메뉴 건너뛰기




Volumn 567, Issue 2, 2015, Pages 103-131

The biological functions of Naa10 - From amino-terminal acetylation to human disease

Author keywords

Acetyltransferases; Amino terminal acetylation; Ard1; Enzymology; NAA10; NAA15; NAA50; Ogden syndrome; Proteins; Proteomics

Indexed keywords

CYCLIN D1; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; ISOPROTEIN; NAA10 PROTEIN; NAA15 PROTEIN; NAA16 PROTEIN; NAA50 PROTEIN; NATA PROTEIN; PROTEASOME; PROTEIN; UNCLASSIFIED DRUG; NAA10 PROTEIN, HUMAN; PEPTIDE ALPHA N ACETYLTRANSFERASE A; PEPTIDE ALPHA N ACETYLTRANSFERASE E;

EID: 84937635572     PISSN: 03781119     EISSN: 18790038     Source Type: Journal    
DOI: 10.1016/j.gene.2015.04.085     Document Type: Review
Times cited : (72)

References (319)
  • 1
    • 84866339835 scopus 로고    scopus 로고
    • Synergistic and selective cancer cell killing mediated by the oncolytic adenoviral mutant Adδδ and dietary phytochemicals in prostate cancer models
    • Adam V., Ekblad M., Sweeney K., Müller H., Busch K.H., Johnsen C.T., Kang N.R., Lemoine N.R., Halldén G. Synergistic and selective cancer cell killing mediated by the oncolytic adenoviral mutant Adδδ and dietary phytochemicals in prostate cancer models. Hum. Gene Ther. 2012, 23:1003-1015.
    • (2012) Hum. Gene Ther. , vol.23 , pp. 1003-1015
    • Adam, V.1    Ekblad, M.2    Sweeney, K.3    Müller, H.4    Busch, K.H.5    Johnsen, C.T.6    Kang, N.R.7    Lemoine, N.R.8    Halldén, G.9
  • 3
    • 84878941023 scopus 로고    scopus 로고
    • Signal recognition particle: an essential protein-targeting machine
    • Akopian D., Shen K., Zhang X., Shan S.O. Signal recognition particle: an essential protein-targeting machine. Annu. Rev. Biochem. 2013, 82:693-721.
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 693-721
    • Akopian, D.1    Shen, K.2    Zhang, X.3    Shan, S.O.4
  • 4
    • 84876175152 scopus 로고    scopus 로고
    • N-terminal acetylation by NatC is not a general determinant for substrate subcellular localization in Saccharomyces cerevisiae
    • Aksnes H., Osberg C., Arnesen T. N-terminal acetylation by NatC is not a general determinant for substrate subcellular localization in Saccharomyces cerevisiae. PLoS One 2013, 8:e61012.
    • (2013) PLoS One , vol.8 , pp. e61012
    • Aksnes, H.1    Osberg, C.2    Arnesen, T.3
  • 5
    • 84925251881 scopus 로고    scopus 로고
    • Molecular, cellular, and physiological significance of N-terminal acetylation
    • Aksnes H., Hole K., Arnesen T. Molecular, cellular, and physiological significance of N-terminal acetylation. Int. Rev. Cell Mol. Biol. 2015, 316:267-305.
    • (2015) Int. Rev. Cell Mol. Biol. , vol.316 , pp. 267-305
    • Aksnes, H.1    Hole, K.2    Arnesen, T.3
  • 8
    • 84924437783 scopus 로고    scopus 로고
    • Biophysical characterization of α-synuclein and its controversial structure
    • Alderson T.R., Markley J.L. Biophysical characterization of α-synuclein and its controversial structure. Intrinsically Disord. Proteins 2013, 1:18-39.
    • (2013) Intrinsically Disord. Proteins , vol.1 , pp. 18-39
    • Alderson, T.R.1    Markley, J.L.2
  • 10
    • 0025900189 scopus 로고
    • Modifiers of position effect are shared between telomeric and silent mating-type loci in S. cerevisiae
    • Aparicio O.M., Billington B.L., Gottschling D.E. Modifiers of position effect are shared between telomeric and silent mating-type loci in S. cerevisiae. Cell 1991, 66:1279-1287.
    • (1991) Cell , vol.66 , pp. 1279-1287
    • Aparicio, O.M.1    Billington, B.L.2    Gottschling, D.E.3
  • 12
    • 0033168717 scopus 로고    scopus 로고
    • Eukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N-terminal acetylation and promote particle assembly
    • Arendt C.S., Hochstrasser M. Eukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N-terminal acetylation and promote particle assembly. EMBO J. 1999, 18:3575-3585.
    • (1999) EMBO J. , vol.18 , pp. 3575-3585
    • Arendt, C.S.1    Hochstrasser, M.2
  • 13
    • 81555212272 scopus 로고    scopus 로고
    • Structural basis of silencing: Sir3 BAH domain in complex with a nucleosome at 3.0Å resolution
    • Armache K.J., Garlick J.D., Canzio D., Narlikar G.J., Kingston R.E. Structural basis of silencing: Sir3 BAH domain in complex with a nucleosome at 3.0Å resolution. Science 2011, 334:977-982.
    • (2011) Science , vol.334 , pp. 977-982
    • Armache, K.J.1    Garlick, J.D.2    Canzio, D.3    Narlikar, G.J.4    Kingston, R.E.5
  • 15
    • 79958039807 scopus 로고    scopus 로고
    • Towards a functional understanding of protein N-terminal acetylation
    • Arnesen T. Towards a functional understanding of protein N-terminal acetylation. PLoS Biol. 2011, 9:e1001074.
    • (2011) PLoS Biol. , vol.9 , pp. e1001074
    • Arnesen, T.1
  • 17
    • 27744450043 scopus 로고    scopus 로고
    • Interaction between HIF-1 alpha (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1 alpha
    • Arnesen T., Kong X., Evjenth R., Gromyko D., Varhaug J.E., Lin Z., Sang N., Caro J., Lillehaug J.R. Interaction between HIF-1 alpha (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1 alpha. FEBS Lett. 2005, 579:6428-6432.
    • (2005) FEBS Lett. , vol.579 , pp. 6428-6432
    • Arnesen, T.1    Kong, X.2    Evjenth, R.3    Gromyko, D.4    Varhaug, J.E.5    Lin, Z.6    Sang, N.7    Caro, J.8    Lillehaug, J.R.9
  • 18
    • 33645757829 scopus 로고    scopus 로고
    • Cloning and characterization of hNAT5/hSAN: an evolutionarily conserved component of the NatA protein N-alpha-acetyltransferase complex
    • Arnesen T., Anderson D., Torsvik J., Halseth H.B., Varhaug J.E., Lillehaug J.R. Cloning and characterization of hNAT5/hSAN: an evolutionarily conserved component of the NatA protein N-alpha-acetyltransferase complex. Gene 2006, 371:291-295.
    • (2006) Gene , vol.371 , pp. 291-295
    • Arnesen, T.1    Anderson, D.2    Torsvik, J.3    Halseth, H.B.4    Varhaug, J.E.5    Lillehaug, J.R.6
  • 20
    • 33744971921 scopus 로고    scopus 로고
    • Induction of apoptosis in human cells by RNAi-mediated knockdown of hARD1 and NATH, components of the protein N-alpha-acetyltransferase complex
    • Arnesen T., Gromyko D., Pendino F., Ryningen A., Varhaug J.E., Lillehaug J.R. Induction of apoptosis in human cells by RNAi-mediated knockdown of hARD1 and NATH, components of the protein N-alpha-acetyltransferase complex. Oncogene 2006, 25:4350-4360.
    • (2006) Oncogene , vol.25 , pp. 4350-4360
    • Arnesen, T.1    Gromyko, D.2    Pendino, F.3    Ryningen, A.4    Varhaug, J.E.5    Lillehaug, J.R.6
  • 24
    • 0033601196 scopus 로고    scopus 로고
    • The action of N-terminal acetyltransferases on yeast ribosomal proteins
    • Arnold R.J., Polevoda B., Reilly J.P., Sherman F. The action of N-terminal acetyltransferases on yeast ribosomal proteins. J. Biol. Chem. 1999, 274:37035-37040.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37035-37040
    • Arnold, R.J.1    Polevoda, B.2    Reilly, J.P.3    Sherman, F.4
  • 25
    • 17044379092 scopus 로고    scopus 로고
    • Interaction of N-terminal acetyltransferase with the cytoplasmic domain of beta-amyloid precursor protein and its effect on A beta secretion
    • Asaumi M., Iijima K., Sumioka A., Iijima-Ando K., Kirino Y., Nakaya T., Suzuki T. Interaction of N-terminal acetyltransferase with the cytoplasmic domain of beta-amyloid precursor protein and its effect on A beta secretion. J. Biochem. 2005, 137:147-155.
    • (2005) J. Biochem. , vol.137 , pp. 147-155
    • Asaumi, M.1    Iijima, K.2    Sumioka, A.3    Iijima-Ando, K.4    Kirino, Y.5    Nakaya, T.6    Suzuki, T.7
  • 26
    • 22444438012 scopus 로고    scopus 로고
    • N-terminal acetylation and protonation of individual hemoglobin subunits: position-dependent effects on tetramer strength and cooperativity
    • Ashiuchi M., Yagami T., Willey R.J., Padovan J.C., Chait B.T., Popowicz A., Manning L.R., Manning J.M. N-terminal acetylation and protonation of individual hemoglobin subunits: position-dependent effects on tetramer strength and cooperativity. Protein Sci. 2005, 14:1458-1471.
    • (2005) Protein Sci. , vol.14 , pp. 1458-1471
    • Ashiuchi, M.1    Yagami, T.2    Willey, R.J.3    Padovan, J.C.4    Chait, B.T.5    Popowicz, A.6    Manning, L.R.7    Manning, J.M.8
  • 27
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair A., Finley D., Varshavsky A. In vivo half-life of a protein is a function of its amino-terminal residue. Science 1986, 234:179-186.
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 29
    • 0028677415 scopus 로고
    • Chemical synthesis and characterisation of rat chaperonin 10: effect of chain length, ions, heat and N-terminal acetylation on unchaperoned folding into its heptameric form
    • Ball H.L., Giuliani P., Lucietto P., Fossati G., Mascagni P. Chemical synthesis and characterisation of rat chaperonin 10: effect of chain length, ions, heat and N-terminal acetylation on unchaperoned folding into its heptameric form. Biomed. Pept. Proteins Nucleic Acids 1994, 1:39-44.
    • (1994) Biomed. Pept. Proteins Nucleic Acids , vol.1 , pp. 39-44
    • Ball, H.L.1    Giuliani, P.2    Lucietto, P.3    Fossati, G.4    Mascagni, P.5
  • 30
    • 84904976220 scopus 로고    scopus 로고
    • N-alpha-acetylation of α-synuclein increases its helical folding propensity, GM1 binding specificity and resistance to aggregation
    • Bartels T., Kim N.C., Luth E.S., Selkoe D.J. N-alpha-acetylation of α-synuclein increases its helical folding propensity, GM1 binding specificity and resistance to aggregation. PLoS One 2014, 9:e103727.
    • (2014) PLoS One , vol.9 , pp. e103727
    • Bartels, T.1    Kim, N.C.2    Luth, E.S.3    Selkoe, D.J.4
  • 31
    • 2342546616 scopus 로고    scopus 로고
    • Targeting of the Arf-like GTPase Arl3p to the Golgi requires N-terminal acetylation and the membrane protein Sys1p
    • Behnia R., Panic B., Whyte J.R., Munro S. Targeting of the Arf-like GTPase Arl3p to the Golgi requires N-terminal acetylation and the membrane protein Sys1p. Nat. Cell Biol. 2004, 6:405-413.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 405-413
    • Behnia, R.1    Panic, B.2    Whyte, J.R.3    Munro, S.4
  • 32
    • 0028832366 scopus 로고
    • The multidomain structure of Orc1p reveals similarity to regulators of DNA replication and transcriptional silencing
    • Bell S.P., Mitchell J., Leber J., Kobayashi R., Stillman B. The multidomain structure of Orc1p reveals similarity to regulators of DNA replication and transcriptional silencing. Cell 1995, 83:563-568.
    • (1995) Cell , vol.83 , pp. 563-568
    • Bell, S.P.1    Mitchell, J.2    Leber, J.3    Kobayashi, R.4    Stillman, B.5
  • 34
    • 4744371446 scopus 로고    scopus 로고
    • The tumor suppressor protein p16(INK4a) and the human papillomavirus oncoprotein-58 E7 are naturally occurring lysine-less proteins that are degraded by the ubiquitin system. Direct evidence for ubiquitination at the N-terminal residue
    • Ben-Saadon R., Fajerman I., Ziv T., Hellman U., Schwartz A.L., Ciechanover A. The tumor suppressor protein p16(INK4a) and the human papillomavirus oncoprotein-58 E7 are naturally occurring lysine-less proteins that are degraded by the ubiquitin system. Direct evidence for ubiquitination at the N-terminal residue. J. Biol. Chem. 2004, 279:41414-41421.
    • (2004) J. Biol. Chem. , vol.279 , pp. 41414-41421
    • Ben-Saadon, R.1    Fajerman, I.2    Ziv, T.3    Hellman, U.4    Schwartz, A.L.5    Ciechanover, A.6
  • 35
    • 84863097876 scopus 로고    scopus 로고
    • Selective N-terminal fluorescent labeling of proteins using 4-chloro-7-nitrobenzofurazan: a method to distinguish protein N-terminal acetylation
    • Bernal-Perez L.F., Prokai L., Ryu Y. Selective N-terminal fluorescent labeling of proteins using 4-chloro-7-nitrobenzofurazan: a method to distinguish protein N-terminal acetylation. Anal. Biochem. 2012, 428:13-15.
    • (2012) Anal. Biochem. , vol.428 , pp. 13-15
    • Bernal-Perez, L.F.1    Prokai, L.2    Ryu, Y.3
  • 38
    • 84859515208 scopus 로고    scopus 로고
    • Comparative large scale characterization of plant versus mammal proteins reveals similar and idiosyncratic N-α-acetylation features
    • (M111.015131)
    • Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C. Comparative large scale characterization of plant versus mammal proteins reveals similar and idiosyncratic N-α-acetylation features. Mol. Cell. Proteomics 2012, 11. (M111.015131).
    • (2012) Mol. Cell. Proteomics , vol.11
    • Bienvenut, W.V.1    Sumpton, D.2    Martinez, A.3    Lilla, S.4    Espagne, C.5    Meinnel, T.6    Giglione, C.7
  • 39
    • 24744460523 scopus 로고    scopus 로고
    • Arrest-defective-1 protein, an acetyltransferase, does not alter stability of hypoxia-inducible factor (HIF)-1alpha and is not induced by hypoxia or HIF
    • Bilton R., Mazure N., Trottier E., Hattab M., Déry M.A., Richard D.E., Pouysségur J., Brahimi-Horn M.C. Arrest-defective-1 protein, an acetyltransferase, does not alter stability of hypoxia-inducible factor (HIF)-1alpha and is not induced by hypoxia or HIF. J. Biol. Chem. 2005, 280:31132-31140.
    • (2005) J. Biol. Chem. , vol.280 , pp. 31132-31140
    • Bilton, R.1    Mazure, N.2    Trottier, E.3    Hattab, M.4    Déry, M.A.5    Richard, D.E.6    Pouysségur, J.7    Brahimi-Horn, M.C.8
  • 42
    • 4644250687 scopus 로고    scopus 로고
    • The stress-induced Tfs1p requires NatB-mediated acetylation to inhibit carboxypeptidase Y and to regulate the protein kinase A pathway
    • Caesar R., Blomberg A. The stress-induced Tfs1p requires NatB-mediated acetylation to inhibit carboxypeptidase Y and to regulate the protein kinase A pathway. J. Biol. Chem. 2004, 279:38532-38543.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38532-38543
    • Caesar, R.1    Blomberg, A.2
  • 43
    • 32944479331 scopus 로고    scopus 로고
    • Physiological importance and identification of novel targets for the N-terminal acetyltransferase NatB
    • Caesar R., Warringer J., Blomberg A. Physiological importance and identification of novel targets for the N-terminal acetyltransferase NatB. Eukaryot. Cell 2006, 5:368-378.
    • (2006) Eukaryot. Cell , vol.5 , pp. 368-378
    • Caesar, R.1    Warringer, J.2    Blomberg, A.3
  • 44
    • 79952435349 scopus 로고    scopus 로고
    • Activation and function of the MAPKs and their substrates, the MAPK-activated protein kinases
    • Cargnello M., Roux P.P. Activation and function of the MAPKs and their substrates, the MAPK-activated protein kinases. Microbiol. Mol. Biol. Rev. 2011, 75:50-83.
    • (2011) Microbiol. Mol. Biol. Rev. , vol.75 , pp. 50-83
    • Cargnello, M.1    Roux, P.P.2
  • 46
    • 84924046259 scopus 로고    scopus 로고
    • Structural basis for substrate-specific acetylation of Nα-acetyltransferase Ard1 from Sulfolobus solfataricus
    • Chang Y.Y., Hsu C.H. Structural basis for substrate-specific acetylation of Nα-acetyltransferase Ard1 from Sulfolobus solfataricus. Sci. Rep. 2015, 5:8673.
    • (2015) Sci. Rep. , vol.5 , pp. 8673
    • Chang, Y.Y.1    Hsu, C.H.2
  • 49
    • 0037048676 scopus 로고    scopus 로고
    • N-terminal acetylation of ectopic recombinant proteins in Escherichia coli
    • Charbaut E., Redeker V., Rossier J., Sobel A. N-terminal acetylation of ectopic recombinant proteins in Escherichia coli. FEBS Lett. 2002, 529:341-345.
    • (2002) FEBS Lett. , vol.529 , pp. 341-345
    • Charbaut, E.1    Redeker, V.2    Rossier, J.3    Sobel, A.4
  • 50
    • 9744227998 scopus 로고    scopus 로고
    • N-acetylation and ubiquitin-independent proteasomal degradation of p21(Cip1)
    • Chen X., Chi Y., Bloecher A., Aebersold R., Clurman B.E., Roberts J.M. N-acetylation and ubiquitin-independent proteasomal degradation of p21(Cip1). Mol. Cell 2004, 16:839-847.
    • (2004) Mol. Cell , vol.16 , pp. 839-847
    • Chen, X.1    Chi, Y.2    Bloecher, A.3    Aebersold, R.4    Clurman, B.E.5    Roberts, J.M.6
  • 51
    • 84908326581 scopus 로고    scopus 로고
    • Daf-31 encodes the catalytic subunit of N alpha-acetyltransferase that regulates Caenorhabditis elegans development, metabolism and adult lifespan
    • Chen D., Zhang J., Minnerly J., Kaul T., Riddle D.L., Jia K. daf-31 encodes the catalytic subunit of N alpha-acetyltransferase that regulates Caenorhabditis elegans development, metabolism and adult lifespan. PLoS Genet. 2014, 10:e1004699.
    • (2014) PLoS Genet. , vol.10 , pp. e1004699
    • Chen, D.1    Zhang, J.2    Minnerly, J.3    Kaul, T.4    Riddle, D.L.5    Jia, K.6
  • 52
    • 79951819919 scopus 로고    scopus 로고
    • A novel acetylation of β-tubulin by San modulates microtubule polymerization via down-regulating tubulin incorporation
    • Chu C.W., Hou F., Zhang J., Phu L., Loktev A.V., Kirkpatrick D.S., Jackson P.K., Zhao Y., Zou H. A novel acetylation of β-tubulin by San modulates microtubule polymerization via down-regulating tubulin incorporation. Mol. Biol. Cell 2011, 22:448-456.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 448-456
    • Chu, C.W.1    Hou, F.2    Zhang, J.3    Phu, L.4    Loktev, A.V.5    Kirkpatrick, D.S.6    Jackson, P.K.7    Zhao, Y.8    Zou, H.9
  • 53
    • 0346059588 scopus 로고    scopus 로고
    • Phorbol ester stimulates the nonhypoxic induction of a novel hypoxia-inducible factor 1alpha isoform: implications for tumor promotion
    • Chun Y.S., Lee K.H., Choi E., Bae S.Y., Yeo E.J., Huang L.E., Kim M.S., Park J.W. Phorbol ester stimulates the nonhypoxic induction of a novel hypoxia-inducible factor 1alpha isoform: implications for tumor promotion. Cancer Res. 2003, 63:8700-8707.
    • (2003) Cancer Res. , vol.63 , pp. 8700-8707
    • Chun, Y.S.1    Lee, K.H.2    Choi, E.3    Bae, S.Y.4    Yeo, E.J.5    Huang, L.E.6    Kim, M.S.7    Park, J.W.8
  • 54
    • 33845663235 scopus 로고    scopus 로고
    • Differential regulation of splicing, localization and stability of mammalian ARD1235 and ARD1225 isoforms
    • Chun K.H., Cho S.J., Choi J.S., Kim S.H., Kim K.W., Lee S.K. Differential regulation of splicing, localization and stability of mammalian ARD1235 and ARD1225 isoforms. Biochem. Biophys. Res. Commun. 2007, 353:18-25.
    • (2007) Biochem. Biophys. Res. Commun. , vol.353 , pp. 18-25
    • Chun, K.H.1    Cho, S.J.2    Choi, J.S.3    Kim, S.H.4    Kim, K.W.5    Lee, S.K.6
  • 55
    • 1442323729 scopus 로고    scopus 로고
    • N-terminal ubiquitination: more protein substrates join in
    • Ciechanover A., Ben-Saadon R. N-terminal ubiquitination: more protein substrates join in. Trends Cell Biol. 2004, 14:103-106.
    • (2004) Trends Cell Biol. , vol.14 , pp. 103-106
    • Ciechanover, A.1    Ben-Saadon, R.2
  • 56
    • 84861986053 scopus 로고    scopus 로고
    • Wnt/β-catenin signaling and disease
    • Clevers H., Nusse R. Wnt/β-catenin signaling and disease. Cell 2012, 149:1192-1205.
    • (2012) Cell , vol.149 , pp. 1192-1205
    • Clevers, H.1    Nusse, R.2
  • 57
    • 77956901465 scopus 로고    scopus 로고
    • The recruitment of acetylated and unacetylated tropomyosin to distinct actin polymers permits the discrete regulation of specific myosins in fission yeast
    • Coulton A.T., East D.A., Galinska-Rakoczy A., Lehman W., Mulvihill D.P. The recruitment of acetylated and unacetylated tropomyosin to distinct actin polymers permits the discrete regulation of specific myosins in fission yeast. J. Cell Sci. 2010, 123:3235-3243.
    • (2010) J. Cell Sci. , vol.123 , pp. 3235-3243
    • Coulton, A.T.1    East, D.A.2    Galinska-Rakoczy, A.3    Lehman, W.4    Mulvihill, D.P.5
  • 58
    • 0018405372 scopus 로고
    • Ribosomal protein modification in Escherichia coli. I. A mutant lacking the N-terminal acetylation of protein S5 exhibits thermosensitivity
    • Cumberlidge A.G., Isono K. Ribosomal protein modification in Escherichia coli. I. A mutant lacking the N-terminal acetylation of protein S5 exhibits thermosensitivity. J. Mol. Biol. 1979, 131:169-189.
    • (1979) J. Mol. Biol. , vol.131 , pp. 169-189
    • Cumberlidge, A.G.1    Isono, K.2
  • 60
    • 0019212095 scopus 로고
    • Influence of N-terminal acetylation and C-terminal proteolysis on the analgesic activity of beta-endorphin
    • Deakin J.F., Doströvsky J.O., Smyth D.G. Influence of N-terminal acetylation and C-terminal proteolysis on the analgesic activity of beta-endorphin. Biochem. J. 1980, 189:501-506.
    • (1980) Biochem. J. , vol.189 , pp. 501-506
    • Deakin, J.F.1    Doströvsky, J.O.2    Smyth, D.G.3
  • 61
    • 79960923840 scopus 로고    scopus 로고
    • Defining the specificity of cotranslationally acting chaperones by systematic analysis of mRNAs associated with ribosome-nascent chain complexes
    • del Alamo M., Hogan D.J., Pechmann S., Albanese V., Brown P.O., Frydman J. Defining the specificity of cotranslationally acting chaperones by systematic analysis of mRNAs associated with ribosome-nascent chain complexes. PLoS Biol. 2011, 9:e1001100.
    • (2011) PLoS Biol. , vol.9 , pp. e1001100
    • del Alamo, M.1    Hogan, D.J.2    Pechmann, S.3    Albanese, V.4    Brown, P.O.5    Frydman, J.6
  • 64
    • 0028289435 scopus 로고
    • Determination of free energies of N-capping in alpha-helices by modification of the Lifson-Roig helix-coil therapy to include N- and C-capping
    • Doig A.J., Chakrabartty A., Klingler T.M., Baldwin R.L. Determination of free energies of N-capping in alpha-helices by modification of the Lifson-Roig helix-coil therapy to include N- and C-capping. Biochemistry 1994, 33:3396-3403.
    • (1994) Biochemistry , vol.33 , pp. 3396-3403
    • Doig, A.J.1    Chakrabartty, A.2    Klingler, T.M.3    Baldwin, R.L.4
  • 67
    • 71449101084 scopus 로고    scopus 로고
    • Human Naa50p (Nat5/San) displays both protein N alpha- and N epsilon-acetyltransferase activity
    • Evjenth R., Hole K., Karlsen O.A., Ziegler M., Arnesen T., Lillehaug J.R. Human Naa50p (Nat5/San) displays both protein N alpha- and N epsilon-acetyltransferase activity. J. Biol. Chem. 2009, 284:31122-31129.
    • (2009) J. Biol. Chem. , vol.284 , pp. 31122-31129
    • Evjenth, R.1    Hole, K.2    Karlsen, O.A.3    Ziegler, M.4    Arnesen, T.5    Lillehaug, J.R.6
  • 68
    • 84858958542 scopus 로고    scopus 로고
    • Human protein N-terminal acetyltransferase hNaa50p (hNAT5/hSAN) follows ordered sequential catalytic mechanism: combined kinetic and NMR study
    • Evjenth R.H., Brenner A.K., Thompson P.R., Arnesen T., Frøystein N., Lillehaug J.R. Human protein N-terminal acetyltransferase hNaa50p (hNAT5/hSAN) follows ordered sequential catalytic mechanism: combined kinetic and NMR study. J. Biol. Chem. 2012, 287:10081-10088.
    • (2012) J. Biol. Chem. , vol.287 , pp. 10081-10088
    • Evjenth, R.H.1    Brenner, A.K.2    Thompson, P.R.3    Arnesen, T.4    Frøystein, N.5    Lillehaug, J.R.6
  • 69
    • 0024506404 scopus 로고
    • Further studies of the helix dipole model: effects of a free alpha-NH3+ or alpha-COO- group on helix stability
    • Fairman R., Shoemaker K.R., York E.J., Stewart J.M., Baldwin R.L. Further studies of the helix dipole model: effects of a free alpha-NH3+ or alpha-COO- group on helix stability. Proteins 1989, 5:1-7.
    • (1989) Proteins , vol.5 , pp. 1-7
    • Fairman, R.1    Shoemaker, K.R.2    York, E.J.3    Stewart, J.M.4    Baldwin, R.L.5
  • 71
    • 33744963443 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors repress the transactivation potential of hypoxia-inducible factors independently of direct acetylation of HIF-alpha
    • Fath D.M., Kong X., Liang D., Lin Z., Chou A., Jiang Y., Fang J., Caro J., Sang N. Histone deacetylase inhibitors repress the transactivation potential of hypoxia-inducible factors independently of direct acetylation of HIF-alpha. J. Biol. Chem. 2006, 281:13612-13619.
    • (2006) J. Biol. Chem. , vol.281 , pp. 13612-13619
    • Fath, D.M.1    Kong, X.2    Liang, D.3    Lin, Z.4    Chou, A.5    Jiang, Y.6    Fang, J.7    Caro, J.8    Sang, N.9
  • 72
    • 84865249504 scopus 로고    scopus 로고
    • Characterization of semisynthetic and naturally Nα-acetylated α-synuclein in vitro and in intact cells: implications for aggregation and cellular properties of α-synuclein
    • Fauvet B., Fares M.B., Samuel F., Dikiy I., Tandon A., Eliezer D., Lashuel H.A. Characterization of semisynthetic and naturally Nα-acetylated α-synuclein in vitro and in intact cells: implications for aggregation and cellular properties of α-synuclein. J. Biol. Chem. 2012, 287:28243-28262.
    • (2012) J. Biol. Chem. , vol.287 , pp. 28243-28262
    • Fauvet, B.1    Fares, M.B.2    Samuel, F.3    Dikiy, I.4    Tandon, A.5    Eliezer, D.6    Lashuel, H.A.7
  • 74
    • 50049116926 scopus 로고    scopus 로고
    • C. elegans dauer formation and the molecular basis of plasticity
    • Fielenbach N., Antebi A. C. elegans dauer formation and the molecular basis of plasticity. Genes Dev. 2008, 22:2149-2165.
    • (2008) Genes Dev. , vol.22 , pp. 2149-2165
    • Fielenbach, N.1    Antebi, A.2
  • 75
    • 0016285595 scopus 로고
    • TMV coat protein synthesis in vivo: analysis of the N-terminal acetylation
    • Filner B., Marcus A. TMV coat protein synthesis in vivo: analysis of the N-terminal acetylation. Virology 1974, 61:537-546.
    • (1974) Virology , vol.61 , pp. 537-546
    • Filner, B.1    Marcus, A.2
  • 76
    • 20544431636 scopus 로고    scopus 로고
    • Analysis of ARD1 function in hypoxia response using retroviral RNA interference
    • Fisher T.S., Etages S.D., Hayes L., Crimin K., Li B. Analysis of ARD1 function in hypoxia response using retroviral RNA interference. J. Biol. Chem. 2005, 280:17749-17757.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17749-17757
    • Fisher, T.S.1    Etages, S.D.2    Hayes, L.3    Crimin, K.4    Li, B.5
  • 78
    • 79958027934 scopus 로고    scopus 로고
    • N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum
    • Forte G.M., Pool M.R., Stirling C.J. N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum. PLoS Biol. 2011, 9:e1001073.
    • (2011) PLoS Biol. , vol.9 , pp. e1001073
    • Forte, G.M.1    Pool, M.R.2    Stirling, C.J.3
  • 79
    • 1842367918 scopus 로고    scopus 로고
    • The origin recognition complex, SIR1, and the S phase requirement for silencing
    • Fox C.A., Ehrenhofer-Murray A.E., Loo S., Rine J. The origin recognition complex, SIR1, and the S phase requirement for silencing. Science 1997, 276:1547-1551.
    • (1997) Science , vol.276 , pp. 1547-1551
    • Fox, C.A.1    Ehrenhofer-Murray, A.E.2    Loo, S.3    Rine, J.4
  • 83
    • 0141640821 scopus 로고    scopus 로고
    • The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides
    • Gautschi M., Just S., Mun A., Ross S., Rücknagel P., Dubaquié Y., Ehrenhofer-Murray A., Rospert S. The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides. Mol. Cell. Biol. 2003, 23:7403-7414.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7403-7414
    • Gautschi, M.1    Just, S.2    Mun, A.3    Ross, S.4    Rücknagel, P.5    Dubaquié, Y.6    Ehrenhofer-Murray, A.7    Rospert, S.8
  • 84
    • 8644228492 scopus 로고    scopus 로고
    • Dependence of ORC silencing function on NatA-mediated Nalpha acetylation in Saccharomyces cerevisiae
    • Geissenhöner A., Weise C., Ehrenhofer-Murray A.E. Dependence of ORC silencing function on NatA-mediated Nalpha acetylation in Saccharomyces cerevisiae. Mol. Cell. Biol. 2004, 24:10300-10312.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10300-10312
    • Geissenhöner, A.1    Weise, C.2    Ehrenhofer-Murray, A.E.3
  • 85
    • 0034076940 scopus 로고    scopus 로고
    • Tubedown-1, a novel acetyltransferase associated with blood vessel development
    • Gendron R.L., Adams L.C., Paradis H. Tubedown-1, a novel acetyltransferase associated with blood vessel development. Dev. Dyn. 2000, 218:300-315.
    • (2000) Dev. Dyn. , vol.218 , pp. 300-315
    • Gendron, R.L.1    Adams, L.C.2    Paradis, H.3
  • 86
    • 33344467064 scopus 로고    scopus 로고
    • Tubedown-1 (Tbdn-1) suppression in oxygen-induced retinopathy and in retinopathy of prematurity
    • Gendron R.L., Good W.V., Miskiewicz E., Tucker S., Phelps D.L., Paradis H. Tubedown-1 (Tbdn-1) suppression in oxygen-induced retinopathy and in retinopathy of prematurity. Mol. Vis. 2006, 12:108-116.
    • (2006) Mol. Vis. , vol.12 , pp. 108-116
    • Gendron, R.L.1    Good, W.V.2    Miskiewicz, E.3    Tucker, S.4    Phelps, D.L.5    Paradis, H.6
  • 89
    • 84888604134 scopus 로고    scopus 로고
    • Mitochondrial protein acetylation as a cell-intrinsic, evolutionary driver of fat storage: chemical and metabolic logic of acetyl-lysine modifications
    • Ghanta S., Grossmann R.E., Brenner C. Mitochondrial protein acetylation as a cell-intrinsic, evolutionary driver of fat storage: chemical and metabolic logic of acetyl-lysine modifications. Crit. Rev. Biochem. Mol. Biol. 2013, 48:561-574.
    • (2013) Crit. Rev. Biochem. Mol. Biol. , vol.48 , pp. 561-574
    • Ghanta, S.1    Grossmann, R.E.2    Brenner, C.3
  • 90
    • 0034329475 scopus 로고    scopus 로고
    • Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms
    • Giglione C., Serero A., Pierre M., Boisson B., Meinnel T. Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms. EMBO J. 2000, 19:5916-5929.
    • (2000) EMBO J. , vol.19 , pp. 5916-5929
    • Giglione, C.1    Serero, A.2    Pierre, M.3    Boisson, B.4    Meinnel, T.5
  • 91
    • 84937641831 scopus 로고    scopus 로고
    • N-terminal protein modifications: bringing back into play the ribosome
    • (Epub ahead of print)
    • Giglione C., Fieulaine S., Meinnel T. N-terminal protein modifications: bringing back into play the ribosome. Biochimie 2014, (Epub ahead of print).
    • (2014) Biochimie
    • Giglione, C.1    Fieulaine, S.2    Meinnel, T.3
  • 93
    • 44949193693 scopus 로고    scopus 로고
    • Acetylation of L12 increases interactions in the Escherichia coli ribosomal stalk complex
    • Gordiyenko Y., Deroo S., Zhou M., Videler H., Robinson C.V. Acetylation of L12 increases interactions in the Escherichia coli ribosomal stalk complex. J. Mol. Biol. 2008, 380:404-414.
    • (2008) J. Mol. Biol. , vol.380 , pp. 404-414
    • Gordiyenko, Y.1    Deroo, S.2    Zhou, M.3    Videler, H.4    Robinson, C.V.5
  • 94
    • 0028258048 scopus 로고
    • The effect of N-terminal acetylation on the structure of an N-terminal tropomyosin peptide and alpha alpha-tropomyosin
    • Greenfield N.J., Stafford W.F., Hitchcock-DeGregori S.E. The effect of N-terminal acetylation on the structure of an N-terminal tropomyosin peptide and alpha alpha-tropomyosin. Protein Sci. 1994, 3:402-410.
    • (1994) Protein Sci. , vol.3 , pp. 402-410
    • Greenfield, N.J.1    Stafford, W.F.2    Hitchcock-DeGregori, S.E.3
  • 96
    • 77955297697 scopus 로고    scopus 로고
    • Depletion of the human Nα-terminal acetyltransferase A induces p53-dependent apoptosis and p53-independent growth inhibition
    • Gromyko D., Arnesen T., Ryningen A., Varhaug J.E., Lillehaug J.R. Depletion of the human Nα-terminal acetyltransferase A induces p53-dependent apoptosis and p53-independent growth inhibition. Int. J. Cancer 2010, 127:2777-2789.
    • (2010) Int. J. Cancer , vol.127 , pp. 2777-2789
    • Gromyko, D.1    Arnesen, T.2    Ryningen, A.3    Varhaug, J.E.4    Lillehaug, J.R.5
  • 97
    • 84878218006 scopus 로고    scopus 로고
    • NMR structure of calmodulin complexed to an N-terminally acetylated α-synuclein peptide
    • Gruschus J.M., Yap T.L., Pistolesi S., Maltsev A.S., Lee J.C. NMR structure of calmodulin complexed to an N-terminally acetylated α-synuclein peptide. Biochemistry 2013.
    • (2013) Biochemistry
    • Gruschus, J.M.1    Yap, T.L.2    Pistolesi, S.3    Maltsev, A.S.4    Lee, J.C.5
  • 98
    • 0022179562 scopus 로고
    • Crystals of the complex between recombinant N-acetyleglin c and subtilisin. A preliminary characterization
    • Grütter M.G., Märki W., Walliser H.P. Crystals of the complex between recombinant N-acetyleglin c and subtilisin. A preliminary characterization. J. Biol. Chem. 1985, 260:11436-11437.
    • (1985) J. Biol. Chem. , vol.260 , pp. 11436-11437
    • Grütter, M.G.1    Märki, W.2    Walliser, H.P.3
  • 99
    • 84860548726 scopus 로고    scopus 로고
    • Mating-type genes and MAT switching in Saccharomyces cerevisiae
    • Haber J.E. Mating-type genes and MAT switching in Saccharomyces cerevisiae. Genetics 2012, 191:33-64.
    • (2012) Genetics , vol.191 , pp. 33-64
    • Haber, J.E.1
  • 100
    • 1542319100 scopus 로고    scopus 로고
    • Structure of the signal recognition particle interacting with the elongation-arrested ribosome
    • Halic M., Becker T., Pool M.R., Spahn C.M., Grassucci R.A., Frank J., Beckmann R. Structure of the signal recognition particle interacting with the elongation-arrested ribosome. Nature 2004, 427:808-814.
    • (2004) Nature , vol.427 , pp. 808-814
    • Halic, M.1    Becker, T.2    Pool, M.R.3    Spahn, C.M.4    Grassucci, R.A.5    Frank, J.6    Beckmann, R.7
  • 103
    • 84856641109 scopus 로고    scopus 로고
    • NF-κB, the first quarter-century: remarkable progress and outstanding questions
    • Hayden M.S., Ghosh S. NF-κB, the first quarter-century: remarkable progress and outstanding questions. Genes Dev. 2012, 26:203-234.
    • (2012) Genes Dev. , vol.26 , pp. 203-234
    • Hayden, M.S.1    Ghosh, S.2
  • 105
    • 79961232419 scopus 로고    scopus 로고
    • Bioinformatics analysis of a Saccharomyces cerevisiae N-terminal proteome provides evidence of alternative translation initiation and post-translational N-terminal acetylation
    • Helsens K., Van Damme P., Degroeve S., Martens L., Arnesen T., Vandekerckhove J., Gevaert K. Bioinformatics analysis of a Saccharomyces cerevisiae N-terminal proteome provides evidence of alternative translation initiation and post-translational N-terminal acetylation. J. Proteome Res. 2011, 10:3578-3589.
    • (2011) J. Proteome Res. , vol.10 , pp. 3578-3589
    • Helsens, K.1    Van Damme, P.2    Degroeve, S.3    Martens, L.4    Arnesen, T.5    Vandekerckhove, J.6    Gevaert, K.7
  • 108
    • 33646174748 scopus 로고    scopus 로고
    • An N-terminally acetylated Arf-like GTPase is localised to lysosomes and affects their motility
    • Hofmann I., Munro S. An N-terminally acetylated Arf-like GTPase is localised to lysosomes and affects their motility. J. Cell Sci. 2006, 119:1494-1503.
    • (2006) J. Cell Sci. , vol.119 , pp. 1494-1503
    • Hofmann, I.1    Munro, S.2
  • 109
    • 84904458790 scopus 로고    scopus 로고
    • Loss of amino-terminal acetylation suppresses a prion phenotype by modulating global protein folding
    • Holmes W.M., Mannakee B.K., Gutenkunst R.N., Serio T.R. Loss of amino-terminal acetylation suppresses a prion phenotype by modulating global protein folding. Nat. Commun. 2014, 5:4383.
    • (2014) Nat. Commun. , vol.5 , pp. 4383
    • Holmes, W.M.1    Mannakee, B.K.2    Gutenkunst, R.N.3    Serio, T.R.4
  • 110
    • 0024577108 scopus 로고
    • Escherichia coli-derived human interferon-gamma with Cys-Tyr-Cys at the N-terminus is partially N alpha-acylated
    • Honda S., Asano T., Kajio T., Nishimura O. Escherichia coli-derived human interferon-gamma with Cys-Tyr-Cys at the N-terminus is partially N alpha-acylated. Arch. Biochem. Biophys. 1989, 269:612-622.
    • (1989) Arch. Biochem. Biophys. , vol.269 , pp. 612-622
    • Honda, S.1    Asano, T.2    Kajio, T.3    Nishimura, O.4
  • 111
    • 0023491646 scopus 로고
    • Expression in Escherichia coli of active human alcohol dehydrogenase lacking N-terminal acetylation
    • Höög J.O., Weis M., Zeppezauer M., Jörnvall H., von Bahr-Lindström H. Expression in Escherichia coli of active human alcohol dehydrogenase lacking N-terminal acetylation. Biosci. Rep. 1987, 7:969-974.
    • (1987) Biosci. Rep. , vol.7 , pp. 969-974
    • Höög, J.O.1    Weis, M.2    Zeppezauer, M.3    Jörnvall, H.4    von Bahr-Lindström, H.5
  • 112
    • 84878701862 scopus 로고    scopus 로고
    • Potential involvement of N-terminal acetylation in the quantitative regulation of the ε subunit of chloroplast ATP synthase under drought stress
    • Hoshiyasu S., Kohzuma K., Yoshida K., Fujiwara M., Fukao Y., Yokota A., Akashi K. Potential involvement of N-terminal acetylation in the quantitative regulation of the ε subunit of chloroplast ATP synthase under drought stress. Biosci. Biotechnol. Biochem. 2013, 77:998-1007.
    • (2013) Biosci. Biotechnol. Biochem. , vol.77 , pp. 998-1007
    • Hoshiyasu, S.1    Kohzuma, K.2    Yoshida, K.3    Fujiwara, M.4    Fukao, Y.5    Yokota, A.6    Akashi, K.7
  • 113
    • 34249009554 scopus 로고    scopus 로고
    • The acetyltransferase activity of San stabilizes the mitotic cohesin at the centromeres in a shugoshin-independent manner
    • Hou F., Chu C.W., Kong X., Yokomori K., Zou H. The acetyltransferase activity of San stabilizes the mitotic cohesin at the centromeres in a shugoshin-independent manner. J. Cell Biol. 2007, 177:587-597.
    • (2007) J. Cell Biol. , vol.177 , pp. 587-597
    • Hou, F.1    Chu, C.W.2    Kong, X.3    Yokomori, K.4    Zou, H.5
  • 115
    • 84884170556 scopus 로고    scopus 로고
    • Proteomic amino-termini profiling reveals targeting information for protein import into complex plastids
    • Huesgen P.F., Alami M., Lange P.F., Foster L.J., Schröder W.P., Overall C.M., Green B.R. Proteomic amino-termini profiling reveals targeting information for protein import into complex plastids. PLoS One 2013, 8:e74483.
    • (2013) PLoS One , vol.8 , pp. e74483
    • Huesgen, P.F.1    Alami, M.2    Lange, P.F.3    Foster, L.J.4    Schröder, W.P.5    Overall, C.M.6    Green, B.R.7
  • 116
    • 33750464206 scopus 로고    scopus 로고
    • Posttranslational modification of the 20S proteasomal proteins of the archaeon Haloferax volcanii
    • Humbard M.A., Stevens S.M., Maupin-Furlow J.A. Posttranslational modification of the 20S proteasomal proteins of the archaeon Haloferax volcanii. J. Bacteriol. 2006, 188:7521-7530.
    • (2006) J. Bacteriol. , vol.188 , pp. 7521-7530
    • Humbard, M.A.1    Stevens, S.M.2    Maupin-Furlow, J.A.3
  • 117
    • 67549150995 scopus 로고    scopus 로고
    • The N-terminal penultimate residue of 20S proteasome alpha1 influences its N(alpha) acetylation and protein levels as well as growth rate and stress responses of Haloferax volcanii
    • Humbard M.A., Zhou G., Maupin-Furlow J.A. The N-terminal penultimate residue of 20S proteasome alpha1 influences its N(alpha) acetylation and protein levels as well as growth rate and stress responses of Haloferax volcanii. J. Bacteriol. 2009, 191:3794-3803.
    • (2009) J. Bacteriol. , vol.191 , pp. 3794-3803
    • Humbard, M.A.1    Zhou, G.2    Maupin-Furlow, J.A.3
  • 118
    • 0032217268 scopus 로고    scopus 로고
    • The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation
    • Huxford T., Huang D.B., Malek S., Ghosh G. The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation. Cell 1998, 95:759-770.
    • (1998) Cell , vol.95 , pp. 759-770
    • Huxford, T.1    Huang, D.B.2    Malek, S.3    Ghosh, G.4
  • 119
    • 77149120798 scopus 로고    scopus 로고
    • N-terminal acetylation of cellular proteins creates specific degradation signals
    • Hwang C.S., Shemorry A., Varshavsky A. N-terminal acetylation of cellular proteins creates specific degradation signals. Science 2010, 327:973-977.
    • (2010) Science , vol.327 , pp. 973-977
    • Hwang, C.S.1    Shemorry, A.2    Varshavsky, A.3
  • 120
    • 0034494265 scopus 로고    scopus 로고
    • Genetic manipulation indicates that ARD1 is an essential N(alpha)-acetyltransferase in Trypanosoma brucei
    • Ingram A.K., Cross G.A., Horn D. Genetic manipulation indicates that ARD1 is an essential N(alpha)-acetyltransferase in Trypanosoma brucei. Mol. Biochem. Parasitol. 2000, 111:309-317.
    • (2000) Mol. Biochem. Parasitol. , vol.111 , pp. 309-317
    • Ingram, A.K.1    Cross, G.A.2    Horn, D.3
  • 121
    • 0018181766 scopus 로고
    • Mutations affecting the structural genes and the genes coding for modifying enzymes for ribosomal proteins in Escherichia coli
    • Isono S., Isono K. Mutations affecting the structural genes and the genes coding for modifying enzymes for ribosomal proteins in Escherichia coli. Mol. Gen. Genet. 1978, 165:15-20.
    • (1978) Mol. Gen. Genet. , vol.165 , pp. 15-20
    • Isono, S.1    Isono, K.2
  • 122
    • 0018870981 scopus 로고
    • Ribosomal protein modification in Escherichia coli. II. Studies of a mutant lacking the N-terminal acetylation of protein S18
    • Isono K., Isono S. Ribosomal protein modification in Escherichia coli. II. Studies of a mutant lacking the N-terminal acetylation of protein S18. Mol. Gen. Genet. 1980, 177:645-651.
    • (1980) Mol. Gen. Genet. , vol.177 , pp. 645-651
    • Isono, K.1    Isono, S.2
  • 123
    • 0019793141 scopus 로고
    • Ribosomal protein modification in Escherichia coli. III. Studies of mutants lacking an acetylase activity specific for protein L12
    • Isono S., Isono K. Ribosomal protein modification in Escherichia coli. III. Studies of mutants lacking an acetylase activity specific for protein L12. Mol. Gen. Genet. 1981, 183:473-477.
    • (1981) Mol. Gen. Genet. , vol.183 , pp. 473-477
    • Isono, S.1    Isono, K.2
  • 124
    • 0032217264 scopus 로고    scopus 로고
    • Structure of an IkappaBalpha/NF-kappaB complex
    • Jacobs M.D., Harrison S.C. Structure of an IkappaBalpha/NF-kappaB complex. Cell 1998, 95:749-758.
    • (1998) Cell , vol.95 , pp. 749-758
    • Jacobs, M.D.1    Harrison, S.C.2
  • 125
    • 0040008534 scopus 로고    scopus 로고
    • Proteasome beta-type subunits: unequal roles of propeptides in core particle maturation and a hierarchy of active site function
    • Jäger S., Groll M., Huber R., Wolf D.H., Heinemeyer W. Proteasome beta-type subunits: unequal roles of propeptides in core particle maturation and a hierarchy of active site function. J. Mol. Biol. 1999, 291:997-1013.
    • (1999) J. Mol. Biol. , vol.291 , pp. 997-1013
    • Jäger, S.1    Groll, M.2    Huber, R.3    Wolf, D.H.4    Heinemeyer, W.5
  • 126
    • 84909607974 scopus 로고    scopus 로고
    • Principles of ER cotranslational translocation revealed by proximity-specific ribosome profiling
    • Jan C.H., Williams C.C., Weissman J.S. Principles of ER cotranslational translocation revealed by proximity-specific ribosome profiling. Science 2014, 346:1257521.
    • (2014) Science , vol.346 , pp. 1257521
    • Jan, C.H.1    Williams, C.C.2    Weissman, J.S.3
  • 127
    • 0028855710 scopus 로고
    • Solution structure of the acetylated and noncleavable mitochondrial targeting signal of rat chaperonin 10
    • Jarvis J.A., Ryan M.T., Hoogenraad N.J., Craik D.J., Høj P.B. Solution structure of the acetylated and noncleavable mitochondrial targeting signal of rat chaperonin 10. J. Biol. Chem. 1995, 270:1323-1331.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1323-1331
    • Jarvis, J.A.1    Ryan, M.T.2    Hoogenraad, N.J.3    Craik, D.J.4    Høj, P.B.5
  • 128
    • 0032858184 scopus 로고    scopus 로고
    • The effect of N-terminal acetylation and the inhibition activity of acetylated enkephalins on the aminopeptidase M-catalyzed hydrolysis of enkephalins
    • Jayawardene D.S., Dass C. The effect of N-terminal acetylation and the inhibition activity of acetylated enkephalins on the aminopeptidase M-catalyzed hydrolysis of enkephalins. Peptides 1999, 20:963-970.
    • (1999) Peptides , vol.20 , pp. 963-970
    • Jayawardene, D.S.1    Dass, C.2
  • 130
    • 40749110680 scopus 로고    scopus 로고
    • N-terminal acetylation protects glucagon-like peptide GLP-1-(7-34)-amide from DPP-IV-mediated degradation retaining cAMP- and insulin-releasing capacity
    • John H., Maronde E., Forssmann W.G., Meyer M., Adermann K. N-terminal acetylation protects glucagon-like peptide GLP-1-(7-34)-amide from DPP-IV-mediated degradation retaining cAMP- and insulin-releasing capacity. Eur. J. Med. Res. 2008, 13:73-78.
    • (2008) Eur. J. Med. Res. , vol.13 , pp. 73-78
    • John, H.1    Maronde, E.2    Forssmann, W.G.3    Meyer, M.4    Adermann, K.5
  • 131
    • 78650832959 scopus 로고    scopus 로고
    • Targeted amino-terminal acetylation of recombinant proteins in E. coli
    • Johnson M., Coulton A.T., Geeves M.A., Mulvihill D.P. Targeted amino-terminal acetylation of recombinant proteins in E. coli. PLoS One 2010, 5:e15801.
    • (2010) PLoS One , vol.5 , pp. e15801
    • Johnson, M.1    Coulton, A.T.2    Geeves, M.A.3    Mulvihill, D.P.4
  • 132
    • 79960430605 scopus 로고    scopus 로고
    • Protein acetylation in prokaryotes
    • Jones J.D., O'Connor C.D. Protein acetylation in prokaryotes. Proteomics 2011, 11:3012-3022.
    • (2011) Proteomics , vol.11 , pp. 3012-3022
    • Jones, J.D.1    O'Connor, C.D.2
  • 133
    • 33947217823 scopus 로고    scopus 로고
    • Interaction between beta-catenin and HIF-1 promotes cellular adaptation to hypoxia
    • Kaidi A., Williams A.C., Paraskeva C. Interaction between beta-catenin and HIF-1 promotes cellular adaptation to hypoxia. Nat. Cell Biol. 2007, 9:210-217.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 210-217
    • Kaidi, A.1    Williams, A.C.2    Paraskeva, C.3
  • 134
    • 84872613178 scopus 로고    scopus 로고
    • Protein N-terminal acetyltransferases in cancer
    • Kalvik T.V., Arnesen T. Protein N-terminal acetyltransferases in cancer. Oncogene 2013, 32:269-276.
    • (2013) Oncogene , vol.32 , pp. 269-276
    • Kalvik, T.V.1    Arnesen, T.2
  • 135
  • 136
    • 0031059069 scopus 로고    scopus 로고
    • Characterization of human recombinant annexin II tetramer purified from bacteria: role of N-terminal acetylation
    • Kang H.M., Kassam G., Jarvis S.E., Fitzpatrick S.L., Waisman D.M. Characterization of human recombinant annexin II tetramer purified from bacteria: role of N-terminal acetylation. Biochemistry 1997, 36:2041-2050.
    • (1997) Biochemistry , vol.36 , pp. 2041-2050
    • Kang, H.M.1    Kassam, G.2    Jarvis, S.E.3    Fitzpatrick, S.L.4    Waisman, D.M.5
  • 137
    • 84862555977 scopus 로고    scopus 로고
    • N-terminal acetylation of α-synuclein induces increased transient helical propensity and decreased aggregation rates in the intrinsically disordered monomer
    • Kang L., Moriarty G.M., Woods L.A., Ashcroft A.E., Radford S.E., Baum J. N-terminal acetylation of α-synuclein induces increased transient helical propensity and decreased aggregation rates in the intrinsically disordered monomer. Protein Sci. 2012, 21:911-917.
    • (2012) Protein Sci. , vol.21 , pp. 911-917
    • Kang, L.1    Moriarty, G.M.2    Woods, L.A.3    Ashcroft, A.E.4    Radford, S.E.5    Baum, J.6
  • 138
    • 84884216544 scopus 로고    scopus 로고
    • Mechanistic insight into the relationship between N-terminal acetylation of α-synuclein and fibril formation rates by NMR and fluorescence
    • Kang L., Janowska M.K., Moriarty G.M., Baum J. Mechanistic insight into the relationship between N-terminal acetylation of α-synuclein and fibril formation rates by NMR and fluorescence. PLoS One 2013, 8:e75018.
    • (2013) PLoS One , vol.8 , pp. e75018
    • Kang, L.1    Janowska, M.K.2    Moriarty, G.M.3    Baum, J.4
  • 141
    • 22044450479 scopus 로고    scopus 로고
    • Down-regulation of the expression of the FIH-1 and ARD-1 genes at the transcriptional level by nickel and cobalt in the human lung adenocarcinoma A549 cell line
    • Ke Q., Kluz T., Costa M. Down-regulation of the expression of the FIH-1 and ARD-1 genes at the transcriptional level by nickel and cobalt in the human lung adenocarcinoma A549 cell line. Int. J. Environ. Res. Public Health 2005, 2:10-13.
    • (2005) Int. J. Environ. Res. Public Health , vol.2 , pp. 10-13
    • Ke, Q.1    Kluz, T.2    Costa, M.3
  • 142
    • 0026703067 scopus 로고
    • Isolation and characterization of the methionine aminopeptidase from porcine liver responsible for the co-translational processing of proteins
    • Kendall R.L., Bradshaw R.A. Isolation and characterization of the methionine aminopeptidase from porcine liver responsible for the co-translational processing of proteins. J. Biol. Chem. 1992, 267:20667-20673.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20667-20673
    • Kendall, R.L.1    Bradshaw, R.A.2
  • 145
    • 84880066266 scopus 로고    scopus 로고
    • Mice lacking α-tubulin acetyltransferase 1 are viable but display α-tubulin acetylation deficiency and dentate gyrus distortion
    • Kim G.W., Li L., Gorbani M., You L., Yang X.J. Mice lacking α-tubulin acetyltransferase 1 are viable but display α-tubulin acetylation deficiency and dentate gyrus distortion. J. Biol. Chem. 2013, 288:20334-20350.
    • (2013) J. Biol. Chem. , vol.288 , pp. 20334-20350
    • Kim, G.W.1    Li, L.2    Gorbani, M.3    You, L.4    Yang, X.J.5
  • 149
    • 59349108429 scopus 로고    scopus 로고
    • Transcriptional regulation of the cyclin D1 gene at a glance
    • Klein E.A., Assoian R.K. Transcriptional regulation of the cyclin D1 gene at a glance. J. Cell Sci. 2008, 121:3853-3857.
    • (2008) J. Cell Sci. , vol.121 , pp. 3853-3857
    • Klein, E.A.1    Assoian, R.K.2
  • 150
    • 63449092252 scopus 로고    scopus 로고
    • Possible paracrine function of alpha-melanocyte-stimulating hormone and inhibition of its melanin-dispersing activity by N-terminal acetylation in the skin of the barfin flounder, Verasper moseri
    • Kobayashi Y., Mizusawa K., Yamanome T., Chiba H., Takahashi A. Possible paracrine function of alpha-melanocyte-stimulating hormone and inhibition of its melanin-dispersing activity by N-terminal acetylation in the skin of the barfin flounder, Verasper moseri. Gen. Comp. Endocrinol. 2009, 161:419-424.
    • (2009) Gen. Comp. Endocrinol. , vol.161 , pp. 419-424
    • Kobayashi, Y.1    Mizusawa, K.2    Yamanome, T.3    Chiba, H.4    Takahashi, A.5
  • 151
    • 45849117967 scopus 로고    scopus 로고
    • Wnt signal transduction pathways
    • Komiya Y., Habas R. Wnt signal transduction pathways. Organogenesis 2008, 4:68-75.
    • (2008) Organogenesis , vol.4 , pp. 68-75
    • Komiya, Y.1    Habas, R.2
  • 152
    • 77950562866 scopus 로고    scopus 로고
    • A dual function for chaperones SSB-RAC and the NAC nascent polypeptide-associated complex on ribosomes
    • Koplin A., Preissler S., Ilina Y., Koch M., Scior A., Erhardt M., Deuerling E. A dual function for chaperones SSB-RAC and the NAC nascent polypeptide-associated complex on ribosomes. J. Cell Biol. 2010, 189:57-68.
    • (2010) J. Cell Biol. , vol.189 , pp. 57-68
    • Koplin, A.1    Preissler, S.2    Ilina, Y.3    Koch, M.4    Scior, A.5    Erhardt, M.6    Deuerling, E.7
  • 153
    • 66849109240 scopus 로고    scopus 로고
    • The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins
    • Kramer G., Boehringer D., Ban N., Bukau B. The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins. Nat. Struct. Mol. Biol. 2009, 16:589-597.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 589-597
    • Kramer, G.1    Boehringer, D.2    Ban, N.3    Bukau, B.4
  • 154
    • 14644401017 scopus 로고    scopus 로고
    • N-terminal polyubiquitination of the ARF tumor suppressor, a natural lysine-less protein
    • Kuo M.L., den Besten W., Sherr C.J. N-terminal polyubiquitination of the ARF tumor suppressor, a natural lysine-less protein. Cell Cycle 2004, 3:1367-1369.
    • (2004) Cell Cycle , vol.3 , pp. 1367-1369
    • Kuo, M.L.1    den Besten, W.2    Sherr, C.J.3
  • 155
    • 70349140915 scopus 로고    scopus 로고
    • Phosphorylation of ARD1 by IKKbeta contributes to its destabilization and degradation
    • Kuo H.P., Lee D.F., Xia W., Lai C.C., Li L.Y., Hung M.C. Phosphorylation of ARD1 by IKKbeta contributes to its destabilization and degradation. Biochem. Biophys. Res. Commun. 2009, 389:156-161.
    • (2009) Biochem. Biophys. Res. Commun. , vol.389 , pp. 156-161
    • Kuo, H.P.1    Lee, D.F.2    Xia, W.3    Lai, C.C.4    Li, L.Y.5    Hung, M.C.6
  • 157
    • 80052290625 scopus 로고    scopus 로고
    • TopFIND, a knowledgebase linking protein termini with function
    • Lange P.F., Overall C.M. TopFIND, a knowledgebase linking protein termini with function. Nat. Methods 2011, 8:703-704.
    • (2011) Nat. Methods , vol.8 , pp. 703-704
    • Lange, P.F.1    Overall, C.M.2
  • 158
    • 84896969045 scopus 로고    scopus 로고
    • Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome
    • Lange P.F., Huesgen P.F., Nguyen K., Overall C.M. Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J. Proteome Res. 2014, 13:2028-2044.
    • (2014) J. Proteome Res. , vol.13 , pp. 2028-2044
    • Lange, P.F.1    Huesgen, P.F.2    Nguyen, K.3    Overall, C.M.4
  • 159
    • 0024428870 scopus 로고
    • N alpha acetylation is required for normal growth and mating of Saccharomyces cerevisiae
    • Lee F.J., Lin L.W., Smith J.A. N alpha acetylation is required for normal growth and mating of Saccharomyces cerevisiae. J. Bacteriol. 1989, 171:5795-5802.
    • (1989) J. Bacteriol. , vol.171 , pp. 5795-5802
    • Lee, F.J.1    Lin, L.W.2    Smith, J.A.3
  • 163
    • 33845293454 scopus 로고    scopus 로고
    • Human arrest defective 1 acetylates and activates beta-catenin, promoting lung cancer cell proliferation
    • Lim J.H., Park J.W., Chun Y.S. Human arrest defective 1 acetylates and activates beta-catenin, promoting lung cancer cell proliferation. Cancer Res. 2006, 66:10677-10682.
    • (2006) Cancer Res. , vol.66 , pp. 10677-10682
    • Lim, J.H.1    Park, J.W.2    Chun, Y.S.3
  • 164
    • 48549098557 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1alpha obstructs a Wnt signaling pathway by inhibiting the hARD1-mediated activation of beta-catenin
    • Lim J.H., Chun Y.S., Park J.W. Hypoxia-inducible factor-1alpha obstructs a Wnt signaling pathway by inhibiting the hARD1-mediated activation of beta-catenin. Cancer Res. 2008, 68:5177-5184.
    • (2008) Cancer Res. , vol.68 , pp. 5177-5184
    • Lim, J.H.1    Chun, Y.S.2    Park, J.W.3
  • 166
    • 84883342432 scopus 로고    scopus 로고
    • Implications for the evolution of eukaryotic amino-terminal acetyltransferase (NAT) enzymes from the structure of an archaeal ortholog
    • Liszczak G., Marmorstein R. Implications for the evolution of eukaryotic amino-terminal acetyltransferase (NAT) enzymes from the structure of an archaeal ortholog. Proc. Natl. Acad. Sci. U. S. A. 2013.
    • (2013) Proc. Natl. Acad. Sci. U. S. A.
    • Liszczak, G.1    Marmorstein, R.2
  • 167
    • 80054694313 scopus 로고    scopus 로고
    • Structure of a ternary Naa50p (NAT5/SAN) N-terminal acetyltransferase complex reveals the molecular basis for substrate-specific acetylation
    • Liszczak G., Arnesen T., Marmorstein R. Structure of a ternary Naa50p (NAT5/SAN) N-terminal acetyltransferase complex reveals the molecular basis for substrate-specific acetylation. J. Biol. Chem. 2011, 286:37002-37010.
    • (2011) J. Biol. Chem. , vol.286 , pp. 37002-37010
    • Liszczak, G.1    Arnesen, T.2    Marmorstein, R.3
  • 169
    • 84874873955 scopus 로고    scopus 로고
    • Identification and analysis of the acetylated status of poplar proteins reveals analogous N-terminal protein processing mechanisms with other eukaryotes
    • Liu C.C., Zhu H.Y., Dong X.M., Ning D.L., Wang H.X., Li W.H., Yang C.P., Wang B.C. Identification and analysis of the acetylated status of poplar proteins reveals analogous N-terminal protein processing mechanisms with other eukaryotes. PLoS One 2013, 8:e58681.
    • (2013) PLoS One , vol.8 , pp. e58681
    • Liu, C.C.1    Zhu, H.Y.2    Dong, X.M.3    Ning, D.L.4    Wang, H.X.5    Li, W.H.6    Yang, C.P.7    Wang, B.C.8
  • 170
    • 84905977478 scopus 로고    scopus 로고
    • Structure of Thermoplasma volcanium Ard1 belongs to N-acetyltransferase family member suggesting multiple ligand binding modes with acetyl coenzyme A and coenzyme A
    • Ma C., Pathak C., Jang S., Lee S.J., Nam M., Kim S.J., Im H., Lee B.J. Structure of Thermoplasma volcanium Ard1 belongs to N-acetyltransferase family member suggesting multiple ligand binding modes with acetyl coenzyme A and coenzyme A. Biochim. Biophys. Acta 2014, 1844:1790-1797.
    • (2014) Biochim. Biophys. Acta , vol.1844 , pp. 1790-1797
    • Ma, C.1    Pathak, C.2    Jang, S.3    Lee, S.J.4    Nam, M.5    Kim, S.J.6    Im, H.7    Lee, B.J.8
  • 171
    • 34250001423 scopus 로고    scopus 로고
    • An acetylase with relaxed specificity catalyses protein N-terminal acetylation in Sulfolobus solfataricus
    • Mackay D.T., Botting C.H., Taylor G.L., White M.F. An acetylase with relaxed specificity catalyses protein N-terminal acetylation in Sulfolobus solfataricus. Mol. Microbiol. 2007, 64:1540-1548.
    • (2007) Mol. Microbiol. , vol.64 , pp. 1540-1548
    • Mackay, D.T.1    Botting, C.H.2    Taylor, G.L.3    White, M.F.4
  • 172
    • 84930190696 scopus 로고    scopus 로고
    • The molecular basis for histone H4- and H2A-specific amino-terminal acetylation by NatD
    • Magin R.S., Liszczak G.P., Marmorstein R. The molecular basis for histone H4- and H2A-specific amino-terminal acetylation by NatD. Structure 2015, 23:332-341.
    • (2015) Structure , vol.23 , pp. 332-341
    • Magin, R.S.1    Liszczak, G.P.2    Marmorstein, R.3
  • 173
    • 84862893457 scopus 로고    scopus 로고
    • Impact of N-terminal acetylation of α-synuclein on its random coil and lipid binding properties
    • Maltsev A.S., Ying J., Bax A. Impact of N-terminal acetylation of α-synuclein on its random coil and lipid binding properties. Biochemistry 2012, 51:5004-5013.
    • (2012) Biochemistry , vol.51 , pp. 5004-5013
    • Maltsev, A.S.1    Ying, J.2    Bax, A.3
  • 174
    • 84903770687 scopus 로고    scopus 로고
    • Writers and readers of histone acetylation: structure, mechanism, and inhibition
    • Marmorstein R., Zhou M.M. Writers and readers of histone acetylation: structure, mechanism, and inhibition. Cold Spring Harb. Perspect. Biol. 2014, 6:a018762.
    • (2014) Cold Spring Harb. Perspect. Biol. , vol.6 , pp. a018762
    • Marmorstein, R.1    Zhou, M.M.2
  • 177
    • 0037274597 scopus 로고    scopus 로고
    • Large-scale identification of Caenorhabditis elegans proteins by multidimensional liquid chromatography-tandem mass spectrometry
    • Mawuenyega K.G., Kaji H., Yamuchi Y., Shinkawa T., Saito H., Taoka M., Takahashi N., Isobe T. Large-scale identification of Caenorhabditis elegans proteins by multidimensional liquid chromatography-tandem mass spectrometry. J. Proteome Res. 2003, 2:23-35.
    • (2003) J. Proteome Res. , vol.2 , pp. 23-35
    • Mawuenyega, K.G.1    Kaji, H.2    Yamuchi, Y.3    Shinkawa, T.4    Saito, H.5    Taoka, M.6    Takahashi, N.7    Isobe, T.8
  • 178
    • 84858722471 scopus 로고    scopus 로고
    • DNA damage-dependent NF-κB activation: NEMO turns nuclear signaling inside out
    • McCool K.W., Miyamoto S. DNA damage-dependent NF-κB activation: NEMO turns nuclear signaling inside out. Immunol. Rev. 2012, 246:311-326.
    • (2012) Immunol. Rev. , vol.246 , pp. 311-326
    • McCool, K.W.1    Miyamoto, S.2
  • 179
    • 0024296223 scopus 로고
    • Tandem mass spectrometry reveals that three photosystem II proteins of spinach chloroplasts contain N-acetyl-O-phosphothreonine at their NH2 termini
    • Michel H., Hunt D.F., Shabanowitz J., Bennett J. Tandem mass spectrometry reveals that three photosystem II proteins of spinach chloroplasts contain N-acetyl-O-phosphothreonine at their NH2 termini. J. Biol. Chem. 1988, 263:1123-1130.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1123-1130
    • Michel, H.1    Hunt, D.F.2    Shabanowitz, J.3    Bennett, J.4
  • 180
    • 84878245198 scopus 로고    scopus 로고
    • N-α-acetyltransferase 10 protein is a negative regulator of 28S proteasome through interaction with PA28β
    • Min L., Xu H., Wang J., Qu L., Jiang B., Zeng Y., Meng L., Jin H., Shou C. N-α-acetyltransferase 10 protein is a negative regulator of 28S proteasome through interaction with PA28β. FEBS Lett. 2013.
    • (2013) FEBS Lett.
    • Min, L.1    Xu, H.2    Wang, J.3    Qu, L.4    Jiang, B.5    Zeng, Y.6    Meng, L.7    Jin, H.8    Shou, C.9
  • 181
    • 84872154184 scopus 로고    scopus 로고
    • Structural conservation of distinctive N-terminal acetylation-dependent interactions across a family of mammalian NEDD8 ligation enzymes
    • Monda J.K., Scott D.C., Miller D.J., Lydeard J., King D., Harper J.W., Bennett E.J., Schulman B.A. Structural conservation of distinctive N-terminal acetylation-dependent interactions across a family of mammalian NEDD8 ligation enzymes. Structure 2013, 21:42-53.
    • (2013) Structure , vol.21 , pp. 42-53
    • Monda, J.K.1    Scott, D.C.2    Miller, D.J.3    Lydeard, J.4    King, D.5    Harper, J.W.6    Bennett, E.J.7    Schulman, B.A.8
  • 182
    • 84864003870 scopus 로고    scopus 로고
    • Sir3 and epigenetic inheritance of silent chromatin in Saccharomyces cerevisiae
    • Motwani T., Poddar M., Holmes S.G. Sir3 and epigenetic inheritance of silent chromatin in Saccharomyces cerevisiae. Mol. Cell. Biol. 2012, 32:2784-2793.
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 2784-2793
    • Motwani, T.1    Poddar, M.2    Holmes, S.G.3
  • 184
    • 84916203269 scopus 로고    scopus 로고
    • Insulin/insulin-like growth factor signaling in C. elegans
    • Murphy C.T., Hu P.J. Insulin/insulin-like growth factor signaling in C. elegans. WormBook 2013, 1-43.
    • (2013) WormBook , pp. 1-43
    • Murphy, C.T.1    Hu, P.J.2
  • 186
    • 25444527940 scopus 로고    scopus 로고
    • Genome-wide screen for inner nuclear membrane protein targeting in Saccharomyces cerevisiae: roles for N-acetylation and an integral membrane protein
    • Murthi A., Hopper A.K. Genome-wide screen for inner nuclear membrane protein targeting in Saccharomyces cerevisiae: roles for N-acetylation and an integral membrane protein. Genetics 2005, 170:1553-1560.
    • (2005) Genetics , vol.170 , pp. 1553-1560
    • Murthi, A.1    Hopper, A.K.2
  • 189
    • 84888279921 scopus 로고    scopus 로고
    • Posttranslational modifications of ribosomal proteins in Escherichia coli
    • Nesterchuk M.V., Sergiev P.V., Dontsova O.A. Posttranslational modifications of ribosomal proteins in Escherichia coli. Acta Nat. 2011, 3:22-33.
    • (2011) Acta Nat. , vol.3 , pp. 22-33
    • Nesterchuk, M.V.1    Sergiev, P.V.2    Dontsova, O.A.3
  • 190
    • 84870252814 scopus 로고    scopus 로고
    • The complex world of WNT receptor signalling
    • Niehrs C. The complex world of WNT receptor signalling. Nat. Rev. Mol. Cell Biol. 2012, 13:767-779.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 767-779
    • Niehrs, C.1
  • 193
    • 84856517954 scopus 로고    scopus 로고
    • Spatio-temporal expression pattern of the NatB complex, Nat5/Mdm20 in the developing mouse brain: implications for co-operative versus non-co-operative actions of Mdm20 and Nat5
    • Ohyama K., Yasuda K., Onga K., Kakizuka A., Mori N. Spatio-temporal expression pattern of the NatB complex, Nat5/Mdm20 in the developing mouse brain: implications for co-operative versus non-co-operative actions of Mdm20 and Nat5. Gene Expr. Patterns 2012, 12:36-45.
    • (2012) Gene Expr. Patterns , vol.12 , pp. 36-45
    • Ohyama, K.1    Yasuda, K.2    Onga, K.3    Kakizuka, A.4    Mori, N.5
  • 194
    • 37349033583 scopus 로고    scopus 로고
    • Role of the conserved Sir3-BAH domain in nucleosome binding and silent chromatin assembly
    • Onishi M., Liou G.G., Buchberger J.R., Walz T., Moazed D. Role of the conserved Sir3-BAH domain in nucleosome binding and silent chromatin assembly. Mol. Cell 2007, 28:1015-1028.
    • (2007) Mol. Cell , vol.28 , pp. 1015-1028
    • Onishi, M.1    Liou, G.G.2    Buchberger, J.R.3    Walz, T.4    Moazed, D.5
  • 195
    • 0033178880 scopus 로고    scopus 로고
    • New yeast genes important for chromosome integrity and segregation identified by dosage effects on genome stability
    • Ouspenski I.I., Elledge S.J., Brinkley B.R. New yeast genes important for chromosome integrity and segregation identified by dosage effects on genome stability. Nucleic Acids Res. 1999, 27:3001-3008.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3001-3008
    • Ouspenski, I.I.1    Elledge, S.J.2    Brinkley, B.R.3
  • 196
    • 68049137925 scopus 로고    scopus 로고
    • Cloning, characterization, and expression analysis of the novel acetyltransferase retrogene Ard1b in the mouse
    • Pang A.L., Peacock S., Johnson W., Bear D.H., Rennert O.M., Chan W.Y. Cloning, characterization, and expression analysis of the novel acetyltransferase retrogene Ard1b in the mouse. Biol. Reprod. 2009, 81:302-309.
    • (2009) Biol. Reprod. , vol.81 , pp. 302-309
    • Pang, A.L.1    Peacock, S.2    Johnson, W.3    Bear, D.H.4    Rennert, O.M.5    Chan, W.Y.6
  • 197
    • 81055138970 scopus 로고    scopus 로고
    • Expression of human NAA11 (ARD1B) gene is tissue-specific and is regulated by DNA methylation
    • Pang A.L., Clark J., Chan W.Y., Rennert O.M. Expression of human NAA11 (ARD1B) gene is tissue-specific and is regulated by DNA methylation. Epigenetics 2011, 6:1391-1399.
    • (2011) Epigenetics , vol.6 , pp. 1391-1399
    • Pang, A.L.1    Clark, J.2    Chan, W.Y.3    Rennert, O.M.4
  • 198
    • 47649112826 scopus 로고    scopus 로고
    • Tubedown associates with cortactin and controls permeability of retinal endothelial cells to albumin
    • Paradis H., Islam T., Tucker S., Tao L., Koubi S., Gendron R.L. Tubedown associates with cortactin and controls permeability of retinal endothelial cells to albumin. J. Cell Sci. 2008, 121:1965-1972.
    • (2008) J. Cell Sci. , vol.121 , pp. 1965-1972
    • Paradis, H.1    Islam, T.2    Tucker, S.3    Tao, L.4    Koubi, S.5    Gendron, R.L.6
  • 199
    • 84861361690 scopus 로고    scopus 로고
    • Mechanisms of Sec61/SecY-mediated protein translocation across membranes
    • Park E., Rapoport T.A. Mechanisms of Sec61/SecY-mediated protein translocation across membranes. Annu. Rev. Biophys. 2012, 41:21-40.
    • (2012) Annu. Rev. Biophys. , vol.41 , pp. 21-40
    • Park, E.1    Rapoport, T.A.2
  • 200
    • 0026605888 scopus 로고
    • ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity
    • Park E.C., Szostak J.W. ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity. EMBO J. 1992, 11:2087-2093.
    • (1992) EMBO J. , vol.11 , pp. 2087-2093
    • Park, E.C.1    Szostak, J.W.2
  • 203
    • 84924769665 scopus 로고    scopus 로고
    • Control of mammalian G protein signaling by N-terminal acetylation and the N-end rule pathway
    • Park S.E., Kim J.M., Seok O.H., Cho H., Wadas B., Kim S.Y., Varshavsky A., Hwang C.S. Control of mammalian G protein signaling by N-terminal acetylation and the N-end rule pathway. Science 2015, 347:1249-1252.
    • (2015) Science , vol.347 , pp. 1249-1252
    • Park, S.E.1    Kim, J.M.2    Seok, O.H.3    Cho, H.4    Wadas, B.5    Kim, S.Y.6    Varshavsky, A.7    Hwang, C.S.8
  • 204
    • 77953501128 scopus 로고    scopus 로고
    • Dual binding mode of the nascent polypeptide-associated complex reveals a novel universal adapter site on the ribosome
    • Pech M., Spreter T., Beckmann R., Beatrix B. Dual binding mode of the nascent polypeptide-associated complex reveals a novel universal adapter site on the ribosome. J. Biol. Chem. 2010, 285:19679-19687.
    • (2010) J. Biol. Chem. , vol.285 , pp. 19679-19687
    • Pech, M.1    Spreter, T.2    Beckmann, R.3    Beatrix, B.4
  • 205
    • 84873419140 scopus 로고    scopus 로고
    • The ribosome as a hub for protein quality control
    • Pechmann S., Willmund F., Frydman J. The ribosome as a hub for protein quality control. Mol. Cell 2013, 49:411-421.
    • (2013) Mol. Cell , vol.49 , pp. 411-421
    • Pechmann, S.1    Willmund, F.2    Frydman, J.3
  • 206
    • 79951855247 scopus 로고    scopus 로고
    • The ins and outs of tubulin acetylation: more than just a post-translational modification?
    • Perdiz D., Mackeh R., Poüs C., Baillet A. The ins and outs of tubulin acetylation: more than just a post-translational modification?. Cell. Signal. 2011, 23:763-771.
    • (2011) Cell. Signal. , vol.23 , pp. 763-771
    • Perdiz, D.1    Mackeh, R.2    Poüs, C.3    Baillet, A.4
  • 210
    • 84904497710 scopus 로고    scopus 로고
    • Amyloid-associated activity contributes to the severity and toxicity of a prion phenotype
    • Pezza J.A., Villali J., Sindi S.S., Serio T.R. Amyloid-associated activity contributes to the severity and toxicity of a prion phenotype. Nat. Commun. 2014, 5:4384.
    • (2014) Nat. Commun. , vol.5 , pp. 4384
    • Pezza, J.A.1    Villali, J.2    Sindi, S.S.3    Serio, T.R.4
  • 212
    • 84881618216 scopus 로고    scopus 로고
    • XLID-causing mutations and associated genes challenged in light of data from large-scale human exome sequencing
    • Piton A., Redin C., Mandel J.L. XLID-causing mutations and associated genes challenged in light of data from large-scale human exome sequencing. Am. J. Hum. Genet. 2013.
    • (2013) Am. J. Hum. Genet.
    • Piton, A.1    Redin, C.2    Mandel, J.L.3
  • 213
    • 0041848257 scopus 로고    scopus 로고
    • Composition and function of the eukaryotic N-terminal acetyltransferase subunits
    • Polevoda B., Sherman F. Composition and function of the eukaryotic N-terminal acetyltransferase subunits. Biochem. Biophys. Res. Commun. 2003, 308:1-11.
    • (2003) Biochem. Biophys. Res. Commun. , vol.308 , pp. 1-11
    • Polevoda, B.1    Sherman, F.2
  • 214
    • 0037462954 scopus 로고    scopus 로고
    • N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins
    • Polevoda B., Sherman F. N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins. J. Mol. Biol. 2003, 325:595-622.
    • (2003) J. Mol. Biol. , vol.325 , pp. 595-622
    • Polevoda, B.1    Sherman, F.2
  • 215
    • 0033231015 scopus 로고    scopus 로고
    • Identification and specificities of N-terminal acetyltransferases from Saccharomyces cerevisiae
    • Polevoda B., Norbeck J., Takakura H., Blomberg A., Sherman F. Identification and specificities of N-terminal acetyltransferases from Saccharomyces cerevisiae. EMBO J. 1999, 18:6155-6168.
    • (1999) EMBO J. , vol.18 , pp. 6155-6168
    • Polevoda, B.1    Norbeck, J.2    Takakura, H.3    Blomberg, A.4    Sherman, F.5
  • 216
    • 0043234609 scopus 로고    scopus 로고
    • Nat3p and Mdm20p are required for function of yeast NatB Nalpha-terminal acetyltransferase and of actin and tropomyosin
    • Polevoda B., Cardillo T.S., Doyle T.C., Bedi G.S., Sherman F. Nat3p and Mdm20p are required for function of yeast NatB Nalpha-terminal acetyltransferase and of actin and tropomyosin. J. Biol. Chem. 2003, 278:30686-30697.
    • (2003) J. Biol. Chem. , vol.278 , pp. 30686-30697
    • Polevoda, B.1    Cardillo, T.S.2    Doyle, T.C.3    Bedi, G.S.4    Sherman, F.5
  • 217
    • 38649122076 scopus 로고    scopus 로고
    • Yeast N(alpha)-terminal acetyltransferases are associated with ribosomes
    • Polevoda B., Brown S., Cardillo T.S., Rigby S., Sherman F. Yeast N(alpha)-terminal acetyltransferases are associated with ribosomes. J. Cell. Biochem. 2008, 103:492-508.
    • (2008) J. Cell. Biochem. , vol.103 , pp. 492-508
    • Polevoda, B.1    Brown, S.2    Cardillo, T.S.3    Rigby, S.4    Sherman, F.5
  • 218
    • 71449089622 scopus 로고    scopus 로고
    • A synopsis of eukaryotic Nalpha-terminal acetyltransferases: nomenclature, subunits and substrates
    • Polevoda B., Arnesen T., Sherman F. A synopsis of eukaryotic Nalpha-terminal acetyltransferases: nomenclature, subunits and substrates. BMC Proc. 2009, 3(Suppl. 6):S2.
    • (2009) BMC Proc. , vol.3 , pp. S2
    • Polevoda, B.1    Arnesen, T.2    Sherman, F.3
  • 219
    • 0037162838 scopus 로고    scopus 로고
    • Distinct modes of signal recognition particle interaction with the ribosome
    • Pool M.R., Stumm J., Fulga T.A., Sinning I., Dobberstein B. Distinct modes of signal recognition particle interaction with the ribosome. Science 2002, 297:1345-1348.
    • (2002) Science , vol.297 , pp. 1345-1348
    • Pool, M.R.1    Stumm, J.2    Fulga, T.A.3    Sinning, I.4    Dobberstein, B.5
  • 220
    • 0031036036 scopus 로고    scopus 로고
    • Acetylation of ribosomal protein S5 affected by defects in the central pseudoknot in 16S ribosomal RNA?
    • Poot R.A., Jeeninga R.E., Pleij C.W., van Duin J. Acetylation of ribosomal protein S5 affected by defects in the central pseudoknot in 16S ribosomal RNA?. FEBS Lett. 1997, 401:175-179.
    • (1997) FEBS Lett. , vol.401 , pp. 175-179
    • Poot, R.A.1    Jeeninga, R.E.2    Pleij, C.W.3    van Duin, J.4
  • 222
    • 33846057724 scopus 로고    scopus 로고
    • NCBI reference sequences (RefSeq): a curated non-redundant sequence database of genomes, transcripts and proteins
    • Pruitt K.D., Tatusova T., Maglott D.R. NCBI reference sequences (RefSeq): a curated non-redundant sequence database of genomes, transcripts and proteins. Nucleic Acids Res. 2007, 35:D61-D65.
    • (2007) Nucleic Acids Res. , vol.35 , pp. D61-D65
    • Pruitt, K.D.1    Tatusova, T.2    Maglott, D.R.3
  • 223
    • 0016154293 scopus 로고
    • Alteration in the acetylation level of ribosomal protein L12 during growth cycle of Escherichia coli
    • Ramagopal S., Subramanian A.R. Alteration in the acetylation level of ribosomal protein L12 during growth cycle of Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 1974, 71:2136-2140.
    • (1974) Proc. Natl. Acad. Sci. U. S. A. , vol.71 , pp. 2136-2140
    • Ramagopal, S.1    Subramanian, A.R.2
  • 225
    • 34247281027 scopus 로고    scopus 로고
    • Association of protein biogenesis factors at the yeast ribosomal tunnel exit is affected by the translational status and nascent polypeptide sequence
    • Raue U., Oellerer S., Rospert S. Association of protein biogenesis factors at the yeast ribosomal tunnel exit is affected by the translational status and nascent polypeptide sequence. J. Biol. Chem. 2007, 282:7809-7816.
    • (2007) J. Biol. Chem. , vol.282 , pp. 7809-7816
    • Raue, U.1    Oellerer, S.2    Rospert, S.3
  • 226
    • 37849012236 scopus 로고    scopus 로고
    • HYPK, a Huntingtin interacting protein, reduces aggregates and apoptosis induced by N-terminal Huntingtin with 40 glutamines in Neuro2a cells and exhibits chaperone-like activity
    • Raychaudhuri S., Sinha M., Mukhopadhyay D., Bhattacharyya N.P. HYPK, a Huntingtin interacting protein, reduces aggregates and apoptosis induced by N-terminal Huntingtin with 40 glutamines in Neuro2a cells and exhibits chaperone-like activity. Hum. Mol. Genet. 2008, 17:240-255.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 240-255
    • Raychaudhuri, S.1    Sinha, M.2    Mukhopadhyay, D.3    Bhattacharyya, N.P.4
  • 227
    • 0035850733 scopus 로고    scopus 로고
    • Central domain assembly: thermodynamics and kinetics of S6 and S18 binding to an S15-RNA complex
    • Recht M.I., Williamson J.R. Central domain assembly: thermodynamics and kinetics of S6 and S18 binding to an S15-RNA complex. J. Mol. Biol. 2001, 313:35-48.
    • (2001) J. Mol. Biol. , vol.313 , pp. 35-48
    • Recht, M.I.1    Williamson, J.R.2
  • 228
    • 33750515887 scopus 로고    scopus 로고
    • The structure of the Sec complex and the problem of protein translocation
    • Robson A., Collinson I. The structure of the Sec complex and the problem of protein translocation. EMBO Rep. 2006, 7:1099-1103.
    • (2006) EMBO Rep. , vol.7 , pp. 1099-1103
    • Robson, A.1    Collinson, I.2
  • 230
    • 44249096370 scopus 로고    scopus 로고
    • Suppression of a cold-sensitive mutation in ribosomal protein S5 reveals a role for RimJ in ribosome biogenesis
    • Roy-Chaudhuri B., Kirthi N., Kelley T., Culver G.M. Suppression of a cold-sensitive mutation in ribosomal protein S5 reveals a role for RimJ in ribosome biogenesis. Mol. Microbiol. 2008, 68:1547-1559.
    • (2008) Mol. Microbiol. , vol.68 , pp. 1547-1559
    • Roy-Chaudhuri, B.1    Kirthi, N.2    Kelley, T.3    Culver, G.M.4
  • 232
    • 79551696674 scopus 로고    scopus 로고
    • Clustering heterochromatin: Sir3 promotes telomere clustering independently of silencing in yeast
    • Ruault M., De Meyer A., Loïodice I., Taddei A. Clustering heterochromatin: Sir3 promotes telomere clustering independently of silencing in yeast. J. Cell Biol. 2011, 192:417-431.
    • (2011) J. Cell Biol. , vol.192 , pp. 417-431
    • Ruault, M.1    De Meyer, A.2    Loïodice, I.3    Taddei, A.4
  • 233
    • 0037636027 scopus 로고    scopus 로고
    • The establishment, inheritance, and function of silenced chromatin in Saccharomyces cerevisiae
    • Rusche L.N., Kirchmaier A.L., Rine J. The establishment, inheritance, and function of silenced chromatin in Saccharomyces cerevisiae. Annu. Rev. Biochem. 2003, 72:481-516.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 481-516
    • Rusche, L.N.1    Kirchmaier, A.L.2    Rine, J.3
  • 234
    • 66349093144 scopus 로고    scopus 로고
    • Mutational analysis of the Sir3 BAH domain reveals multiple points of interaction with nucleosomes
    • Sampath V., Yuan P., Wang I.X., Prugar E., van Leeuwen F., Sternglanz R. Mutational analysis of the Sir3 BAH domain reveals multiple points of interaction with nucleosomes. Mol. Cell. Biol. 2009, 29:2532-2545.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 2532-2545
    • Sampath, V.1    Yuan, P.2    Wang, I.X.3    Prugar, E.4    van Leeuwen, F.5    Sternglanz, R.6
  • 235
    • 33746491112 scopus 로고    scopus 로고
    • Characterization of the native and fibrillar conformation of the human Nalpha-acetyltransferase ARD1
    • Sánchez-Puig N., Fersht A.R. Characterization of the native and fibrillar conformation of the human Nalpha-acetyltransferase ARD1. Protein Sci. 2006, 15:1968-1976.
    • (2006) Protein Sci. , vol.15 , pp. 1968-1976
    • Sánchez-Puig, N.1    Fersht, A.R.2
  • 236
    • 0029074893 scopus 로고
    • Some effects of post-translational N-terminal acetylation of the human embryonic zeta globin protein
    • Scheepens A., Mould R., Hofmann O., Brittain T. Some effects of post-translational N-terminal acetylation of the human embryonic zeta globin protein. Biochem. J. 1995, 310(Pt 2):597-600.
    • (1995) Biochem. J. , vol.310 , pp. 597-600
    • Scheepens, A.1    Mould, R.2    Hofmann, O.3    Brittain, T.4
  • 237
    • 80555131132 scopus 로고    scopus 로고
    • N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex
    • Scott D.C., Monda J.K., Bennett E.J., Harper J.W., Schulman B.A. N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex. Science 2011, 334:674-678.
    • (2011) Science , vol.334 , pp. 674-678
    • Scott, D.C.1    Monda, J.K.2    Bennett, E.J.3    Harper, J.W.4    Schulman, B.A.5
  • 238
    • 84903125623 scopus 로고    scopus 로고
    • Structure of a RING E3 trapped in action reveals ligation mechanism for the ubiquitin-like protein NEDD8
    • Scott D.C., Sviderskiy V.O., Monda J.K., Lydeard J.R., Cho S.E., Harper J.W., Schulman B.A. Structure of a RING E3 trapped in action reveals ligation mechanism for the ubiquitin-like protein NEDD8. Cell 2014, 157:1671-1684.
    • (2014) Cell , vol.157 , pp. 1671-1684
    • Scott, D.C.1    Sviderskiy, V.O.2    Monda, J.K.3    Lydeard, J.R.4    Cho, S.E.5    Harper, J.W.6    Schulman, B.A.7
  • 239
    • 79960915567 scopus 로고    scopus 로고
    • SRP and NAC: guiding a nascent protein's first steps
    • Sedwick C. SRP and NAC: guiding a nascent protein's first steps. PLoS Biol. 2011, 9:e1001103.
    • (2011) PLoS Biol. , vol.9 , pp. e1001103
    • Sedwick, C.1
  • 242
    • 84918581492 scopus 로고    scopus 로고
    • Different subcellular localizations and functions of human ARD1 variants
    • Seo J.H., Park J.H., Lee E.J., Kim K.W. Different subcellular localizations and functions of human ARD1 variants. Int. J. Oncol. 2015, 46:701-707.
    • (2015) Int. J. Oncol. , vol.46 , pp. 701-707
    • Seo, J.H.1    Park, J.H.2    Lee, E.J.3    Kim, K.W.4
  • 243
    • 2342497804 scopus 로고    scopus 로고
    • Golgi targeting of ARF-like GTPase Arl3p requires its Nalpha-acetylation and the integral membrane protein Sys1p
    • Setty S.R., Strochlic T.I., Tong A.H., Boone C., Burd C.G. Golgi targeting of ARF-like GTPase Arl3p requires its Nalpha-acetylation and the integral membrane protein Sys1p. Nat. Cell Biol. 2004, 6:414-419.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 414-419
    • Setty, S.R.1    Strochlic, T.I.2    Tong, A.H.3    Boone, C.4    Burd, C.G.5
  • 244
    • 84924777167 scopus 로고    scopus 로고
    • Structure and assembly pathway of the ribosome quality control complex
    • Shao S., Brown A., Santhanam B., Hegde R.S. Structure and assembly pathway of the ribosome quality control complex. Mol. Cell 2015, 57:433-444.
    • (2015) Mol. Cell , vol.57 , pp. 433-444
    • Shao, S.1    Brown, A.2    Santhanam, B.3    Hegde, R.S.4
  • 245
    • 0026701688 scopus 로고
    • Isolation and characterization of the rat liver actin N-acetylaminopeptidase
    • Sheff D.R., Rubenstein P.A. Isolation and characterization of the rat liver actin N-acetylaminopeptidase. J. Biol. Chem. 1992, 267:20217-20224.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20217-20224
    • Sheff, D.R.1    Rubenstein, P.A.2
  • 246
    • 84878195272 scopus 로고    scopus 로고
    • Control of protein quality and stoichiometries by N-terminal acetylation and the N-end rule pathway
    • Shemorry A., Hwang C.S., Varshavsky A. Control of protein quality and stoichiometries by N-terminal acetylation and the N-end rule pathway. Mol. Cell 2013, 50:540-551.
    • (2013) Mol. Cell , vol.50 , pp. 540-551
    • Shemorry, A.1    Hwang, C.S.2    Varshavsky, A.3
  • 247
    • 78650731392 scopus 로고    scopus 로고
    • The major alpha-tubulin K40 acetyltransferase alphaTAT1 promotes rapid ciliogenesis and efficient mechanosensation
    • Shida T., Cueva J.G., Xu Z., Goodman M.B., Nachury M.V. The major alpha-tubulin K40 acetyltransferase alphaTAT1 promotes rapid ciliogenesis and efficient mechanosensation. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:21517-21522.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 21517-21522
    • Shida, T.1    Cueva, J.G.2    Xu, Z.3    Goodman, M.B.4    Nachury, M.V.5
  • 248
    • 70449379394 scopus 로고    scopus 로고
    • Arrest defective-1 controls tumor cell behavior by acetylating myosin light chain kinase
    • Shin D.H., Chun Y.S., Lee K.H., Shin H.W., Park J.W. Arrest defective-1 controls tumor cell behavior by acetylating myosin light chain kinase. PLoS One 2009, 4:e7451.
    • (2009) PLoS One , vol.4 , pp. e7451
    • Shin, D.H.1    Chun, Y.S.2    Lee, K.H.3    Shin, H.W.4    Park, J.W.5
  • 249
    • 84928016447 scopus 로고    scopus 로고
    • Arrest defective 1 regulates the oxidative stress response in human cells and mice by acetylating methionine sulfoxide reductase A
    • Shin S.H., Yoon H., Chun Y.S., Shin H.W., Lee M.N., Oh G.T., Park J.W. Arrest defective 1 regulates the oxidative stress response in human cells and mice by acetylating methionine sulfoxide reductase A. Cell Death Dis. 2014, 5:e1490.
    • (2014) Cell Death Dis. , vol.5 , pp. e1490
    • Shin, S.H.1    Yoon, H.2    Chun, Y.S.3    Shin, H.W.4    Lee, M.N.5    Oh, G.T.6    Park, J.W.7
  • 250
    • 0023122030 scopus 로고
    • Tests of the helix dipole model for stabilization of alpha-helices
    • Shoemaker K.R., Kim P.S., York E.J., Stewart J.M., Baldwin R.L. Tests of the helix dipole model for stabilization of alpha-helices. Nature 1987, 326:563-567.
    • (1987) Nature , vol.326 , pp. 563-567
    • Shoemaker, K.R.1    Kim, P.S.2    York, E.J.3    Stewart, J.M.4    Baldwin, R.L.5
  • 251
    • 0038271935 scopus 로고    scopus 로고
    • Mdm20 protein functions with Nat3 protein to acetylate Tpm1 protein and regulate tropomyosin-actin interactions in budding yeast
    • Singer J.M., Shaw J.M. Mdm20 protein functions with Nat3 protein to acetylate Tpm1 protein and regulate tropomyosin-actin interactions in budding yeast. Proc. Natl. Acad. Sci. U. S. A. 2003, 100:7644-7649.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 7644-7649
    • Singer, J.M.1    Shaw, J.M.2
  • 253
    • 80054958053 scopus 로고    scopus 로고
    • The N-end rule pathway: emerging functions and molecular principles of substrate recognition
    • Sriram S.M., Kim B.Y., Kwon Y.T. The N-end rule pathway: emerging functions and molecular principles of substrate recognition. Nat. Rev. Mol. Cell Biol. 2011, 12:735-747.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 735-747
    • Sriram, S.M.1    Kim, B.Y.2    Kwon, Y.T.3
  • 254
    • 67650085001 scopus 로고    scopus 로고
    • Knockdown of human N alpha-terminal acetyltransferase complex C leads to p53-dependent apoptosis and aberrant human Arl8b localization
    • Starheim K.K., Gromyko D., Evjenth R., Ryningen A., Varhaug J.E., Lillehaug J.R., Arnesen T. Knockdown of human N alpha-terminal acetyltransferase complex C leads to p53-dependent apoptosis and aberrant human Arl8b localization. Mol. Cell. Biol. 2009, 29:3569-3581.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 3569-3581
    • Starheim, K.K.1    Gromyko, D.2    Evjenth, R.3    Ryningen, A.4    Varhaug, J.E.5    Lillehaug, J.R.6    Arnesen, T.7
  • 255
    • 77952890311 scopus 로고    scopus 로고
    • Composition and biological significance of the human Nalpha-terminal acetyltransferases
    • Starheim K.K., Gromyko D., Velde R., Varhaug J.E., Arnesen T. Composition and biological significance of the human Nalpha-terminal acetyltransferases. BMC Proc. 2009, 3(Suppl. 6):S3.
    • (2009) BMC Proc. , vol.3 , pp. S3
    • Starheim, K.K.1    Gromyko, D.2    Velde, R.3    Varhaug, J.E.4    Arnesen, T.5
  • 256
    • 84859490749 scopus 로고    scopus 로고
    • Protein N-terminal acetyltransferases: when the start matters
    • Starheim K.K., Gevaert K., Arnesen T. Protein N-terminal acetyltransferases: when the start matters. Trends Biochem. Sci. 2012, 37:152-161.
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 152-161
    • Starheim, K.K.1    Gevaert, K.2    Arnesen, T.3
  • 257
    • 0030582382 scopus 로고    scopus 로고
    • The effect of N-terminal acetylation on Ca(2+)-ATPase inhibition by phospholamban
    • Starling A.P., Sharma R.P., East J.M., Lee A.G. The effect of N-terminal acetylation on Ca(2+)-ATPase inhibition by phospholamban. Biochem. Biophys. Res. Commun. 1996, 226:352-355.
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 352-355
    • Starling, A.P.1    Sharma, R.P.2    East, J.M.3    Lee, A.G.4
  • 258
    • 84887476450 scopus 로고    scopus 로고
    • Transcriptional regulation at the yeast nuclear envelope
    • Steglich B., Sazer S., Ekwall K. Transcriptional regulation at the yeast nuclear envelope. Nucleus 2013, 4:379-389.
    • (2013) Nucleus , vol.4 , pp. 379-389
    • Steglich, B.1    Sazer, S.2    Ekwall, K.3
  • 259
    • 0026061252 scopus 로고
    • The SIR1 gene of Saccharomyces cerevisiae and its role as an extragenic suppressor of several mating-defective mutants
    • Stone E.M., Swanson M.J., Romeo A.M., Hicks J.B., Sternglanz R. The SIR1 gene of Saccharomyces cerevisiae and its role as an extragenic suppressor of several mating-defective mutants. Mol. Cell. Biol. 1991, 11:2253-2262.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2253-2262
    • Stone, E.M.1    Swanson, M.J.2    Romeo, A.M.3    Hicks, J.B.4    Sternglanz, R.5
  • 260
    • 0034046081 scopus 로고    scopus 로고
    • Two classes of sir3 mutants enhance the sir1 mutant mating defect and abolish telomeric silencing in Saccharomyces cerevisiae
    • Stone E.M., Reifsnyder C., McVey M., Gazo B., Pillus L. Two classes of sir3 mutants enhance the sir1 mutant mating defect and abolish telomeric silencing in Saccharomyces cerevisiae. Genetics 2000, 155:509-522.
    • (2000) Genetics , vol.155 , pp. 509-522
    • Stone, E.M.1    Reifsnyder, C.2    McVey, M.3    Gazo, B.4    Pillus, L.5
  • 261
    • 0015845499 scopus 로고
    • Synthesis of lens protein in vitro. N-terminal acetylation of alpha-crystallin
    • Strous G.J., van Westreenen H., Bloemendal H. Synthesis of lens protein in vitro. N-terminal acetylation of alpha-crystallin. Eur. J. Biochem. 1973, 38:79-85.
    • (1973) Eur. J. Biochem. , vol.38 , pp. 79-85
    • Strous, G.J.1    van Westreenen, H.2    Bloemendal, H.3
  • 263
    • 0035957960 scopus 로고    scopus 로고
    • N-methyl-d-aspartate receptors regulate a group of transiently expressed genes in the developing brain
    • Sugiura N., Patel R.G., Corriveau R.A. N-methyl-d-aspartate receptors regulate a group of transiently expressed genes in the developing brain. J. Biol. Chem. 2001, 276:14257-14263.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14257-14263
    • Sugiura, N.1    Patel, R.G.2    Corriveau, R.A.3
  • 264
    • 0141925607 scopus 로고    scopus 로고
    • An evolutionarily conserved N-terminal acetyltransferase complex associated with neuronal development
    • Sugiura N., Adams S.M., Corriveau R.A. An evolutionarily conserved N-terminal acetyltransferase complex associated with neuronal development. J. Biol. Chem. 2003, 278:40113-40120.
    • (2003) J. Biol. Chem. , vol.278 , pp. 40113-40120
    • Sugiura, N.1    Adams, S.M.2    Corriveau, R.A.3
  • 265
    • 63049114323 scopus 로고    scopus 로고
    • Prion proteostasis: Hsp104 meets its supporting cast
    • Sweeny E.A., Shorter J. Prion proteostasis: Hsp104 meets its supporting cast. Prion 2008, 2:135-140.
    • (2008) Prion , vol.2 , pp. 135-140
    • Sweeny, E.A.1    Shorter, J.2
  • 266
    • 0026612309 scopus 로고
    • NH2-terminal acetylation of ribosomal proteins of Saccharomyces cerevisiae
    • Takakura H., Tsunasawa S., Miyagi M., Warner J.R. NH2-terminal acetylation of ribosomal proteins of Saccharomyces cerevisiae. J. Biol. Chem. 1992, 267:5442-5445.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5442-5445
    • Takakura, H.1    Tsunasawa, S.2    Miyagi, M.3    Warner, J.R.4
  • 267
    • 0023194763 scopus 로고
    • Chemical characterization of recombinant human leukocyte interferon A using fast atom bombardment mass spectrometry
    • Takao T., Kobayashi M., Nishimura O., Shimonishi Y. Chemical characterization of recombinant human leukocyte interferon A using fast atom bombardment mass spectrometry. J. Biol. Chem. 1987, 262:3541-3547.
    • (1987) J. Biol. Chem. , vol.262 , pp. 3541-3547
    • Takao, T.1    Kobayashi, M.2    Nishimura, O.3    Shimonishi, Y.4
  • 268
    • 0033870281 scopus 로고    scopus 로고
    • The expression and distribution of the hypoxia-inducible factors HIF-1alpha and HIF-2alpha in normal human tissues, cancers, and tumor-associated macrophages
    • Talks K.L., Turley H., Gatter K.C., Maxwell P.H., Pugh C.W., Ratcliffe P.J., Harris A.L. The expression and distribution of the hypoxia-inducible factors HIF-1alpha and HIF-2alpha in normal human tissues, cancers, and tumor-associated macrophages. Am. J. Pathol. 2000, 157:411-421.
    • (2000) Am. J. Pathol. , vol.157 , pp. 411-421
    • Talks, K.L.1    Turley, H.2    Gatter, K.C.3    Maxwell, P.H.4    Pugh, C.W.5    Ratcliffe, P.J.6    Harris, A.L.7
  • 269
    • 0024381096 scopus 로고
    • Cloning and molecular characterization of the gene rimL which encodes an enzyme acetylating ribosomal protein L12 of Escherichia coli K12
    • Tanaka S., Matsushita Y., Yoshikawa A., Isono K. Cloning and molecular characterization of the gene rimL which encodes an enzyme acetylating ribosomal protein L12 of Escherichia coli K12. Mol. Gen. Genet. 1989, 217:289-293.
    • (1989) Mol. Gen. Genet. , vol.217 , pp. 289-293
    • Tanaka, S.1    Matsushita, Y.2    Yoshikawa, A.3    Isono, K.4
  • 270
    • 0034663894 scopus 로고    scopus 로고
    • Mechanism of regulation of the hypoxia-inducible factor-1 alpha by the von Hippel-Lindau tumor suppressor protein
    • Tanimoto K., Makino Y., Pereira T., Poellinger L. Mechanism of regulation of the hypoxia-inducible factor-1 alpha by the von Hippel-Lindau tumor suppressor protein. EMBO J. 2000, 19:4298-4309.
    • (2000) EMBO J. , vol.19 , pp. 4298-4309
    • Tanimoto, K.1    Makino, Y.2    Pereira, T.3    Poellinger, L.4
  • 271
    • 0015912063 scopus 로고
    • The primary structure of an acidic protein from 50-S ribosomes of Escherichia coli which is involved in GTP hydrolysis dependent on elongation factors G and T
    • Terhorst C., Möller W., Laursen R., Wittmann-Liebold B. The primary structure of an acidic protein from 50-S ribosomes of Escherichia coli which is involved in GTP hydrolysis dependent on elongation factors G and T. Eur. J. Biochem. 1973, 34:138-152.
    • (1973) Eur. J. Biochem. , vol.34 , pp. 138-152
    • Terhorst, C.1    Möller, W.2    Laursen, R.3    Wittmann-Liebold, B.4
  • 272
    • 55949109442 scopus 로고    scopus 로고
    • In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104
    • Tipton K.A., Verges K.J., Weissman J.S. In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104. Mol. Cell 2008, 32:584-591.
    • (2008) Mol. Cell , vol.32 , pp. 584-591
    • Tipton, K.A.1    Verges, K.J.2    Weissman, J.S.3
  • 273
    • 0025195135 scopus 로고
    • The NH2-terminal residues of rat liver proteasome (multicatalytic proteinase complex) subunits, C2, C3 and C8, are N alpha-acetylated
    • Tokunaga F., Aruga R., Iwanaga S., Tanaka K., Ichihara A., Takao T., Shimonishi Y. The NH2-terminal residues of rat liver proteasome (multicatalytic proteinase complex) subunits, C2, C3 and C8, are N alpha-acetylated. FEBS Lett. 1990, 263:373-375.
    • (1990) FEBS Lett. , vol.263 , pp. 373-375
    • Tokunaga, F.1    Aruga, R.2    Iwanaga, S.3    Tanaka, K.4    Ichihara, A.5    Takao, T.6    Shimonishi, Y.7
  • 274
    • 84860172516 scopus 로고    scopus 로고
    • N-terminal acetylation is critical for forming α-helical oligomer of α-synuclein
    • Trexler A.J., Rhoades E. N-terminal acetylation is critical for forming α-helical oligomer of α-synuclein. Protein Sci. 2012, 21:601-605.
    • (2012) Protein Sci. , vol.21 , pp. 601-605
    • Trexler, A.J.1    Rhoades, E.2
  • 275
    • 0028222543 scopus 로고
    • Isolation of new genes in distal Xq28: transcriptional map and identification of a human homologue of the ARD1 N-acetyl transferase of Saccharomyces cerevisiae
    • Tribioli C., Mancini M., Plassart E., Bione S., Rivella S., Sala C., Torri G., Toniolo D. Isolation of new genes in distal Xq28: transcriptional map and identification of a human homologue of the ARD1 N-acetyl transferase of Saccharomyces cerevisiae. Hum. Mol. Genet. 1994, 3:1061-1067.
    • (1994) Hum. Mol. Genet. , vol.3 , pp. 1061-1067
    • Tribioli, C.1    Mancini, M.2    Plassart, E.3    Bione, S.4    Rivella, S.5    Sala, C.6    Torri, G.7    Toniolo, D.8
  • 276
    • 0035971107 scopus 로고    scopus 로고
    • Amino acid residue penultimate to the amino-terminal gly residue strongly affects two cotranslational protein modifications, N-myristoylation and N-acetylation
    • Utsumi T., Sato M., Nakano K., Takemura D., Iwata H., Ishisaka R. Amino acid residue penultimate to the amino-terminal gly residue strongly affects two cotranslational protein modifications, N-myristoylation and N-acetylation. J. Biol. Chem. 2001, 276:10505-10513.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10505-10513
    • Utsumi, T.1    Sato, M.2    Nakano, K.3    Takemura, D.4    Iwata, H.5    Ishisaka, R.6
  • 277
    • 80053415277 scopus 로고    scopus 로고
    • Protein alpha-N-acetylation studied by N-terminomics
    • Van Damme P., Arnesen T., Gevaert K. Protein alpha-N-acetylation studied by N-terminomics. FEBS J. 2011, 278:3822-3834.
    • (2011) FEBS J. , vol.278 , pp. 3822-3834
    • Van Damme, P.1    Arnesen, T.2    Gevaert, K.3
  • 278
    • 79955761504 scopus 로고    scopus 로고
    • Proteome-derived peptide libraries allow detailed analysis of the substrate specificities of N(alpha)-acetyltransferases and point to hNaa10p as the post-translational actin N(alpha)-acetyltransferase
    • (M110.004580)
    • Van Damme P., Evjenth R., Foyn H., Demeyer K., De Bock P.J., Lillehaug J.R., Vandekerckhove J., Arnesen T., Gevaert K. Proteome-derived peptide libraries allow detailed analysis of the substrate specificities of N(alpha)-acetyltransferases and point to hNaa10p as the post-translational actin N(alpha)-acetyltransferase. Mol. Cell. Proteomics 2011, 10. (M110.004580).
    • (2011) Mol. Cell. Proteomics , vol.10
    • Van Damme, P.1    Evjenth, R.2    Foyn, H.3    Demeyer, K.4    De Bock, P.J.5    Lillehaug, J.R.6    Vandekerckhove, J.7    Arnesen, T.8    Gevaert, K.9
  • 281
    • 84904481340 scopus 로고    scopus 로고
    • A Saccharomyces cerevisiae model reveals in vivo functional impairment of the Ogden syndrome N-terminal acetyltransferase Naa10S37P mutant
    • Van Damme P., Støve S.I., Glomnes N., Gevaert K., Arnesen T. A Saccharomyces cerevisiae model reveals in vivo functional impairment of the Ogden syndrome N-terminal acetyltransferase Naa10S37P mutant. Mol. Cell. Proteomics 2014.
    • (2014) Mol. Cell. Proteomics
    • Van Damme, P.1    Støve, S.I.2    Glomnes, N.3    Gevaert, K.4    Arnesen, T.5
  • 282
    • 84961935704 scopus 로고    scopus 로고
    • N-terminal acetylation and replicative age affect proteasome localization and cell fitness during aging
    • van Deventer S., Menendez-Benito V., van Leeuwen F., Neefjes J. N-terminal acetylation and replicative age affect proteasome localization and cell fitness during aging. J. Cell Sci. 2014.
    • (2014) J. Cell Sci.
    • van Deventer, S.1    Menendez-Benito, V.2    van Leeuwen, F.3    Neefjes, J.4
  • 284
    • 44349128482 scopus 로고    scopus 로고
    • Synthetic lethal screens identify gene silencing processes in yeast and implicate the acetylated amino terminus of Sir3 in recognition of the nucleosome core
    • van Welsem T., Frederiks F., Verzijlbergen K.F., Faber A.W., Nelson Z.W., Egan D.A., Gottschling D.E., van Leeuwen F. Synthetic lethal screens identify gene silencing processes in yeast and implicate the acetylated amino terminus of Sir3 in recognition of the nucleosome core. Mol. Cell. Biol. 2008, 28:3861-3872.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 3861-3872
    • van Welsem, T.1    Frederiks, F.2    Verzijlbergen, K.F.3    Faber, A.W.4    Nelson, Z.W.5    Egan, D.A.6    Gottschling, D.E.7    van Leeuwen, F.8
  • 285
    • 79960683356 scopus 로고    scopus 로고
    • The N-end rule pathway and regulation by proteolysis
    • Varshavsky A. The N-end rule pathway and regulation by proteolysis. Protein Sci. 2011, 20:1298-1345.
    • (2011) Protein Sci. , vol.20 , pp. 1298-1345
    • Varshavsky, A.1
  • 287
    • 52949119208 scopus 로고    scopus 로고
    • Crystal structure of RimI from Salmonella typhimurium LT2, the GNAT responsible for N(alpha)-acetylation of ribosomal protein S18
    • Vetting M.W., Bareich D.C., Yu M., Blanchard J.S. Crystal structure of RimI from Salmonella typhimurium LT2, the GNAT responsible for N(alpha)-acetylation of ribosomal protein S18. Protein Sci. 2008, 17:1781-1790.
    • (2008) Protein Sci. , vol.17 , pp. 1781-1790
    • Vetting, M.W.1    Bareich, D.C.2    Yu, M.3    Blanchard, J.S.4
  • 288
    • 84903310310 scopus 로고    scopus 로고
    • Structure of the mammalian ribosome-Sec61 complex to 3.4A resolution
    • Voorhees R.M., Fernandez I.S., Scheres S.H., Hegde R.S. Structure of the mammalian ribosome-Sec61 complex to 3.4A resolution. Cell 2014, 157:1632-1643.
    • (2014) Cell , vol.157 , pp. 1632-1643
    • Voorhees, R.M.1    Fernandez, I.S.2    Scheres, S.H.3    Hegde, R.S.4
  • 289
    • 84876368699 scopus 로고    scopus 로고
    • Nα-acetyltransferase NatA is involved in ribosome synthesis in Saccharomyces cerevisiae
    • Wan K., Tsuchihashi K., Kanda K., Shimoji K., Mizuta K. Nα-acetyltransferase NatA is involved in ribosome synthesis in Saccharomyces cerevisiae. Biosci. Biotechnol. Biochem. 2013, 77:631-638.
    • (2013) Biosci. Biotechnol. Biochem. , vol.77 , pp. 631-638
    • Wan, K.1    Tsuchihashi, K.2    Kanda, K.3    Shimoji, K.4    Mizuta, K.5
  • 290
    • 5144232518 scopus 로고    scopus 로고
    • Importance of the Sir3 N terminus and its acetylation for yeast transcriptional silencing
    • Wang X., Connelly J.J., Wang C.L., Sternglanz R. Importance of the Sir3 N terminus and its acetylation for yeast transcriptional silencing. Genetics 2004, 168:547-551.
    • (2004) Genetics , vol.168 , pp. 547-551
    • Wang, X.1    Connelly, J.J.2    Wang, C.L.3    Sternglanz, R.4
  • 291
    • 33947380146 scopus 로고    scopus 로고
    • Mass spectrometric characterization of the affinity-purified human 26S proteasome complex
    • Wang X., Chen C.F., Baker P.R., Chen P.L., Kaiser P., Huang L. Mass spectrometric characterization of the affinity-purified human 26S proteasome complex. Biochemistry 2007, 46:3553-3565.
    • (2007) Biochemistry , vol.46 , pp. 3553-3565
    • Wang, X.1    Chen, C.F.2    Baker, P.R.3    Chen, P.L.4    Kaiser, P.5    Huang, L.6
  • 292
    • 77958608444 scopus 로고    scopus 로고
    • Drosophila variable nurse cells encodes arrest defective 1 (ARD1), the catalytic subunit of the major N-terminal acetyltransferase complex
    • Wang Y., Mijares M., Gall M.D., Turan T., Javier A., Bornemann D.J., Manage K., Warrior R. Drosophila variable nurse cells encodes arrest defective 1 (ARD1), the catalytic subunit of the major N-terminal acetyltransferase complex. Dev. Dyn. 2010, 239:2813-2827.
    • (2010) Dev. Dyn. , vol.239 , pp. 2813-2827
    • Wang, Y.1    Mijares, M.2    Gall, M.D.3    Turan, T.4    Javier, A.5    Bornemann, D.J.6    Manage, K.7    Warrior, R.8
  • 293
  • 294
    • 84878129207 scopus 로고    scopus 로고
    • Heterochromatin protein Sir3 induces contacts between the amino terminus of histone H4 and nucleosomal DNA
    • Wang F., Li G., Altaf M., Lu C., Currie M.A., Johnson A., Moazed D. Heterochromatin protein Sir3 induces contacts between the amino terminus of histone H4 and nucleosomal DNA. Proc. Natl. Acad. Sci. U. S. A. 2013, 110:8495-8500.
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 8495-8500
    • Wang, F.1    Li, G.2    Altaf, M.3    Lu, C.4    Currie, M.A.5    Johnson, A.6    Moazed, D.7
  • 295
    • 84908325353 scopus 로고    scopus 로고
    • The DAF-16 FOXO transcription factor regulates natc-1 to modulate stress resistance in Caenorhabditis elegans, linking insulin/IGF-1 signaling to protein N-terminal acetylation
    • Warnhoff K., Murphy J.T., Kumar S., Schneider D.L., Peterson M., Hsu S., Guthrie J., Robertson J.D., Kornfeld K. The DAF-16 FOXO transcription factor regulates natc-1 to modulate stress resistance in Caenorhabditis elegans, linking insulin/IGF-1 signaling to protein N-terminal acetylation. PLoS Genet. 2014, 10:e1004703.
    • (2014) PLoS Genet. , vol.10 , pp. e1004703
    • Warnhoff, K.1    Murphy, J.T.2    Kumar, S.3    Schneider, D.L.4    Peterson, M.5    Hsu, S.6    Guthrie, J.7    Robertson, J.D.8    Kornfeld, K.9
  • 296
    • 33646354930 scopus 로고    scopus 로고
    • A conserved motif is prerequisite for the interaction of NAC with ribosomal protein L23 and nascent chains
    • Wegrzyn R.D., Hofmann D., Merz F., Nikolay R., Rauch T., Graf C., Deuerling E. A conserved motif is prerequisite for the interaction of NAC with ribosomal protein L23 and nascent chains. J. Biol. Chem. 2006, 281:2847-2857.
    • (2006) J. Biol. Chem. , vol.281 , pp. 2847-2857
    • Wegrzyn, R.D.1    Hofmann, D.2    Merz, F.3    Nikolay, R.4    Rauch, T.5    Graf, C.6    Deuerling, E.7
  • 297
    • 0022407123 scopus 로고
    • The ARD1 gene of yeast functions in the switch between the mitotic cell cycle and alternative developmental pathways
    • Whiteway M., Szostak J.W. The ARD1 gene of yeast functions in the switch between the mitotic cell cycle and alternative developmental pathways. Cell 1985, 43:483-492.
    • (1985) Cell , vol.43 , pp. 483-492
    • Whiteway, M.1    Szostak, J.W.2
  • 298
    • 0023426588 scopus 로고
    • The yeast ARD1 gene product is required for repression of cryptic mating-type information at the HML locus
    • Whiteway M., Freedman R., Van Arsdell S., Szostak J.W., Thorner J. The yeast ARD1 gene product is required for repression of cryptic mating-type information at the HML locus. Mol. Cell. Biol. 1987, 7:3713-3722.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3713-3722
    • Whiteway, M.1    Freedman, R.2    Van Arsdell, S.3    Szostak, J.W.4    Thorner, J.5
  • 299
    • 0036330852 scopus 로고    scopus 로고
    • The N-acetyltransferase RimJ responds to environmental stimuli to repress pap fimbrial transcription in Escherichia coli
    • White-Ziegler C.A., Black A.M., Eliades S.H., Young S., Porter K. The N-acetyltransferase RimJ responds to environmental stimuli to repress pap fimbrial transcription in Escherichia coli. J. Bacteriol. 2002, 184:4334-4342.
    • (2002) J. Bacteriol. , vol.184 , pp. 4334-4342
    • White-Ziegler, C.A.1    Black, A.M.2    Eliades, S.H.3    Young, S.4    Porter, K.5
  • 300
    • 0344663967 scopus 로고    scopus 로고
    • Two putative acetyltransferases, san and deco, are required for establishing sister chromatid cohesion in Drosophila
    • Williams B.C., Garrett-Engele C.M., Li Z., Williams E.V., Rosenman E.D., Goldberg M.L. Two putative acetyltransferases, san and deco, are required for establishing sister chromatid cohesion in Drosophila. Curr. Biol. 2003, 13:2025-2036.
    • (2003) Curr. Biol. , vol.13 , pp. 2025-2036
    • Williams, B.C.1    Garrett-Engele, C.M.2    Li, Z.3    Williams, E.V.4    Rosenman, E.D.5    Goldberg, M.L.6
  • 302
    • 0036812245 scopus 로고    scopus 로고
    • A genomics-based screen for yeast mutants with an altered recombination/end-joining repair ratio
    • Wilson T.E. A genomics-based screen for yeast mutants with an altered recombination/end-joining repair ratio. Genetics 2002, 162:677-688.
    • (2002) Genetics , vol.162 , pp. 677-688
    • Wilson, T.E.1
  • 303
    • 33745436635 scopus 로고    scopus 로고
    • Identification of N-terminal acetylation of recombinant human prothymosin alpha in Escherichia coli
    • Wu J., Chang S., Gong X., Liu D., Ma Q. Identification of N-terminal acetylation of recombinant human prothymosin alpha in Escherichia coli. Biochim. Biophys. Acta 2006, 1760:1241-1247.
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 1241-1247
    • Wu, J.1    Chang, S.2    Gong, X.3    Liu, D.4    Ma, Q.5
  • 305
    • 77954194681 scopus 로고    scopus 로고
    • Protein N-terminal processing: substrate specificity of Escherichia coli and human methionine aminopeptidases
    • Xiao Q., Zhang F., Nacev B.A., Liu J.O., Pei D. Protein N-terminal processing: substrate specificity of Escherichia coli and human methionine aminopeptidases. Biochemistry 2010, 49:5588-5599.
    • (2010) Biochemistry , vol.49 , pp. 5588-5599
    • Xiao, Q.1    Zhang, F.2    Nacev, B.A.3    Liu, J.O.4    Pei, D.5
  • 306
    • 84864294419 scopus 로고    scopus 로고
    • N-α-acetyltransferase 10 protein inhibits apoptosis through RelA/p65-regulated MCL1 expression
    • Xu H., Jiang B., Meng L., Ren T., Zeng Y., Wu J., Qu L., Shou C. N-α-acetyltransferase 10 protein inhibits apoptosis through RelA/p65-regulated MCL1 expression. Carcinogenesis 2012, 33:1193-1202.
    • (2012) Carcinogenesis , vol.33 , pp. 1193-1202
    • Xu, H.1    Jiang, B.2    Meng, L.3    Ren, T.4    Zeng, Y.5    Wu, J.6    Qu, L.7    Shou, C.8
  • 307
    • 0026092211 scopus 로고
    • Rat liver polysome N alpha-acetyltransferase: isolation and characterization
    • Yamada R., Bradshaw R.A. Rat liver polysome N alpha-acetyltransferase: isolation and characterization. Biochemistry 1991, 30:1010-1016.
    • (1991) Biochemistry , vol.30 , pp. 1010-1016
    • Yamada, R.1    Bradshaw, R.A.2
  • 310
    • 33645322383 scopus 로고    scopus 로고
    • Metastasis-associated protein 1 enhances stability of hypoxia-inducible factor-1alpha protein by recruiting histone deacetylase 1
    • Yoo Y.G., Kong G., Lee M.O. Metastasis-associated protein 1 enhances stability of hypoxia-inducible factor-1alpha protein by recruiting histone deacetylase 1. EMBO J. 2006, 25:1231-1241.
    • (2006) EMBO J. , vol.25 , pp. 1231-1241
    • Yoo, Y.G.1    Kong, G.2    Lee, M.O.3
  • 312
    • 0023427972 scopus 로고
    • Cloning and nucleotide sequencing of the genes rimI and rimJ which encode enzymes acetylating ribosomal proteins S18 and S5 of Escherichia coli K12
    • Yoshikawa A., Isono S., Sheback A., Isono K. Cloning and nucleotide sequencing of the genes rimI and rimJ which encode enzymes acetylating ribosomal proteins S18 and S5 of Escherichia coli K12. Mol. Gen. Genet. 1987, 209:481-488.
    • (1987) Mol. Gen. Genet. , vol.209 , pp. 481-488
    • Yoshikawa, A.1    Isono, S.2    Sheback, A.3    Isono, K.4
  • 314
    • 84875478507 scopus 로고    scopus 로고
    • N-terminal acetylation of the yeast Derlin Der1 is essential for Hrd1 ubiquitin-ligase activity toward luminal ER substrates
    • Zattas D., Adle D.J., Rubenstein E.M., Hochstrasser M. N-terminal acetylation of the yeast Derlin Der1 is essential for Hrd1 ubiquitin-ligase activity toward luminal ER substrates. Mol. Biol. Cell 2013, 24:890-900.
    • (2013) Mol. Biol. Cell , vol.24 , pp. 890-900
    • Zattas, D.1    Adle, D.J.2    Rubenstein, E.M.3    Hochstrasser, M.4
  • 316
    • 84865238560 scopus 로고    scopus 로고
    • NAC functions as a modulator of SRP during the early steps of protein targeting to the endoplasmic reticulum
    • Zhang Y., Berndt U., Gölz H., Tais A., Oellerer S., Wölfle T., Fitzke E., Rospert S. NAC functions as a modulator of SRP during the early steps of protein targeting to the endoplasmic reticulum. Mol. Biol. Cell 2012, 23:3027-3040.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 3027-3040
    • Zhang, Y.1    Berndt, U.2    Gölz, H.3    Tais, A.4    Oellerer, S.5    Wölfle, T.6    Fitzke, E.7    Rospert, S.8
  • 318
    • 84893058636 scopus 로고    scopus 로고
    • In silico identification and characterization of N-terminal acetyltransferase genes of poplar (Populus trichocarpa)
    • Zhu H.Y., Li C.M., Wang L.F., Bai H., Li Y.P., Yu W.X., Xia D.A., Liu C.C. In silico identification and characterization of N-terminal acetyltransferase genes of poplar (Populus trichocarpa). Int. J. Mol. Sci. 2014, 15:1852-1864.
    • (2014) Int. J. Mol. Sci. , vol.15 , pp. 1852-1864
    • Zhu, H.Y.1    Li, C.M.2    Wang, L.F.3    Bai, H.4    Li, Y.P.5    Yu, W.X.6    Xia, D.A.7    Liu, C.C.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.