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Volumn 9, Issue 8, 2013, Pages 475-484

Chemical reporters for biological discovery

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID TRANSFER RNA LIGASE; BACTERIAL PROTEIN; LIPID; NUCLEIC ACID; PHOSPHOPROTEIN; PROTEIN; PROTEIN ARGININE METHYLTRANSFERASE; PROTEIN METHYLTRANSFERASE; PROTEOME; SONIC HEDGEHOG PROTEIN;

EID: 84880891125     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.1296     Document Type: Review
Times cited : (284)

References (100)
  • 2
    • 80052989876 scopus 로고    scopus 로고
    • From mechanism to mouse: A tale of two bioorthogonal reactions
    • Sletten, E.M. & Bertozzi, C.R. From mechanism to mouse: A tale of two bioorthogonal reactions. Acc. Chem. Res. 44, 666-676 (2011
    • (2011) Acc. Chem. Res , vol.44 , pp. 666-676
    • Sletten, E.M.1    Bertozzi, C.R.2
  • 3
    • 77955983759 scopus 로고    scopus 로고
    • Activity-based protein profiling for biochemical pathway discovery in cancer
    • Nomura, D.K., Dix, M.M. & Cravatt, B.F. Activity-based protein profiling for biochemical pathway discovery in cancer. Nat. Rev. Cancer 10, 630-638 (2010
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 630-638
    • Nomura, D.K.1    Dix, M.M.2    Cravatt, B.F.3
  • 4
    • 40649111377 scopus 로고    scopus 로고
    • A chemical method for fast and sensitive detection of DNA synthesis in vivo
    • Salic, A. & Mitchison, T.J. A chemical method for fast and sensitive detection of DNA synthesis in vivo. Proc. Natl. Acad. Sci. USA 105, 2415-2420 (2008
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 2415-2420
    • Salic, A.1    Mitchison, T.J.2
  • 5
    • 57349121991 scopus 로고    scopus 로고
    • Exploring RNA transcription and turnover in vivo by using click chemistry
    • Jao, C.Y. & Salic, A. Exploring RNA transcription and turnover in vivo by using click chemistry. Proc. Natl. Acad. Sci. USA 105, 15779-15784 (2008
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 15779-15784
    • Jao, C.Y.1    Salic, A.2
  • 6
    • 84855517711 scopus 로고    scopus 로고
    • Dynamic metabolic labeling of DNA in vivo with arabinosyl nucleosides
    • Neef, A.B. & Luedtke, N.W. Dynamic metabolic labeling of DNA in vivo with arabinosyl nucleosides. Proc. Natl. Acad. Sci. USA 108, 20404-20409 (2011
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 20404-20409
    • Neef, A.B.1    Luedtke, N.W.2
  • 7
    • 80052762967 scopus 로고    scopus 로고
    • Intracellular detection of cytosine incorporation in genomic DNA by using 5-ethynyl-2′- deoxycytidine
    • Guan, L., van der Heijden, G.W., Bortvin, A. & Greenberg, M.M. Intracellular detection of cytosine incorporation in genomic DNA by using 5-ethynyl-2′- deoxycytidine. ChemBioChem 12, 2184-2190 (2011
    • (2011) ChemBioChem , vol.12 , pp. 2184-2190
    • Guan, L.1    Van Der Heijden, G.W.2    Bortvin, A.3    Greenberg, M.M.4
  • 8
    • 84861446300 scopus 로고    scopus 로고
    • Chemical reporters for monitoring RNA synthesis and poly(A) tail dynamics
    • Grammel, M., Hang, H. & Conrad, N.K. Chemical reporters for monitoring RNA synthesis and poly(A) tail dynamics. ChemBioChem 13, 1112-1115 (2012
    • (2012) ChemBioChem , vol.13 , pp. 1112-1115
    • Grammel, M.1    Hang, H.2    Conrad, N.K.3
  • 9
    • 79955047997 scopus 로고    scopus 로고
    • Imaging of EdU, an alkyne-tagged cell proliferation probe, by Raman microscopy
    • Yamakoshi, H. et al. Imaging of EdU, an alkyne-tagged cell proliferation probe, by Raman microscopy. J. Am. Chem. Soc. 27, 6102-6105 (2011
    • (2011) J. Am. Chem. Soc , vol.27 , pp. 6102-6105
    • Yamakoshi, H.1
  • 10
    • 78651280460 scopus 로고    scopus 로고
    • Selective chemical labeling reveals the genome-wide distribution of 5-hydroxymethylcytosine
    • Song, C.X. et al. Selective chemical labeling reveals the genome-wide distribution of 5-hydroxymethylcytosine. Nat. Biotechnol. 29, 68-72 (2011
    • (2011) Nat. Biotechnol , vol.29 , pp. 68-72
    • Song, C.X.1
  • 11
    • 80052495940 scopus 로고    scopus 로고
    • Tet-mediated formation of 5-carboxylcytosine and its excision by TDG in mammalian DNA
    • He, Y.F. et al. Tet-mediated formation of 5-carboxylcytosine and its excision by TDG in mammalian DNA. Science 333, 1303-1307 (2011
    • (2011) Science , vol.333 , pp. 1303-1307
    • He, Y.F.1
  • 12
    • 80052461558 scopus 로고    scopus 로고
    • Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine
    • Ito, S. et al. Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine. Science 333, 1300-1303 (2011
    • (2011) Science , vol.333 , pp. 1300-1303
    • Ito, S.1
  • 13
    • 77953643054 scopus 로고    scopus 로고
    • Adding new chemistries to the genetic code
    • Liu, C.C. & Schultz, P.G. Adding new chemistries to the genetic code. Annu. Rev. Biochem. 79, 413-444 (2010
    • (2010) Annu. Rev. Biochem , vol.79 , pp. 413-444
    • Liu, C.C.1    Schultz, P.G.2
  • 14
    • 80052570495 scopus 로고    scopus 로고
    • Expanding the genetic code of an animal
    • Greiss, S. & Chin, J.W. Expanding the genetic code of an animal. J. Am. Chem. Soc. 133, 14196-14199 (2011
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 14196-14199
    • Greiss, S.1    Chin, J.W.2
  • 16
    • 84863443015 scopus 로고    scopus 로고
    • Genetic encoding of bicyclononynes and trans-cyclooctenes for site-specific protein labeling in vitro and in live mammalian cells via rapid fluorogenic Diels-Alder reactions
    • Lang, K. et al. Genetic encoding of bicyclononynes and trans-cyclooctenes for site-specific protein labeling in vitro and in live mammalian cells via rapid fluorogenic Diels-Alder reactions. J. Am. Chem. Soc. 134, 10317-10320 (2012
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 10317-10320
    • Lang, K.1
  • 17
    • 78649829465 scopus 로고    scopus 로고
    • Residue-specific incorporation of non-canonical amino acids into proteins: Recent developments and applications
    • Johnson, J.A., Lu, Y.Y., Van Deventer, J.A. & Tirrell, D.A. Residue-specific incorporation of non-canonical amino acids into proteins: Recent developments and applications. Curr. Opin. Chem. Biol. 14, 774-780 (2010
    • (2010) Curr. Opin. Chem. Biol , vol.14 , pp. 774-780
    • Johnson, J.A.1    Lu, Y.Y.2    Van Deventer, J.A.3    Tirrell, D.A.4
  • 18
    • 84862908426 scopus 로고    scopus 로고
    • Imaging protein synthesis in cells and tissues with an alkyne analog of puromycin
    • Liu, J., Xu, Y., Stoleru, D. & Salic, A. Imaging protein synthesis in cells and tissues with an alkyne analog of puromycin. Proc. Natl. Acad. Sci. USA 109, 413-418 (2012
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 413-418
    • Liu, J.1    Xu, Y.2    Stoleru, D.3    Salic, A.4
  • 19
    • 77952996319 scopus 로고    scopus 로고
    • Genome-wide kinetics of nucleosome turnover determined by metabolic labeling of histones
    • Deal, R.B., Henikoff, J.G. & Henikoff, S. Genome-wide kinetics of nucleosome turnover determined by metabolic labeling of histones. Science 328, 1161-1164 (2010
    • (2010) Science , vol.328 , pp. 1161-1164
    • Deal, R.B.1    Henikoff, J.G.2    Henikoff, S.3
  • 20
    • 84867362036 scopus 로고    scopus 로고
    • Selective enrichment of newly synthesized proteins for quantitative secretome analysis
    • Eichelbaum, K., Winter, M., Diaz, M.B., Herzig, S. & Krijgsveld, J. Selective enrichment of newly synthesized proteins for quantitative secretome analysis. Nat. Biotechnol. 30, 984-990 (2012
    • (2012) Nat. Biotechnol , vol.30 , pp. 984-990
    • Eichelbaum, K.1    Winter, M.2    Diaz, M.B.3    Herzig, S.4    Krijgsveld, J.5
  • 21
    • 84875755186 scopus 로고    scopus 로고
    • QuaNCAT: Quantitating proteome dynamics in primary cells
    • Howden, A.J. et al. QuaNCAT: Quantitating proteome dynamics in primary cells. Nat. Methods 10, 343-346 (2013
    • (2013) Nat. Methods , vol.10 , pp. 343-346
    • Howden, A.J.1
  • 22
    • 77954095160 scopus 로고    scopus 로고
    • In situ visualization and dynamics of newly synthesized proteins in rat hippocampal neurons
    • Dieterich, D.C. et al. In situ visualization and dynamics of newly synthesized proteins in rat hippocampal neurons. Nat. Neurosci. 13, 897-905 (2010
    • (2010) Nat. Neurosci , vol.13 , pp. 897-905
    • Dieterich, D.C.1
  • 23
    • 77952486777 scopus 로고    scopus 로고
    • Transmembrane receptor DCC associates with protein synthesis machinery and regulates translation
    • Tcherkezian, J., Brittis, P.A., Thomas, F., Roux, P.P. & Flanagan, J.G. Transmembrane receptor DCC associates with protein synthesis machinery and regulates translation. Cell 141, 632-644 (2010
    • (2010) Cell , vol.141 , pp. 632-644
    • Tcherkezian, J.1    Brittis, P.A.2    Thomas, F.3    Roux, P.P.4    Flanagan, J.G.5
  • 24
    • 70349327398 scopus 로고    scopus 로고
    • Cell-selective metabolic labeling of proteins
    • Ngo, J.T. et al. Cell-selective metabolic labeling of proteins. Nat. Chem. Biol. 5, 715-717 (2009
    • (2009) Nat. Chem. Biol , vol.5 , pp. 715-717
    • Ngo, J.T.1
  • 25
    • 77955575354 scopus 로고    scopus 로고
    • Orthogonal alkynyl amino acid reporter for selective labeling of bacterial proteomes during infection
    • Grammel, M., Zhang, M.M. & Hang, H.C. Orthogonal alkynyl amino acid reporter for selective labeling of bacterial proteomes during infection. Angew. Chem. Int. Ed. Engl. 49, 5970-5974 (2010
    • (2010) Angew. Chem. Int. Ed. Engl , vol.49 , pp. 5970-5974
    • Grammel, M.1    Zhang, M.M.2    Hang, H.C.3
  • 26
    • 84855643309 scopus 로고    scopus 로고
    • Cell-selective labeling of bacterial proteomes with an orthogonal phenylalanine amino acid reporter
    • Grammel, M., Dossa, P.D., Taylor-Salmon, E. & Hang, H.C. Cell-selective labeling of bacterial proteomes with an orthogonal phenylalanine amino acid reporter. Chem. Commun. (Camb.) 48, 1473-1474 (2012
    • (2012) Chem. Commun. (Camb , vol.48 , pp. 1473-1474
    • Grammel, M.1    Dossa, P.D.2    Taylor-Salmon, E.3    Hang, H.C.4
  • 27
    • 0034677879 scopus 로고    scopus 로고
    • Cell surface engineering by a modified staudinger reaction
    • Saxon, E. & Bertozzi, C.R. Cell surface engineering by a modified Staudinger reaction. Science 287, 2007-2010 (2000
    • (2000) Science , vol.287 , pp. 2007-2010
    • Saxon, E.1    Bertozzi, C.R.2
  • 29
    • 0035006049 scopus 로고    scopus 로고
    • Metabolic selection of glycosylation defects in human cells
    • Yarema, K.J., Goon, S. & Bertozzi, C.R. Metabolic selection of glycosylation defects in human cells. Nat. Biotechnol. 19, 553-558 (2001
    • (2001) Nat. Biotechnol , vol.19 , pp. 553-558
    • Yarema, K.J.1    Goon, S.2    Bertozzi, C.R.3
  • 30
    • 43249099890 scopus 로고    scopus 로고
    • In vivo imaging of membrane-associated glycans in developing zebrafish
    • Laughlin, S.T., Baskin, J.M., Amacher, S.L. & Bertozzi, C.R. In vivo imaging of membrane-associated glycans in developing zebrafish. Science 320, 664-667 (2008
    • (2008) Science , vol.320 , pp. 664-667
    • Laughlin, S.T.1    Baskin, J.M.2    Amacher, S.L.3    Bertozzi, C.R.4
  • 31
    • 84858785499 scopus 로고    scopus 로고
    • Clickmediated labeling of bacterial membranes through metabolic modification of the lipopolysaccharide inner core
    • Dumont, A., Malleron, A., Awwad, M., Dukan, S. & Vauzeilles, B. Clickmediated labeling of bacterial membranes through metabolic modification of the lipopolysaccharide inner core. Angew. Chem. Int. Ed. Engl. 51, 3143-3146 (2012
    • (2012) Angew. Chem. Int. Ed. Engl , vol.51 , pp. 3143-3146
    • Dumont, A.1    Malleron, A.2    Awwad, M.3    Dukan, S.4    Vauzeilles, B.5
  • 32
    • 67651173016 scopus 로고    scopus 로고
    • The engineering of bacteria bearing azido-pseudaminic acid-modified flagella
    • Liu, F., Aubry, A.J., Schoenhofen, I.C., Logan, S.M. & Tanner, M.E. The engineering of bacteria bearing azido-pseudaminic acid-modified flagella. ChemBioChem 10, 1317-1320 (2009
    • (2009) ChemBioChem , vol.10 , pp. 1317-1320
    • Liu, F.1    Aubry, A.J.2    Schoenhofen, I.C.3    Logan, S.M.4    Tanner, M.E.5
  • 33
    • 84867050665 scopus 로고    scopus 로고
    • Probing the mycobacterial trehalome with bioorthogonal chemistry
    • Swarts, B.M. et al. Probing the mycobacterial trehalome with bioorthogonal chemistry. J. Am. Chem. Soc. 134, 16123-16126 (2012
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 16123-16126
    • Swarts, B.M.1
  • 34
    • 84856389100 scopus 로고    scopus 로고
    • Metabolic click-labeling with a fucose analog reveals pectin delivery, architecture, and dynamics in Arabidopsis cell walls
    • Anderson, C.T., Wallace, I.S. & Somerville, C.R. Metabolic click-labeling with a fucose analog reveals pectin delivery, architecture, and dynamics in Arabidopsis cell walls. Proc. Natl. Acad. Sci. USA 109, 1329-1334 (2012
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 1329-1334
    • Anderson, C.T.1    Wallace, I.S.2    Somerville, C.R.3
  • 35
    • 79959381299 scopus 로고    scopus 로고
    • Cross talk between O-GlcNAcylation and phosphorylation: Roles in signaling, transcription, and chronic disease
    • Hart, G.W., Slawson, C., Ramirez-Correa, G. & Lagerlof, O. Cross talk between O-GlcNAcylation and phosphorylation: Roles in signaling, transcription, and chronic disease. Annu. Rev. Biochem. 80, 825-858 (2011
    • (2011) Annu. Rev. Biochem , vol.80 , pp. 825-858
    • Hart, G.W.1    Slawson, C.2    Ramirez-Correa, G.3    Lagerlof, O.4
  • 37
    • 79957694784 scopus 로고    scopus 로고
    • Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1
    • Zaro, B.W., Yang, Y.Y., Hang, H.C. & Pratt, M.R. Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1. Proc. Natl. Acad. Sci. USA 108, 8146-8151 (2011
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 8146-8151
    • Zaro, B.W.1    Yang, Y.Y.2    Hang, H.C.3    Pratt, M.R.4
  • 38
    • 38349064791 scopus 로고    scopus 로고
    • Chemical approaches to understanding O-GlcNAc glycosylation in the brain
    • Rexach, J.E., Clark, P.M. & Hsieh-Wilson, L.C. Chemical approaches to understanding O-GlcNAc glycosylation in the brain. Nat. Chem. Biol. 4, 97-106 (2008
    • (2008) Nat. Chem. Biol , vol.4 , pp. 97-106
    • Rexach, J.E.1    Clark, P.M.2    Hsieh-Wilson, L.C.3
  • 39
    • 77955865876 scopus 로고    scopus 로고
    • Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags
    • Rexach, J.E. et al. Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags. Nat. Chem. Biol. 6, 645-651 (2010
    • (2010) Nat. Chem. Biol , vol.6 , pp. 645-651
    • Rexach, J.E.1
  • 40
    • 84857193629 scopus 로고    scopus 로고
    • Dynamic O-GlcNAc modification regulates CREBmediated gene expression and memory formation
    • Rexach, J.E. et al. Dynamic O-GlcNAc modification regulates CREBmediated gene expression and memory formation. Nat. Chem. Biol. 8, 253-261 (2012
    • (2012) Nat. Chem. Biol , vol.8 , pp. 253-261
    • Rexach, J.E.1
  • 41
    • 3343023761 scopus 로고    scopus 로고
    • Deconvoluting the functions of polypeptide N- αacetylgalactosaminyltransferase family members by glycopeptide substrate profiling
    • Pratt, M.R. et al. Deconvoluting the functions of polypeptide N-αacetylgalactosaminyltransferase family members by glycopeptide substrate profiling. Chem. Biol. 11, 1009-1016 (2004
    • (2004) Chem. Biol , vol.11 , pp. 1009-1016
    • Pratt, M.R.1
  • 42
    • 79955390922 scopus 로고    scopus 로고
    • Tracking N-acetyllactosamine on cell-surface glycans in vivo
    • Zheng, T. et al. Tracking N-acetyllactosamine on cell-surface glycans in vivo. Angew. Chem. Int. Ed. Engl. 50, 4113-4118 (2011
    • (2011) Angew. Chem. Int. Ed. Engl , vol.50 , pp. 4113-4118
    • Zheng, T.1
  • 43
    • 33750266831 scopus 로고    scopus 로고
    • Trafficking and signaling by fatty-acylated and prenylated proteins
    • Resh, M.D. Trafficking and signaling by fatty-acylated and prenylated proteins. Nat. Chem. Biol. 2, 584-590 (2006
    • (2006) Nat. Chem. Biol , vol.2 , pp. 584-590
    • Resh, M.D.1
  • 44
    • 80052999602 scopus 로고    scopus 로고
    • Bioorthogonal chemical reporters for analyzing protein lipidation and lipid trafficking
    • Hang, H.C., Wilson, J.P. & Charron, G. Bioorthogonal chemical reporters for analyzing protein lipidation and lipid trafficking. Acc. Chem. Res. 44, 699-708 (2011
    • (2011) Acc. Chem. Res , vol.44 , pp. 699-708
    • Hang, H.C.1    Wilson, J.P.2    Charron, G.3
  • 45
    • 4344584507 scopus 로고    scopus 로고
    • A tagging-via-substrate technology for detection and proteomics of farnesylated proteins
    • Kho, Y. et al. A tagging-via-substrate technology for detection and proteomics of farnesylated proteins. Proc. Natl. Acad. Sci. USA 101, 12479-12484 (2004
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 12479-12484
    • Kho, Y.1
  • 46
    • 78650092789 scopus 로고    scopus 로고
    • Alkynylfarnesol reporters for detection of protein S-prenylation in cells
    • Charron, G., Tsou, L.K., Maguire, W., Yount, J.S. & Hang, H.C. Alkynylfarnesol reporters for detection of protein S-prenylation in cells. Mol. Biosyst. 7, 67-73 (2011
    • (2011) Mol. Biosyst , vol.7 , pp. 67-73
    • Charron, G.1    Tsou, L.K.2    Maguire, W.3    Yount, J.S.4    Hang, H.C.5
  • 47
    • 78349284828 scopus 로고    scopus 로고
    • Evaluation of alkyne-modified isoprenoids as chemical reporters of protein prenylation
    • DeGraw, A.J. et al. Evaluation of alkyne-modified isoprenoids as chemical reporters of protein prenylation. Chem. Biol. Drug Des. 76, 460-471 (2010
    • (2010) Chem. Biol. Drug Des , vol.76 , pp. 460-471
    • DeGraw, A.J.1
  • 48
    • 84879730573 scopus 로고    scopus 로고
    • Prenylome profiling reveals S-farnesylation is crucial for membrane targeting and antiviral activity of ZAP long-isoform
    • Charron, G., Li, M., MacDonald, M. & Hang, H.C. Prenylome profiling reveals S-farnesylation is crucial for membrane targeting and antiviral activity of ZAP long-isoform. Proc. Natl. Acad. Sci. USA http://dx.doi.org/10.1073/ pnas.1302564110 (2013
    • (2013) Proc. Natl. Acad. Sci. USA
    • Charron, G.1    Li, M.2    MacDonald, M.3    Hang, H.C.4
  • 49
    • 84875899190 scopus 로고    scopus 로고
    • Proteolytic elimination of N-myristoyl modifications by the Shigella virulence factor IpaJ
    • Burnaevskiy, N. et al. Proteolytic elimination of N-myristoyl modifications by the Shigella virulence factor IpaJ. Nature 496, 106-109 (2013
    • (2013) Nature , vol.496 , pp. 106-109
    • Burnaevskiy, N.1
  • 50
    • 77249134163 scopus 로고    scopus 로고
    • Protein palmitoylation in neuronal development and synaptic plasticity
    • Fukata, Y. & Fukata, M. Protein palmitoylation in neuronal development and synaptic plasticity. Nat. Rev. Neurosci. 11, 161-175 (2010
    • (2010) Nat. Rev. Neurosci , vol.11 , pp. 161-175
    • Fukata, Y.1    Fukata, M.2
  • 51
    • 59349119386 scopus 로고    scopus 로고
    • Large-scale profiling of protein palmitoylation in mammalian cells
    • Martin, B.R. & Cravatt, B.F. Large-scale profiling of protein palmitoylation in mammalian cells. Nat. Methods 6, 135-138 (2009
    • (2009) Nat. Methods , vol.6 , pp. 135-138
    • Martin, B.R.1    Cravatt, B.F.2
  • 52
    • 79953195562 scopus 로고    scopus 로고
    • Proteomic analysis of fatty-acylated proteins in mammalian cells with chemical reporters reveals S-acylation of histone H3 variants
    • M110.001198
    • Wilson, J.P., Raghavan, A.S., Yang, Y.Y., Charron, G. & Hang, H.C. Proteomic analysis of fatty-acylated proteins in mammalian cells with chemical reporters reveals S-acylation of histone H3 variants. Mol. Cell. Proteomics 10, M110.001198 (2011
    • (2011) Mol. Cell. Proteomics , vol.10
    • Wilson, J.P.1    Raghavan, A.S.2    Yang, Y.Y.3    Charron, G.4    Hang, H.C.5
  • 53
    • 77955892540 scopus 로고    scopus 로고
    • Palmitoylome profiling reveals S-palmitoylation-dependent antiviral activity of IFITM3
    • Yount, J.S. et al. Palmitoylome profiling reveals S-palmitoylation- dependent antiviral activity of IFITM3. Nat. Chem. Biol. 6, 610-614 (2010
    • (2010) Nat. Chem. Biol , vol.6 , pp. 610-614
    • Yount, J.S.1
  • 54
    • 84855253929 scopus 로고    scopus 로고
    • DHHC5 protein palmitoylates flotillin-2 and is rapidly degraded on induction of neuronal differentiation in cultured cells
    • Li, Y., Martin, B.R., Cravatt, B.F. & Hofmann, S.L. DHHC5 protein palmitoylates flotillin-2 and is rapidly degraded on induction of neuronal differentiation in cultured cells. J. Biol. Chem. 287, 523-530 (2012
    • (2012) J. Biol. Chem , vol.287 , pp. 523-530
    • Li, Y.1    Martin, B.R.2    Cravatt, B.F.3    Hofmann, S.L.4
  • 57
    • 84880959257 scopus 로고    scopus 로고
    • Quantitative control protein S-palmitoylation regulates meiotic entry in fission yeast
    • Zhang, C.H., Wu, P-Y.J., Kelly, F.D., Nurse, P. & Hang, H.C. Quantitative control protein S-palmitoylation regulates meiotic entry in fission yeast. PLoS Biol. 11, e1001501 (2013
    • (2013) PLoS Biol , vol.11
    • Zhang, C.H.1    Wu, P.-Y.J.2    Kelly, F.D.3    Nurse, P.4    Hang, H.C.5
  • 58
    • 47749112412 scopus 로고    scopus 로고
    • Lipid-independent secretion of a Drosophila Wnt protein
    • Ching, W., Hang, H.C. & Nusse, R. Lipid-independent secretion of a Drosophila Wnt protein. J. Biol. Chem. 283, 17092-17098 (2008
    • (2008) J. Biol. Chem , vol.283 , pp. 17092-17098
    • Ching, W.1    Hang, H.C.2    Nusse, R.3
  • 59
    • 79955036748 scopus 로고    scopus 로고
    • Bioorthogonal chemical tagging of protein cholesterylation in living cells
    • Heal, W.P. et al. Bioorthogonal chemical tagging of protein cholesterylation in living cells. Chem. Commun. (Camb.) 47, 4081-4083 (2011
    • (2011) Chem. Commun. (Camb , vol.47 , pp. 4081-4083
    • Heal, W.P.1
  • 60
    • 84875881601 scopus 로고    scopus 로고
    • SIRT6 regulates TNF-α secretion through hydrolysis of longchain fatty acyl lysine
    • Jiang, H. et al. SIRT6 regulates TNF-α secretion through hydrolysis of longchain fatty acyl lysine. Nature 496, 110-113 (2013
    • (2013) Nature , vol.496 , pp. 110-113
    • Jiang, H.1
  • 61
    • 70349342948 scopus 로고    scopus 로고
    • Metabolic labeling and direct imaging of choline phospholipids in vivo
    • Jao, C.Y., Roth, M., Welti, R. & Salic, A. Metabolic labeling and direct imaging of choline phospholipids in vivo. Proc. Natl. Acad. Sci. USA 106, 15332-15337 (2009
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 15332-15337
    • Jao, C.Y.1    Roth, M.2    Welti, R.3    Salic, A.4
  • 62
    • 84864202913 scopus 로고    scopus 로고
    • Live-cell imaging of cyclopropene tags with fluorogenic tetrazine cycloadditions
    • Yang, J., Seckute, J., Cole, C.M. & Devaraj, N.K. Live-cell imaging of cyclopropene tags with fluorogenic tetrazine cycloadditions. Angew. Chem. Int. Ed. Engl. 51, 7476-7479 (2012
    • (2012) Angew. Chem. Int. Ed. Engl , vol.51 , pp. 7476-7479
    • Yang, J.1    Seckute, J.2    Cole, C.M.3    Devaraj, N.K.4
  • 63
    • 77249149896 scopus 로고    scopus 로고
    • Capture and release of alkyne-derivatized glycerophospholipids using cobalt chemistry
    • Milne, S.B. et al. Capture and release of alkyne-derivatized glycerophospholipids using cobalt chemistry. Nat. Chem. Biol. 6, 205-207 (2010
    • (2010) Nat. Chem. Biol , vol.6 , pp. 205-207
    • Milne, S.B.1
  • 64
    • 84871534161 scopus 로고    scopus 로고
    • Tracing fatty acid metabolism by click chemistry
    • Thiele, C. et al. Tracing fatty acid metabolism by click chemistry. ACS Chem. Biol. 7, 2004-2011 (2012
    • (2012) ACS Chem. Biol , vol.7 , pp. 2004-2011
    • Thiele, C.1
  • 65
    • 77953754676 scopus 로고    scopus 로고
    • Rapid visualization and large-scale profiling of bacterial lipoproteins with chemical reporters
    • Rangan, K.J., Yang, Y.Y., Charron, G. & Hang, H.C. Rapid visualization and large-scale profiling of bacterial lipoproteins with chemical reporters. J. Am. Chem. Soc. 132, 10628-10629 (2010
    • (2010) J. Am. Chem. Soc , vol.132 , pp. 10628-10629
    • Rangan, K.J.1    Yang, Y.Y.2    Charron, G.3    Hang, H.C.4
  • 66
    • 33645972887 scopus 로고    scopus 로고
    • A database of bacterial lipoproteins (DOLOP) with functional assignments to predicted lipoproteins
    • Babu, M.M. et al. A database of bacterial lipoproteins (DOLOP) with functional assignments to predicted lipoproteins. J. Bacteriol. 188, 2761-2773 (2006
    • (2006) J. Bacteriol , vol.188 , pp. 2761-2773
    • Babu, M.M.1
  • 67
    • 84862573534 scopus 로고    scopus 로고
    • Protein lysine acylation and cysteine succination by intermediates of energy metabolism
    • Lin, H., Su, X. & He, B. Protein lysine acylation and cysteine succination by intermediates of energy metabolism. ACS Chem. Biol. 7, 947-960 (2012
    • (2012) ACS Chem. Biol , vol.7 , pp. 947-960
    • Lin, H.1    Su, X.2    He, B.3
  • 68
    • 77949822323 scopus 로고    scopus 로고
    • Bioorthogonal chemical reporters for monitoring protein acetylation
    • Yang, Y.Y., Ascano, J.M. & Hang, H.C. Bioorthogonal chemical reporters for monitoring protein acetylation. J. Am. Chem. Soc. 132, 3640-3641 (2010
    • (2010) J. Am. Chem. Soc , vol.132 , pp. 3640-3641
    • Yang, Y.Y.1    Ascano, J.M.2    Hang, H.C.3
  • 69
    • 80051787788 scopus 로고    scopus 로고
    • Identification of lysine acetyltransferase p300 substrates using 4-pentynoyl-coenzyme A and bioorthogonal proteomics
    • erratum 21 6613 2011
    • Yang, Y.Y., Grammel, M. & Hang, H.C. Identification of lysine acetyltransferase p300 substrates using 4-pentynoyl-coenzyme A and bioorthogonal proteomics. Bioorg. Med. Chem. Lett. 21, 4976-4979 (2011); erratum 21, 6613 (2011
    • (2011) Bioorg. Med. Chem. Lett , vol.21 , pp. 4976-4979
    • Yang, Y.Y.1    Grammel, M.2    Hang, H.C.3
  • 70
    • 66249126298 scopus 로고    scopus 로고
    • Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans
    • Arnesen, T. et al. Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans. Proc. Natl. Acad. Sci. USA 106, 8157-8162 (2009
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 8157-8162
    • Arnesen, T.1
  • 71
    • 34247869836 scopus 로고    scopus 로고
    • A newly discovered post-translational modification-the acetylation of serine and threonine residues
    • Mukherjee, S., Hao, Y.H. & Orth, K. A newly discovered post-translational modification-the acetylation of serine and threonine residues. Trends Biochem. Sci. 32, 210-216 (2007
    • (2007) Trends Biochem. Sci , vol.32 , pp. 210-216
    • Mukherjee, S.1    Hao, Y.H.2    Orth, K.3
  • 73
    • 84859893371 scopus 로고    scopus 로고
    • Histone methylation: A dynamic mark in health, disease and inheritance
    • Greer, E.L. & Shi, Y. Histone methylation: A dynamic mark in health, disease and inheritance. Nat. Rev. Genet. 13, 343-357 (2012
    • (2012) Nat. Rev. Genet , vol.13 , pp. 343-357
    • Greer, E.L.1    Shi, Y.2
  • 74
    • 33645240950 scopus 로고    scopus 로고
    • Direct transfer of extended groups from synthetic cofactors by DNA methyltransferases
    • Dalhoff, C., Lukinavicius, G., Klimasauskas, S. & Weinhold, E. Direct transfer of extended groups from synthetic cofactors by DNA methyltransferases. Nat. Chem. Biol. 2, 31-32 (2006
    • (2006) Nat. Chem. Biol , vol.2 , pp. 31-32
    • Dalhoff, C.1    Lukinavicius, G.2    Klimasauskas, S.3    Weinhold, E.4
  • 75
    • 77954851029 scopus 로고    scopus 로고
    • Enzymatic site-specific functionalization of protein methyltransferase substrates with alkynes for click labeling
    • Peters, W. et al. Enzymatic site-specific functionalization of protein methyltransferase substrates with alkynes for click labeling. Angew. Chem. Int. Ed. Engl. 49, 5170-5173 (2010
    • (2010) Angew. Chem. Int. Ed. Engl , vol.49 , pp. 5170-5173
    • Peters, W.1
  • 76
    • 79960496067 scopus 로고    scopus 로고
    • Expanding cofactor repertoire of protein lysine methyltransferase for substrate labeling
    • Islam, K., Zheng, W., Yu, H., Deng, H. & Luo, M. Expanding cofactor repertoire of protein lysine methyltransferase for substrate labeling. ACS Chem. Biol. 6, 679-684 (2011
    • (2011) ACS Chem. Biol , vol.6 , pp. 679-684
    • Islam, K.1    Zheng, W.2    Yu, H.3    Deng, H.4    Luo, M.5
  • 77
    • 79957762180 scopus 로고    scopus 로고
    • Labeling substrates of protein arginine methyltransferase with engineered enzymes and matched S-adenosyll- methionine analogues
    • Wang, R., Zheng, W., Yu, H., Deng, H. & Luo, M. Labeling substrates of protein arginine methyltransferase with engineered enzymes and matched S-adenosyll- methionine analogues. J. Am. Chem. Soc. 133, 7648-7651 (2011
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 7648-7651
    • Wang, R.1    Zheng, W.2    Yu, H.3    Deng, H.4    Luo, M.5
  • 78
    • 84872784135 scopus 로고    scopus 로고
    • Profiling genome-wide chromatin methylation with engineered posttranslation apparatus within living cells
    • Wang, R. et al. Profiling genome-wide chromatin methylation with engineered posttranslation apparatus within living cells. J. Am. Chem. Soc. 135, 1048-1056 (2013
    • (2013) J. Am. Chem. Soc , vol.135 , pp. 1048-1056
    • Wang, R.1
  • 79
    • 84861453173 scopus 로고    scopus 로고
    • A selenium-based click AdoMet analogue for versatile substrate labeling with wild-type protein methyltransferases
    • Willnow, S., Martin, M., Luscher, B. & Weinhold, E. A selenium-based click AdoMet analogue for versatile substrate labeling with wild-type protein methyltransferases. ChemBioChem 13, 1167-1173 (2012
    • (2012) ChemBioChem , vol.13 , pp. 1167-1173
    • Willnow, S.1    Martin, M.2    Luscher, B.3    Weinhold, E.4
  • 80
    • 84866414211 scopus 로고    scopus 로고
    • Se-adenosyl-l-selenomethionine cofactor analogue as a reporter of protein methylation
    • Bothwell, I.R. et al. Se-adenosyl-l-selenomethionine cofactor analogue as a reporter of protein methylation. J. Am. Chem. Soc. 134, 14905-14912 (2012
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 14905-14912
    • Bothwell, I.R.1
  • 81
    • 84862758175 scopus 로고    scopus 로고
    • New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs
    • Gibson, B.A. & Kraus, W.L. New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs. Nat. Rev. Mol. Cell Biol. 13, 411-424 (2012
    • (2012) Nat. Rev. Mol. Cell Biol , vol.13 , pp. 411-424
    • Gibson, B.A.1    Kraus, W.L.2
  • 82
    • 77955810108 scopus 로고    scopus 로고
    • Clickable NAD analogues for labeling substrate proteins of poly(ADP-ribose) polymerases
    • Jiang, H., Kim, J.H., Frizzell, K.M., Kraus, W.L. & Lin, H. Clickable NAD analogues for labeling substrate proteins of poly(ADP-ribose) polymerases. J. Am. Chem. Soc. 132, 9363-9372 (2010
    • (2010) J. Am. Chem. Soc , vol.132 , pp. 9363-9372
    • Jiang, H.1    Kim, J.H.2    Frizzell, K.M.3    Kraus, W.L.4    Lin, H.5
  • 83
    • 0035233367 scopus 로고    scopus 로고
    • Recent advances in chemical approaches to the study of biological systems
    • Shogren-Knaak, M.A., Alaimo, P.J. & Shokat, K.M. Recent advances in chemical approaches to the study of biological systems. Annu. Rev. Cell Dev. Biol. 17, 405-433 (2001
    • (2001) Annu. Rev. Cell Dev. Biol , vol.17 , pp. 405-433
    • Shogren-Knaak, M.A.1    Alaimo, P.J.2    Shokat, K.M.3
  • 84
    • 58149400542 scopus 로고    scopus 로고
    • Ampylation of rho gtpases by vibrio vops disrupts effector binding and downstream signaling
    • Yarbrough, M.L. et al. AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling. Science 323, 269-272 (2009
    • (2009) Science , vol.323 , pp. 269-272
    • Yarbrough, M.L.1
  • 86
    • 77955872117 scopus 로고    scopus 로고
    • The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b
    • Müller, M.P. et al. The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b. Science 329, 946-949 (2010
    • (2010) Science , vol.329 , pp. 946-949
    • Müller, M.P.1
  • 87
    • 79960929331 scopus 로고    scopus 로고
    • Legionella pneumophila SidD is a deAMPylase that modifies Rab1
    • Tan, Y. & Luo, Z.Q. Legionella pneumophila SidD is a deAMPylase that modifies Rab1. Nature 475, 506-509 (2011
    • (2011) Nature , vol.475 , pp. 506-509
    • Tan, Y.1    Luo, Z.Q.2
  • 88
    • 80055015456 scopus 로고    scopus 로고
    • A chemical reporter for protein ampylation
    • Grammel, M., Luong, P., Orth, K. & Hang, H.C. A chemical reporter for protein AMPylation. J. Am. Chem. Soc. 133, 17103-17105 (2011
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 17103-17105
    • Grammel, M.1    Luong, P.2    Orth, K.3    Hang, H.C.4
  • 89
    • 65249137629 scopus 로고    scopus 로고
    • Global and site-specific quantitative phosphoproteomics: Principles and applications
    • Macek, B., Mann, M. & Olsen, J.V. Global and site-specific quantitative phosphoproteomics: Principles and applications. Annu. Rev. Pharmacol. Toxicol. 49, 199-221 (2009
    • (2009) Annu. Rev. Pharmacol. Toxicol , vol.49 , pp. 199-221
    • Macek, B.1    Mann, M.2    Olsen, J.V.3
  • 90
    • 34249778657 scopus 로고    scopus 로고
    • A semisynthetic epitope for kinase substrates
    • Allen, J.J. et al. A semisynthetic epitope for kinase substrates. Nat. Methods 4, 511-516 (2007
    • (2007) Nat. Methods , vol.4 , pp. 511-516
    • Allen, J.J.1
  • 91
    • 40349092941 scopus 로고    scopus 로고
    • Covalent capture of kinase-specific phosphopeptides reveals Cdk1-cyclin B substrates
    • Blethrow, J.D., Glavy, J.S., Morgan, D.O. & Shokat, K.M. Covalent capture of kinase-specific phosphopeptides reveals Cdk1-cyclin B substrates. Proc. Natl. Acad. Sci. USA 105, 1442-1447 (2008
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 1442-1447
    • Blethrow, J.D.1    Glavy, J.S.2    Morgan, D.O.3    Shokat, K.M.4
  • 92
    • 83655163927 scopus 로고    scopus 로고
    • Peroxide-dependent sulfenylation of the EGFR catalytic site enhances kinase activity
    • Paulsen, C.E. et al. Peroxide-dependent sulfenylation of the EGFR catalytic site enhances kinase activity. Nat. Chem. Biol. 8, 57-64 (2012
    • (2012) Nat. Chem. Biol , vol.8 , pp. 57-64
    • Paulsen, C.E.1
  • 93
    • 53849105464 scopus 로고    scopus 로고
    • Tetrazine ligation: Fast bioconjugation based on inverse-electron-demand Diels-Alder reactivity.J
    • Blackman, M.L., Royzen, M. & Fox, J.M. Tetrazine ligation: Fast bioconjugation based on inverse-electron-demand Diels-Alder reactivity.J. Am. Chem. Soc. 130, 13518-13519 (2008
    • (2008) Am. Chem. Soc , vol.130 , pp. 13518-13519
    • Blackman, M.L.1    Royzen, M.2    Fox, J.M.3
  • 94
    • 80053031240 scopus 로고    scopus 로고
    • Biomedical applications of tetrazine cycloadditions
    • Devaraj, N.K. & Weissleder, R. Biomedical applications of tetrazine cycloadditions. Acc. Chem. Res. 44, 816-827 (2011
    • (2011) Acc. Chem. Res , vol.44 , pp. 816-827
    • Devaraj, N.K.1    Weissleder, R.2
  • 95
    • 79951821202 scopus 로고    scopus 로고
    • Chemical contrast for imaging living systems: Molecular vibrations drive CARS microscopy
    • Pezacki, J.P. et al. Chemical contrast for imaging living systems: Molecular vibrations drive CARS microscopy. Nat. Chem. Biol. 7, 137-145 (2011
    • (2011) Nat. Chem. Biol , vol.7 , pp. 137-145
    • Pezacki, J.P.1
  • 96
    • 77954649534 scopus 로고    scopus 로고
    • A strategy for the selective imaging of glycans using caged metabolic precursors
    • Chang, P.V., Dube, D.H., Sletten, E.M. & Bertozzi, C.R. A strategy for the selective imaging of glycans using caged metabolic precursors. J. Am. Chem. Soc. 132, 9516-9518 (2010
    • (2010) J. Am. Chem. Soc , vol.132 , pp. 9516-9518
    • Chang, P.V.1    Dube, D.H.2    Sletten, E.M.3    Bertozzi, C.R.4
  • 97
    • 84862518173 scopus 로고    scopus 로고
    • Cell-selective metabolic glycan labeling based on ligand-targeted liposomes
    • Xie, R., Hong, S., Feng, L., Rong, J. & Chen, X. Cell-selective metabolic glycan labeling based on ligand-targeted liposomes. J. Am. Chem. Soc. 134, 9914-9917 (2012
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 9914-9917
    • Xie, R.1    Hong, S.2    Feng, L.3    Rong, J.4    Chen, X.5
  • 98
    • 51049094897 scopus 로고    scopus 로고
    • Cu-catalyzed azide-alkyne cycloaddition
    • Meldal, M. & Tornøe, C.W. Cu-catalyzed azide-alkyne cycloaddition. Chem. Rev. 108, 2952-3015 (2008
    • (2008) Chem. Rev , vol.108 , pp. 2952-3015
    • Meldal, M.1    Tornøe, C.W.2
  • 99
    • 0000096835 scopus 로고    scopus 로고
    • Click chemistry: Diverse chemical function from a few good reactions
    • Kolb, H.C., Finn, M.G. & Sharpless, K.B. Click chemistry: Diverse chemical function from a few good reactions. Angew. Chem. Int. Ed. Engl. 40, 2004-2021 (2001
    • (2001) Angew. Chem. Int. Ed. Engl , vol.40 , pp. 2004-2021
    • Kolb, H.C.1    Finn, M.G.2    Sharpless, K.B.3
  • 100
    • 36749014055 scopus 로고
    • 1,3-Dipolar cycloadditions past and future
    • Huisgen, R. 1,3-Dipolar cycloadditions. past and future. Angew. Chem. Int. Ed. Engl. 2, 565-598 (1963
    • (1963) Angew. Chem. Int. Ed. Engl , vol.2 , pp. 565-598
    • Huisgen, R.1


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