메뉴 건너뛰기




Volumn 2011, Issue , 2011, Pages

Elongator: An ancestral complex driving transcription and migration through protein acetylation

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA TUBULIN; CELL PROTEIN; CYCLINE; ELONGATION FACTOR 1; ELONGATION FACTOR 3; ELONGATOR; HISTONE H3; I KAPPA B; PROTEIN KTI12; RNA POLYMERASE II; STAT3 PROTEIN; TRANSCRIPTION ELONGATION FACTOR; UNCLASSIFIED DRUG; HISTONE; HISTONE ACETYLTRANSFERASE; NERVE PROTEIN; TUBULIN;

EID: 79952211581     PISSN: 11107243     EISSN: 11107251     Source Type: Journal    
DOI: 10.1155/2011/924898     Document Type: Review
Times cited : (19)

References (80)
  • 2
    • 0035171624 scopus 로고    scopus 로고
    • Characterization of a six-subunit Holo-Elongator complex required for the regulated expression of a group of genes in Saccharomyces cerevisiae
    • DOI 10.1128/MCB.21.23.8203-8212.2001
    • Krogan N. J., Greenblatt J. F., Characterization of a six-subunit Holo-Elongator complex required for the regulated expression of a group of genes in Saccharomyces cerevisiae Molecular and Cellular Biology 2001 21 23 8203 8212 (Pubitemid 33051809)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.23 , pp. 8203-8212
    • Krogan, N.J.1    Greenblatt, J.F.2
  • 7
    • 59249093238 scopus 로고    scopus 로고
    • Loss of mouse ikbkap, a subunit of elongator, leads to transcriptional deficits and embryonic lethality that can be rescued by human IKBKAP
    • Chen Y. T., Hims M. M., Shetty R. S., Mull J., Liu L., Leyne M., Slaugenhaupt S. A., Loss of mouse ikbkap, a subunit of elongator, leads to transcriptional deficits and embryonic lethality that can be rescued by human IKBKAP Molecular and Cellular Biology 2009 29 3 736 744
    • (2009) Molecular and Cellular Biology , vol.29 , Issue.3 , pp. 736-744
    • Chen, Y.T.1    Hims, M.M.2    Shetty, R.S.3    Mull, J.4    Liu, L.5    Leyne, M.6    Slaugenhaupt, S.A.7
  • 11
    • 0036360126 scopus 로고    scopus 로고
    • Protein interactions within Saccharomyces cerevisiae elongator, a complex essential for Kluyveromyces lactis zymocicity
    • DOI 10.1046/j.1365-2958.2002.03055.x
    • Fichtner L., Frohloff F., Jablonowski D., Stark M. J. R., Schaffrath R., Protein interactions within Saccharomyces cerevisiae elongator, a complex essential for Kluyveromyces lactis zymocicity Molecular Microbiology 2002 45 3 817 826 (Pubitemid 34989187)
    • (2002) Molecular Microbiology , vol.45 , Issue.3 , pp. 817-826
    • Fichtner, L.1    Frohloff, F.2    Jablonowski, D.3    Stark, M.J.R.4    Schaffrath, R.5
  • 12
    • 0036241663 scopus 로고    scopus 로고
    • Exchange of RNA polymerase II initiation and elongation factors during gene expression in vivo
    • DOI 10.1016/S1097-2765(02)00502-6
    • Pokholok D. K., Hannett N. M., Young R. A., Exchange of RNA polymerase II initiation and elongation factors during gene expression in vivo Molecular Cell 2002 9 4 799 809 (Pubitemid 34454890)
    • (2002) Molecular Cell , vol.9 , Issue.4 , pp. 799-809
    • Pokholok, D.K.1    Hannett, N.M.2    Young, R.A.3
  • 13
    • 34250305505 scopus 로고    scopus 로고
    • Elongator complex: how many roles does it play?
    • DOI 10.1016/j.ceb.2007.04.005, PII S0955067407000579, Nucleus and Gene Expression
    • Svejstrup J. Q., Elongator complex: how many roles does it play? Current Opinion in Cell Biology 2007 19 3 331 336 (Pubitemid 46908882)
    • (2007) Current Opinion in Cell Biology , vol.19 , Issue.3 , pp. 331-336
    • Svejstrup, J.Q.1
  • 15
    • 33749078546 scopus 로고    scopus 로고
    • Elevated Levels of Two tRNA Species Bypass the Requirement for Elongator Complex in Transcription and Exocytosis
    • DOI 10.1016/j.molcel.2006.07.031, PII S1097276506005338
    • Esberg A., Huang BO., Johansson M. J. O., Bystrm A. S., Elevated levels of two tRNA species bypass the requirement for elongator complex in transcription and exocytosis Molecular Cell 2006 24 1 139 148 (Pubitemid 44466676)
    • (2006) Molecular Cell , vol.24 , Issue.1 , pp. 139-148
    • Esberg, A.1    Huang, B.2    Johansson, M.J.O.3    Bystrom, A.S.4
  • 16
    • 15444371415 scopus 로고    scopus 로고
    • An early step in wobble uridine tRNA modification requires the Elongator complex
    • DOI 10.1261/rna.7247705
    • Huang BO., Johansson M. J. O., Bystrm A. S., An early step in wobble uridine tRNA modification requires the Elongator complex RNA 2005 11 4 424 436 (Pubitemid 40397176)
    • (2005) RNA , vol.11 , Issue.4 , pp. 424-436
    • Huang, B.1    Johansson, M.J.O.2    Bystrom, A.S.3
  • 17
    • 15244355534 scopus 로고    scopus 로고
    • Elp1p, the yeast homolog of the FD disease syndrome protein, negatively regulates exocytosis independently of transcriptional elongation
    • DOI 10.1016/j.molcel.2005.02.018
    • Rahl P. B., Chen C. Z., Collins R. N., Elp1p, the yeast homolog of the FD disease syndrome protein, negatively regulates exocytosis independently of transcriptional elongation Molecular Cell 2005 17 6 841 853 (Pubitemid 40386945)
    • (2005) Molecular Cell , vol.17 , Issue.6 , pp. 841-853
    • Rahl, P.B.1    Chen, C.Z.2    Collins, R.N.3
  • 19
    • 33748648400 scopus 로고    scopus 로고
    • Mutations in ABO1/ELO2, a subunit of holo-elongator, increase abscisic acid sensitivity and drought tolerance in Arabidopsis thaliana
    • DOI 10.1128/MCB.00433-06
    • Chen Z., Zhang H., Jablonowski D., Zhou X., Ren X., Hong X., Schaffrath R., Zhu J. K., Gong Z., Mutations in ABO1/ELO2, a subunit of holo-elongator, increase abscisic acid sensitivity and drought tolerance in Arabidopsis thaliana Molecular and Cellular Biology 2006 26 18 6902 6912 (Pubitemid 44387639)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.18 , pp. 6902-6912
    • Chen, Z.1    Zhang, H.2    Jablonowski, D.3    Zhou, X.4    Ren, X.5    Hong, X.6    Schaffrath, R.7    Zhu, J.-K.8    Gong, Z.9
  • 20
    • 20044367838 scopus 로고    scopus 로고
    • The Elp3 subunit of human Elongator complex is functionally similar to its counterpart in yeast
    • DOI 10.1007/s00438-005-1120-2
    • Li F., Lu J., Han Q., Zhang G., Huang B., The Elp3 subunit of human Elongator complex is functionally similar to its counterpart in yeast Molecular Genetics and Genomics 2005 273 3 264 272 (Pubitemid 40768513)
    • (2005) Molecular Genetics and Genomics , vol.273 , Issue.3 , pp. 264-272
    • Li, F.1    Lu, J.2    Han, Q.3    Zhang, G.4    Huang, B.5
  • 21
    • 0037428386 scopus 로고    scopus 로고
    • Subunit communications crucial for the functional integrity of the yeast RNA polymerase II elongator (γ-toxin target (TOT)) complex
    • DOI 10.1074/jbc.M210060200
    • Frohloff F., Jablonowski D., Fichtner L., Schaffrath R., Subunit communications crucial for the functional integrity of the yeast RNA polymerase II elongator ( -toxin target (TOT)) complex Journal of Biological Chemistry 2003 278 2 956 961 (Pubitemid 36790771)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.2 , pp. 956-961
    • Frohloff, F.1    Jablonowski, D.2    Fichtner, L.3    Schaffrath, R.4
  • 23
    • 0034724683 scopus 로고    scopus 로고
    • The Elp2 subunit of elongator and elongating RNA polymerase II holoenzyme is a WD40 repeat protein
    • DOI 10.1074/jbc.275.17.12896
    • Fellows J., Erdjument-Bromage H., Tempst P., Svejstrup J. Q., The Elp2 subunit of elongator and elongating RNA polymerase II holoenzyme is a WD40 repeat protein Journal of Biological Chemistry 2000 275 17 12896 12899 (Pubitemid 30241445)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.17 , pp. 12896-12899
    • Fellows, J.1    Erdjument-Bromage, H.2    Tempst, P.3    Svejstrup, J.Q.4
  • 24
    • 3543038157 scopus 로고    scopus 로고
    • Molecular architecture, structure-function relationship, and importance of the Elp3 subunit for the RNA binding of holo-Elongator
    • DOI 10.1074/jbc.M403361200
    • Petrakis T. G., Wittschieben B.., Svejstrup J. Q., Molecular architecture, structure-function relationship, and importance of the Elp3 subunit for the RNA binding of holo-Elongator Journal of Biological Chemistry 2004 279 31 32087 32092 (Pubitemid 39014654)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.31 , pp. 32087-32092
    • Petrakis, T.G.1    Wittschieben, B.O.2    Svejstrup, J.Q.3
  • 25
    • 0034660330 scopus 로고    scopus 로고
    • Overlapping roles for the histone acetyltransferase activities of SAGA and Elongator in vivo
    • Wittschieben B.., Fellows J., Wendy DU., Stillman D. J., Svejstrup J. Q., Overlapping roles for the histone acetyltransferase activities of SAGA and Elongator in vivo EMBO Journal 2000 19 12 3060 3068 (Pubitemid 30386776)
    • (2000) EMBO Journal , vol.19 , Issue.12 , pp. 3060-3068
    • Wittschieben, B.O.1    Fellows, J.2    Wendy, D.3    Stillman, D.J.4    Svejstrup, J.Q.5
  • 28
    • 0036495007 scopus 로고    scopus 로고
    • A second catalytic domain in the Elp3 histone acetyltransferases: A candidate for histone demethylase activity?
    • DOI 10.1016/S0968-0004(02)02058-3, PII S0968000402020583
    • Chinenov Y., A second catalytic domain in the Elp3 histone acetyltransferases: a candidate for histone demethylase activity? Trends in Biochemical Sciences 2002 27 3 115 117 (Pubitemid 34219316)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.3 , pp. 115-117
    • Chinenov, Y.1
  • 29
    • 34250826536 scopus 로고    scopus 로고
    • HELP3 subunit of the Elongator complex regulates the transcription of HSP70 gene in human cells
    • DOI 10.1111/j.1745-7270.2007.00293.x
    • Han Q., Hou X., Su D., Pan L., Duan J., Cui L., Huang B., Lu J., HELP3 subunit of the Elongator complex regulates the transcription of HSP70 gene in human cells Acta Biochimica et Biophysica Sinica 2007 39 6 453 461 (Pubitemid 46990237)
    • (2007) Acta Biochimica et Biophysica Sinica , vol.39 , Issue.6 , pp. 453-461
    • Han, Q.1    Hou, X.2    Su, D.3    Pan, L.4    Duan, J.5    Cui, L.6    Huang, B.7    Lu, J.8
  • 30
    • 75749142980 scopus 로고    scopus 로고
    • A role for the elongator complex in zygotic paternal genome demethylation
    • Okada Y., Yamagata K., Hong K., Wakayama T., Zhang YI., A role for the elongator complex in zygotic paternal genome demethylation Nature 2010 463 7280 554 558
    • (2010) Nature , vol.463 , Issue.7280 , pp. 554-558
    • Okada, Y.1    Yamagata, K.2    Hong, K.3    Wakayama, T.4    Zhang, Y.I.5
  • 31
    • 0036713442 scopus 로고    scopus 로고
    • Novel domains and orthologues of eukaryotic transcription elongation factors
    • Ponting C. P., Novel domains and orthologues of eukaryotic transcription elongation factors Nucleic Acids Research 2002 30 17 3643 3652 (Pubitemid 35021228)
    • (2002) Nucleic Acids Research , vol.30 , Issue.17 , pp. 3643-3652
    • Ponting, C.P.1
  • 32
    • 73349133725 scopus 로고    scopus 로고
    • The elongator complex interacts with PCNA and modulates transcriptional silencing and sensitivity to DNA damage agents
    • Li Q., Fazly A. M., Zhou H., Huang S., Zhang Z., Stillman B., The elongator complex interacts with PCNA and modulates transcriptional silencing and sensitivity to DNA damage agents PLoS Genetics 2009 5 10
    • (2009) PLoS Genetics , vol.5 , Issue.10
    • Li, Q.1    Fazly, A.M.2    Zhou, H.3    Huang, S.4    Zhang, Z.5    Stillman, B.6
  • 33
    • 0035901529 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Elongator mutations confer resistance to the Kluyveromyces lactis zymocin
    • DOI 10.1093/emboj/20.8.1993
    • Frohloff F., Fichtner L., Jablonowski D., Breunig K. D., Schaffrath R., Saccharomyces cerevisiae Elongator mutations confer resistance to the Kluyveromyces lactis zymocin EMBO Journal 2001 20 8 1993 2003 (Pubitemid 32397401)
    • (2001) EMBO Journal , vol.20 , Issue.8 , pp. 1993-2003
    • Frohloff, F.1    Fichtner, L.2    Jablonowski, D.3    Breunig, K.D.4    Schaffrath, R.5
  • 35
    • 0032541670 scopus 로고    scopus 로고
    • IKAP is a scaffold protein of the IκB kinase complex
    • DOI 10.1038/26254
    • Cohen L., Henzel W. J., Baeuerle P. A., IKAP is a scaffold protein of the I B kinase complex Nature 1998 395 6699 292 296 (Pubitemid 28447556)
    • (1998) Nature , vol.395 , Issue.6699 , pp. 292-296
    • Cohen, L.1    Henzel, W.J.2    Baeuerle, P.A.3
  • 37
    • 1542373731 scopus 로고    scopus 로고
    • The Yeast Elongator Histone Acetylase Requires Sit4-dependent Dephosphorylation for Toxin-Target Capacity
    • DOI 10.1091/mbc.E03-10-0750
    • Jablonowski D., Fichtner L., Stark M. J. R., Schaffrath R., The yeast elongator histone acetylase requires Sit4-dependent dephosphorylation for toxin-target capacity Molecular Biology of the Cell 2004 15 3 1459 1469 (Pubitemid 38316251)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.3 , pp. 1459-1469
    • Jablonowski, D.1    Fichtner, L.2    Stark, M.J.R.3    Schaffrath, R.4
  • 38
    • 70350179460 scopus 로고    scopus 로고
    • Elongator function depends on antagonistic regulation by casein kinase Hrr25 and protein phosphatase Sit4
    • Mehlgarten C., Jablonowski D., Breunig K. D., Stark M. J. R., Schaffrath R., Elongator function depends on antagonistic regulation by casein kinase Hrr25 and protein phosphatase Sit4 Molecular Microbiology 2009 73 5 869 881
    • (2009) Molecular Microbiology , vol.73 , Issue.5 , pp. 869-881
    • Mehlgarten, C.1    Jablonowski, D.2    Breunig, K.D.3    Stark, M.J.R.4    Schaffrath, R.5
  • 40
    • 36549013619 scopus 로고    scopus 로고
    • RNA polymerase stalling at developmental control genes in the Drosophila melanogaster embryo
    • DOI 10.1038/ng.2007.26, PII NG200726
    • Zeitlinger J., Stark A., Kellis M., Hong J. W., Nechaev S., Adelman K., Levine M., Young R. A., RNA polymerase stalling at developmental control genes in the Drosophila melanogaster embryo Nature Genetics 2007 39 12 1512 1516 (Pubitemid 350191345)
    • (2007) Nature Genetics , vol.39 , Issue.12 , pp. 1512-1516
    • Zeitlinger, J.1    Stark, A.2    Kellis, M.3    Hong, J.-W.4    Nechaev, S.5    Adelman, K.6    Levine, M.7    Young, R.A.8
  • 41
    • 5444225805 scopus 로고    scopus 로고
    • Elongation by RNA polymerase II: The short and long of it
    • DOI 10.1101/gad.1235904
    • Sims R. J., Belotserkovskaya R., Reinberg D., Elongation by RNA polymerase II: the short and long of it Genes and Development 2004 18 20 2437 2468 (Pubitemid 39362887)
    • (2004) Genes and Development , vol.18 , Issue.20 , pp. 2437-2468
    • Sims III, R.J.1    Belotserkovskaya, R.2    Reinberg, D.3
  • 45
    • 13444292904 scopus 로고    scopus 로고
    • Histone modifications defining active genes persist after transcriptional and mitotic in activation
    • DOI 10.1038/sj.emboj.7600516
    • Kouskouti A., Talianidis I., Histone modifications defining active genes persist after transcriptional and mitotic in activation EMBO Journal 2005 24 2 347 357 (Pubitemid 40216139)
    • (2005) EMBO Journal , vol.24 , Issue.2 , pp. 347-357
    • Kouskouti, A.1    Talianidis, I.2
  • 46
    • 2442425954 scopus 로고    scopus 로고
    • Elongator interactions with nascent mRNA revealed by RNA immunoprecipitation
    • DOI 10.1016/S1097-2765(04)00239-4, PII S1097276504002394
    • Gilbert C., Kristjuhan A., Winkler G. S., Svejstrup J. Q., Elongator interactions with nascent mRNA revealed by RNA immunoprecipitation Molecular Cell 2004 14 4 457 464 (Pubitemid 38648799)
    • (2004) Molecular Cell , vol.14 , Issue.4 , pp. 457-464
    • Gilbert, C.1    Kristjuhan, A.2    Winkler, G.S.3    Svejstrup, J.Q.4
  • 47
    • 2642544592 scopus 로고    scopus 로고
    • Estrogen receptor-α directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter
    • DOI 10.1016/S0092-8674(03)00934-6
    • Mtivier R., Penot G., Hbner M. R., Reid G., Brand H., Ko M., Gannon F., Estrogen receptor- directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter Cell 2003 115 6 751 763 (Pubitemid 38030303)
    • (2003) Cell , vol.115 , Issue.6 , pp. 751-763
    • Metivier, R.1    Penot, G.2    Hubner, M.R.3    Reid, G.4    Brand, H.5    Kos, M.6    Gannon, F.7
  • 48
    • 0036964090 scopus 로고    scopus 로고
    • Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisiae cause dependence on the Hir/Hpc pathway: Polymerase passage may degrade chromatin structure
    • Formosa T., Ruone S., Adams M. D., Olsen A. E., Eriksson P., Yu Y., Rhoades A. R., Kaufman P. D., Stillman D. J., Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisiae cause dependence on the Hir/Hpc pathway: polymerase passage may degrade chromatin structure Genetics 2002 162 4 1557 1571 (Pubitemid 36114646)
    • (2002) Genetics , vol.162 , Issue.4 , pp. 1557-1571
    • Formosa, T.1    Ruone, S.2    Adams, M.D.3    Olsen, A.E.4    Eriksson, P.5    Yu, Y.6    Rhoades, A.R.7    Kaufman, P.D.8    Stillman, D.J.9
  • 49
    • 3142763039 scopus 로고    scopus 로고
    • Actin and microtubules in cell motility: Which one is in control?
    • DOI 10.1111/j.1600-0854.2004.00196.x
    • Etienne-Manneville S., Actin and microtubules in cell motility: which one is in control? Traffic 2004 5 7 470 477 (Pubitemid 38923174)
    • (2004) Traffic , vol.5 , Issue.7 , pp. 470-477
    • Etienne-Manneville, S.1
  • 50
    • 0028857104 scopus 로고
    • Low concentrations of nocodazole interfere with fibroblast locomotion without significantly affecting microtubule level: Implications for the role of dynamic microtubules in cell locomotion
    • Liao G., Nagasaki T., Gundersen G. G., Low concentrations of nocodazole interfere with fibroblast locomotion without significantly affecting microtubule level: implications for the role of dynamic microtubules in cell locomotion Journal of Cell Science 1995 108 11 3473 3483
    • (1995) Journal of Cell Science , vol.108 , Issue.11 , pp. 3473-3483
    • Liao, G.1    Nagasaki, T.2    Gundersen, G.G.3
  • 51
    • 0032426329 scopus 로고    scopus 로고
    • Tubulin structure: Insights into microtubule properties and functions
    • DOI 10.1016/S0959-440X(98)80099-7
    • Downing K. H., Nogales E., Tubulin structure: insights into microtubule properties and functions Current Opinion in Structural Biology 1998 8 6 785 791 (Pubitemid 29004677)
    • (1998) Current Opinion in Structural Biology , vol.8 , Issue.6 , pp. 785-791
    • Downing, K.H.1    Nogales, E.2
  • 52
    • 0022492523 scopus 로고
    • Visualization of the dynamic instability of individual microtubules by dark-field microscopy
    • Horio T., Hotani H., Visualization of the dynamic instability of individual microtubules by dark-field microscopy Nature 1986 321 6070 605 607 (Pubitemid 16042210)
    • (1986) Nature , vol.321 , Issue.6070 , pp. 605-607
    • Horio, T.1    Hotani, H.2
  • 53
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • DOI 10.1038/312237a0
    • Mitchinson T., Kirschner M., Dynamic instability of microtubule growth Nature 1984 312 5991 237 242 (Pubitemid 15201998)
    • (1984) Nature , vol.312 , Issue.5991 , pp. 237-242
    • Mitchinson, T.1    Kirschner, M.2
  • 54
    • 0037221714 scopus 로고    scopus 로고
    • Microtubules meet substrate adhesions to arrange cell polarity
    • DOI 10.1016/S0955-0674(02)00008-X
    • Small J. V., Kaverina I., Microtubules meet substrate adhesions to arrange cell polarity Current Opinion in Cell Biology 2003 15 1 40 47 (Pubitemid 36044713)
    • (2003) Current Opinion in Cell Biology , vol.15 , Issue.1 , pp. 40-47
    • Small, J.V.1    Kaverina, I.2
  • 56
    • 34548830425 scopus 로고    scopus 로고
    • The tubulin code
    • Verhey K. J., Gaertig J., The tubulin code Cell Cycle 2007 6 17 2152 2160 (Pubitemid 47450417)
    • (2007) Cell Cycle , vol.6 , Issue.17 , pp. 2152-2160
    • Verhey, K.J.1    Gaertig, J.2
  • 57
    • 0032005075 scopus 로고    scopus 로고
    • Tubulin and microtubule structure
    • DOI 10.1016/S0955-0674(98)80082-3
    • Downing K. H., Nogales E., Tubulin and microtubule structure Current Opinion in Cell Biology 1998 10 1 16 22 (Pubitemid 28066117)
    • (1998) Current Opinion in Cell Biology , vol.10 , Issue.1 , pp. 16-22
    • Downing, K.H.1    Nogales, E.2
  • 58
    • 0021993649 scopus 로고
    • Chlamydomonas α-tubulin is posttranslationally modified by acetylation on the ε-amino group of a lysine
    • DOI 10.1021/bi00323a034
    • L'Hernault S. W., Rosenbaum J. L., Chlamydomonas -tubulin is posttranslationally modified by acetylation on the -amino group of a lysine Biochemistry 1985 24 2 473 478 (Pubitemid 15105622)
    • (1985) Biochemistry , vol.24 , Issue.2 , pp. 473-478
    • L'Hernault, S.W.1    Rosenbaum, J.L.2
  • 61
    • 0037416151 scopus 로고    scopus 로고
    • HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo
    • DOI 10.1093/emboj/cdg115
    • Zhang Y., Li N., Caron C., Matthias G., Hess D., Khochbin S., Matthias P., HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo The EMBO Journal 2003 22 5 1168 1179 (Pubitemid 36313600)
    • (2003) EMBO Journal , vol.22 , Issue.5 , pp. 1168-1179
    • Zhang, Y.1    Li, N.2    Caron, C.3    Matthias, G.4    Hess, D.5    Khochbin, S.6    Matthias, P.7
  • 62
    • 0037291214 scopus 로고    scopus 로고
    • +-dependent tubulin deacetylase
    • DOI 10.1016/S1097-2765(03)00038-8
    • North B. J., Marshall B. L., Borra M. T., Denu J. M., Verdin E., The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase Molecular Cell 2003 11 2 437 444 (Pubitemid 36293837)
    • (2003) Molecular Cell , vol.11 , Issue.2 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 65
    • 34047175919 scopus 로고    scopus 로고
    • Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation
    • DOI 10.1523/JNEUROSCI.0037-07.2007
    • Dompierre J. P., Godin J. D., Charrin B. C., Cordelires F. P., King S. J., Humbert S., Saudou F., Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation Journal of Neuroscience 2007 27 13 3571 3583 (Pubitemid 46515140)
    • (2007) Journal of Neuroscience , vol.27 , Issue.13 , pp. 3571-3583
    • Dompierre, J.P.1    Godin, J.D.2    Charrin, B.C.3    Cordelieres, F.P.4    King, S.J.5    Humbert, S.6    Saudou, F.7
  • 66
    • 33750618516 scopus 로고    scopus 로고
    • Microtubule Acetylation Promotes Kinesin-1 Binding and Transport
    • DOI 10.1016/j.cub.2006.09.014, PII S096098220602207X
    • Reed N. A., Cai D., Blasius T. L., Jih G. T., Meyhofer E., Gaertig J., Verhey K. J., Microtubule acetylation promotes kinesin-1 binding and transport Current Biology 2006 16 21 2166 2172 (Pubitemid 44692098)
    • (2006) Current Biology , vol.16 , Issue.21 , pp. 2166-2172
    • Reed, N.A.1    Cai, D.2    Blasius, T.L.3    Jih, G.T.4    Meyhofer, E.5    Gaertig, J.6    Verhey, K.J.7
  • 68
    • 0033563155 scopus 로고    scopus 로고
    • Microtubule motors in spindle and chromosome motility
    • DOI 10.1046/j.1432-1327.1999.00339.x
    • Endow S. A., Microtubule motors in spindle and chromosome motility European Journal of Biochemistry 1999 262 1 12 18 (Pubitemid 29242603)
    • (1999) European Journal of Biochemistry , vol.262 , Issue.1 , pp. 12-18
    • Endow, S.A.1
  • 69
    • 0032558718 scopus 로고    scopus 로고
    • Direction determination in the minus-end-directed kinesin motor ncd
    • DOI 10.1038/27463
    • Sablin E. P., Case R. B., Dai S. C., Hart C. L., Ruby A., Vale R. D., Fletterick R. J., Direction determination in the minus-end-directed kinesin motor ncd Nature 1998 395 6704 813 816 (Pubitemid 28485450)
    • (1998) Nature , vol.395 , Issue.6704 , pp. 813-816
    • Sablin, E.P.1    Case, R.B.2    Dai, S.C.3    Hart, C.L.4    Ruby, A.5    Vale, R.D.6    Fletterick, R.J.7
  • 70
    • 9244232349 scopus 로고    scopus 로고
    • Molecular motors: Strategies to get along
    • Mallik R., Gross S. P., Molecular motors: strategies to get along Current Biology 2004 14 22 R971 R982
    • (2004) Current Biology , vol.14 , Issue.22
    • Mallik, R.1    Gross, S.P.2
  • 71
    • 0037452091 scopus 로고    scopus 로고
    • Molecular motors
    • DOI 10.1038/nature01601
    • Schliwa M., Woehlke G., Molecular motors Nature 2003 422 6933 759 765 (Pubitemid 36514119)
    • (2003) Nature , vol.422 , Issue.6933 , pp. 759-765
    • Schliwa, M.1    Woehlke, G.2
  • 74
    • 1442328913 scopus 로고    scopus 로고
    • Familial dysautonomia
    • DOI 10.1002/mus.10499
    • Axelrod F. B., Familial dysautonomia Muscle and Nerve 2004 29 3 352 363 (Pubitemid 38269753)
    • (2004) Muscle and Nerve , vol.29 , Issue.3 , pp. 352-363
    • Axelrod, F.B.1
  • 80
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • DOI 10.1038/47412
    • Strahl B. D., Allis C. D., The language of covalent histone modifications Nature 2000 403 6765 41 45 (Pubitemid 30038513
    • (2000) Nature , vol.403 , Issue.6765 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.