904
    • (1994) Mol Cell Biol , vol.14 , Issue.5 , pp. 2895-2904
    • Melki, R.1    Cowan, N.J.2
  • 92
    • 0035783387 scopus 로고    scopus 로고
    • Review: Nucleotide-dependent conformational changes of the chaperonin containing TCP-1
    • 1:CAS:528:DC%2BD3MXntFKqurk%3D 11580266 10.1006/jsbi.2001.4388
    • Melki R (2001) Review: nucleotide-dependent conformational changes of the chaperonin containing TCP-1. J Struct Biol 135(2):170-175
    • (2001) J Struct Biol , vol.135 , Issue.2 , pp. 170-175
    • Melki, R.1
  • 93
    • 0028822679 scopus 로고
    • Quasi-native chaperonin-bound intermediates in facilitated protein folding
    • 1:CAS:528:DyaK2MXovVSgsLo%3D 7592580 10.1074/jbc.270.41.23910
    • Tian G, Vainberg IE, Tap WD, Lewis SA, Cowan NJ (1995) Quasi-native chaperonin-bound intermediates in facilitated protein folding. J Biol Chem 270(41):23910-23913
    • (1995) J Biol Chem , vol.270 , Issue.41 , pp. 23910-23913
    • Tian, G.1    Vainberg, I.E.2    Tap, W.D.3    Lewis, S.A.4    Cowan, N.J.5
  • 94
    • 0037115711 scopus 로고    scopus 로고
    • Assembly of the SMRT-histone deacetylase 3 repression complex requires the TCP-1 ring complex
    • DOI 10.1101/gad.1037502
    • Guenther MG, Yu J, Kao GD, Yen TJ, Lazar MA (2002) Assembly of the SMRT-histone deacetylase 3 repression complex requires the TCP-1 ring complex. Genes Dev 16(24):3130-3135 (Pubitemid 36025967)
    • (2002) Genes and Development , vol.16 , Issue.24 , pp. 3130-3135
    • Guenther, M.G.1    Yu, J.2    Kao, G.D.3    Yen, T.J.4    Lazar, M.A.5
  • 95
    • 69549122198 scopus 로고    scopus 로고
    • Nesprin-2 interacts with meckelin and mediates ciliogenesis via remodelling of the actin cytoskeleton
    • 1:CAS:528:DC%2BD1MXhtVGhsLzP 19596800 10.1242/jcs.043794
    • Dawe HR, Adams M, Wheway G, Szymanska K, Logan CV, Noegel AA, Gull K, Johnson CA (2009) Nesprin-2 interacts with meckelin and mediates ciliogenesis via remodelling of the actin cytoskeleton. J Cell Sci 122(Pt 15):2716-2726
    • (2009) J Cell Sci , vol.122 , Issue.PART 15 , pp. 2716-2726
    • Dawe, H.R.1    Adams, M.2    Wheway, G.3    Szymanska, K.4    Logan, C.V.5    Noegel, A.A.6    Gull, K.7    Johnson, C.A.8
  • 96
    • 77951128108 scopus 로고    scopus 로고
    • Functional genomic screen for modulators of ciliogenesis and cilium length
    • 1:CAS:528:DC%2BC3cXkslart7w%3D 2929961 20393563 10.1038/nature08895
    • Kim J, Lee JE, Heynen-Genel S, Suyama E, Ono K, Lee K, Ideker T, Aza-Blanc P, Gleeson JG (2010) Functional genomic screen for modulators of ciliogenesis and cilium length. Nature 464(7291):1048-1051
    • (2010) Nature , vol.464 , Issue.7291 , pp. 1048-1051
    • Kim, J.1    Lee, J.E.2    Heynen-Genel, S.3    Suyama, E.4    Ono, K.5    Lee, K.6    Ideker, T.7    Aza-Blanc, P.8    Gleeson, J.G.9
  • 97
    • 84879880339 scopus 로고    scopus 로고
    • Xenopus laevis nucleotide-binding protein 1 (xNubp1) is important for convergent extension movements and controls ciliogenesis via regulation of the actin cytoskeleton
    • doi: 10.1016/j.ydbio.2013.05.004. [Epub ahead of print]
    • Ioannou A, Santama N, Skourides P (2013) Xenopus laevis nucleotide-binding protein 1 (xNubp1) is important for convergent extension movements and controls ciliogenesis via regulation of the actin cytoskeleton. Dev Biol. doi: 10.1016/j.ydbio.2013.05.004. [Epub ahead of print]
    • (2013) Dev Biol
    • Ioannou, A.1    Santama, N.2    Skourides, P.3
  • 98
    • 79952844342 scopus 로고    scopus 로고
    • Soluble levels of cytosolic tubulin regulate ciliary length control
    • 1:CAS:528:DC%2BC3MXjs1Gkt74%3D 3057705 21270438 10.1091/mbc.E10-03-0269
    • Sharma N, Kosan ZA, Stallworth JE, Berbari NF, Yoder BK (2011) Soluble levels of cytosolic tubulin regulate ciliary length control. Mol Biol Cell 22(6):806-816
    • (2011) Mol Biol Cell , vol.22 , Issue.6 , pp. 806-816
    • Sharma, N.1    Kosan, Z.A.2    Stallworth, J.E.3    Berbari, N.F.4    Yoder, B.K.5
  • 99
    • 79956193249 scopus 로고    scopus 로고
    • Regulating the transition from centriole to basal body
    • 1:CAS:528:DC%2BC3MXlvFKmsL8%3D 21536747 10.1083/jcb.201101005
    • Kobayashi T, Dynlacht BD (2011) Regulating the transition from centriole to basal body. J Cell Biol 193(3):435-444
    • (2011) J Cell Biol , vol.193 , Issue.3 , pp. 435-444
    • Kobayashi, T.1    Dynlacht, B.D.2
  • 100
    • 63849291991 scopus 로고    scopus 로고
    • A microtubule depolymerizing kinesin functions during both flagellar disassembly and flagellar assembly in Chlamydomonas
    • 1:CAS:528:DC%2BD1MXktFOgtL8%3D 19264963 10.1073/pnas.0808671106
    • Piao T, Luo M, Wang L, Guo Y, Li D, Li P, Snell WJ, Pan J (2009) A microtubule depolymerizing kinesin functions during both flagellar disassembly and flagellar assembly in Chlamydomonas. Proc Natl Acad Sci USA 106(12):4713-4718
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.12 , pp. 4713-4718
    • Piao, T.1    Luo, M.2    Wang, L.3    Guo, Y.4    Li, D.5    Li, P.6    Snell, W.J.7    Pan, J.8
  • 101
    • 84866454997 scopus 로고    scopus 로고
    • Nubp1 is required for lung branching morphogenesis and distal progenitor cell survival in mice
    • 10.1371/journal.pone.0044871
    • Schnatwin C, Niswander L (2012) Nubp1 is required for lung branching morphogenesis and distal progenitor cell survival in mice. PLoS One 7(9):e44871
    • (2012) PLoS One , vol.7 , Issue.9 , pp. 44871
    • Schnatwin, C.1    Niswander, L.2
  • 102
    • 79951855247 scopus 로고    scopus 로고
    • The ins and outs of tubulin acetylation: More than just a post-translational modification?
    • 1:CAS:528:DC%2BC3MXisFalt7Y%3D 20940043 10.1016/j.cellsig.2010.10.014
    • Perdiz D, Mackeh R, Poüs C, Baillet A (2011) The ins and outs of tubulin acetylation: more than just a post-translational modification? Cell Signal 23(5):763-771
    • (2011) Cell Signal , vol.23 , Issue.5 , pp. 763-771
    • Perdiz, D.1    Mackeh, R.2    Poüs, C.3    Baillet, A.4
  • 103
    • 0023293040 scopus 로고
    • Microtubules containing acetylated alpha-tubulin in mammalian cells in culture
    • 1:CAS:528:DyaL2sXhtFKqtLw%3D 2879846 10.1083/jcb.104.2.289
    • Piperno G, LeDizet M, Chang XJ (1987) Microtubules containing acetylated alpha-tubulin in mammalian cells in culture. J Cell Biol 104(2):289-302
    • (1987) J Cell Biol , vol.104 , Issue.2 , pp. 289-302
    • Piperno, G.1    Ledizet, M.2    Chang, X.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.