메뉴 건너뛰기




Volumn 5, Issue 3, 2015, Pages 2140-2159

The altered hepatic tubulin code in alcoholic liver disease

Author keywords

Acetylation; Ethanol; Hepatocytes; Liver; Microtubules; Post translational modifications; Tubulin

Indexed keywords

ALDEHYDE DEHYDROGENASE; ALPHA TUBULIN; CYTOCHROME P450; HISTONE DEACETYLASE 6; MALONALDEHYDE; MICROTUBULE ASSOCIATED PROTEIN; PACLITAXEL; REACTIVE OXYGEN METABOLITE; SIRTUIN 2; STAT5B PROTEIN; TRICHOSTATIN A; TUBULIN;

EID: 85012049366     PISSN: None     EISSN: 2218273X     Source Type: Journal    
DOI: 10.3390/biom5032140     Document Type: Review
Times cited : (16)

References (139)
  • 1
    • 84966603444 scopus 로고    scopus 로고
    • World Health Organization: Geneva, Switzerland
    • World Health Organization. Global Status Report on Alcohol and Health; World Health Organization: Geneva, Switzerland, 2014; pp. 48–51
    • (2014) Global Status Report on Alcohol and Health , pp. 48-51
  • 2
    • 0023375567 scopus 로고
    • Covalent binding of acetaldehyde to tubulin: Evidence for preferential binding to the alpha-chain
    • Jennett, R.B.; Sorrell, M.F.; Johnson, E.L.; Tuma, D.J. Covalent binding of acetaldehyde to tubulin: Evidence for preferential binding to the alpha-chain. Arch. Biochem. Biophys. 1987, 256, 10–18
    • (1987) Arch. Biochem. Biophys , vol.256 , pp. 10-18
    • Jennett, R.B.1    Sorrell, M.F.2    Johnson, E.L.3    Tuma, D.J.4
  • 3
    • 0024493970 scopus 로고
    • Preferential covalent binding of acetaldehyde to the alpha-chain of purified rat liver tubulin
    • Jennett, R.B.; Sorrell, M.F.; Saffari-Fard, A.; Ockner, J.L.; Tuma, D.J. Preferential covalent binding of acetaldehyde to the alpha-chain of purified rat liver tubulin. Hepatology 1989, 9, 57–62
    • (1989) Hepatology , vol.9 , pp. 57-62
    • Jennett, R.B.1    Sorrell, M.F.2    Saffari-Fard, A.3    Ockner, J.L.4    Tuma, D.J.5
  • 4
    • 0020478787 scopus 로고
    • Effects of reductive methylation on microtubule assembly. Evidence for an essential amino group in the alpha-chain
    • Szasz, J.; Burns, R.; Sternlicht, H. Effects of reductive methylation on microtubule assembly. Evidence for an essential amino group in the alpha-chain. J. Biol. Chem. 1982, 257, 3697–3704
    • (1982) J. Biol. Chem , vol.257 , pp. 3697-3704
    • Szasz, J.1    Burns, R.2    Sternlicht, H.3
  • 5
    • 0022521740 scopus 로고
    • Microtubule assembly is dependent on a cluster of basic residues in alpha-tubulin
    • Szasz, J.; Yaffe, M.B.; Elzinga, M.; Blank, G.S.; Sternlicht, H. Microtubule assembly is dependent on a cluster of basic residues in alpha-tubulin. Biochemistry 1986, 25, 4572–4582
    • (1986) Biochemistry , vol.25 , pp. 4572-4582
    • Szasz, J.1    Yaffe, M.B.2    Elzinga, M.3    Blank, G.S.4    Sternlicht, H.5
  • 6
    • 0023160659 scopus 로고
    • The interaction of acetaldehyde with tubulin
    • Tuma, D.J.; Jennett, R.B.; Sorrell, M.F. The interaction of acetaldehyde with tubulin. Ann. NY Acad. Sci. 1987, 492, 277–286
    • (1987) Ann. NY Acad. Sci , vol.492 , pp. 277-286
    • Tuma, D.J.1    Jennett, R.B.2    Sorrell, M.F.3
  • 8
    • 0031957743 scopus 로고    scopus 로고
    • Ethanol-induced alterations of the microtubule cytoskeleton in hepatocytes
    • Yoon, Y.; Torok, N.; Krueger, E.; Oswald, B.; McNiven, M.A. Ethanol-induced alterations of the microtubule cytoskeleton in hepatocytes. Am. J. Physiol. 1998, 274, G757–G766
    • (1998) Am. J. Physiol , vol.274
    • Yoon, Y.1    Torok, N.2    Krueger, E.3    Oswald, B.4    McNiven, M.A.5
  • 9
    • 34548830425 scopus 로고    scopus 로고
    • The tubulin code
    • Verhey, K.J.; Gaertig, J. The tubulin code. Cell Cycle 2007, 6, 2152–2160
    • (2007) Cell Cycle , vol.6 , pp. 2152-2160
    • Verhey, K.J.1    Gaertig, J.2
  • 10
    • 84906491034 scopus 로고    scopus 로고
    • The tubulin code: Molecular components, readout mechanisms, and functions
    • Janke, C. The tubulin code: Molecular components, readout mechanisms, and functions. J. Cell Biol. 2014, 206, 461–472
    • (2014) J. Cell Biol , vol.206 , pp. 461-472
    • Janke, C.1
  • 11
    • 81855196008 scopus 로고    scopus 로고
    • Post-translational regulation of the microtubule cytoskeleton: Mechanisms and functions
    • Janke, C.; Bulinski, J.C. Post-translational regulation of the microtubule cytoskeleton: Mechanisms and functions. Nat. Rev. Mol. Cell Biol. 2011, 12, 773–786
    • (2011) Nat. Rev. Mol. Cell Biol , vol.12 , pp. 773-786
    • Janke, C.1    Bulinski, J.C.2
  • 12
    • 84923222368 scopus 로고    scopus 로고
    • Post-translational modifications of tubulin: Pathways to functional diversity of microtubules
    • Song, Y.; Brady, S.T. Post-translational modifications of tubulin: Pathways to functional diversity of microtubules. Trends Cell Biol. 2015, 25, 125–136
    • (2015) Trends Cell Biol , vol.25 , pp. 125-136
    • Song, Y.1    Brady, S.T.2
  • 13
    • 18844475127 scopus 로고
    • Microtubules are acetylated in domains that turn over slowly
    • Webster, D.R.; Borisy, G.G. Microtubules are acetylated in domains that turn over slowly. J. Cell Sci. 1989, 92, 57–65
    • (1989) J. Cell Sci , vol.92 , pp. 57-65
    • Webster, D.R.1    Borisy, G.G.2
  • 14
    • 0345169048 scopus 로고    scopus 로고
    • Post-translational modifications regulate microtubule function
    • Westermann, S.; Weber, K. Post-translational modifications regulate microtubule function. Nat. Rev. Mol. Cell Biol. 2003, 4, 938–947
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 938-947
    • Westermann, S.1    Weber, K.2
  • 15
  • 16
    • 76649103368 scopus 로고    scopus 로고
    • The perennial organelle: Assembly and disassembly of the primary cilium
    • Seeley, E.S.; Nachury, M.V. The perennial organelle: Assembly and disassembly of the primary cilium. J. Cell Sci. 2010, 123, 511–518
    • (2010) J. Cell Sci , vol.123 , pp. 511-518
    • Seeley, E.S.1    Nachury, M.V.2
  • 18
    • 79953304482 scopus 로고    scopus 로고
    • The posttranslational modification of tubulin undergoes a switch from detyrosination to acetylation as epithelial cells become polarized
    • Quinones, G.B.; Danowski, B.A.; Devaraj, A.; Singh, V.; Ligon, L.A. The posttranslational modification of tubulin undergoes a switch from detyrosination to acetylation as epithelial cells become polarized. Mol. Biol. Cell 2011, 22, 1045–1057
    • (2011) Mol. Biol. Cell , vol.22 , pp. 1045-1057
    • Quinones, G.B.1    Danowski, B.A.2    Devaraj, A.3    Singh, V.4    Ligon, L.A.5
  • 19
    • 84875629022 scopus 로고    scopus 로고
    • Tubulin detyrosination promotes monolayer formation and apical trafficking in epithelial cells
    • Zink, S.; Grosse, L.; Freikamp, A.; Banfer, S.; Muksch, F.; Jacob, R. Tubulin detyrosination promotes monolayer formation and apical trafficking in epithelial cells. J.Cell Sci. 2012, 125, 5998–6008
    • (2012) J.Cell Sci , vol.125 , pp. 5998-6008
    • Zink, S.1    Grosse, L.2    Freikamp, A.3    Banfer, S.4    Muksch, F.5    Jacob, R.6
  • 20
    • 33645758040 scopus 로고    scopus 로고
    • Microtubules are more stable and more highly acetylated in ethanol-treated hepatic cells
    • Kannarkat, G.T.; Tuma, D.J.; Tuma, P.L. Microtubules are more stable and more highly acetylated in ethanol-treated hepatic cells. J. Hepatol. 2006, 44, 963–970
    • (2006) J. Hepatol , vol.44 , pp. 963-970
    • Kannarkat, G.T.1    Tuma, D.J.2    Tuma, P.L.3
  • 22
    • 84871280921 scopus 로고    scopus 로고
    • Hepatic microtubule acetylation and stability induced by chronic alcohol exposure impair nuclear translocation of STAT3 and STAT5B, but not Smad2/3
    • Fernandez, D.J.; Tuma, D.J.; Tuma, P.L. Hepatic microtubule acetylation and stability induced by chronic alcohol exposure impair nuclear translocation of STAT3 and STAT5B, but not Smad2/3. Am. J. Physiol. Gastrointest. Liver Physiol. 2012, 303, G1402–G1415
    • (2012) Am. J. Physiol. Gastrointest. Liver Physiol , vol.303
    • Fernandez, D.J.1    Tuma, D.J.2    Tuma, P.L.3
  • 25
    • 84883307077 scopus 로고    scopus 로고
    • Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation
    • Weinert, B.T.; Scholz, C.; Wagner, S.A.; Iesmantavicius, V.; Su, D.; Daniel, J.A.; Choudhary, C. Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. Cell Rep. 2013, 4, 842–851
    • (2013) Cell Rep , vol.4 , pp. 842-851
    • Weinert, B.T.1    Scholz, C.2    Wagner, S.A.3    Iesmantavicius, V.4    Su, D.5    Daniel, J.A.6    Choudhary, C.7
  • 27
    • 0023188734 scopus 로고
    • Acetylation of alpha-tubulin in cultured neurons and the induction of alpha-tubulin acetylation in PC12 cells by treatment with nerve growth factor
    • Black, M.M.; Keyser, P. Acetylation of alpha-tubulin in cultured neurons and the induction of alpha-tubulin acetylation in PC12 cells by treatment with nerve growth factor. J. Neurosci. 1987, 7, 1833–1842
    • (1987) J. Neurosci , vol.7 , pp. 1833-1842
    • Black, M.M.1    Keyser, P.2
  • 28
    • 0027537548 scopus 로고
    • Composite microtubules of the axon: Quantitative analysis of tyrosinated and acetylated tubulin along individual axonal microtubules
    • Brown, A.; Li, Y.; Slaughter, T.; Black, M.M. Composite microtubules of the axon: Quantitative analysis of tyrosinated and acetylated tubulin along individual axonal microtubules. J. Cell Sci. 1993, 104, 339–352
    • (1993) J. Cell Sci , vol.104 , pp. 339-352
    • Brown, A.1    Li, Y.2    Slaughter, T.3    Black, M.M.4
  • 29
    • 0023187071 scopus 로고
    • Posttranslational modifications of alpha-tubulin: Acetylated and detyrosinated forms in axons of rat cerebellum
    • Cambray-Deakin, M.A.; Burgoyne, R.D. Posttranslational modifications of alpha-tubulin: Acetylated and detyrosinated forms in axons of rat cerebellum. J. Cell Biol. 1987, 104, 1569–1574
    • (1987) J. Cell Biol , vol.104 , pp. 1569-1574
    • Cambray-Deakin, M.A.1    Burgoyne, R.D.2
  • 30
    • 0026055072 scopus 로고
    • Depletion of acetylated alpha-tubulin during microtubule purification from bovine brain gray and white matter regions
    • Kim, H. Depletion of acetylated alpha-tubulin during microtubule purification from bovine brain gray and white matter regions. J.Neurosci.Res. 1991, 30, 172–182
    • (1991) J.Neurosci.Res , vol.30 , pp. 172-182
    • Kim, H.1
  • 31
    • 0020540736 scopus 로고
    • Chlamydomonas alpha-tubulin is posttranslationally modified in the flagella during flagellar assembly
    • L’Hernault, S.W.; Rosenbaum, J.L. Chlamydomonas alpha-tubulin is posttranslationally modified in the flagella during flagellar assembly. J. Cell Biol. 1983, 97, 258–263
    • (1983) J. Cell Biol , vol.97 , pp. 258-263
    • L’Hernault, S.W.1    Rosenbaum, J.L.2
  • 32
    • 0022399572 scopus 로고
    • Monoclonal antibodies specific for an acetylated form of alpha-tubulin recognize the antigen in cilia and flagella from a variety of organisms
    • Piperno, G.; Fuller, M.T. Monoclonal antibodies specific for an acetylated form of alpha-tubulin recognize the antigen in cilia and flagella from a variety of organisms. J. Cell Biol. 1985, 101, 2085–2094
    • (1985) J. Cell Biol , vol.101 , pp. 2085-2094
    • Piperno, G.1    Fuller, M.T.2
  • 33
    • 0023293040 scopus 로고
    • Microtubules containing acetylated alpha-tubulin in mammalian cells in culture
    • Piperno, G.; LeDizet, M.; Chang, X.J. Microtubules containing acetylated alpha-tubulin in mammalian cells in culture. J. Cell Biol. 1987, 104, 289–302
    • (1987) J. Cell Biol , vol.104 , pp. 289-302
    • Piperno, G.1    Ledizet, M.2    Chang, X.J.3
  • 34
    • 79951819919 scopus 로고    scopus 로고
    • A novel acetylation of beta-tubulin by San modulates microtubule polymerization via down-regulating tubulin incorporation. Mol. Biol
    • Chu, C.W.; Hou, F.; Zhang, J.; Phu, L.; Loktev, A.V.; Kirkpatrick, D.S.; Jackson, P.K.; Zhao, Y.; Zou, H. A novel acetylation of beta-tubulin by San modulates microtubule polymerization via down-regulating tubulin incorporation. Mol. Biol. Cell 2011, 22, 448–456
    • (2011) Cell , vol.22 , pp. 448-456
    • Chu, C.W.1    Hou, F.2    Zhang, J.3    Phu, L.4    Loktev, A.V.5    Kirkpatrick, D.S.6    Jackson, P.K.7    Zhao, Y.8    Zou, H.9
  • 35
    • 0025313509 scopus 로고
    • Individual microtubules in the axon consist of domains that differ in both composition and stability
    • Baas, P.W.; Black, M.M. Individual microtubules in the axon consist of domains that differ in both composition and stability. J. Cell Biol. 1990, 111, 495–509
    • (1990) J. Cell Biol , vol.111 , pp. 495-509
    • Baas, P.W.1    Black, M.M.2
  • 37
    • 0022976646 scopus 로고
    • Ultrastructural colocalization of tyrosinated and detyrosinated alpha-tubulin in interphase and mitotic cells
    • Geuens, G.; Gundersen, G.G.; Nuydens, R.; Cornelissen, F.; Bulinski, J.C.; DeBrabander, M. Ultrastructural colocalization of tyrosinated and detyrosinated alpha-tubulin in interphase and mitotic cells. J. Cell Biol. 1986, 103, 1883–1893
    • (1986) J. Cell Biol , vol.103 , pp. 1883-1893
    • Geuens, G.1    Gundersen, G.G.2    Nuydens, R.3    Cornelissen, F.4    Bulinski, J.C.5    Debrabander, M.6
  • 38
    • 0022501223 scopus 로고
    • Distribution of tyrosinated and nontyrosinated alpha-tubulin during mitosis
    • Gundersen, G.G.; Bulinski, J.C. Distribution of tyrosinated and nontyrosinated alpha-tubulin during mitosis. J. Cell Biol. 1986, 102, 1118–1126
    • (1986) J. Cell Biol , vol.102 , pp. 1118-1126
    • Gundersen, G.G.1    Bulinski, J.C.2
  • 39
    • 0021752265 scopus 로고
    • Distinct populations of microtubules: Tyrosinated and nontyrosinated alpha tubulin are distributed differently in vivo
    • Gundersen, G.G.; Kalnoski, M.H.; Bulinski, J.C. Distinct populations of microtubules: Tyrosinated and nontyrosinated alpha tubulin are distributed differently in vivo. Cell 1984, 38, 779–789
    • (1984) Cell , vol.38 , pp. 779-789
    • Gundersen, G.G.1    Kalnoski, M.H.2    Bulinski, J.C.3
  • 40
    • 0031905985 scopus 로고    scopus 로고
    • The axonemal microtubules of the Chlamydomonas flagellum differ in tubulin isoform content
    • Johnson, K.A. The axonemal microtubules of the Chlamydomonas flagellum differ in tubulin isoform content. J. Cell Sci. 1998, 111, 313–320
    • (1998) J. Cell Sci , vol.111 , pp. 313-320
    • Johnson, K.A.1
  • 41
    • 0017406215 scopus 로고
    • Enzyme which specifically adds tyrosine to the alpha chain of tubulin
    • Raybin, D.; Flavin, M. Enzyme which specifically adds tyrosine to the alpha chain of tubulin. Biochemistry 1977, 16, 2189–2194
    • (1977) Biochemistry , vol.16 , pp. 2189-2194
    • Raybin, D.1    Flavin, M.2
  • 42
    • 0024511885 scopus 로고
    • Differential localisation of tyrosinated, detyrosinated, and acetylated alpha-tubulins in neurites and growth cones of dorsal root ganglion neurons
    • Robson, S.J.; Burgoyne, R.D. Differential localisation of tyrosinated, detyrosinated, and acetylated alpha-tubulins in neurites and growth cones of dorsal root ganglion neurons. Cell Motil. Cytoskelet. 1989, 12, 273–282
    • (1989) Cell Motil. Cytoskelet , vol.12 , pp. 273-282
    • Robson, S.J.1    Burgoyne, R.D.2
  • 44
    • 0028283568 scopus 로고
    • Job, D. Accumulation of delta 2-tubulin, a major tubulin variant that cannot be tyrosinated, in neuronal tissues and in stable microtubule assemblies
    • Paturle-Lafanechere, L.; Manier, M.; Trigault, N.; Pirollet, F.; Mazarguil, H.; Job, D. Accumulation of delta 2-tubulin, a major tubulin variant that cannot be tyrosinated, in neuronal tissues and in stable microtubule assemblies. J. Cell Sci. 1994, 107, 1529–1543
    • (1994) J. Cell Sci , vol.107 , pp. 1529-1543
    • Paturle-Lafanechere, L.1    Manier, M.2    Trigault, N.3    Pirollet, F.4    Mazarguil, H.5
  • 48
    • 0027934789 scopus 로고
    • Developmental regulation of polyglutamylated alpha- and beta-tubulin in mouse brain neurons
    • Audebert, S.; Koulakoff, A.; Berwald-Netter, Y.; Gros, F.; Denoulet, P.; Edde, B. Developmental regulation of polyglutamylated alpha- and beta-tubulin in mouse brain neurons. J. Cell Sci. 1994, 107, 2313–2322
    • (1994) J. Cell Sci , vol.107 , pp. 2313-2322
    • Audebert, S.1    Koulakoff, A.2    Berwald-Netter, Y.3    Gros, F.4    Denoulet, P.5    Edde, B.6
  • 49
    • 0032517865 scopus 로고    scopus 로고
    • Centriole disassembly in vivo and its effect on centrosome structure and function in vertebrate cells
    • Bobinnec, Y.; Khodjakov, A.; Mir, L.M.; Rieder, C.L.; Edde, B.; Bornens, M. Centriole disassembly in vivo and its effect on centrosome structure and function in vertebrate cells. J. Cell Biol. 1998, 143, 1575–1589
    • (1998) J. Cell Biol , vol.143 , pp. 1575-1589
    • Bobinnec, Y.1    Khodjakov, A.2    Mir, L.M.3    Rieder, C.L.4    Edde, B.5    Bornens, M.6
  • 50
    • 0028210453 scopus 로고
    • Glutamylated tubulin probed in ciliates with the monoclonal antibody GT335
    • Bre, M.H.; de Nechaud, B.; Wolff, A.; Fleury, A. Glutamylated tubulin probed in ciliates with the monoclonal antibody GT335. Cell Motil.Cytoskelet. 1994, 27, 337–349
    • (1994) Cell Motil.Cytoskelet , vol.27 , pp. 337-349
    • Bre, M.H.1    De Nechaud, B.2    Wolff, A.3    Fleury, A.4
  • 53
    • 0028071995 scopus 로고
    • Class I and IVa beta-tubulin isotypes expressed in adult mouse brain are glutamylated
    • Mary, J.; Redeker, V.; le Caer, J.P.; Prome, J.C.; Rossier, J. Class I and IVa beta-tubulin isotypes expressed in adult mouse brain are glutamylated. FEBS Lett. 1994, 353, 89–94
    • (1994) FEBS Lett , vol.353 , pp. 89-94
    • Mary, J.1    Redeker, V.2    Le Caer, J.P.3    Prome, J.C.4    Rossier, J.5
  • 54
    • 0029966076 scopus 로고    scopus 로고
    • Posttranslational modifications in the C-terminal tail of axonemal tubulin from sea urchin sperm
    • Mary, J.; Redeker, V.; le Caer, J.P.; Rossier, J.; Schmitter, J.M. Posttranslational modifications in the C-terminal tail of axonemal tubulin from sea urchin sperm. J. Biol. Chem. 1996, 271, 9928–9933
    • (1996) J. Biol. Chem , vol.271 , pp. 9928-9933
    • Mary, J.1    Redeker, V.2    Le Caer, J.P.3    Rossier, J.4    Schmitter, J.M.5
  • 56
    • 0026773956 scopus 로고
    • Tubulin, the major brain beta tubulin isotype is polyglutamylated on glutamic acid residue 435
    • Rudiger, M.; Plessman, U.; Kloppel, K.D.; Wehland, J.; Weber, K. Class II tubulin, the major brain beta tubulin isotype is polyglutamylated on glutamic acid residue 435. FEBS Lett. 1992, 308, 101–105
    • (1992) FEBS Lett , vol.308 , pp. 101-105
    • Rudiger, M.1    Plessman, U.2    Kloppel, K.D.3    Wehland, J.4    Weber, K.5    Class, I.I.6
  • 58
    • 9244261065 scopus 로고    scopus 로고
    • Axonemal tubulin polyglycylation probed with two monoclonal antibodies: Widespread evolutionary distribution, appearance during spermatozoan maturation and possible function in motility
    • Bre, M.H.; Redeker, V.; Quibell, M.; Darmanaden-Delorme, J.; Bressac, C.; Cosson, J.; Huitorel, P.; Schmitter, J.M.; Rossler, J.; Johnson, T., et al. Axonemal tubulin polyglycylation probed with two monoclonal antibodies: Widespread evolutionary distribution, appearance during spermatozoan maturation and possible function in motility. J. Cell Sci. 1996, 109, 727–738
    • (1996) J. Cell Sci , vol.109 , pp. 727-738
    • Bre, M.H.1    Redeker, V.2    Quibell, M.3    Darmanaden-Delorme, J.4    Bressac, C.5    Cosson, J.6    Huitorel, P.7    Schmitter, J.M.8    Rossler, J.9    Johnson, T.10
  • 59
    • 0029125382 scopus 로고
    • Monoclonal and polyclonal antibodies detect a new type of post-translational modification of axonemal tubulin
    • Levilliers, N.; Fleury, A.; Hill, A.M. Monoclonal and polyclonal antibodies detect a new type of post-translational modification of axonemal tubulin. J.Cell Sci. 1995, 108, 3013–3028
    • (1995) J.Cell Sci , vol.108 , pp. 3013-3028
    • Levilliers, N.1    Fleury, A.2    Hill, A.M.3
  • 62
    • 0041851031 scopus 로고    scopus 로고
    • Glycosylation of the alpha and beta tubulin by sialyloligosaccharides
    • Hino, M.; Kijima-Suda, I.; Nagai, Y.; Hosoya, H. Glycosylation of the alpha and beta tubulin by sialyloligosaccharides. Zool.Sci. 2003, 20, 709–715
    • (2003) Zool.Sci , vol.20 , pp. 709-715
    • Hino, M.1    Kijima-Suda, I.2    Nagai, Y.3    Hosoya, H.4
  • 63
    • 79954435787 scopus 로고    scopus 로고
    • O-GlcNAcylation of tubulin inhibits its polymerization
    • Ji, S.; Kang, J.G.; Park, S.Y.; Lee, J.; Oh, Y.J.; Cho, J.W. O-GlcNAcylation of tubulin inhibits its polymerization. Amino Acids 2011, 40, 809–818
    • (2011) Amino Acids , vol.40 , pp. 809-818
    • Ji, S.1    Kang, J.G.2    Park, S.Y.3    Lee, J.4    Oh, Y.J.5    Cho, J.W.6
  • 64
    • 0037304213 scopus 로고    scopus 로고
    • High glucose and insulin promote O-GlcNAc modification of proteins, including alpha-tubulin
    • Walgren, J.L.; Vincent, T.S.; Schey, K.L.; Buse, M.G. High glucose and insulin promote O-GlcNAc modification of proteins, including alpha-tubulin. Am.J.Physiol.Endocrinol.Metab. 2003, 284, E424–E434
    • (2003) Am.J.Physiol.Endocrinol.Metab , vol.284
    • Walgren, J.L.1    Vincent, T.S.2    Schey, K.L.3    Buse, M.G.4
  • 65
    • 0035166773 scopus 로고    scopus 로고
    • Single site alpha-tubulin mutation affects astral microtubules and nuclear positioning during anaphase in Saccharomyces cerevisiae: Possible role for palmitoylation of alpha-tubulin
    • Caron, J.M.; Vega, L.R.; Fleming, J.; Bishop, R.; Solomon, F. Single site alpha-tubulin mutation affects astral microtubules and nuclear positioning during anaphase in Saccharomyces cerevisiae: Possible role for palmitoylation of alpha-tubulin. Mol.Biol.Cell 2001, 12, 2672–2687
    • (2001) Mol.Biol.Cell , vol.12 , pp. 2672-2687
    • Caron, J.M.1    Vega, L.R.2    Fleming, J.3    Bishop, R.4    Solomon, F.5
  • 66
    • 77249134163 scopus 로고    scopus 로고
    • Protein palmitoylation in neuronal development and synaptic plasticity
    • Fukata, Y.; Fukata, M. Protein palmitoylation in neuronal development and synaptic plasticity. Nat.Rev.Neurosci. 2010, 11, 161–175
    • (2010) Nat.Rev.Neurosci , vol.11 , pp. 161-175
    • Fukata, Y.1    Fukata, M.2
  • 67
    • 0030964954 scopus 로고    scopus 로고
    • Posttranslational modification of tubulin by palmitoylation: II. Identification of sites of palmitoylation
    • Ozols, J.; Caron, J.M. Posttranslational modification of tubulin by palmitoylation: II. Identification of sites of palmitoylation. Mol.Biol.Cell 1997, 8, 637–645
    • (1997) Mol.Biol.Cell , vol.8 , pp. 637-645
    • Ozols, J.1    Caron, J.M.2
  • 69
    • 0015984215 scopus 로고
    • Properties of rat brain tubulin
    • Eipper, B.A. Properties of rat brain tubulin. J.Biol.Chem. 1974, 249, 1407–1416
    • (1974) J.Biol.Chem , vol.249 , pp. 1407-1416
    • Eipper, B.A.1
  • 71
    • 0021990889 scopus 로고
    • A polymer-dependent increase in phosphorylation of beta-tubulin accompanies differentiation of a mouse neuroblastoma cell line
    • Gard, D.L.; Kirschner, M.W. A polymer-dependent increase in phosphorylation of beta-tubulin accompanies differentiation of a mouse neuroblastoma cell line. J. Cell Biol. 1985, 100, 764–774
    • (1985) J. Cell Biol , vol.100 , pp. 764-774
    • Gard, D.L.1    Kirschner, M.W.2
  • 72
    • 6344242879 scopus 로고    scopus 로고
    • The human C-Fes tyrosine kinase binds tubulin and microtubules through separate domains and promotes microtubule assembly
    • Laurent, C.E.; Delfino, F.J.; Cheng, H.Y.; Smithgall, T.E. The human C-Fes tyrosine kinase binds tubulin and microtubules through separate domains and promotes microtubule assembly. Mol. Cell Biol. 2004, 24, 9351–9358
    • (2004) Mol. Cell Biol , vol.24 , pp. 9351-9358
    • Laurent, C.E.1    Delfino, F.J.2    Cheng, H.Y.3    Smithgall, T.E.4
  • 73
    • 4744360999 scopus 로고    scopus 로고
    • Proteome-wide approach identifies sumoylated substrate proteins in yeast
    • Panse, V.G.; Hardeland, U.; Werner, T.; Kuster, B.; Hurt, E. A proteome-wide approach identifies sumoylated substrate proteins in yeast. J. Biol. Chem. 2004, 279, 41346–41351
    • (2004) J. Biol. Chem , vol.279 , pp. 41346-41351
    • Panse, V.G.1    Hardeland, U.2    Werner, T.3    Kuster, B.4    Hurt, E.A.5
  • 75
    • 69449094091 scopus 로고    scopus 로고
    • The ubiquitin conjugation system is involved in the disassembly of cilia and flagella
    • Huang, K.; Diener, D.R.; Rosenbaum, J.L. The ubiquitin conjugation system is involved in the disassembly of cilia and flagella. J. Cell Biol. 2009, 186, 601–613
    • (2009) J. Cell Biol , vol.186 , pp. 601-613
    • Huang, K.1    Diener, D.R.2    Rosenbaum, J.L.3
  • 76
    • 0037738525 scopus 로고    scopus 로고
    • Parkin binds to alpha/beta tubulin and increases their ubiquitination and degradation
    • Ren, Y.; Zhao, J.; Feng, J. Parkin binds to alpha/beta tubulin and increases their ubiquitination and degradation. J. Neurosci. 2003, 23, 3316–3324
    • (2003) J. Neurosci , vol.23 , pp. 3316-3324
    • Ren, Y.1    Zhao, J.2    Feng, J.3
  • 77
    • 78651225388 scopus 로고    scopus 로고
    • Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling
    • Xu, G.; Paige, J.S.; Jaffrey, S.R. Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling. Nat. Biotechnol. 2010, 28, 868–873
    • (2010) Nat. Biotechnol , vol.28 , pp. 868-873
    • Xu, G.1    Paige, J.S.2    Jaffrey, S.R.3
  • 79
    • 16544373246 scopus 로고    scopus 로고
    • Dangerous byproducts of alcohol breakdown—Focus on adducts
    • Tuma, D.J.; Casey, C.A. Dangerous byproducts of alcohol breakdown—Focus on adducts. Alcohol. Res. Health 2003, 27, 285–290
    • (2003) Alcohol. Res. Health , vol.27 , pp. 285-290
    • Tuma, D.J.1    Casey, C.A.2
  • 80
    • 0018966073 scopus 로고
    • Effect of ethanol and its metabolites on microtubule formation
    • Jennett, R.B.; Tuma, D.J.; Sorrell, M.F. Effect of ethanol and its metabolites on microtubule formation. Pharmacology 1980, 21, 363–368
    • (1980) Pharmacology , vol.21 , pp. 363-368
    • Jennett, R.B.1    Tuma, D.J.2    Sorrell, M.F.3
  • 81
    • 0026636629 scopus 로고
    • Substoichiometric inhibition of microtubule formation by acetaldehyde-tubulin adducts
    • Smith, S.L.; Jennett, R.B.; Sorrell, M.F.; Tuma, D.J. Substoichiometric inhibition of microtubule formation by acetaldehyde-tubulin adducts. Biochem. Pharmacol. 1992, 44, 65–72
    • (1992) Biochem. Pharmacol , vol.44 , pp. 65-72
    • Smith, S.L.1    Jennett, R.B.2    Sorrell, M.F.3    Tuma, D.J.4
  • 83
    • 77954563433 scopus 로고    scopus 로고
    • S-nitrosoglutathione a physiologic nitric oxide carrier attenuates experimental autoimmune encephalomyelitis
    • Nath, N.; Morinaga, O.; Singh, I. S-nitrosoglutathione a physiologic nitric oxide carrier attenuates experimental autoimmune encephalomyelitis. J. Neuroimmune Pharmacol. 2010, 5, 240–251
    • (2010) J. Neuroimmune Pharmacol , vol.5 , pp. 240-251
    • Nath, N.1    Morinaga, O.2    Singh, I.3
  • 84
    • 84888126980 scopus 로고    scopus 로고
    • Differential S-nitrosylation of proteins in Alzheimer’s disease
    • Zahid, S.; Khan, R.; Oellerich, M.; Ahmed, N.; Asif, A.R. Differential S-nitrosylation of proteins in Alzheimer’s disease. Neuroscience 2014, 256, 126–136
    • (2014) Neuroscience , vol.256 , pp. 126-136
    • Zahid, S.1    Khan, R.2    Oellerich, M.3    Ahmed, N.4    Asif, A.R.5
  • 85
    • 34548477636 scopus 로고    scopus 로고
    • Residue-specific adduction of tubulin by 4-hydroxynonenal and 4-oxononenal causes cross-linking and inhibits polymerization
    • Stewart, B.J.; Doorn, J.A.; Petersen, D.R. Residue-specific adduction of tubulin by 4-hydroxynonenal and 4-oxononenal causes cross-linking and inhibits polymerization. Chem. Res. Toxicol. 2007, 20, 1111–1119
    • (2007) Chem. Res. Toxicol , vol.20 , pp. 1111-1119
    • Stewart, B.J.1    Doorn, J.A.2    Petersen, D.R.3
  • 87
    • 33644500142 scopus 로고    scopus 로고
    • Increased oxidation and degradation of cytosolic proteins in alcohol-exposed mouse liver and hepatoma cells
    • Kim, B.J.; Hood, B.L.; Aragon, R.A.; Hardwick, J.P.; Conrads, T.P.; Veenstra, T.D.; Song, B.J. Increased oxidation and degradation of cytosolic proteins in alcohol-exposed mouse liver and hepatoma cells. Proteomics 2006, 6, 1250–1260
    • (2006) Proteomics , vol.6 , pp. 1250-1260
    • Kim, B.J.1    Hood, B.L.2    Aragon, R.A.3    Hardwick, J.P.4    Conrads, T.P.5    Veenstra, T.D.6    Song, B.J.7
  • 88
    • 43949101050 scopus 로고    scopus 로고
    • Microtubule acetylation and stability may explain alcohol-induced alterations in hepatic protein trafficking
    • Joseph, R.A.; Shepard, B.D.; Kannarkat, G.T.; Rutledge, T.M.; Tuma, D.J.; Tuma, P.L. Microtubule acetylation and stability may explain alcohol-induced alterations in hepatic protein trafficking. Hepatology 2008, 47, 1745–1753
    • (2008) Hepatology , vol.47 , pp. 1745-1753
    • Joseph, R.A.1    Shepard, B.D.2    Kannarkat, G.T.3    Rutledge, T.M.4    Tuma, D.J.5    Tuma, P.L.6
  • 91
    • 78650731392 scopus 로고    scopus 로고
    • The major alpha-tubulin K40 acetyltransferase alphaTAT1 promotes rapid ciliogenesis and efficient mechanosensation
    • Shida, T.; Cueva, J.G.; Xu, Z.; Goodman, M.B.; Nachury, M.V. The major alpha-tubulin K40 acetyltransferase alphaTAT1 promotes rapid ciliogenesis and efficient mechanosensation. Proc. Natl. Acad. Sci. USA 2010, 107, 21517–21522
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 21517-21522
    • Shida, T.1    Cueva, J.G.2    Xu, Z.3    Goodman, M.B.4    Nachury, M.V.5
  • 94
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NAD+ -dependent tubulin deacetylase
    • 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. Mol.Cell 2003, 11, 437–444
    • (2003) Mol.Cell , vol.11 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 95
    • 0037416151 scopus 로고    scopus 로고
    • HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo
    • 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. EMBO J. 2003, 22, 1168–1179
    • (2003) EMBO J , vol.22 , pp. 1168-1179
    • Zhang, Y.1    Li, N.2    Caron, C.3    Matthias, G.4    Hess, D.5    Khochbin, S.6    Matthias, P.7
  • 96
    • 56149125341 scopus 로고    scopus 로고
    • Alcohol-induced alterations in hepatic microtubule dynamics can be explained by impaired histone deacetylase 6 function
    • Shepard, B.D.; Joseph, R.A.; Kannarkat, G.T.; Rutledge, T.M.; Tuma, D.J.; Tuma, P.L. Alcohol-induced alterations in hepatic microtubule dynamics can be explained by impaired histone deacetylase 6 function. Hepatology 2008, 48, 1671–1679
    • (2008) Hepatology , vol.48 , pp. 1671-1679
    • Shepard, B.D.1    Joseph, R.A.2    Kannarkat, G.T.3    Rutledge, T.M.4    Tuma, D.J.5    Tuma, P.L.6
  • 97
    • 0028228643 scopus 로고
    • Possible role for stable microtubules in intracellular transport from the endoplasmic reticulum to the Golgi apparatus
    • Mizuno, M.; Singer, S.J. A possible role for stable microtubules in intracellular transport from the endoplasmic reticulum to the Golgi apparatus. J. Cell Sci. 1994, 107, 1321–1331
    • (1994) J. Cell Sci , vol.107 , pp. 1321-1331
    • Mizuno, M.1    Singer, S.2
  • 99
    • 77955984502 scopus 로고    scopus 로고
    • Alcohol consumption impairs hepatic protein trafficking: Mechanisms and consequences
    • Shepard, B.D.; Fernandez, D.J.; Tuma, P.L. Alcohol consumption impairs hepatic protein trafficking: Mechanisms and consequences. Genes Nutr. 2009, 5, 129–140
    • (2009) Genes Nutr , vol.5 , pp. 129-140
    • Shepard, B.D.1    Fernandez, D.J.2    Tuma, P.L.3
  • 100
    • 57649116078 scopus 로고    scopus 로고
    • The gregarious lipid droplet
    • Goodman, J.M. The gregarious lipid droplet. J. Biol. Chem. 2008, 283, 28005–28009
    • (2008) J. Biol. Chem , vol.283 , pp. 28005-28009
    • Goodman, J.M.1
  • 101
    • 84862313783 scopus 로고    scopus 로고
    • The proteomics of lipid droplets: Structure, dynamics, and functions of the organelle conserved from bacteria to humans
    • Yang, L.; Ding, Y.; Chen, Y.; Zhang, S.; Huo, C.; Wang, Y.; Yu, J.; Zhang, P.; Na, H.; Zhang, H., et al. The proteomics of lipid droplets: Structure, dynamics, and functions of the organelle conserved from bacteria to humans. J. Lipid Res. 2012, 53, 1245–1253
    • (2012) J. Lipid Res , vol.53 , pp. 1245-1253
    • Yang, L.1    Ding, Y.2    Chen, Y.3    Zhang, S.4    Huo, C.5    Wang, Y.6    Yu, J.7    Zhang, P.8    Na, H.9    Zhang, H.10
  • 102
    • 84896991817 scopus 로고    scopus 로고
    • Recent insights into the molecular pathophysiology of lipid droplet formation in hepatocytes
    • Sahini, N.; Borlak, J. Recent insights into the molecular pathophysiology of lipid droplet formation in hepatocytes. Prog. Lipid Res. 2014, 54, 86–112
    • (2014) Prog. Lipid Res , vol.54 , pp. 86-112
    • Sahini, N.1    Borlak, J.2
  • 106
    • 0034611001 scopus 로고    scopus 로고
    • Dynein-mediated cargo transport in vivo. A switch controls travel distance
    • Gross, S.P.; Welte, M.A.; Block, S.M.; Wieschaus, E.F. Dynein-mediated cargo transport in vivo. A switch controls travel distance. J. Cell Biol. 2000, 148, 945–956
    • (2000) J. Cell Biol , vol.148 , pp. 945-956
    • Gross, S.P.1    Welte, M.A.2    Block, S.M.3    Wieschaus, E.F.4
  • 107
    • 57149145788 scopus 로고    scopus 로고
    • Consequences of motor copy number on the intracellular transport of kinesin-1-driven lipid droplets
    • Shubeita, G.T.; Tran, S.L.; Xu, J.; Vershinin, M.; Cermelli, S.; Cotton, S.L.; Welte, M.A.; Gross, S.P. Consequences of motor copy number on the intracellular transport of kinesin-1-driven lipid droplets. Cell 2008, 135, 1098–1107
    • (2008) Cell , vol.135 , pp. 1098-1107
    • Shubeita, G.T.1    Tran, S.L.2    Xu, J.3    Vershinin, M.4    Cermelli, S.5    Cotton, S.L.6    Welte, M.A.7    Gross, S.P.8
  • 110
    • 84879367440 scopus 로고    scopus 로고
    • Dynamics and molecular determinants of cytoplasmic lipid droplet clustering and dispersion
    • Orlicky, D.J.; Monks, J.; Stefanski, A.L.; McManaman, J.L. Dynamics and molecular determinants of cytoplasmic lipid droplet clustering and dispersion. PLoS ONE 2013, 8, e66837
    • (2013) Plos ONE , vol.8
    • Orlicky, D.J.1    Monks, J.2    Stefanski, A.L.3    McManaman, J.L.4
  • 111
    • 84872441219 scopus 로고    scopus 로고
    • Regulation of adipogenesis by cytoskeleton remodelling is facilitated by acetyltransferase MEC-17-dependent acetylation of alpha-tubulin
    • Yang, W.; Guo, X.; Thein, S.; Xu, F.; Sugii, S.; Baas, P.W.; Radda, G.K.; Han, W. Regulation of adipogenesis by cytoskeleton remodelling is facilitated by acetyltransferase MEC-17-dependent acetylation of alpha-tubulin. Biochem. J. 2013, 449, 605–612
    • (2013) Biochem. J , vol.449 , pp. 605-612
    • Yang, W.1    Guo, X.2    Thein, S.3    Xu, F.4    Sugii, S.5    Baas, P.W.6    Radda, G.K.7    Han, W.8
  • 112
    • 84899444482 scopus 로고    scopus 로고
    • Reactive oxygen species, AMP-activated protein kinase, and the transcription cofactor p300 regulate alpha-tubulin acetyltransferase-1 (AlphaTAT-1/MEC-17)-dependent microtubule hyperacetylation during cell stress
    • Mackeh, R.; Lorin, S.; Ratier, A.; Mejdoubi-Charef, N.; Baillet, A.; Bruneel, A.; Hamai, A.; Codogno, P.; Pous, C.; Perdiz, D. Reactive oxygen species, AMP-activated protein kinase, and the transcription cofactor p300 regulate alpha-tubulin acetyltransferase-1 (alphaTAT-1/MEC-17)-dependent microtubule hyperacetylation during cell stress. J.Biol.Chem. 2014, 289, 11816–11828
    • (2014) J.Biol.Chem , vol.289 , pp. 11816-11828
    • Mackeh, R.1    Lorin, S.2    Ratier, A.3    Mejdoubi-Charef, N.4    Baillet, A.5    Bruneel, A.6    Hamai, A.7    Codogno, P.8    Pous, C.9    Perdiz, D.10
  • 113
    • 34848817401 scopus 로고    scopus 로고
    • Alcohol-induced steatosis in liver cells
    • Donohue, T.M., Alcohol-induced steatosis in liver cells. World J.Gastroenterol. 2007, 13, 4974–4978
    • (2007) World J.Gastroenterol , vol.13 , pp. 4974-4978
    • Donohue, T.M.1
  • 114
    • 68149136576 scopus 로고    scopus 로고
    • Adiponectin: A key adipokine in alcoholic fatty liver
    • You, M.; Rogers, C.Q. Adiponectin: A key adipokine in alcoholic fatty liver. Exp.Biol.Med. 2009, 234, 850–859
    • (2009) Exp.Biol.Med , vol.234 , pp. 850-859
    • You, M.1    Rogers, C.Q.2
  • 115
    • 77950848987 scopus 로고    scopus 로고
    • Alcohol-induced alterations of the hepatocyte cytoskeleton
    • Shepard, B.D.; Tuma, P.L. Alcohol-induced alterations of the hepatocyte cytoskeleton. World J. Gastroenterol. 2010, 16, 1358–1365
    • (2010) World J. Gastroenterol , vol.16 , pp. 1358-1365
    • Shepard, B.D.1    Tuma, P.L.2
  • 116
    • 0037817352 scopus 로고    scopus 로고
    • Transcytosis: Crossing cellular barriers
    • Tuma, P.L.; Hubbard, A.L. Transcytosis: Crossing cellular barriers. Physiol. Rev. 2003, 83, 871–932
    • (2003) Physiol. Rev , vol.83 , pp. 871-932
    • Tuma, P.L.1    Hubbard, A.L.2
  • 117
    • 77955057326 scopus 로고    scopus 로고
    • Linking molecular motors to membrane cargo
    • Akhmanova, A.; Hammer, J.A., Linking molecular motors to membrane cargo. Curr. Opin. Cell Biol. 2010, 22, 479–487
    • (2010) Curr. Opin. Cell Biol , vol.22 , pp. 479-487
    • Akhmanova, A.1    Hammer, J.A.2
  • 118
    • 70450228589 scopus 로고    scopus 로고
    • Regulators of the cytoplasmic dynein motor
    • Kardon, J.R.; Vale, R.D. Regulators of the cytoplasmic dynein motor. Nat. Rev. Mol Cell Biol. 2009, 10, 854–865
    • (2009) Nat. Rev. Mol Cell Biol , vol.10 , pp. 854-865
    • Kardon, J.R.1    Vale, R.D.2
  • 119
    • 84911867061 scopus 로고    scopus 로고
    • Alcohol-induced defects in hepatic transcytosis may be explained by impaired dynein function
    • Groebner, J.L.; Fernandez, D.J.; Tuma, D.J.; Tuma, P.L. Alcohol-induced defects in hepatic transcytosis may be explained by impaired dynein function. Mol. Cell Biochem. 2014, 397, 223–233
    • (2014) Mol. Cell Biochem , vol.397 , pp. 223-233
    • Groebner, J.L.1    Fernandez, D.J.2    Tuma, D.J.3    Tuma, P.L.4
  • 120
    • 0030784959 scopus 로고    scopus 로고
    • Vesicle movement in rat hepatocytes is reduced by ethanol exposure: Alterations in microtubule-based motor enzymes
    • Torok, N.; Marks, D.; Hsiao, K.; Oswald, B.J.; McNiven, M.A. Vesicle movement in rat hepatocytes is reduced by ethanol exposure: Alterations in microtubule-based motor enzymes. Gastroenterology 1997, 113, 1938–1948
    • (1997) Gastroenterology , vol.113 , pp. 1938-1948
    • Torok, N.1    Marks, D.2    Hsiao, K.3    Oswald, B.J.4    McNiven, M.A.5
  • 121
    • 65649095105 scopus 로고    scopus 로고
    • Alcohol-induced protein hyperacetylation: Mechanisms and consequences
    • Shepard, B.D.; Tuma, P.L. Alcohol-induced protein hyperacetylation: Mechanisms and consequences. World J. Gastroenterol. 2009, 15, 1219–1230
    • (2009) World J. Gastroenterol , vol.15 , pp. 1219-1230
    • Shepard, B.D.1    Tuma, P.L.2
  • 123
    • 84892547110 scopus 로고    scopus 로고
    • Effects of tubulin acetylation and tubulin acetyltransferase binding on microtubule structure
    • Howes, S.C.; Alushin, G.M.; Shida, T.; Nachury, M.V.; Nogales, E. Effects of tubulin acetylation and tubulin acetyltransferase binding on microtubule structure. Mol.Biol.Cell 2014, 25, 257–266
    • (2014) Mol.Biol.Cell , vol.25 , pp. 257-266
    • Howes, S.C.1    Alushin, G.M.2    Shida, T.3    Nachury, M.V.4    Nogales, E.5
  • 124
    • 0032540307 scopus 로고    scopus 로고
    • Kinesin is a candidate for cross-bridging microtubules and intermediate filaments. Selective binding of kinesin to detyrosinated tubulin and vimentin
    • Liao, G.; Gundersen, G.G. Kinesin is a candidate for cross-bridging microtubules and intermediate filaments. Selective binding of kinesin to detyrosinated tubulin and vimentin. J. Biol. Chem. 1998, 273, 9797–9803
    • (1998) J. Biol. Chem , vol.273 , pp. 9797-9803
    • Liao, G.1    Gundersen, G.G.2
  • 126
    • 34047175919 scopus 로고    scopus 로고
    • Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington’s disease by increasing tubulin acetylation
    • Dompierre, J.P.; Godin, J.D.; Charrin, B.C.; Cordelieres, 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. J. Neurosci. 2007, 27, 3571–3583
    • (2007) J. Neurosci , vol.27 , 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
  • 127
    • 84864746082 scopus 로고    scopus 로고
    • Tubulin acetylation alone does not affect kinesin-1 velocity and run length in vitro
    • Walter, W.J.; Beranek, V.; Fischermeier, E.; Diez, S. Tubulin acetylation alone does not affect kinesin-1 velocity and run length in vitro. PLoS ONE 2012, 7, e42218
    • (2012) Plos ONE , vol.7
    • Walter, W.J.1    Beranek, V.2    Fischermeier, E.3    Diez, S.4
  • 128
    • 84880014019 scopus 로고    scopus 로고
    • Microtubule-based transport—Basic mechanisms, traffic rules and role in neurological pathogenesis
    • Franker, M.A.; Hoogenraad, C.C. Microtubule-based transport—Basic mechanisms, traffic rules and role in neurological pathogenesis. J.Cell Sci. 2013, 126, 2319–2329
    • (2013) J.Cell Sci , vol.126 , pp. 2319-2329
    • Franker, M.A.1    Hoogenraad, C.C.2
  • 129
    • 78449269612 scopus 로고    scopus 로고
    • Molecular motors in neurons: Transport mechanisms and roles in brain function, development, and disease
    • Hirokawa, N.; Niwa, S.; Tanaka, Y., Molecular motors in neurons: Transport mechanisms and roles in brain function, development, and disease. Neuron 2010, 68, 610–638
    • (2010) Neuron , vol.68 , pp. 610-638
    • Hirokawa, N.1    Niwa, S.2    Tanaka, Y.3
  • 130
    • 79957626260 scopus 로고    scopus 로고
    • Phenotypic spectrum of the tubulin-related disorders and functional implications of disease-causing mutations
    • Tischfield, M.A.; Cederquist, G.Y.; Gupta, M.L.; Engle, E.C., Phenotypic spectrum of the tubulin-related disorders and functional implications of disease-causing mutations. Curr.Opin.Genet.Dev. 2011, 21, 286–294
    • (2011) Curr.Opin.Genet.Dev , vol.21 , pp. 286-294
    • Tischfield, M.A.1    Cederquist, G.Y.2    Gupta, M.L.3    Engle, E.C.4
  • 131
    • 84856478716 scopus 로고    scopus 로고
    • Endothelial dysfunction as a cellular mechanism for vascular failure
    • Hirase, T.; Node, K. Endothelial dysfunction as a cellular mechanism for vascular failure. Am. J. Physiol. Heart Circ. Physiol. 2011, 302, H499–H505
    • (2011) Am. J. Physiol. Heart Circ. Physiol , vol.302
    • Hirase, T.1    Node, K.2
  • 132
    • 78649842747 scopus 로고    scopus 로고
    • Cytoplasmic dynein tail mutation impairs motor processivity
    • Ori-McKenney, K.M.; Xu, J.; Gross, S.P.; Vallee, R.B. A cytoplasmic dynein tail mutation impairs motor processivity. Nat. Cell Biol. 2010, 12, 1228–1234
    • (2010) Nat. Cell Biol , vol.12 , pp. 1228-1234
    • Ori-McKenney, K.M.1    Xu, J.2    Gross, S.P.3    Vallee, R.4
  • 133
  • 134
    • 84901493375 scopus 로고    scopus 로고
    • Small molecule inhibitors of histone acetyltransferases and deacetylases are potential drugs for inflammatory diseases
    • Dekker, F.J.; van den Bosch, T.; Martin, N.I. Small molecule inhibitors of histone acetyltransferases and deacetylases are potential drugs for inflammatory diseases. Drug Discov. Today 2014, 19, 654–660
    • (2014) Drug Discov. Today , vol.19 , pp. 654-660
    • Dekker, F.J.1    Van Den Bosch, T.2    Martin, N.I.3
  • 135
    • 67649379393 scopus 로고    scopus 로고
    • Histone acetyltransferase inhibitors and preclinical studies
    • Manzo, F.; Tambaro, F.P.; Mai, A.; Altucci, L. Histone acetyltransferase inhibitors and preclinical studies. Expert Opin.Ther.Pat. 2009, 19, 761–774
    • (2009) Expert Opin.Ther.Pat , vol.19 , pp. 761-774
    • Manzo, F.1    Tambaro, F.P.2    Mai, A.3    Altucci, L.4
  • 136
    • 77649171884 scopus 로고    scopus 로고
    • Novel histone deacetylase inhibitors in clinical trials as anti-cancer agents
    • Tan, J.; Cang, S.; Ma, Y.; Petrillo, R.L.; Liu, D. Novel histone deacetylase inhibitors in clinical trials as anti-cancer agents. J.Hematol.Oncol. 2010, doi:10.1186/1756-8722-3-5
    • (2010) J.Hematol.Oncol
    • Tan, J.1    Cang, S.2    Ma, Y.3    Petrillo, R.L.4    Liu, D.5
  • 138
    • 74549209572 scopus 로고    scopus 로고
    • Chronic Ethanol Consumption Induces Global Hepatic Protein Hyperacetylation
    • Shepard, B.D.; Tuma, D.J.; Tuma, P.L. Chronic Ethanol Consumption Induces Global Hepatic Protein Hyperacetylation. Alcohol. Clin. Exp. Res. 2010, 34, 280–291
    • (2010) Alcohol. Clin. Exp. Res , vol.34 , pp. 280-291
    • Shepard, B.D.1    Tuma, D.J.2    Tuma, P.L.3
  • 139
    • 53149113000 scopus 로고    scopus 로고
    • Ethanol intoxication increases hepatic N-lysyl protein acetylation. Biochem
    • Picklo, M.J., Ethanol intoxication increases hepatic N-lysyl protein acetylation. Biochem. Biophys. Res. Commun. 2008, 21, 615–619.
    • (2008) Biophys. Res. Commun , vol.21 , pp. 615-619
    • Picklo, M.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.