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Volumn 9, Issue 1, 2013, Pages

A Newly Uncovered Group of Distantly Related Lysine Methyltransferases Preferentially Interact with Molecular Chaperones to Regulate Their Activity

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ARGININE; CHAPERONE; GLUTAMINE; GLYCINE; HEAT SHOCK COGNATE PROTEIN 70; HISTIDINE; HISTONE LYSINE METHYLTRANSFERASE; ISOPROTEIN; LYSINE; PROTEIN ASPSCR1; PROTEIN KIN; PROTEIN KIN17; PROTEIN METHYLTRANSFERASE; PROTEIN METTL21D; PROTEIN P97; PROTEIN UBX; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 84873513121     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1003210     Document Type: Article
Times cited : (138)

References (81)
  • 1
    • 0036917889 scopus 로고    scopus 로고
    • SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold
    • Martin JL, McMillan FM, (2002) SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold. Curr Opin Struct Biol 12: 783-793.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 783-793
    • Martin, J.L.1    McMillan, F.M.2
  • 3
    • 0038374971 scopus 로고    scopus 로고
    • Many paths to methyltransfer: a chronicle of convergence
    • Schubert HL, Blumenthal RM, Cheng X, (2003) Many paths to methyltransfer: a chronicle of convergence. Trends Biochem Sci 28: 329-335.
    • (2003) Trends Biochem Sci , vol.28 , pp. 329-335
    • Schubert, H.L.1    Blumenthal, R.M.2    Cheng, X.3
  • 4
    • 45849104577 scopus 로고    scopus 로고
    • The human mitochondrial translation release factor HMRF1L is methylated in the GGQ motif by the methyltransferase HMPrmC
    • Ishizawa T, Nozaki Y, Ueda T, Takeuchi N, (2008) The human mitochondrial translation release factor HMRF1L is methylated in the GGQ motif by the methyltransferase HMPrmC. Biochem Biophys Res Commun 373: 99-103.
    • (2008) Biochem Biophys Res Commun , vol.373 , pp. 99-103
    • Ishizawa, T.1    Nozaki, Y.2    Ueda, T.3    Takeuchi, N.4
  • 5
    • 0023024145 scopus 로고
    • Post-translational methylation of asparaginyl residues. Identification of beta-71 gamma-N-methylasparagine in allophycocyanin
    • Klotz AV, Leary JA, Glazer AN, (1986) Post-translational methylation of asparaginyl residues. Identification of beta-71 gamma-N-methylasparagine in allophycocyanin. J Biol Chem 261: 15891-15894.
    • (1986) J Biol Chem , vol.261 , pp. 15891-15894
    • Klotz, A.V.1    Leary, J.A.2    Glazer, A.N.3
  • 6
    • 78549293943 scopus 로고    scopus 로고
    • A novel 3-methylhistidine modification of yeast ribosomal protein Rpl3 is dependent upon the YIL110W methyltransferase
    • Webb KJ, Zurita-Lopez CI, Al-Hadid Q, Laganowsky A, Young BD, et al. (2010) A novel 3-methylhistidine modification of yeast ribosomal protein Rpl3 is dependent upon the YIL110W methyltransferase. J Biol Chem 285: 37598-37606.
    • (2010) J Biol Chem , vol.285 , pp. 37598-37606
    • Webb, K.J.1    Zurita-Lopez, C.I.2    Al-Hadid, Q.3    Laganowsky, A.4    Young, B.D.5
  • 7
    • 0025195404 scopus 로고
    • Mammalian O6-alkylguanine-DNA alkyltransferase: regulation and importance in response to alkylating carcinogenic and therapeutic agents
    • Pegg AE, (1990) Mammalian O6-alkylguanine-DNA alkyltransferase: regulation and importance in response to alkylating carcinogenic and therapeutic agents. Cancer Res 50: 6119-6129.
    • (1990) Cancer Res , vol.50 , pp. 6119-6129
    • Pegg, A.E.1
  • 8
    • 44449117052 scopus 로고    scopus 로고
    • Identification and validation of eukaryotic aspartate and glutamate methylation in proteins
    • Sprung R, Chen Y, Zhang K, Cheng D, Zhang T, et al. (2008) Identification and validation of eukaryotic aspartate and glutamate methylation in proteins. J Proteome Res 7: 1001-1006.
    • (2008) J Proteome Res , vol.7 , pp. 1001-1006
    • Sprung, R.1    Chen, Y.2    Zhang, K.3    Cheng, D.4    Zhang, T.5
  • 9
    • 0026735063 scopus 로고
    • Protein isoprenylation and methylation at carboxyl-terminal cysteine residues
    • Clarke S, (1992) Protein isoprenylation and methylation at carboxyl-terminal cysteine residues. Annu Rev Biochem 61: 355-386.
    • (1992) Annu Rev Biochem , vol.61 , pp. 355-386
    • Clarke, S.1
  • 11
    • 0034331296 scopus 로고    scopus 로고
    • Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo
    • Wu J, Tolstykh T, Lee J, Boyd K, Stock JB, et al. (2000) Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo. Embo J 19: 5672-5681.
    • (2000) Embo J , vol.19 , pp. 5672-5681
    • Wu, J.1    Tolstykh, T.2    Lee, J.3    Boyd, K.4    Stock, J.B.5
  • 12
    • 0037172665 scopus 로고    scopus 로고
    • Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain
    • Feng Q, Wang H, Ng HH, Erdjument-Bromage H, Tempst P, et al. (2002) Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain. Curr Biol 12: 1052-1058.
    • (2002) Curr Biol , vol.12 , pp. 1052-1058
    • Feng, Q.1    Wang, H.2    Ng, H.H.3    Erdjument-Bromage, H.4    Tempst, P.5
  • 13
    • 27644589675 scopus 로고    scopus 로고
    • The diverse functions of histone lysine methylation
    • Martin C, Zhang Y, (2005) The diverse functions of histone lysine methylation. Nat Rev Mol Cell Biol 6: 838-849.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 838-849
    • Martin, C.1    Zhang, Y.2
  • 14
    • 33845786515 scopus 로고    scopus 로고
    • The control of histone lysine methylation in epigenetic regulation
    • Volkel P, Angrand PO, (2007) The control of histone lysine methylation in epigenetic regulation. Biochimie 89: 1-20.
    • (2007) Biochimie , vol.89 , pp. 1-20
    • Volkel, P.1    Angrand, P.O.2
  • 15
    • 34249026300 scopus 로고    scopus 로고
    • High-resolution profiling of histone methylations in the human genome
    • Barski A, Cuddapah S, Cui K, Roh TY, Schones DE, et al. (2007) High-resolution profiling of histone methylations in the human genome. Cell 129: 823-837.
    • (2007) Cell , vol.129 , pp. 823-837
    • Barski, A.1    Cuddapah, S.2    Cui, K.3    Roh, T.Y.4    Schones, D.E.5
  • 16
    • 34250307630 scopus 로고    scopus 로고
    • The landscape of histone modifications across 1% of the human genome in five human cell lines
    • Koch CM, Andrews RM, Flicek P, Dillon SC, Karaoz U, et al. (2007) The landscape of histone modifications across 1% of the human genome in five human cell lines. Genome Res 17: 691-707.
    • (2007) Genome Res , vol.17 , pp. 691-707
    • Koch, C.M.1    Andrews, R.M.2    Flicek, P.3    Dillon, S.C.4    Karaoz, U.5
  • 17
    • 64849110610 scopus 로고    scopus 로고
    • Determination of enriched histone modifications in non-genic portions of the human genome
    • Rosenfeld JA, Wang Z, Schones DE, Zhao K, DeSalle R, et al. (2009) Determination of enriched histone modifications in non-genic portions of the human genome. BMC Genomics 10: 143.
    • (2009) BMC Genomics , vol.10 , pp. 143
    • Rosenfeld, J.A.1    Wang, Z.2    Schones, D.E.3    Zhao, K.4    DeSalle, R.5
  • 18
    • 9244247669 scopus 로고    scopus 로고
    • Regulation of p53 activity through lysine methylation
    • Chuikov S, Kurash JK, Wilson JR, Xiao B, Justin N, et al. (2004) Regulation of p53 activity through lysine methylation. Nature 432: 353-360.
    • (2004) Nature , vol.432 , pp. 353-360
    • Chuikov, S.1    Kurash, J.K.2    Wilson, J.R.3    Xiao, B.4    Justin, N.5
  • 19
    • 0024636180 scopus 로고
    • Post-translational modifications in the large subunit of ribulose bisphosphate carboxylase/oxygenase
    • Houtz RL, Stults JT, Mulligan RM, Tolbert NE, (1989) Post-translational modifications in the large subunit of ribulose bisphosphate carboxylase/oxygenase. Proc Natl Acad Sci U S A 86: 1855-1859.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 1855-1859
    • Houtz, R.L.1    Stults, J.T.2    Mulligan, R.M.3    Tolbert, N.E.4
  • 21
    • 0018075073 scopus 로고
    • Modification of yeast ribosomal proteins. Methylation
    • Kruiswijk T, Kunst A, Planta RJ, Mager WH, (1978) Modification of yeast ribosomal proteins. Methylation. Biochem J 175: 221-225.
    • (1978) Biochem J , vol.175 , pp. 221-225
    • Kruiswijk, T.1    Kunst, A.2    Planta, R.J.3    Mager, W.H.4
  • 22
    • 0037197887 scopus 로고    scopus 로고
    • Direct mass spectrometric analysis of intact proteins of the yeast large ribosomal subunit using capillary LC/FTICR
    • Lee SW, Berger SJ, Martinovic S, Pasa-Tolic L, Anderson GA, et al. (2002) Direct mass spectrometric analysis of intact proteins of the yeast large ribosomal subunit using capillary LC/FTICR. Proc Natl Acad Sci U S A 99: 5942-5947.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 5942-5947
    • Lee, S.W.1    Berger, S.J.2    Martinovic, S.3    Pasa-Tolic, L.4    Anderson, G.A.5
  • 23
    • 78650308842 scopus 로고    scopus 로고
    • Lysine methylation of the NF-kappaB subunit RelA by SETD6 couples activity of the histone methyltransferase GLP at chromatin to tonic repression of NF-kappaB signaling
    • Levy D, Kuo AJ, Chang Y, Schaefer U, Kitson C, et al. (2011) Lysine methylation of the NF-kappaB subunit RelA by SETD6 couples activity of the histone methyltransferase GLP at chromatin to tonic repression of NF-kappaB signaling. Nat Immunol 12: 29-36.
    • (2011) Nat Immunol , vol.12 , pp. 29-36
    • Levy, D.1    Kuo, A.J.2    Chang, Y.3    Schaefer, U.4    Kitson, C.5
  • 24
    • 0021763631 scopus 로고
    • Methylated proteins and amino acids in the ribosomes of Saccharomyces cerevisiae
    • Lhoest J, Lobet Y, Costers E, Colson C, (1984) Methylated proteins and amino acids in the ribosomes of Saccharomyces cerevisiae. Eur J Biochem 141: 585-590.
    • (1984) Eur J Biochem , vol.141 , pp. 585-590
    • Lhoest, J.1    Lobet, Y.2    Costers, E.3    Colson, C.4
  • 25
    • 0023472129 scopus 로고
    • Purification and properties of calmodulin-lysine N-methyltransferase from rat brain cytosol
    • Morino H, Kawamoto T, Miyake M, Kakimoto Y, (1987) Purification and properties of calmodulin-lysine N-methyltransferase from rat brain cytosol. J Neurochem 48: 1201-1208.
    • (1987) J Neurochem , vol.48 , pp. 1201-1208
    • Morino, H.1    Kawamoto, T.2    Miyake, M.3    Kakimoto, Y.4
  • 27
    • 67349285384 scopus 로고    scopus 로고
    • Negative regulation of NF-kappaB action by Set9-mediated lysine methylation of the RelA subunit
    • Yang XD, Huang B, Li M, Lamb A, Kelleher NL, et al. (2009) Negative regulation of NF-kappaB action by Set9-mediated lysine methylation of the RelA subunit. Embo J 28: 1055-1066.
    • (2009) Embo J , vol.28 , pp. 1055-1066
    • Yang, X.D.1    Huang, B.2    Li, M.3    Lamb, A.4    Kelleher, N.L.5
  • 28
    • 67849097183 scopus 로고    scopus 로고
    • High-resolution mapping of the protein interaction network for the human transcription machinery and affinity purification of RNA polymerase II-associated complexes
    • Cloutier P, Al-Khoury R, Lavallee-Adam M, Faubert D, Jiang H, et al. (2009) High-resolution mapping of the protein interaction network for the human transcription machinery and affinity purification of RNA polymerase II-associated complexes. Methods 48: 381-386.
    • (2009) Methods , vol.48 , pp. 381-386
    • Cloutier, P.1    Al-Khoury, R.2    Lavallee-Adam, M.3    Faubert, D.4    Jiang, H.5
  • 29
    • 77950601816 scopus 로고    scopus 로고
    • New insights into the biogenesis of nuclear RNA polymerases?
    • Cloutier P, Coulombe B, (2010) New insights into the biogenesis of nuclear RNA polymerases? Biochem Cell Biol 88: 211-221.
    • (2010) Biochem Cell Biol , vol.88 , pp. 211-221
    • Cloutier, P.1    Coulombe, B.2
  • 30
    • 79953152680 scopus 로고    scopus 로고
    • Transcription factor IIS cooperates with the E3 ligase UBR5 to ubiquitinate the CDK9 subunit of the positive transcription elongation factor B
    • Cojocaru M, Bouchard A, Cloutier P, Cooper JJ, Varzavand K, et al. (2011) Transcription factor IIS cooperates with the E3 ligase UBR5 to ubiquitinate the CDK9 subunit of the positive transcription elongation factor B. J Biol Chem 286: 5012-5022.
    • (2011) J Biol Chem , vol.286 , pp. 5012-5022
    • Cojocaru, M.1    Bouchard, A.2    Cloutier, P.3    Cooper, J.J.4    Varzavand, K.5
  • 31
    • 42149133591 scopus 로고    scopus 로고
    • Steps towards a repertoire of comprehensive maps of human protein interaction networks: the Human Proteotheque Initiative (HuPI)
    • Coulombe B, Blanchette M, Jeronimo C, (2008) Steps towards a repertoire of comprehensive maps of human protein interaction networks: the Human Proteotheque Initiative (HuPI). Biochem Cell Biol 86: 149-156.
    • (2008) Biochem Cell Biol , vol.86 , pp. 149-156
    • Coulombe, B.1    Blanchette, M.2    Jeronimo, C.3
  • 32
    • 78650077626 scopus 로고    scopus 로고
    • The protein interaction network of the human transcription machinery reveals a role for the conserved GTPase RPAP4/GPN1 and microtubule assembly in nuclear import and biogenesis of RNA polymerase II
    • Forget D, Lacombe AA, Cloutier P, Al-Khoury R, Bouchard A, et al. (2010) The protein interaction network of the human transcription machinery reveals a role for the conserved GTPase RPAP4/GPN1 and microtubule assembly in nuclear import and biogenesis of RNA polymerase II. Mol Cell Proteomics 9: 2827-2839.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 2827-2839
    • Forget, D.1    Lacombe, A.A.2    Cloutier, P.3    Al-Khoury, R.4    Bouchard, A.5
  • 33
    • 34447321025 scopus 로고    scopus 로고
    • Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme
    • Jeronimo C, Forget D, Bouchard A, Li Q, Chua G, et al. (2007) Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme. Mol Cell 27: 262-274.
    • (2007) Mol Cell , vol.27 , pp. 262-274
    • Jeronimo, C.1    Forget, D.2    Bouchard, A.3    Li, Q.4    Chua, G.5
  • 34
    • 3543034591 scopus 로고    scopus 로고
    • RPAP1, a novel human RNA polymerase II-associated protein affinity purified with recombinant wild-type and mutated polymerase subunits
    • Jeronimo C, Langelier MF, Zeghouf M, Cojocaru M, Bergeron D, et al. (2004) RPAP1, a novel human RNA polymerase II-associated protein affinity purified with recombinant wild-type and mutated polymerase subunits. Mol Cell Biol 24: 7043-7058.
    • (2004) Mol Cell Biol , vol.24 , pp. 7043-7058
    • Jeronimo, C.1    Langelier, M.F.2    Zeghouf, M.3    Cojocaru, M.4    Bergeron, D.5
  • 35
    • 42449086866 scopus 로고    scopus 로고
    • LARP7 is a stable component of the 7SK snRNP while P-TEFb, HEXIM1 and hnRNP A1 are reversibly associated
    • Krueger BJ, Jeronimo C, Roy BB, Bouchard A, Barrandon C, et al. (2008) LARP7 is a stable component of the 7SK snRNP while P-TEFb, HEXIM1 and hnRNP A1 are reversibly associated. Nucleic Acids Res 36: 2219-2229.
    • (2008) Nucleic Acids Res , vol.36 , pp. 2219-2229
    • Krueger, B.J.1    Jeronimo, C.2    Roy, B.B.3    Bouchard, A.4    Barrandon, C.5
  • 37
    • 0037084028 scopus 로고    scopus 로고
    • Role of the ubiquitin-selective CDC48(UFD1/NPL4)chaperone (segregase) in ERAD of OLE1 and other substrates
    • Braun S, Matuschewski K, Rape M, Thoms S, Jentsch S, (2002) Role of the ubiquitin-selective CDC48(UFD1/NPL4)chaperone (segregase) in ERAD of OLE1 and other substrates. Embo J 21: 615-621.
    • (2002) Embo J , vol.21 , pp. 615-621
    • Braun, S.1    Matuschewski, K.2    Rape, M.3    Thoms, S.4    Jentsch, S.5
  • 38
    • 0036173013 scopus 로고    scopus 로고
    • Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48
    • Jarosch E, Taxis C, Volkwein C, Bordallo J, Finley D, et al. (2002) Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. Nat Cell Biol 4: 134-139.
    • (2002) Nat Cell Biol , vol.4 , pp. 134-139
    • Jarosch, E.1    Taxis, C.2    Volkwein, C.3    Bordallo, J.4    Finley, D.5
  • 39
    • 0036136901 scopus 로고    scopus 로고
    • AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation
    • Rabinovich E, Kerem A, Frohlich KU, Diamant N, Bar-Nun S, (2002) AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Mol Cell Biol 22: 626-634.
    • (2002) Mol Cell Biol , vol.22 , pp. 626-634
    • Rabinovich, E.1    Kerem, A.2    Frohlich, K.U.3    Diamant, N.4    Bar-Nun, S.5
  • 40
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye Y, Meyer HH, Rapoport TA, (2001) The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 414: 652-656.
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 41
    • 0035144438 scopus 로고    scopus 로고
    • Rrb1p, a yeast nuclear WD-repeat protein involved in the regulation of ribosome biosynthesis
    • Iouk TL, Aitchison JD, Maguire S, Wozniak RW, (2001) Rrb1p, a yeast nuclear WD-repeat protein involved in the regulation of ribosome biosynthesis. Mol Cell Biol 21: 1260-1271.
    • (2001) Mol Cell Biol , vol.21 , pp. 1260-1271
    • Iouk, T.L.1    Aitchison, J.D.2    Maguire, S.3    Wozniak, R.W.4
  • 42
    • 84871462256 scopus 로고    scopus 로고
    • Calmodulin methyltransferase is an evolutionarily conserved enzyme that trimethylates Lys-115 in calmodulin
    • Magnani R, Dirk LM, Trievel RC, Houtz RL, (2010) Calmodulin methyltransferase is an evolutionarily conserved enzyme that trimethylates Lys-115 in calmodulin. Nat Commun 1: 43.
    • (2010) Nat Commun , vol.1 , pp. 43
    • Magnani, R.1    Dirk, L.M.2    Trievel, R.C.3    Houtz, R.L.4
  • 43
    • 0942276237 scopus 로고    scopus 로고
    • Differentiation between peptides containing acetylated or tri-methylated lysines by mass spectrometry: an application for determining lysine 9 acetylation and methylation of histone H3
    • Zhang K, Yau PM, Chandrasekhar B, New R, Kondrat R, et al. (2004) Differentiation between peptides containing acetylated or tri-methylated lysines by mass spectrometry: an application for determining lysine 9 acetylation and methylation of histone H3. Proteomics 4: 1-10.
    • (2004) Proteomics , vol.4 , pp. 1-10
    • Zhang, K.1    Yau, P.M.2    Chandrasekhar, B.3    New, R.4    Kondrat, R.5
  • 44
    • 0035846546 scopus 로고    scopus 로고
    • Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln
    • Meister G, Eggert C, Buhler D, Brahms H, Kambach C, et al. (2001) Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln. Curr Biol 11: 1990-1994.
    • (2001) Curr Biol , vol.11 , pp. 1990-1994
    • Meister, G.1    Eggert, C.2    Buhler, D.3    Brahms, H.4    Kambach, C.5
  • 45
    • 52649138958 scopus 로고    scopus 로고
    • UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnover
    • Alexandru G, Graumann J, Smith GT, Kolawa NJ, Fang R, et al. (2008) UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnover. Cell 134: 804-816.
    • (2008) Cell , vol.134 , pp. 804-816
    • Alexandru, G.1    Graumann, J.2    Smith, G.T.3    Kolawa, N.J.4    Fang, R.5
  • 46
    • 84857464993 scopus 로고    scopus 로고
    • The ubiquitin regulatory X (UBX) domain-containing protein TUG regulates the p97 ATPase and resides at the endoplasmic reticulum-golgi intermediate compartment
    • Orme CM, Bogan JS, (2012) The ubiquitin regulatory X (UBX) domain-containing protein TUG regulates the p97 ATPase and resides at the endoplasmic reticulum-golgi intermediate compartment. J Biol Chem 287: 6679-6692.
    • (2012) J Biol Chem , vol.287 , pp. 6679-6692
    • Orme, C.M.1    Bogan, J.S.2
  • 48
    • 1842483843 scopus 로고    scopus 로고
    • Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein
    • Watts GD, Wymer J, Kovach MJ, Mehta SG, Mumm S, et al. (2004) Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein. Nat Genet 36: 377-381.
    • (2004) Nat Genet , vol.36 , pp. 377-381
    • Watts, G.D.1    Wymer, J.2    Kovach, M.J.3    Mehta, S.G.4    Mumm, S.5
  • 49
    • 80055070959 scopus 로고    scopus 로고
    • The structural and functional basis of the p97/valosin-containing protein (VCP)-interacting motif (VIM): mutually exclusive binding of cofactors to the N-terminal domain of p97
    • Hanzelmann P, Schindelin H, (2011) The structural and functional basis of the p97/valosin-containing protein (VCP)-interacting motif (VIM): mutually exclusive binding of cofactors to the N-terminal domain of p97. J Biol Chem 286: 38679-38690.
    • (2011) J Biol Chem , vol.286 , pp. 38679-38690
    • Hanzelmann, P.1    Schindelin, H.2
  • 50
    • 49249130739 scopus 로고    scopus 로고
    • UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97
    • Schuberth C, Buchberger A, (2008) UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97. Cell Mol Life Sci 65: 2360-2371.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 2360-2371
    • Schuberth, C.1    Buchberger, A.2
  • 52
    • 0041856469 scopus 로고    scopus 로고
    • D1 ring is stable and nucleotide-independent, whereas D2 ring undergoes major conformational changes during the ATPase cycle of p97-VCP
    • Wang Q, Song C, Yang X, Li CC, (2003) D1 ring is stable and nucleotide-independent, whereas D2 ring undergoes major conformational changes during the ATPase cycle of p97-VCP. J Biol Chem 278: 32784-32793.
    • (2003) J Biol Chem , vol.278 , pp. 32784-32793
    • Wang, Q.1    Song, C.2    Yang, X.3    Li, C.C.4
  • 53
    • 0742323006 scopus 로고    scopus 로고
    • Distinct roles for the AAA ATPases NSF and p97 in the secretory pathway
    • Dalal S, Rosser MF, Cyr DM, Hanson PI, (2004) Distinct roles for the AAA ATPases NSF and p97 in the secretory pathway. Mol Biol Cell 15: 637-648.
    • (2004) Mol Biol Cell , vol.15 , pp. 637-648
    • Dalal, S.1    Rosser, M.F.2    Cyr, D.M.3    Hanson, P.I.4
  • 54
    • 0021252067 scopus 로고
    • Arsenite-induced changes in methylation of the 70,000 dalton heat shock proteins in chicken embryo fibroblasts
    • Wang C, Lazarides E, (1984) Arsenite-induced changes in methylation of the 70,000 dalton heat shock proteins in chicken embryo fibroblasts. Biochem Biophys Res Commun 119: 735-743.
    • (1984) Biochem Biophys Res Commun , vol.119 , pp. 735-743
    • Wang, C.1    Lazarides, E.2
  • 55
    • 0026649471 scopus 로고
    • Methylations of 70,000-Da heat shock proteins in 3T3 cells: alterations by arsenite treatment, by different stages of growth and by virus transformation
    • Wang C, Lin JM, Lazarides E, (1992) Methylations of 70,000-Da heat shock proteins in 3T3 cells: alterations by arsenite treatment, by different stages of growth and by virus transformation. Arch Biochem Biophys 297: 169-175.
    • (1992) Arch Biochem Biophys , vol.297 , pp. 169-175
    • Wang, C.1    Lin, J.M.2    Lazarides, E.3
  • 56
    • 24744466925 scopus 로고    scopus 로고
    • Akt-mediated valosin-containing protein 97 phosphorylation regulates its association with ubiquitinated proteins
    • Klein JB, Barati MT, Wu R, Gozal D, Sachleben LR Jr, et al. (2005) Akt-mediated valosin-containing protein 97 phosphorylation regulates its association with ubiquitinated proteins. J Biol Chem 280: 31870-31881.
    • (2005) J Biol Chem , vol.280 , pp. 31870-31881
    • Klein, J.B.1    Barati, M.T.2    Wu, R.3    Gozal, D.4    Sachleben Jr., L.R.5
  • 57
    • 77954379485 scopus 로고    scopus 로고
    • Valosin-containing protein (VCP) in novel feedback machinery between abnormal protein accumulation and transcriptional suppression
    • Koike M, Fukushi J, Ichinohe Y, Higashimae N, Fujishiro M, et al. (2010) Valosin-containing protein (VCP) in novel feedback machinery between abnormal protein accumulation and transcriptional suppression. J Biol Chem 285: 21736-21749.
    • (2010) J Biol Chem , vol.285 , pp. 21736-21749
    • Koike, M.1    Fukushi, J.2    Ichinohe, Y.3    Higashimae, N.4    Fujishiro, M.5
  • 58
    • 50249121223 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of ATPase p97 regulates its activity during ERAD
    • Li G, Zhao G, Schindelin H, Lennarz WJ, (2008) Tyrosine phosphorylation of ATPase p97 regulates its activity during ERAD. Biochem Biophys Res Commun 375: 247-251.
    • (2008) Biochem Biophys Res Commun , vol.375 , pp. 247-251
    • Li, G.1    Zhao, G.2    Schindelin, H.3    Lennarz, W.J.4
  • 59
    • 24744434431 scopus 로고    scopus 로고
    • Valosin-containing protein phosphorylation at Ser784 in response to DNA damage
    • Livingstone M, Ruan H, Weiner J, Clauser KR, Strack P, et al. (2005) Valosin-containing protein phosphorylation at Ser784 in response to DNA damage. Cancer Res 65: 7533-7540.
    • (2005) Cancer Res , vol.65 , pp. 7533-7540
    • Livingstone, M.1    Ruan, H.2    Weiner, J.3    Clauser, K.R.4    Strack, P.5
  • 60
    • 63349112395 scopus 로고    scopus 로고
    • p97/valosin-containing protein (VCP) is highly modulated by phosphorylation and acetylation
    • Mori-Konya C, Kato N, Maeda R, Yasuda K, Higashimae N, et al. (2009) p97/valosin-containing protein (VCP) is highly modulated by phosphorylation and acetylation. Genes Cells 14: 483-497.
    • (2009) Genes Cells , vol.14 , pp. 483-497
    • Mori-Konya, C.1    Kato, N.2    Maeda, R.3    Yasuda, K.4    Higashimae, N.5
  • 61
    • 68949098348 scopus 로고    scopus 로고
    • Hereditary inclusion body myopathy-linked p97/VCP mutations in the NH2 domain and the D1 ring modulate p97/VCP ATPase activity and D2 ring conformation
    • Halawani D, LeBlanc AC, Rouiller I, Michnick SW, Servant MJ, et al. (2009) Hereditary inclusion body myopathy-linked p97/VCP mutations in the NH2 domain and the D1 ring modulate p97/VCP ATPase activity and D2 ring conformation. Mol Cell Biol 29: 4484-4494.
    • (2009) Mol Cell Biol , vol.29 , pp. 4484-4494
    • Halawani, D.1    LeBlanc, A.C.2    Rouiller, I.3    Michnick, S.W.4    Servant, M.J.5
  • 62
    • 77954724848 scopus 로고    scopus 로고
    • Enhanced ATPase activities as a primary defect of mutant valosin-containing proteins that cause inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia
    • Manno A, Noguchi M, Fukushi J, Motohashi Y, Kakizuka A, (2010) Enhanced ATPase activities as a primary defect of mutant valosin-containing proteins that cause inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia. Genes Cells 15: 911-922.
    • (2010) Genes Cells , vol.15 , pp. 911-922
    • Manno, A.1    Noguchi, M.2    Fukushi, J.3    Motohashi, Y.4    Kakizuka, A.5
  • 63
    • 0024571620 scopus 로고
    • KIN, a mammalian nuclear protein immunologically related to E. coli RecA protein
    • Angulo JF, Moreau PL, Maunoury R, Laporte J, Hill AM, et al. (1989) KIN, a mammalian nuclear protein immunologically related to E. coli RecA protein. Mutat Res 217: 123-134.
    • (1989) Mutat Res , vol.217 , pp. 123-134
    • Angulo, J.F.1    Moreau, P.L.2    Maunoury, R.3    Laporte, J.4    Hill, A.M.5
  • 64
    • 0037598686 scopus 로고    scopus 로고
    • Participation of kin17 protein in replication factories and in other DNA transactions mediated by high molecular weight nuclear complexes
    • Biard DS, Miccoli L, Despras E, Harper F, Pichard E, et al. (2003) Participation of kin17 protein in replication factories and in other DNA transactions mediated by high molecular weight nuclear complexes. Mol Cancer Res 1: 519-531.
    • (2003) Mol Cancer Res , vol.1 , pp. 519-531
    • Biard, D.S.1    Miccoli, L.2    Despras, E.3    Harper, F.4    Pichard, E.5
  • 65
    • 0033863436 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the human KIN17 cDNA encoding a component of the UVC response that is conserved among metazoans
    • Kannouche P, Mauffrey P, Pinon-Lataillade G, Mattei MG, Sarasin A, et al. (2000) Molecular cloning and characterization of the human KIN17 cDNA encoding a component of the UVC response that is conserved among metazoans. Carcinogenesis 21: 1701-1710.
    • (2000) Carcinogenesis , vol.21 , pp. 1701-1710
    • Kannouche, P.1    Mauffrey, P.2    Pinon-Lataillade, G.3    Mattei, M.G.4    Sarasin, A.5
  • 66
    • 17644425300 scopus 로고    scopus 로고
    • The human stress-activated protein kin17 belongs to the multiprotein DNA replication complex and associates in vivo with mammalian replication origins
    • Miccoli L, Frouin I, Novac O, Di Paola D, Harper F, et al. (2005) The human stress-activated protein kin17 belongs to the multiprotein DNA replication complex and associates in vivo with mammalian replication origins. Mol Cell Biol 25: 3814-3830.
    • (2005) Mol Cell Biol , vol.25 , pp. 3814-3830
    • Miccoli, L.1    Frouin, I.2    Novac, O.3    Di Paola, D.4    Harper, F.5
  • 67
    • 0037073946 scopus 로고    scopus 로고
    • Small nuclear ribonucleoprotein remodeling during catalytic activation of the spliceosome
    • Makarov EM, Makarova OV, Urlaub H, Gentzel M, Will CL, et al. (2002) Small nuclear ribonucleoprotein remodeling during catalytic activation of the spliceosome. Science 298: 2205-2208.
    • (2002) Science , vol.298 , pp. 2205-2208
    • Makarov, E.M.1    Makarova, O.V.2    Urlaub, H.3    Gentzel, M.4    Will, C.L.5
  • 68
    • 0036674269 scopus 로고    scopus 로고
    • Large-scale proteomic analysis of the human spliceosome
    • Rappsilber J, Ryder U, Lamond AI, Mann M, (2002) Large-scale proteomic analysis of the human spliceosome. Genome Res 12: 1231-1245.
    • (2002) Genome Res , vol.12 , pp. 1231-1245
    • Rappsilber, J.1    Ryder, U.2    Lamond, A.I.3    Mann, M.4
  • 69
    • 84856290619 scopus 로고    scopus 로고
    • Smyd2 controls cytoplasmic lysine methylation of Hsp90 and myofilament organization
    • Donlin LT, Andresen C, Just S, Rudensky E, Pappas CT, et al. (2012) Smyd2 controls cytoplasmic lysine methylation of Hsp90 and myofilament organization. Genes Dev 26: 114-119.
    • (2012) Genes Dev , vol.26 , pp. 114-119
    • Donlin, L.T.1    Andresen, C.2    Just, S.3    Rudensky, E.4    Pappas, C.T.5
  • 70
    • 4444281106 scopus 로고    scopus 로고
    • Sequential Peptide Affinity (SPA) system for the identification of mammalian and bacterial protein complexes
    • Zeghouf M, Li J, Butland G, Borkowska A, Canadien V, et al. (2004) Sequential Peptide Affinity (SPA) system for the identification of mammalian and bacterial protein complexes. J Proteome Res 3: 463-468.
    • (2004) J Proteome Res , vol.3 , pp. 463-468
    • Zeghouf, M.1    Li, J.2    Butland, G.3    Borkowska, A.4    Canadien, V.5
  • 71
    • 0034841844 scopus 로고    scopus 로고
    • The tandem affinity purification (TAP) method: a general procedure of protein complex purification
    • Puig O, Caspary F, Rigaut G, Rutz B, Bouveret E, et al. (2001) The tandem affinity purification (TAP) method: a general procedure of protein complex purification. Methods 24: 218-229.
    • (2001) Methods , vol.24 , pp. 218-229
    • Puig, O.1    Caspary, F.2    Rigaut, G.3    Rutz, B.4    Bouveret, E.5
  • 72
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut G, Shevchenko A, Rutz B, Wilm M, Mann M, et al. (1999) A generic protein purification method for protein complex characterization and proteome exploration. Nat Biotechnol 17: 1030-1032.
    • (1999) Nat Biotechnol , vol.17 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5
  • 74
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins DN, Pappin DJ, Creasy DM, Cottrell JS, (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20: 3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 75
    • 33847068262 scopus 로고    scopus 로고
    • Methylation of Smad6 by protein arginine N-methyltransferase 1
    • Inamitsu M, Itoh S, Hellman U, Ten Dijke P, Kato M, (2006) Methylation of Smad6 by protein arginine N-methyltransferase 1. FEBS Lett 580: 6603-6611.
    • (2006) FEBS Lett , vol.580 , pp. 6603-6611
    • Inamitsu, M.1    Itoh, S.2    Hellman, U.3    Ten Dijke, P.4    Kato, M.5
  • 76
    • 0032533881 scopus 로고    scopus 로고
    • Ligand-independent recruitment of steroid receptor coactivators to estrogen receptor by cyclin D1
    • Zwijsen RM, Buckle RS, Hijmans EM, Loomans CJ, Bernards R, (1998) Ligand-independent recruitment of steroid receptor coactivators to estrogen receptor by cyclin D1. Genes Dev 12: 3488-3498.
    • (1998) Genes Dev , vol.12 , pp. 3488-3498
    • Zwijsen, R.M.1    Buckle, R.S.2    Hijmans, E.M.3    Loomans, C.J.4    Bernards, R.5
  • 80
    • 0023375195 scopus 로고
    • The neighbor-joining method: a new method for reconstructing phylogenetic trees
    • Saitou N, Nei M, (1987) The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4: 406-425.
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 81
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • Henikoff S, Henikoff JG, (1992) Amino acid substitution matrices from protein blocks. Proc Natl Acad Sci U S A 89: 10915-10919.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 10915-10919
    • Henikoff, S.1    Henikoff, J.G.2


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