메뉴 건너뛰기




Volumn 7, Issue 1, 2010, Pages 79-92

Systems-wide proteomic characterization of combinatorial post-translational modification patterns

Author keywords

Electron capture dissociation; Electron transfer dissociation; Histone code; Mass spectrometry; Middle down approach; Post translational modification; Proteomics; Top down approach

Indexed keywords

HETEROCHROMATIN PROTEIN 1; HISTONE; N ACETYLGLUCOSAMINE; PROLINE; PROTEIN P53; RNA POLYMERASE II; TUBULIN; TUMOR SUPPRESSOR PROTEIN;

EID: 77951634725     PISSN: 14789450     EISSN: 17448387     Source Type: Journal    
DOI: 10.1586/epr.09.100     Document Type: Review
Times cited : (56)

References (145)
  • 1
    • 28844475262 scopus 로고    scopus 로고
    • Histone H3 serine 10 phosphorylation by Aurora B causes HP1 dissociation from heterochromatin
    • Hirota T, Lipp JJ, Toh BH, Peters JM. Histone H3 serine 10 phosphorylation by Aurora B causes HP1 dissociation from heterochromatin. Nature 438(7071), 1176-1180 (2005).
    • (2005) Nature , vol.438 , Issue.7071 , pp. 1176-1180
    • Hirota, T.1    Lipp, J.J.2    Toh, B.H.3    Peters, J.M.4
  • 2
    • 28844477653 scopus 로고    scopus 로고
    • Regulation of HP1-chromatin binding by histone H3 methylation and phosphorylation
    • Fischle W, Tseng BS, Dormann HL et al. Regulation of HP1-chromatin binding by histone H3 methylation and phosphorylation. Nature 438(7071), 1116-1122 (2005).
    • (2005) Nature , vol.438 , Issue.7071 , pp. 1116-1122
    • Fischle, W.1    Tseng, B.S.2    Dormann, H.L.3
  • 3
    • 0141929385 scopus 로고    scopus 로고
    • Binary switches and modifcation cassettes in histone biology and beyond
    • Fischle W, Wang Y, Allis CD. Binary switches and modifcation cassettes in histone biology and beyond. Nature 425(6957), 475-479 (2003).
    • (2003) Nature , vol.425 , Issue.6957 , pp. 475-479
    • Fischle, W.1    Wang, Y.2    Allis, C.D.3
  • 4
    • 25444442032 scopus 로고    scopus 로고
    • Modifcations of human histone H3 variants during mitosis
    • Garcia BA, Barber CM, Hake SB et al. Modifcations of human histone H3 variants during mitosis. Biochemistry 44(39), 13202-13213 (2005).
    • (2005) Biochemistry , vol.44 , Issue.39 , pp. 13202-13213
    • Garcia, B.A.1    Barber, C.M.2    Hake, S.B.3
  • 5
    • 33846113751 scopus 로고    scopus 로고
    • N-formylation of lysine in histone proteins as a secondary modifcation arising from oxidative DNA damage
    • Jiang T, Zhou X, Taghizadeh K, Dong M, Dedon PC. N-formylation of lysine in histone proteins as a secondary modifcation arising from oxidative DNA damage. Proc. Natl Acad. Sci. USA 104(1), 60-65 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , Issue.1 , pp. 60-65
    • Jiang, T.1    Zhou, X.2    Taghizadeh, K.3    Dong, M.4    Dedon, P.C.5
  • 6
    • 33846488609 scopus 로고    scopus 로고
    • Mass spectrometric mapping of linker histone H1 variants reveals multiple acetylations, methylations, and phosphorylation as well as differences between cell culture and tissue
    • Wisniewski JR, Zougman A, Kruger S, Mann M. Mass spectrometric mapping of linker histone H1 variants reveals multiple acetylations, methylations, and phosphorylation as well as differences between cell culture and tissue. Mol. Cell. Proteomics 6(1), 72-87 (2007).
    • (2007) Mol. Cell. Proteomics , vol.6 , Issue.1 , pp. 72-87
    • Wisniewski, J.R.1    Zougman, A.2    Kruger, S.3    Mann, M.4
  • 7
    • 25844437172 scopus 로고    scopus 로고
    • Mutual interactions between the SUMO and ubiquitin systems: A plea of no contest
    • Ulrich HD. Mutual interactions between the SUMO and ubiquitin systems: a plea of no contest. Trends Cell Biol. 15(10), 525-532 (2005).
    • (2005) Trends Cell Biol. , vol.15 , Issue.10 , pp. 525-532
    • Ulrich, H.D.1
  • 8
    • 63049116472 scopus 로고    scopus 로고
    • Genome stability roles of SUMO-targeted ubiquitin ligases
    • Heideker J, Perry JJ, Boddy MN. Genome stability roles of SUMO-targeted ubiquitin ligases. DNA Repair (Amst.) 8(4), 517-524 (2009).
    • (2009) DNA Repair (Amst.) , vol.8 , Issue.4 , pp. 517-524
    • Heideker, J.1    Perry, J.J.2    Boddy, M.N.3
  • 9
    • 34648840192 scopus 로고    scopus 로고
    • SUMO-targeted ubiquitin ligases in genome stability
    • Prudden J, Pebernard S, Raffa G et al. SUMO-targeted ubiquitin ligases in genome stability. EMBO J. 26(18), 4089-4101 (2007).
    • (2007) EMBO J. , vol.26 , Issue.18 , pp. 4089-4101
    • Prudden, J.1    Pebernard, S.2    Raffa, G.3
  • 10
    • 36348964395 scopus 로고    scopus 로고
    • The yeast Hex3.Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation
    • Xie Y, Kerscher O, Kroetz MB, McConchie HF, Sung P, Hochstrasser M. The yeast Hex3.Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation. J. Biol. Chem. 282(47), 34176-34184 (2007).
    • (2007) J. Biol. Chem. , vol.282 , Issue.47 , pp. 34176-34184
    • Xie, Y.1    Kerscher, O.2    Kroetz, M.B.3    McConchie, H.F.4    Sung, P.5    Hochstrasser, M.6
  • 11
    • 34648816891 scopus 로고    scopus 로고
    • Conserved function of RNF4 family proteins in eukaryotes: Targeting a ubiquitin ligase to SUMOylated proteins
    • Sun H, Leverson JD, Hunter T. Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins. EMBO J. 26(18), 4102-4112 (2007).
    • (2007) EMBO J. , vol.26 , Issue.18 , pp. 4102-4112
    • Sun, H.1    Leverson, J.D.2    Hunter, T.3
  • 12
    • 43049093756 scopus 로고    scopus 로고
    • RNF4 is a poly-SUMO-specifc E3 ubiquitin ligase required for arsenic-induced PML degradation
    • Tatham MH, Geoffroy MC, Shen L et al. RNF4 is a poly-SUMO-specifc E3 ubiquitin ligase required for arsenic-induced PML degradation. Nat. Cell. Biol 10(5), 538-546 (2008).
    • (2008) Nat. Cell. Biol , vol.10 , Issue.5 , pp. 538-546
    • Tatham, M.H.1    Geoffroy, M.C.2    Shen, L.3
  • 13
    • 43049096803 scopus 로고    scopus 로고
    • Arsenic degrades PML or PML-RARa through a SUMO-triggered RNF4/ubiquitin-mediated pathway
    • Lallemand-Breitenbach V, Jeanne M, Benhenda S et al. Arsenic degrades PML or PML-RARa through a SUMO-triggered RNF4/ubiquitin-mediated pathway. Nat. Cell. Biol. 10(5), 547-555 (2008).
    • (2008) Nat. Cell. Biol. , vol.10 , Issue.5 , pp. 547-555
    • Lallemand-Breitenbach, V.1    Jeanne, M.2    Benhenda, S.3
  • 14
    • 57049091711 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system is a key component of the SUMO-2/3 cycle
    • Schimmel J, Larsen KM, Matic I et al. The ubiquitin-proteasome system is a key component of the SUMO-2/3 cycle. Mol Cell. Proteomics 7 (11), 2107-2122 (2008).
    • (2008) Mol Cell. Proteomics , vol.7 , Issue.11 , pp. 2107-2122
    • Schimmel, J.1    Larsen, K.M.2    Matic, I.3
  • 15
    • 33744963540 scopus 로고    scopus 로고
    • A trans-tail histone code defned by monomethylated H4 Lys-20 and H3 Lys-9 demarcates distinct regions of silent chromatin
    • Sims JK, Houston SI, Magazinnik T, Rice JC. A trans-tail histone code defned by monomethylated H4 Lys-20 and H3 Lys-9 demarcates distinct regions of silent chromatin. J. Biol. Chem. 281(18), 12760-12766 (2006).
    • (2006) J. Biol. Chem. , vol.281 , Issue.18 , pp. 12760-12766
    • Sims, J.K.1    Houston, S.I.2    Magazinnik, T.3    Rice, J.C.4
  • 16
    • 33845666681 scopus 로고    scopus 로고
    • Structural basis for the methylation state-specifc recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair
    • Botuyan MV, Lee J, Ward IM et al. Structural basis for the methylation state-specifc recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair. Cell 127(7), 1361-1373 (2006).
    • (2006) Cell , vol.127 , Issue.7 , pp. 1361-1373
    • Botuyan, M.V.1    Lee, J.2    Ward, I.M.3
  • 17
    • 9244252580 scopus 로고    scopus 로고
    • Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks
    • Huyen Y, Zgheib O, Ditullio RA Jr et al Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks. Nature 432(7015), 406-411 (2004).
    • (2004) Nature , vol.432 , Issue.7015 , pp. 406-411
    • Huyen, Y.1    Zgheib, O.2    Ditullio Jr., R.A.3
  • 18
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifcations
    • Strahl BD, Allis CD. The language of covalent histone modifcations. Nature 403(6765), 41-45 (2000).
    • (2000) Nature , vol.403 , Issue.6765 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 20
    • 33846025127 scopus 로고    scopus 로고
    • Dynamic regulation of histone lysine methylation by demethylases
    • Shi Y, Whetstine JR. Dynamic regulation of histone lysine methylation by demethylases. Mol. Cell 25(1), 1-14 (2007).
    • (2007) Mol. Cell , vol.25 , Issue.1 , pp. 1-14
    • Shi, Y.1    Whetstine, J.R.2
  • 21
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifcations and their function
    • Kouzarides T. Chromatin modifcations and their function. Cell 128(4), 693-705 (2007).
    • (2007) Cell , vol.128 , Issue.4 , pp. 693-705
    • Kouzarides, T.1
  • 22
    • 33846809241 scopus 로고    scopus 로고
    • Characterization of histones and their post-translational modifcations by mass spectrometry
    • Garcia BA, Shabanowitz J, Hunt DF. Characterization of histones and their post-translational modifcations by mass spectrometry. Curr. Opin. Chem. Biol. 11(1), 66-73 (2007).
    • (2007) Curr. Opin. Chem. Biol. , vol.11 , Issue.1 , pp. 66-73
    • Garcia, B.A.1    Shabanowitz, J.2    Hunt, D.F.3
  • 23
    • 14844361808 scopus 로고    scopus 로고
    • Multisite protein modifcation and intramolecular signaling
    • Yang XJ. Multisite protein modifcation and intramolecular signaling. Oncogene 24(10), 1653-1662 (2005).
    • (2005) Oncogene , vol.24 , Issue.10 , pp. 1653-1662
    • Yang, X.J.1
  • 24
    • 65149105339 scopus 로고    scopus 로고
    • A post-translational modifcation code for transcription factors: Sorting through a sea of signals
    • Benayoun BA, Veitia RA. A post-translational modifcation code for transcription factors: sorting through a sea of signals. Trends Cell Biol. 19(5), 189-197 (2009).
    • (2009) Trends Cell Biol. , vol.19 , Issue.5 , pp. 189-197
    • Benayoun, B.A.1    Veitia, R.A.2
  • 26
    • 58049203867 scopus 로고    scopus 로고
    • Role for 53BP1 Tudor domain recognition of p53 dimethylated at lysine 382 in DNA damage signaling
    • Kachirskaia I, Shi X, Yamaguchi H et al. Role for 53BP1 Tudor domain recognition of p53 dimethylated at lysine 382 in DNA damage signaling. J. Biol. Chem. 283(50), 34660-34666 (2008).
    • (2008) J. Biol. Chem. , vol.283 , Issue.50 , pp. 34660-34666
    • Kachirskaia, I.1    Shi, X.2    Yamaguchi, H.3
  • 27
    • 0037184969 scopus 로고    scopus 로고
    • Acetylation of p53 inhibits its ubiquitination by Mdm2
    • Li M, Luo J, Brooks CL, Gu W. Acetylation of p53 inhibits its ubiquitination by Mdm2. J. Biol. Chem. 277(52), 50607-50611 (2002).
    • (2002) J. Biol. Chem. , vol.277 , Issue.52 , pp. 50607-50611
    • Li, M.1    Luo, J.2    Brooks, C.L.3    Gu, W.4
  • 28
    • 0026663552 scopus 로고
    • Phosphorylation of the p53 tumour-suppressor protein at three N-terminal sites by a novel casein kinase I-like enzyme
    • Milne DM, Palmer RH, Campbell DG, Meek DW. Phosphorylation of the p53 tumour-suppressor protein at three N-terminal sites by a novel casein kinase I-like enzyme. Oncogene 7(7), 1361-1369 (1992).
    • (1992) Oncogene , vol.7 , Issue.7 , pp. 1361-1369
    • Milne, D.M.1    Palmer, R.H.2    Campbell, D.G.3    Meek, D.W.4
  • 29
    • 0000303499 scopus 로고    scopus 로고
    • ATM associates with and phosphorylates p53: Mapping the region of interaction
    • Khanna KK, Keating KE, Kozlov S et al. ATM associates with and phosphorylates p53: mapping the region of interaction. Nat. Genet. 20(4), 398-400 (1998).
    • (1998) Nat. Genet. , vol.20 , Issue.4 , pp. 398-400
    • Khanna, K.K.1    Keating, K.E.2    Kozlov, S.3
  • 30
    • 0033429271 scopus 로고    scopus 로고
    • Protein kinase CK1 is a p53-threonine 18 kinase which requires prior phosphorylation of serine 15
    • Dumaz N, Milne DM, Meek DW. Protein kinase CK1 is a p53-threonine 18 kinase which requires prior phosphorylation of serine 15. FEBS Lett. 463(3), 312-316 (1999).
    • (1999) FEBS Lett. , vol.463 , Issue.3 , pp. 312-316
    • Dumaz, N.1    Milne, D.M.2    Meek, D.W.3
  • 31
    • 0034721101 scopus 로고    scopus 로고
    • The human vaccinia-related kinase 1 (VRK1) phosphorylates threonine-18 within the Mdm-2 binding site of the p53 tumour suppressor protein
    • Lopez-Borges S, Lazo PA. The human vaccinia-related kinase 1 (VRK1) phosphorylates threonine-18 within the Mdm-2 binding site of the p53 tumour suppressor protein. Oncogene 19(32), 3656-3664 (2000).
    • (2000) Oncogene , vol.19 , Issue.32 , pp. 3656-3664
    • Lopez-Borges, S.1    Lazo, P.A.2
  • 32
    • 0030826733 scopus 로고    scopus 로고
    • Induced N-and C-terminal cleavage of p53: A core fragment of p53, generated by interaction with damaged DNA, promotes cleavage of the N-terminus of full-length p53, whereas ssDNA induces C-terminal cleavage of p53
    • Okorokov AL, Ponchel F, Milner J. Induced N-and C-terminal cleavage of p53: a core fragment of p53, generated by interaction with damaged DNA, promotes cleavage of the N-terminus of full-length p53, whereas ssDNA induces C-terminal cleavage of p53. EMBO J. 16(19), 6008-6017 (1997).
    • (1997) EMBO J. , vol.16 , Issue.19 , pp. 6008-6017
    • Okorokov, A.L.1    Ponchel, F.2    Milner, J.3
  • 33
    • 0033598754 scopus 로고    scopus 로고
    • Phosphorylation of Ser-20 mediates stabilization of human p53 in response to DNA damage
    • Chehab NH, Malikzay A, Stavridi ES, Halazonetis TD. Phosphorylation of Ser-20 mediates stabilization of human p53 in response to DNA damage. Proc. Natl Acad. Sci. USA 96(24), 13777-13782 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , Issue.24 , pp. 13777-13782
    • Chehab, N.H.1    Malikzay, A.2    Stavridi, E.S.3    Halazonetis, T.D.4
  • 34
    • 2342549202 scopus 로고    scopus 로고
    • Glycogen synthase kinase3 b phosphorylates serine 33 of p53 and activates p53's transcriptional activity
    • Turenne GA, Price BD. Glycogen synthase kinase3 b phosphorylates serine 33 of p53 and activates p53's transcriptional activity. BMC Cell. Biol. 2, 12 (2001).
    • (2001) BMC Cell. Biol. , vol.2 , pp. 12
    • Turenne, G.A.1    Price, B.D.2
  • 35
    • 33644758287 scopus 로고    scopus 로고
    • CDK9 phosphorylates p53 on serine residues 33, 315 and 392
    • Radhakrishnan SK, Gartel AL. CDK9 phosphorylates p53 on serine residues 33, 315 and 392. Cell Cycle 5(5), 519-521 (2006).
    • (2006) Cell Cycle , vol.5 , Issue.5 , pp. 519-521
    • Radhakrishnan, S.K.1    Gartel, A.L.2
  • 36
    • 18644384688 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 is a regulator of p53 in genotoxic response
    • Zheng H, You H, Zhou XZ et al. The prolyl isomerase Pin1 is a regulator of p53 in genotoxic response. Nature 419(6909), 849-853 (2002).
    • (2002) Nature , vol.419 , Issue.6909 , pp. 849-853
    • Zheng, H.1    You, H.2    Zhou, X.Z.3
  • 37
    • 0032530486 scopus 로고    scopus 로고
    • DNA damage activates p53 through a phosphorylation-acetylation cascade
    • Sakaguchi K, Herrera JE, Saito S et al. DNA damage activates p53 through a phosphorylation-acetylation cascade. Genes Dev. 12(18), 2831-2841 (1998).
    • (1998) Genes Dev. , vol.12 , Issue.18 , pp. 2831-2841
    • Sakaguchi, K.1    Herrera, J.E.2    Saito, S.3
  • 38
    • 0037073713 scopus 로고    scopus 로고
    • Role of Pin1 in the regulation of p53 stability and p21 transactivation, and cell cycle checkpoints in response to DNA damage
    • Wulf GM, Liou YC, Ryo A, Lee SW, Lu K P. Role of Pin1 in the regulation of p53 stability and p21 transactivation, and cell cycle checkpoints in response to DNA damage. J. Biol. Chem. 277(50), 47976-47979 (2002).
    • (2002) J. Biol. Chem. , vol.277 , Issue.50 , pp. 47976-47979
    • Wulf, G.M.1    Liou, Y.C.2    Ryo, A.3    Lee, S.W.4    Lu, K.P.5
  • 39
    • 18644384283 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 reveals a mechanism to control p53 functions after genotoxic insults
    • Zacchi P, Gostissa M, Uchida T et al. The prolyl isomerase Pin1 reveals a mechanism to control p53 functions after genotoxic insults. Nature 419(6909), 853-857 (2002).
    • (2002) Nature , vol.419 , Issue.6909 , pp. 853-857
    • Zacchi, P.1    Gostissa, M.2    Uchida, T.3
  • 40
    • 18244379872 scopus 로고    scopus 로고
    • Homeodomain-interacting protein kinase-2 phosphorylates p53 at ser 46 and mediates apoptosis
    • D'Orazi G, Cecchinelli B, Bruno T et al. Homeodomain-interacting protein kinase-2 phosphorylates p53 at Ser 46 and mediates apoptosis. Nat. Cell Biol. 4(1), 11-19 (2002).
    • (2002) Nat. Cell Biol. , vol.4 , Issue.1 , pp. 11-19
    • D'Orazi, G.1    Cecchinelli, B.2    Bruno, T.3
  • 41
    • 0034814954 scopus 로고    scopus 로고
    • Nuclear extracellular signal-regulated kinase 2 phosphorylates p53 at Thr55 in response to doxorubicin
    • Yeh PY, Chuang SE, Yeh KH, Song YC, Cheng AL. Nuclear extracellular signal-regulated kinase 2 phosphorylates p53 at Thr55 in response to doxorubicin. Biochem. Biophys. Res. Commun. 284(4), 880-886 (2001).
    • (2001) Biochem. Biophys. Res. Commun. , vol.284 , Issue.4 , pp. 880-886
    • Yeh, P.Y.1    Chuang, S.E.2    Yeh, K.H.3    Song, Y.C.4    Cheng, A.L.5
  • 42
    • 0034745050 scopus 로고    scopus 로고
    • 2-terminal kinase phosphorylation of p53 on Thr-81 is important for p53 stabilization and transcriptional activities in response to stress
    • 2-terminal kinase phosphorylation of p53 on Thr-81 is important for p53 stabilization and transcriptional activities in response to stress. Mol. Cell. Biol. 21(8), 2743-2754 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , Issue.8 , pp. 2743-2754
    • Buschmann, T.1    Potapova, O.2    Bar-Shira, A.3
  • 43
    • 20744432450 scopus 로고    scopus 로고
    • Mutations in proline 82 of p53 impair its activation by Pin1 and Chk2 in response to DNA damage
    • Berger M, Stahl N, Del Sal G, Haupt Y. Mutations in proline 82 of p53 impair its activation by Pin1 and Chk2 in response to DNA damage. Mol. Cell. Biol. 25(13), 5380-5388 (2005).
    • (2005) Mol. Cell. Biol. , vol.25 , Issue.13 , pp. 5380-5388
    • Berger, M.1    Stahl, N.2    Del Sal, G.3    Haupt, Y.4
  • 44
    • 34249947699 scopus 로고    scopus 로고
    • ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage
    • Matsuoka S, Ballif BA, Smogorzewska A et al. ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science 316(5828), 1160-1166 (2007).
    • (2007) Science , vol.316 , Issue.5828 , pp. 1160-1166
    • Matsuoka, S.1    Ballif, B.A.2    Smogorzewska, A.3
  • 45
    • 33845668241 scopus 로고    scopus 로고
    • Tip60-dependent acetylation of p53 modulates the decision between cell-cycle arrest and apoptosis
    • Tang Y, Luo J, Zhang W, Gu W. Tip60-dependent acetylation of p53 modulates the decision between cell-cycle arrest and apoptosis. Mol. Cell 24(6), 827-839 (2006).
    • (2006) Mol. Cell , vol.24 , Issue.6 , pp. 827-839
    • Tang, Y.1    Luo, J.2    Zhang, W.3    Gu, W.4
  • 46
    • 33845656738 scopus 로고    scopus 로고
    • Acetylation of the p53 DNA-binding domain regulates apoptosis induction
    • Sykes SM, Mellert HS, Holbert MA et al. Acetylation of the p53 DNA-binding domain regulates apoptosis induction. Mol. Cell 24(6), 841-851 (2006).
    • (2006) Mol. Cell , vol.24 , Issue.6 , pp. 841-851
    • Sykes, S.M.1    Mellert, H.S.2    Holbert, M.A.3
  • 47
    • 33749160125 scopus 로고    scopus 로고
    • Modifcation of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability
    • Yang WH, Kim JE, Nam HW et al. Modifcation of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability. Nat. Cell. Biol. 8(10), 1074-1083 (2006).
    • (2006) Nat. Cell. Biol. , vol.8 , Issue.10 , pp. 1074-1083
    • Yang, W.H.1    Kim, J.E.2    Nam, H.W.3
  • 48
    • 0344837349 scopus 로고    scopus 로고
    • Protein kinase CK2 and protein kinase D are associated with the COP9 signalosome
    • Uhle S, Medalia O, Waldron R et al. Protein kinase CK2 and protein kinase D are associated with the COP9 signalosome. EMBO J. 22(6), 1302-1312 (2003).
    • (2003) EMBO J. , vol.22 , Issue.6 , pp. 1302-1312
    • Uhle, S.1    Medalia, O.2    Waldron, R.3
  • 49
    • 0035794541 scopus 로고    scopus 로고
    • COP9 signalosome-specifc phosphorylation targets p53 to degradation by the ubiquitin system
    • Bech-Otschir D, Kraft R, Huang X et al. COP9 signalosome-specifc phosphorylation targets p53 to degradation by the ubiquitin system. EMBO J. 20(7), 1630-1639 (2001).
    • (2001) EMBO J. , vol.20 , Issue.7 , pp. 1630-1639
    • Bech-Otschir, D.1    Kraft, R.2    Huang, X.3
  • 50
    • 43049163953 scopus 로고    scopus 로고
    • Acetylation is indispensable for p53 activation
    • Tang Y, Zhao W, Chen Y, Zhao Y, Gu W. Acetylation is indispensable for p53 activation. Cell 133(4), 612-626 (2008).
    • (2008) Cell , vol.133 , Issue.4 , pp. 612-626
    • Tang, Y.1    Zhao, W.2    Chen, Y.3    Zhao, Y.4    Gu, W.5
  • 51
    • 0038491354 scopus 로고    scopus 로고
    • Identifcation and characterization of a novel p300-mediated p53 acetylation site, lysine 305
    • Wang YH, Tsay YG, Tan BC, Lo WY, Lee SC. Identifcation and characterization of a novel p300-mediated p53 acetylation site, lysine 305. J. Biol. Chem. 278(28), 25568-25576 (2003).
    • (2003) J. Biol. Chem. , vol.278 , Issue.28 , pp. 25568-25576
    • Wang, Y.H.1    Tsay, Y.G.2    Tan, B.C.3    Lo, W.Y.4    Lee, S.C.5
  • 52
    • 0029132301 scopus 로고
    • Cdk2 kinase phosphorylates serine 315 of human p53 in vitro
    • Price BD, Hughes-Davies L, Park SJ. Cdk2 kinase phosphorylates serine 315 of human p53 in vitro. Oncogene 11(1), 73-80 (1995).
    • (1995) Oncogene , vol.11 , Issue.1 , pp. 73-80
    • Price, B.D.1    Hughes-Davies, L.2    Park, S.J.3
  • 53
    • 33750834640 scopus 로고    scopus 로고
    • E4F1 is an atypical ubiquitin ligase that modulates p53 effector functions independently of degradation
    • Le Cam L, Linares LK, Paul C et al. E4F1 is an atypical ubiquitin ligase that modulates p53 effector functions independently of degradation. Cell 127(4), 775-788 (2006).
    • (2006) Cell , vol.127 , Issue.4 , pp. 775-788
    • Le Cam, L.1    Linares, L.K.2    Paul, C.3
  • 54
    • 33847328747 scopus 로고    scopus 로고
    • FBXO11 promotes the Neddylation of p53 and inhibits its transcriptional activity
    • Abida WM, Nikolaev A, Zhao W, Zhang W, Gu W. FBXO11 promotes the Neddylation of p53 and inhibits its transcriptional activity. J. Biol. Chem. 282(3), 1797-1804 (2007).
    • (2007) J. Biol. Chem. , vol.282 , Issue.3 , pp. 1797-1804
    • Abida, W.M.1    Nikolaev, A.2    Zhao, W.3    Zhang, W.4    Gu, W.5
  • 55
    • 59149085299 scopus 로고    scopus 로고
    • MSL2 promotes Mdm2-independent cytoplasmic localization of p53
    • Kruse JP, Gu W. MSL2 promotes Mdm2-independent cytoplasmic localization of p53. J. Biol. Chem. 284(5), 3250-3263 (2009).
    • (2009) J. Biol. Chem. , vol.284 , Issue.5 , pp. 3250-3263
    • Kruse, J.P.1    Gu, W.2
  • 56
    • 16344381702 scopus 로고    scopus 로고
    • P53 C-terminal phosphorylation by CHK1 and CHK2 participates in the regulation of DNA-damage-induced C-terminal acetylation
    • Ou YH, Chung PH, Sun TP, Shieh SY. p53 C-terminal phosphorylation by CHK1 and CHK2 participates in the regulation of DNA-damage-induced C-terminal acetylation. Mol. Biol. Cell. 16(4), 1684-1695 (2005).
    • (2005) Mol. Biol. Cell. , vol.16 , Issue.4 , pp. 1684-1695
    • Ou, Y.H.1    Chung, P.H.2    Sun, T.P.3    Shieh, S.Y.4
  • 57
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specifc DNA binding by acetylation of the p53 C-terminal domain
    • Gu W, Roeder RG. Activation of p53 sequence-specifc DNA binding by acetylation of the p53 C-terminal domain. Cell 90(4), 595-606 (1997).
    • (1997) Cell , vol.90 , Issue.4 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 58
    • 33845204856 scopus 로고    scopus 로고
    • Repression of p53 activity by Smyd2-mediated methylation
    • Huang J, Perez-Burgos L, Placek BJ et al. Repression of p53 activity by Smyd2-mediated methylation. Nature 444(7119), 629-632 (2006).
    • (2006) Nature , vol.444 , Issue.7119 , pp. 629-632
    • Huang, J.1    Perez-Burgos, L.2    Placek, B.J.3
  • 59
    • 34548513035 scopus 로고    scopus 로고
    • P53 is regulated by the lysine demethylase LSD1
    • Huang J, Sengupta R, Espejo AB et al. p53 is regulated by the lysine demethylase LSD1. Nature 449(7158), 105-108 (2007).
    • (2007) Nature , vol.449 , Issue.7158 , pp. 105-108
    • Huang, J.1    Sengupta, R.2    Espejo, A.B.3
  • 60
    • 0033767235 scopus 로고    scopus 로고
    • Multiple C-terminal lysine residues target p53 for ubiquitin-proteasome- mediated degradation
    • Rodriguez MS, Desterro JM, Lain S, Lane DP, Hay RT. Multiple C-terminal lysine residues target p53 for ubiquitin-proteasome-mediated degradation. Mol. Cell. Biol. 20(22), 8458-8467 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , Issue.22 , pp. 8458-8467
    • Rodriguez, M.S.1    Desterro, J.M.2    Lain, S.3    Lane, D.P.4    Hay, R.T.5
  • 61
    • 3142570737 scopus 로고    scopus 로고
    • Mdm2-mediated NEDD8 conjugation of p53 inhibits its transcriptional activity
    • Xirodimas DP, Saville MK, Bourdon JC, Hay RT, Lane DP. Mdm2-mediated NEDD8 conjugation of p53 inhibits its transcriptional activity. Cell 118(1), 83-97 (2004).
    • (2004) Cell , vol.118 , Issue.1 , pp. 83-97
    • Xirodimas, D.P.1    Saville, M.K.2    Bourdon, J.C.3    Hay, R.T.4    Lane, D.P.5
  • 62
    • 0032540088 scopus 로고    scopus 로고
    • Regulation of the p53 protein by protein kinase C a and protein kinase C z
    • Youmell M, Park SJ, Basu S, Price BD. Regulation of the p53 protein by protein kinase C a and protein kinase C z. Biochem. Biophys. Res. Commun. 245(2), 514-518 (1998).
    • (1998) Biochem. Biophys. Res. Commun. , vol.245 , Issue.2 , pp. 514-518
    • Youmell, M.1    Park, S.J.2    Basu, S.3    Price, B.D.4
  • 63
    • 9244247669 scopus 로고    scopus 로고
    • Regulation of p53 activity through lysine methylation
    • Chuikov S, Kurash JK, Wilson JR et al. Regulation of p53 activity through lysine methylation. Nature 432(7015), 353-360 (2004).
    • (2004) Nature , vol.432 , Issue.7015 , pp. 353-360
    • Chuikov, S.1    Kurash, J.K.2    Wilson, J.R.3
  • 64
    • 0031840253 scopus 로고    scopus 로고
    • ATM-dependent activation of p53 involves dephosphorylation and association with 14-13-3 proteins
    • Waterman MJ, Stavridi ES, Waterman JL, Halazonetis TD. ATM-dependent activation of p53 involves dephosphorylation and association with 14-13-3 proteins. Nat. Genet. 19(2), 175-178 (1998).
    • (1998) Nat. Genet. , vol.19 , Issue.2 , pp. 175-178
    • Waterman, M.J.1    Stavridi, E.S.2    Waterman, J.L.3    Halazonetis, T.D.4
  • 65
    • 34547809957 scopus 로고    scopus 로고
    • Modulation of p53 function by SET8-mediated methylation at lysine 382
    • Shi X, Kachirskaia I, Yamaguchi H et al. Modulation of p53 function by SET8-mediated methylation at lysine 382. Mol. Cell 27(4), 636-646 (2007).
    • (2007) Mol. Cell , vol.27 , Issue.4 , pp. 636-646
    • Shi, X.1    Kachirskaia, I.2    Yamaguchi, H.3
  • 66
    • 0033570892 scopus 로고    scopus 로고
    • Activation of p53 by conjugation to the ubiquitin-like protein SUMO-1
    • Gostissa M, Hengstermann A, Fogal V et al. Activation of p53 by conjugation to the ubiquitin-like protein SUMO-1. EMBO J. 18(22), 6462-6471 (1999).
    • (1999) EMBO J. , vol.18 , Issue.22 , pp. 6462-6471
    • Gostissa, M.1    Hengstermann, A.2    Fogal, V.3
  • 67
    • 0035804223 scopus 로고    scopus 로고
    • Increased p53 phosphorylation after microtubule disruption is mediated in a microtubule inhibitor-and cell-specifc manner
    • Stewart ZA, Tang LJ, Pietenpol JA. Increased p53 phosphorylation after microtubule disruption is mediated in a microtubule inhibitor-and cell-specifc manner. Oncogene 20(1), 113-124 (2001).
    • (2001) Oncogene , vol.20 , Issue.1 , pp. 113-124
    • Stewart, Z.A.1    Tang, L.J.2    Pietenpol, J.A.3
  • 68
    • 33646817028 scopus 로고    scopus 로고
    • Distinct p53 acetylation cassettes differentially infuence gene-expression patterns and cell fate
    • Knights CD, Catania J, Di Giovanni S et al. Distinct p53 acetylation cassettes differentially infuence gene-expression patterns and cell fate. J. Cell. Biol. 173(4), 533-544 (2006).
    • (2006) J. Cell. Biol. , vol.173 , Issue.4 , pp. 533-544
    • Knights, C.D.1    Catania, J.2    Di Giovanni, S.3
  • 69
  • 70
    • 34748898280 scopus 로고    scopus 로고
    • Methylation-acetylation interplay activates p53 in response to DNA damage
    • Ivanov GS, Ivanova T, Kurash J et al. Methylation-acetylation interplay activates p53 in response to DNA damage. Mol. Cell. Biol. 27(19), 6756-6769 (2007).
    • (2007) Mol. Cell. Biol. , vol.27 , Issue.19 , pp. 6756-6769
    • Ivanov, G.S.1    Ivanova, T.2    Kurash, J.3
  • 71
    • 0031971228 scopus 로고    scopus 로고
    • Multisite phosphorylation and the integration of stress signals at p53
    • Meek DW. Multisite phosphorylation and the integration of stress signals at p53. Cell Signal. 10(3), 159-166 (1998).
    • (1998) Cell Signal. , vol.10 , Issue.3 , pp. 159-166
    • Meek, D.W.1
  • 72
    • 0037336041 scopus 로고    scopus 로고
    • Phosphorylation of RNA polymerase II CTD regulates H3 methylation in yeast
    • Xiao T, Hall H, Kizer KO et al. Phosphorylation of RNA polymerase II CTD regulates H3 methylation in yeast. Genes Dev. 17(5), 654-663 (2003).
    • (2003) Genes Dev. , vol.17 , Issue.5 , pp. 654-663
    • Xiao, T.1    Hall, H.2    Kizer, K.O.3
  • 73
    • 0025079058 scopus 로고
    • Tails of RNA polymerase II
    • Corden JL. Tails of RNA polymerase II. Trends Biochem. Sci. 15(10), 383-387 (1990).
    • (1990) Trends Biochem. Sci. , vol.15 , Issue.10 , pp. 383-387
    • Corden, J.L.1
  • 74
    • 65549156025 scopus 로고    scopus 로고
    • TFIIH kinase places bivalent marks on the carboxy-terminal domain of RNA polymerase II
    • Akhtar MS, Heidemann M, Tietjen JR et al. TFIIH kinase places bivalent marks on the carboxy-terminal domain of RNA polymerase II. Mol. Cell 34(3), 387-393 (2009).
    • (2009) Mol. Cell , vol.34 , Issue.3 , pp. 387-393
    • Akhtar, M.S.1    Heidemann, M.2    Tietjen, J.R.3
  • 75
    • 0027289130 scopus 로고
    • RNA polymerase II is a glycoprotein. Modifcation of the COOH-terminal domain by O-GlcNAc
    • Kelly WG, Dahmus ME, Hart GW. RNA polymerase II is a glycoprotein. Modifcation of the COOH-terminal domain by O-GlcNAc. J. Biol. Chem. 268(14), 10416-10424 (1993).
    • (1993) J. Biol. Chem. , vol.268 , Issue.14 , pp. 10416-10424
    • Kelly, W.G.1    Dahmus, M.E.2    Hart, G.W.3
  • 76
    • 4644283087 scopus 로고    scopus 로고
    • Pinning down transcription: Regulation of RNA polymerase II activity during the cell cycle
    • Xu YX, Manley JL. Pinning down transcription: regulation of RNA polymerase II activity during the cell cycle. Cell Cycle 3(4), 432-435 (2004).
    • (2004) Cell Cycle , vol.3 , Issue.4 , pp. 432-435
    • Xu, Y.X.1    Manley, J.L.2
  • 77
    • 0028140121 scopus 로고
    • High-performance liquid chromatographic separation of cis-trans isomers of proline-containing peptides. II. Fractionation in different cyclodextrin systems
    • Friebe S, Hartrodt B, Neubert K, Krauss GJ. High-performance liquid chromatographic separation of cis-trans isomers of proline-containing peptides. II. Fractionation in different cyclodextrin systems. J. Chromatogr. A 661(1-2), 7-12 (1994).
    • (1994) J. Chromatogr. A , vol.661 , Issue.1-2 , pp. 7-12
    • Friebe, S.1    Hartrodt, B.2    Neubert, K.3    Krauss, G.J.4
  • 79
    • 2442655625 scopus 로고    scopus 로고
    • Chiral analyses of peptides by ion/molecule reactions
    • Grigorean G, Cong X, Lebrilla CB. Chiral analyses of peptides by ion/molecule reactions. Int. J. Mass Spectrom. 234(1-3), 71-77 (2004).
    • (2004) Int. J. Mass Spectrom. , vol.234 , Issue.1-3 , pp. 71-77
    • Grigorean, G.1    Cong, X.2    Lebrilla, C.B.3
  • 80
    • 42349100379 scopus 로고    scopus 로고
    • Detecting D-amino acid-containing neuropeptides using selective enzymatic digestion
    • Ewing MA, Wang J, Sheeley SA, Sweedler J V. Detecting D-amino acid-containing neuropeptides using selective enzymatic digestion. Anal. Chem. 80(8), 2874-2880 (2008).
    • (2008) Anal. Chem. , vol.80 , Issue.8 , pp. 2874-2880
    • Ewing, M.A.1    Wang, J.2    Sheeley, S.A.3    Sweedler, J.V.4
  • 82
    • 0027204631 scopus 로고
    • Reversible polyglutamylation of a-and b-tubulin and microtubule dynamics in mouse brain neurons
    • Audebert S, Desbruyeres E, Gruszczynski C et al. Reversible polyglutamylation of a-and b-tubulin and microtubule dynamics in mouse brain neurons. Mol. Biol. Cell 4(6), 615-626 (1993).
    • (1993) Mol. Biol. Cell , vol.4 , Issue.6 , pp. 615-626
    • Audebert, S.1    Desbruyeres, E.2    Gruszczynski, C.3
  • 83
    • 34247620196 scopus 로고    scopus 로고
    • A targeted multienzyme mechanism for selective microtubule polyglutamylation
    • van Dijk J, Rogowski K, Miro J, Lacroix B, Edde B, Janke C. A targeted multienzyme mechanism for selective microtubule polyglutamylation. Mol. Cell 26(3), 437-448 (2007).
    • (2007) Mol. Cell , vol.26 , Issue.3 , pp. 437-448
    • Van Dijk, J.1    Rogowski, K.2    Miro, J.3    Lacroix, B.4    Edde, B.5    Janke, C.6
  • 84
    • 20544457358 scopus 로고    scopus 로고
    • Tubulin polyglutamylase enzymes are members of the TTL domain protein family
    • Janke C, Rogowski K, Wloga D et al. Tubulin polyglutamylase enzymes are members of the TTL domain protein family. Science 308(5729), 1758-1762 (2005).
    • (2005) Science , vol.308 , Issue.5729 , pp. 1758-1762
    • Janke, C.1    Rogowski, K.2    Wloga, D.3
  • 85
    • 0028574349 scopus 로고
    • Polyglycylation of tubulin: A posttranslational modifcation in axonemal microtubules
    • Redeker V, Levilliers N, Schmitter JM et al. Polyglycylation of tubulin: a posttranslational modifcation in axonemal microtubules. Science 266(5191), 1688-1691 (1994).
    • (1994) Science , vol.266 , Issue.5191 , pp. 1688-1691
    • Redeker, V.1    Levilliers, N.2    Schmitter, J.M.3
  • 87
    • 0017577442 scopus 로고
    • Release of tyrosine from tyrosinated tubulin. Some common factors that affect this process and the assembly of tubulin
    • Hallak ME, Rodriguez JA, Barra HS, Caputto R. Release of tyrosine from tyrosinated tubulin. Some common factors that affect this process and the assembly of tubulin. FEBS Lett. 73(2), 147-150 (1977).
    • (1977) FEBS Lett. , vol.73 , Issue.2 , pp. 147-150
    • Hallak, M.E.1    Rodriguez, J.A.2    Barra, H.S.3    Caputto, R.4
  • 88
    • 0024583552 scopus 로고
    • Complete separation of tyrosinated, detyrosinated, and nontyrosinatable brain tubulin subpopulations using affnity chromatography
    • Paturle L, Wehland J, Margolis RL, Job D. Complete separation of tyrosinated, detyrosinated, and nontyrosinatable brain tubulin subpopulations using affnity chromatography. Biochemistry 28(6), 2698-2704 (1989).
    • (1989) Biochemistry , vol.28 , Issue.6 , pp. 2698-2704
    • Paturle, L.1    Wehland, J.2    Margolis, R.L.3    Job, D.4
  • 90
    • 0026339889 scopus 로고
    • Characterization of a major brain tubulin variant which cannot be tyrosinated
    • Paturle-Lafanechere L, Edde B, Denoulet P et al. Characterization of a major brain tubulin variant which cannot be tyrosinated. Biochemistry 30(43), 10523-10528 (1991).
    • (1991) Biochemistry , vol.30 , Issue.43 , pp. 10523-10528
    • Paturle-Lafanechere, L.1    Edde, B.2    Denoulet, P.3
  • 91
    • 0021993649 scopus 로고
    • Chlamydomonas a-tubulin is posttranslationally modifed by acetylation on the e-amino group of a lysine
    • L'Hernault SW, Rosenbaum JL. Chlamydomonas a-tubulin is posttranslationally modifed by acetylation on the e-amino group of a lysine. Biochemistry 24(2), 473-478 (1985).
    • (1985) Biochemistry , vol.24 , Issue.2 , pp. 473-478
    • L'Hernault, S.W.1    Rosenbaum, J.L.2
  • 92
    • 0015984215 scopus 로고
    • Properties of rat brain tubulin
    • Eipper BA. Properties of rat brain tubulin. J. Biol. Chem. 249(5), 1407-1416 (1974).
    • (1974) J. Biol. Chem. , vol.249 , Issue.5 , pp. 1407-1416
    • Eipper, B.A.1
  • 93
    • 0015952164 scopus 로고
    • Rat brain tubulin and protein kinase activity
    • Eipper BA. Rat brain tubulin and protein kinase activity. J. Biol. Chem. 249(5), 1398-1406 (1974).
    • (1974) J. Biol. Chem. , vol.249 , Issue.5 , pp. 1398-1406
    • Eipper, B.A.1
  • 94
    • 0021990889 scopus 로고
    • A polymer-dependent increase in phosphorylation of b-tubulin accompanies differentiation of a mouse neuroblastoma cell line
    • Gard DL, Kirschner MW. A polymer-dependent increase in phosphorylation of b-tubulin accompanies differentiation of a mouse neuroblastoma cell line. J. Cell. Biol. 100(3), 764-774 (1985).
    • (1985) J. Cell. Biol. , vol.100 , Issue.3 , pp. 764-774
    • Gard, D.L.1    Kirschner, M.W.2
  • 95
    • 0030983113 scopus 로고    scopus 로고
    • Posttranslational modifcation of tubulin by palmitoylation: I in vivo and cell-free studies
    • Caron JM. Posttranslational modifcation of tubulin by palmitoylation: I. In vivo and cell-free studies. Mol. Biol. Cell 8(4), 621-636 (1997).
    • (1997) Mol. Biol. Cell , vol.8 , Issue.4 , pp. 621-636
    • Caron, J.M.1
  • 96
    • 0030964954 scopus 로고    scopus 로고
    • Posttranslational modifcation of tubulin by palmitoylation: II. Identifcation of sites of palmitoylation
    • Ozols J, Caron JM. Posttranslational modifcation of tubulin by palmitoylation: II. Identifcation of sites of palmitoylation. Mol. Biol. Cell 8(4), 637-645 (1997).
    • (1997) Mol. Biol. Cell , vol.8 , Issue.4 , pp. 637-645
    • Ozols, J.1    Caron, J.M.2
  • 97
    • 33750618516 scopus 로고    scopus 로고
    • Microtubule acetylation promotes kinesin-1 binding and transport
    • Reed NA, Cai D, Blasius TL et al. Microtubule acetylation promotes kinesin-1 binding and transport. Curr. Biol. 16(21), 2166-2172 (2006).
    • (2006) Curr. Biol. , vol.16 , Issue.21 , pp. 2166-2172
    • Reed, N.A.1    Cai, D.2    Blasius, T.L.3
  • 98
    • 0036156394 scopus 로고    scopus 로고
    • Export from pericentriolar endocytic recycling compartment to cell surface depends on stable, detyrosinated (glu) microtubules and kinesin
    • Lin SX, Gundersen GG, Maxfeld FR. Export from pericentriolar endocytic recycling compartment to cell surface depends on stable, detyrosinated (glu) microtubules and kinesin. Mol. Biol. Cell 13(1), 96-109 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , Issue.1 , pp. 96-109
    • Lin, S.X.1    Gundersen, G.G.2    Maxfeld, F.R.3
  • 99
    • 33748557490 scopus 로고    scopus 로고
    • Tubulin tyrosination is a major factor affecting the recruitment of CAP-Gly proteins at microtubule plus ends
    • Peris L, Thery M, Faure J et al. Tubulin tyrosination is a major factor affecting the recruitment of CAP-Gly proteins at microtubule plus ends. J. Cell Biol. 174(6), 839-849 (2006).
    • (2006) J. Cell Biol. , vol.174 , Issue.6 , pp. 839-849
    • Peris, L.1    Thery, M.2    Faure, J.3
  • 100
    • 12844266799 scopus 로고    scopus 로고
    • Mutations of tubulin glycylation sites reveal cross-talk between the C termini of a-and b-tubulin and affect the ciliary matrix in Tetrahymena
    • Redeker V, Levilliers N, Vinolo E et al. Mutations of tubulin glycylation sites reveal cross-talk between the C termini of a-and b-tubulin and affect the ciliary matrix in Tetrahymena. J. Biol. Chem. 280(1), 596-606 (2005).
    • (2005) J. Biol. Chem. , vol.280 , Issue.1 , pp. 596-606
    • Redeker, V.1    Levilliers, N.2    Vinolo, E.3
  • 101
    • 39149121834 scopus 로고    scopus 로고
    • Tubulin modifcations and their cellular functions
    • Hammond JW, Cai D, Verhey KJ. Tubulin modifcations and their cellular functions. Curr. Opin. Cell Biol. 20(1), 71-76 (2008).
    • (2008) Curr. Opin. Cell Biol. , vol.20 , Issue.1 , pp. 71-76
    • Hammond, J.W.1    Cai, D.2    Verhey, K.J.3
  • 102
    • 34548830425 scopus 로고    scopus 로고
    • The tubulin code
    • Verhey KJ, Gaertig J. The tubulin code. Cell Cycle, 6(17), 2152-2160 (2007).
    • (2007) Cell Cycle , vol.6 , Issue.17 , pp. 2152-2160
    • Verhey, K.J.1    Gaertig, J.2
  • 103
    • 0345169048 scopus 로고    scopus 로고
    • Post-translational modifcations regulate microtubule function
    • Westermann S, Weber K. Post-translational modifcations regulate microtubule function. Nat. Rev. Mol. Cell Biol. 4(12), 938-947 (2003).
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , Issue.12 , pp. 938-947
    • Westermann, S.1    Weber, K.2
  • 104
    • 0028197368 scopus 로고
    • HMG domain proteins: Architectural elements in the assembly of nucleoprotein structures
    • Grosschedl R, Giese K, Pagel J. HMG domain proteins: architectural elements in the assembly of nucleoprotein structures. Trends Genet. 10(3), 94-100 (1994).
    • (1994) Trends Genet. , vol.10 , Issue.3 , pp. 94-100
    • Grosschedl, R.1    Giese, K.2    Pagel, J.3
  • 105
    • 0028970056 scopus 로고
    • The expression of the high mobility group HMGI (Y) proteins correlates with the malignant phenotype of human thyroid neoplasias
    • Chiappetta G, Bandiera A, Berlingieri MT et al. The expression of the high mobility group HMGI (Y) proteins correlates with the malignant phenotype of human thyroid neoplasias. Oncogene 10(7), 1307-1314 (1995).
    • (1995) Oncogene , vol.10 , Issue.7 , pp. 1307-1314
    • Chiappetta, G.1    Bandiera, A.2    Berlingieri, M.T.3
  • 106
    • 0022410391 scopus 로고
    • Changes in nuclear proteins on transformation of rat epithelial thyroid cells by a murine sarcoma retrovirus
    • Giancotti V, Berlingieri MT, DiFiore PP, Fusco A, Vecchio G, Crane-Robinson C. Changes in nuclear proteins on transformation of rat epithelial thyroid cells by a murine sarcoma retrovirus. Cancer Res. 45(12 Pt 1), 6051-6057 (1985).
    • (1985) Cancer Res. , vol.45 , Issue.12 PART 1 , pp. 6051-6057
    • Giancotti, V.1    Berlingieri, M.T.2    Difiore, P.P.3    Fusco, A.4    Vecchio, G.5    Crane-Robinson, C.6
  • 107
    • 0024443958 scopus 로고
    • Analysis of the HMGI nuclear proteins in mouse neoplastic cells induced by different procedures
    • Giancotti V, Buratti E, Perissin L et al. Analysis of the HMGI nuclear proteins in mouse neoplastic cells induced by different procedures. Exp. Cell Res. 184(2), 538-545 (1989).
    • (1989) Exp. Cell Res. , vol.184 , Issue.2 , pp. 538-545
    • Giancotti, V.1    Buratti, E.2    Perissin, L.3
  • 108
    • 8044225313 scopus 로고    scopus 로고
    • High level expression of the HMGI (Y) gene during embryonic development
    • Chiappetta G, Avantaggiato V, Visconti R et al. High level expression of the HMGI (Y) gene during embryonic development. Oncogene 13(11), 2439-2446 (1996).
    • (1996) Oncogene , vol.13 , Issue.11 , pp. 2439-2446
    • Chiappetta, G.1    Avantaggiato, V.2    Visconti, R.3
  • 109
    • 0029094755 scopus 로고
    • Mutation responsible for the mouse pygmy phenotype in the developmentally regulated factor HMGI-C
    • Zhou X, Benson KF, Ashar HR, Chada K. Mutation responsible for the mouse pygmy phenotype in the developmentally regulated factor HMGI-C. Nature 376(6543), 771-774 (1995).
    • (1995) Nature , vol.376 , Issue.6543 , pp. 771-774
    • Zhou, X.1    Benson, K.F.2    Ashar, H.R.3    Chada, K.4
  • 110
    • 0029915384 scopus 로고    scopus 로고
    • Substrate structure infuences binding of the non-histone protein HMG-I(Y) to free nucleosomal DNA
    • Reeves R, Wolffe AP. Substrate structure infuences binding of the non-histone protein HMG-I(Y) to free nucleosomal DNA. Biochemistry 35(15), 5063-5074 (1996).
    • (1996) Biochemistry , vol.35 , Issue.15 , pp. 5063-5074
    • Reeves, R.1    Wolffe, A.P.2
  • 111
    • 0027493415 scopus 로고
    • Interaction of high mobility group-I (Y) nonhistone proteins with nucleosome core particles
    • Reeves R, Nissen MS. Interaction of high mobility group-I (Y) nonhistone proteins with nucleosome core particles. J. Biol. Chem. 268(28), 21137-21146 (1993).
    • (1993) J. Biol. Chem. , vol.268 , Issue.28 , pp. 21137-21146
    • Reeves, R.1    Nissen, M.S.2
  • 112
    • 0034121077 scopus 로고    scopus 로고
    • Binding of HMG-I(Y) imparts architectural specifcity to a positioned nucleosome on the promoter of the human interleukin-2 receptor a gene
    • Reeves R, Leonard WJ, Nissen MS. Binding of HMG-I(Y) imparts architectural specifcity to a positioned nucleosome on the promoter of the human interleukin-2 receptor a gene. Mol. Cell Biol. 20(13), 4666-4679 (2000).
    • (2000) Mol. Cell Biol. , vol.20 , Issue.13 , pp. 4666-4679
    • Reeves, R.1    Leonard, W.J.2    Nissen, M.S.3
  • 113
    • 53149084916 scopus 로고    scopus 로고
    • High mobility group proteins and their post-translational modifcations
    • Zhang Q, Wang Y. High mobility group proteins and their post-translational modifcations. Biochim. Biophys. Acta 1784(9), 1159-1166 (2008).
    • (2008) Biochim. Biophys. Acta , vol.1784 , Issue.9 , pp. 1159-1166
    • Zhang, Q.1    Wang, Y.2
  • 114
    • 0022552760 scopus 로고
    • Purifcation and postsynthetic modifcations of Friend erythroleukemic cell high mobility group protein HMG-I
    • Elton TS, Reeves R. Purifcation and postsynthetic modifcations of Friend erythroleukemic cell high mobility group protein HMG-I. Anal. Biochem. 157(1), 53-62 (1986).
    • (1986) Anal. Biochem. , vol.157 , Issue.1 , pp. 53-62
    • Elton, T.S.1    Reeves, R.2
  • 115
    • 0021998631 scopus 로고
    • On the phosphorylation of low molecular mass HMG (high mobility group) proteins in Ehrlich ascites cells
    • Lund T, Holtlund J, Laland SG. On the phosphorylation of low molecular mass HMG (high mobility group) proteins in Ehrlich ascites cells. FEBS Lett. 180(2), 275-279 (1985).
    • (1985) FEBS Lett. , vol.180 , Issue.2 , pp. 275-279
    • Lund, T.1    Holtlund, J.2    Laland, S.G.3
  • 116
    • 53149084916 scopus 로고    scopus 로고
    • High mobility group proteins and their post-translational modifcations
    • Zhang Q, Wang Y. High mobility group proteins and their post-translational modifcations. Biochim. Biophys. Acta 1784(9), 1159-1166 (2008).
    • (2008) Biochim. Biophys. Acta , vol.1784 , Issue.9 , pp. 1159-1166
    • Zhang, Q.1    Wang, Y.2
  • 117
    • 0025724096 scopus 로고
    • Phosphorylation by cdc2 kinase modulates DNA binding activity of high mobility group i nonhistone chromatin protein
    • Nissen MS, Langan TA, Reeves R. Phosphorylation by cdc2 kinase modulates DNA binding activity of high mobility group I nonhistone chromatin protein. J. Biol. Chem. 266(30), 19945-19952 (1991).
    • (1991) J. Biol. Chem. , vol.266 , Issue.30 , pp. 19945-19952
    • Nissen, M.S.1    Langan, T.A.2    Reeves, R.3
  • 118
    • 4444254840 scopus 로고    scopus 로고
    • Dynamic interaction of HMGA1a proteins with chromatin
    • Harrer M, Luhrs H, Bustin M, Scheer U, Hock R. Dynamic interaction of HMGA1a proteins with chromatin. J. Cell. Sci. 117(Pt 16), 3459-3471 (2004).
    • (2004) J. Cell. Sci. , vol.117 , Issue.PART 16 , pp. 3459-3471
    • Harrer, M.1    Luhrs, H.2    Bustin, M.3    Scheer, U.4    Hock, R.5
  • 119
    • 0034682565 scopus 로고    scopus 로고
    • Differential in vivo modifcations of the HMGI(Y) nonhistone chromatin proteins modulate nucleosome and DNA interactions
    • Banks GC, Li Y, Reeves R. Differential in vivo modifcations of the HMGI(Y) nonhistone chromatin proteins modulate nucleosome and DNA interactions. Biochemistry 39(28), 8333-8346 (2000).
    • (2000) Biochemistry , vol.39 , Issue.28 , pp. 8333-8346
    • Banks, G.C.1    Li, Y.2    Reeves, R.3
  • 120
    • 4444277135 scopus 로고    scopus 로고
    • In vivo posttranslational modifcations of the high mobility group A1a proteins in breast cancer cells of differing metastatic potential
    • Edberg DD, Bruce JE, Siems WF, Reeves R. In vivo posttranslational modifcations of the high mobility group A1a proteins in breast cancer cells of differing metastatic potential. Biochemistry 43(36), 11500-11515 (2004).
    • (2004) Biochemistry , vol.43 , Issue.36 , pp. 11500-11515
    • Edberg, D.D.1    Bruce, J.E.2    Siems, W.F.3    Reeves, R.4
  • 121
    • 0034646638 scopus 로고    scopus 로고
    • Acetylation of novel sites in the nucleosomal binding domain of chromosomal protein HMG-14 by p300 alters its interaction with nucleosomes
    • Bergel M, Herrera JE, Thatcher BJ et al. Acetylation of novel sites in the nucleosomal binding domain of chromosomal protein HMG-14 by p300 alters its interaction with nucleosomes. J. Biol. Chem. 275(15), 11514-11520 (2000).
    • (2000) J. Biol. Chem. , vol.275 , Issue.15 , pp. 11514-11520
    • Bergel, M.1    Herrera, J.E.2    Thatcher, B.J.3
  • 122
    • 0032933141 scopus 로고    scopus 로고
    • Specifc acetylation of chromosomal protein HMG-17 by PCAF alters its interaction with nucleosomes
    • Herrera JE, Sakaguchi K, Bergel M, Trieschmann L, Nakatani Y, Bustin M. Specifc acetylation of chromosomal protein HMG-17 by PCAF alters its interaction with nucleosomes. Mol. Cell. Biol. 19(5), 3466-3473 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , Issue.5 , pp. 3466-3473
    • Herrera, J.E.1    Sakaguchi, K.2    Bergel, M.3    Trieschmann, L.4    Nakatani, Y.5    Bustin, M.6
  • 123
    • 0000944563 scopus 로고    scopus 로고
    • Electron capture dissociation of multiply charged protein cations. a nonergodic process
    • Zubarev RA, Kelleher NL, McLafferty FW. Electron capture dissociation of multiply charged protein cations. a nonergodic process. J. Am. Chem. Soc. 120(13), 3265-3266 (1998).
    • (1998) J. Am. Chem. Soc. , vol.120 , Issue.13 , pp. 3265-3266
    • Zubarev, R.A.1    Kelleher, N.L.2    McLafferty, F.W.3
  • 124
    • 3042789073 scopus 로고    scopus 로고
    • Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
    • Syka JE, Coon JJ, Schroeder MJ, Shabanowitz J, Hunt DF. Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. Proc. Natl Acad. Sci. USA 101(26), 9528-9533 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , Issue.26 , pp. 9528-9533
    • Syka, J.E.1    Coon, J.J.2    Schroeder, M.J.3    Shabanowitz, J.4    Hunt, D.F.5
  • 125
    • 43549095027 scopus 로고    scopus 로고
    • Electron capture/transfer versus collisionally activated/induced dissociations: Solo or duet?
    • Zubarev RA, Zubarev AR, Savitski MM. Electron capture/transfer versus collisionally activated/induced dissociations: solo or duet? J. Am. Soc. Mass Spectrom. 19(6), 753-761 (2008).
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , Issue.6 , pp. 753-761
    • Zubarev, R.A.1    Zubarev, A.R.2    Savitski, M.M.3
  • 126
    • 33646899550 scopus 로고    scopus 로고
    • Top-down protein sequencing and MS3 on a hybrid linear quadrupole ion trap-orbitrap mass spectrometer
    • Macek B, Waanders LF, Olsen JV, Mann M. Top-down protein sequencing and MS3 on a hybrid linear quadrupole ion trap-orbitrap mass spectrometer. Mol. Cell. Proteomics 5(5), 949-958 (2006).
    • (2006) Mol. Cell. Proteomics , vol.5 , Issue.5 , pp. 949-958
    • MacEk, B.1    Waanders, L.F.2    Olsen, J.V.3    Mann, M.4
  • 127
    • 0034501099 scopus 로고    scopus 로고
    • Mobile and localized protons: A framework for understanding peptide dissociation
    • Wysocki VH, Tsaprailis G, Smith LL, Breci LA. Mobile and localized protons: a framework for understanding peptide dissociation. J. Mass Spectrom. 35(12), 1399-1406 (2000).
    • (2000) J. Mass Spectrom. , vol.35 , Issue.12 , pp. 1399-1406
    • Wysocki, V.H.1    Tsaprailis, G.2    Smith, L.L.3    Breci, L.A.4
  • 128
    • 35848949043 scopus 로고    scopus 로고
    • Decoding protein modifcations using top-down mass spectrometry Nat
    • Siuti N, Kelleher NL. Decoding protein modifcations using top-down mass spectrometry Nat. Methods 4(10), 817-821 (2007).
    • (2007) Methods , vol.4 , Issue.10 , pp. 817-821
    • Siuti, N.1    Kelleher, N.L.2
  • 129
    • 46249090762 scopus 로고    scopus 로고
    • Analysis of histones, histone variants, and their post-translationally modifed forms
    • Lindner HH. Analysis of histones, histone variants, and their post-translationally modifed forms. Electrophoresis 29(12), 2516-2532 (2008).
    • (2008) Electrophoresis , vol.29 , Issue.12 , pp. 2516-2532
    • Lindner, H.H.1
  • 130
    • 77951628036 scopus 로고    scopus 로고
    • Characterization of histone H2A and H2B variants and their post-translational modifcations by mass spectrometry
    • Bonenfant D, Coulot M, Towbin H, Schindler P, van Oostrum J. Characterization of histone H2A and H2B variants and their post-translational modifcations by mass spectrometry. Mol. Cell Proteomics 6 (11), 1917-1932 (2006).
    • (2006) Mol. Cell Proteomics , vol.6 , Issue.11 , pp. 1917-1932
    • Bonenfant, D.1    Coulot, M.2    Towbin, H.3    Schindler, P.4    Van Oostrum, J.5
  • 131
    • 33644853355 scopus 로고    scopus 로고
    • Expression patterns and post-translational modifcations associated with mammalian histone H3 variants
    • Hake SB, Garcia BA, Duncan EM et al. Expression patterns and post-translational modifcations associated with mammalian histone H3 variants. J. Biol. Chem. 281(1), 559-568 (2006).
    • (2006) J. Biol. Chem. , vol.281 , Issue.1 , pp. 559-568
    • Hake, S.B.1    Garcia, B.A.2    Duncan, E.M.3
  • 132
    • 18144370095 scopus 로고    scopus 로고
    • Serine 31 phosphorylation of histone variant H3.3 is specifc to regions bordering centromeres in metaphase chromosomes
    • Hake SB, Garcia BA, Kauer M et al. Serine 31 phosphorylation of histone variant H3.3 is specifc to regions bordering centromeres in metaphase chromosomes. Proc. Natl Acad. Sci. USA 102(18), 6344-6349 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , Issue.18 , pp. 6344-6349
    • Hake, S.B.1    Garcia, B.A.2    Kauer, M.3
  • 133
    • 34249779529 scopus 로고    scopus 로고
    • Pervasive combinatorial modifcation of histone H3 in human cells
    • Garcia BA, Pesavento JJ, Mizzen CA, Kelleher NL. Pervasive combinatorial modifcation of histone H3 in human cells. Nat. Methods 4(6), 487-489 (2007).
    • (2007) Nat. Methods , vol.4 , Issue.6 , pp. 487-489
    • Garcia, B.A.1    Pesavento, J.J.2    Mizzen, C.A.3    Kelleher, N.L.4
  • 134
    • 41949086475 scopus 로고    scopus 로고
    • Mass spectrometry identifes and quantifes 74 unique histone H4 isoforms in differentiating human embryonic stem cells
    • Phanstiel D, Brumbaugh J, Berggren WT et al. Mass spectrometry identifes and quantifes 74 unique histone H4 isoforms in differentiating human embryonic stem cells. Proc. Natl Acad. Sci. USA 105(11), 4093-4098 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , Issue.11 , pp. 4093-4098
    • Phanstiel, D.1    Brumbaugh, J.2    Berggren, W.T.3
  • 136
    • 47249157351 scopus 로고    scopus 로고
    • Combinatorial modifcation of human histone H4 quantitated by two-dimensional liquid chromatography coupled with top down mass spectrometry J
    • Pesavento JJ, Bullock CR, LeDuc RD, Mizzen CA, Kelleher NL. Combinatorial modifcation of human histone H4 quantitated by two-dimensional liquid chromatography coupled with top down mass spectrometry J. Biol. Chem. 283(22), 14927-14937 (2008).
    • (2008) Biol. Chem. , vol.283 , Issue.22 , pp. 14927-14937
    • Pesavento, J.J.1    Bullock, C.R.2    Leduc, R.D.3    Mizzen, C.A.4    Kelleher, N.L.5
  • 137
    • 34948821302 scopus 로고    scopus 로고
    • Global assessment of combinatorial post-translational modifcation of core histones in yeast using contemporary mass spectrometry. LYS4 trimethylation correlates with degree of acetylation on the same H3 tail
    • Jiang L, Smith JN, Anderson SL, Ma P, Mizzen CA, Kelleher NL. Global assessment of combinatorial post-translational modifcation of core histones in yeast using contemporary mass spectrometry. LYS4 trimethylation correlates with degree of acetylation on the same H3 tail. J. Biol. Chem. 282(38), 27923-27934 (2007).
    • (2007) J. Biol. Chem. , vol.282 , Issue.38 , pp. 27923-27934
    • Jiang, L.1    Smith, J.N.2    Anderson, S.L.3    Ma, P.4    Mizzen, C.A.5    Kelleher, N.L.6
  • 138
    • 5644231221 scopus 로고    scopus 로고
    • Characterization of Tetrahymena histone H2B variants and posttranslational populations by electron capture dissociation (ECD) Fourier transform ion cyclotron mass spectrometry (FT-ICR MS)
    • Medzihradszky KF, Zhang X, Chalkley RJ et al. Characterization of Tetrahymena histone H2B variants and posttranslational populations by electron capture dissociation (ECD) Fourier transform ion cyclotron mass spectrometry (FT-ICR MS). Mol. Cell Proteomics 3(9), 872-886 (2004).
    • (2004) Mol. Cell Proteomics , vol.3 , Issue.9 , pp. 872-886
    • Medzihradszky, K.F.1    Zhang, X.2    Chalkley, R.J.3
  • 139
    • 32344453537 scopus 로고    scopus 로고
    • Gene-specifc characterization of human histone H2B by electron capture dissociation
    • Siuti N, Roth MJ, Mizzen CA, Kelleher NL, Pesavento JJ. Gene-specifc characterization of human histone H2B by electron capture dissociation. J. Proteome Res. 5(2), 233-239 (2006)
    • (2006) J. Proteome Res. , vol.5 , Issue.2 , pp. 233-239
    • Siuti, N.1    Roth, M.J.2    Mizzen, C.A.3    Kelleher, N.L.4    Pesavento, J.J.5
  • 140
    • 32344452605 scopus 로고    scopus 로고
    • Precise characterization of human histones in the H2A gene family by top down mass spectrometry
    • Boyne MT 2nd, Pesavento JJ, Mizzen CA, Kelleher NL. Precise characterization of human histones in the H2A gene family by top down mass spectrometry. J. Proteome Res. 5(2), 248-253 (2006).
    • (2006) J. Proteome Res. , vol.5 , Issue.2 , pp. 248-253
    • Mt, B.Ii.1    Pesavento, J.J.2    Mizzen, C.A.3    Kelleher, N.L.4
  • 141
    • 32344453899 scopus 로고    scopus 로고
    • Mass spectrometric characterization of human histone H3: A bird's eye view
    • Thomas CE, Kelleher NL, Mizzen CA. Mass spectrometric characterization of human histone H3: a bird's eye view. J. Proteome Res. 5(2), 240-247 (2006).
    • (2006) J. Proteome Res. , vol.5 , Issue.2 , pp. 240-247
    • Thomas, C.E.1    Kelleher, N.L.2    Mizzen, C.A.3
  • 142
    • 33847768829 scopus 로고    scopus 로고
    • Long-distance combinatorial linkage between methylation and acetylation on histone H3 N termini
    • Taverna SD, Ueberheide BM, Liu Y et al. Long-distance combinatorial linkage between methylation and acetylation on histone H3 N termini. Proc. Natl Acad. Sci. USA 104(7), 2086-2091 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , Issue.7 , pp. 2086-2091
    • Taverna, S.D.1    Ueberheide, B.M.2    Liu, Y.3
  • 143
    • 33745621292 scopus 로고    scopus 로고
    • Absolute quantifcation of multisite phosphorylation by selective reaction monitoring mass spectrometry: Determination of inhibitory phosphorylation status of cyclin-dependent kinases
    • Mayya V, Rezual K, Wu L, Fong MB, Han DK. Absolute quantifcation of multisite phosphorylation by selective reaction monitoring mass spectrometry: determination of inhibitory phosphorylation status of cyclin-dependent kinases. Mol. Cell. Proteomics 5(6), 1146-1157 (2006).
    • (2006) Mol. Cell. Proteomics , vol.5 , Issue.6 , pp. 1146-1157
    • Mayya, V.1    Rezual, K.2    Wu, L.3    Fong, M.B.4    Han, D.K.5
  • 144
    • 52649125713 scopus 로고    scopus 로고
    • The Ser/Thr/Tyr phosphoproteome of Lactococcus lactis IL1403 reveals multiply phosphorylated proteins
    • Souf B, Gnad F, Jensen PR et al. The Ser/Thr/Tyr phosphoproteome of Lactococcus lactis IL1403 reveals multiply phosphorylated proteins. Proteomics 8(17), 3486-3493 (2008).
    • (2008) Proteomics , vol.8 , Issue.17 , pp. 3486-3493
    • Souf, B.1    Gnad, F.2    Jensen, P.R.3
  • 145
    • 57349161921 scopus 로고    scopus 로고
    • Constitutive and dynamic phosphorylation and acetylation sites on NUCKS, a hypermodifed nuclear protein, studied by quantitative proteomics
    • Wisniewski JR, Zougman A, Kruger S et al. Constitutive and dynamic phosphorylation and acetylation sites on NUCKS, a hypermodifed nuclear protein, studied by quantitative proteomics. Proteins 73(3), 710-718 (2008).
    • (2008) Proteins , vol.73 , Issue.3 , pp. 710-718
    • Wisniewski, J.R.1    Zougman, A.2    Kruger, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.