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Volumn 9, Issue 6, 2014, Pages

Most human proteins made in both nucleus and cytoplasm turn over within minutes

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE DERIVATIVE; AMINO ACID; CARBON 13; LEVO AZIDOHOMOALANINE; NITROGEN 15; PUROMYCIN; RNA; UNCLASSIFIED DRUG; MESSENGER RNA; PEPTIDE; PROTEIN;

EID: 84902593560     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0099346     Document Type: Article
Times cited : (21)

References (50)
  • 1
    • 0014960630 scopus 로고
    • Visualization of bacterial genes in action
    • doi: 10.1126/science.169.3943.392
    • Miller OL Jr, Hamkalo BA, Thomas CA Jr (1970) Visualization of bacterial genes in action. Science 169: 392-395. doi: 10.1126/science.169.3943.392.
    • (1970) Science , vol.169 , pp. 392-395
    • Miller Jr., O.L.1    Hamkalo, B.A.2    Thomas Jr., C.A.3
  • 2
    • 0018075458 scopus 로고
    • Does protein synthesis occurs within the nucleus?
    • Goidl JA, Allen WR (1978) Does protein synthesis occurs within the nucleus? Trends Biochem Sci 3: N225-N228.
    • (1978) Trends Biochem Sci , vol.3
    • Goidl, J.A.1    Allen, W.R.2
  • 3
    • 0037099212 scopus 로고    scopus 로고
    • NASty effects on fibrillin pre-mRNA splicing: Another case of ESE does it, but proposals for translation-dependent splice site choice live on
    • doi: 10.1101/gad.1014502
    • Maquat LE (2002) NASty effects on fibrillin pre-mRNA splicing: another case of ESE does it, but proposals for translation-dependent splice site choice live on. Genes Dev 16: 1743-1753. doi: 10.1101/gad.1014502.
    • (2002) Genes Dev , vol.16 , pp. 1743-1753
    • Maquat, L.E.1
  • 4
    • 0035839002 scopus 로고    scopus 로고
    • Coupled transcription and translation within nuclei of mammalian cells
    • DOI 10.1126/science.1061216
    • Iborra FJ, Jackson DA, Cook PR (2001) Coupled transcription and translation within nuclei of mammalian cells. Science 293: 1139-1142. doi: 10.1126/science.1061216. (Pubitemid 32758095)
    • (2001) Science , vol.293 , Issue.5532 , pp. 1139-1142
    • Iborra, F.J.1    Jackson, D.A.2    Cook, P.R.3
  • 5
    • 84860274834 scopus 로고    scopus 로고
    • Nuclear translation visualized by ribosome-bound nascent chain puromycylation
    • doi: 10.1083/jcb.201112145
    • David A, Dolan BP, Hickman HD, Knowlton JJ, Clavarino G, et al. (2012) Nuclear translation visualized by ribosome-bound nascent chain puromycylation. J Cell Biol 197: 45-57. doi: 10.1083/jcb.201112145.
    • (2012) J Cell Biol , vol.197 , pp. 45-57
    • David, A.1    Dolan, B.P.2    Hickman, H.D.3    Knowlton, J.J.4    Clavarino, G.5
  • 6
    • 84887092896 scopus 로고    scopus 로고
    • Visualization of the joining of ribosomal subunits reveals the presence of 80S ribosomes in the nucleus
    • doi: 10.1261/rna.038356.113
    • Al-Jubran K, Wen J, Abdullahi A, Roy Chaudhury S, Li M, et al. (2013) Visualization of the joining of ribosomal subunits reveals the presence of 80S ribosomes in the nucleus. RNA 19: 1669-1683. doi: 10.1261/rna.038356.113.
    • (2013) RNA , vol.19 , pp. 1669-1683
    • Al-Jubran, K.1    Wen, J.2    Abdullahi, A.3    Roy Chaudhury, S.4    Li, M.5
  • 7
    • 84887046208 scopus 로고    scopus 로고
    • Translation of pre-spliced RNAs in the nuclear compartment generates peptides for the MHC class I pathway
    • doi: 10.1073/pnas.1309956110
    • Apcher S, Millot G, Daskalogianni C, Scherl A, Manoury B, et al (2013) Translation of pre-spliced RNAs in the nuclear compartment generates peptides for the MHC class I pathway. Proc Natl Acad Sci USA 110: 17951-17956. doi: 10.1073/pnas.1309956110.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 17951-17956
    • Apcher, S.1    Millot, G.2    Daskalogianni, C.3    Scherl, A.4    Manoury, B.5
  • 8
    • 84887050463 scopus 로고    scopus 로고
    • Nuclear translation for immunosurveillance
    • doi: 10.1073/pnas.1318259110
    • Yewdell JW, David A (2013) Nuclear translation for immunosurveillance. Proc. Natl. Acad. Sci. USA 110: 17612-17613. doi: 10.1073/pnas.1318259110.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 17612-17613
    • Yewdell, J.W.1    David, A.2
  • 9
    • 84863856132 scopus 로고    scopus 로고
    • Nuclear translation or nuclear peptidyl transferase?
    • doi: 10.4161/nucl.20754
    • Dahlberg J, Lund E (2012) Nuclear translation or nuclear peptidyl transferase? Nucleus 3: 320-321. doi: 10.4161/nucl.20754.
    • (2012) Nucleus , vol.3 , pp. 320-321
    • Dahlberg, J.1    Lund, E.2
  • 10
    • 0019218158 scopus 로고
    • Kinetics of degradation of 'short-' and 'long-lived' proteins in cultured mammalian cells
    • DOI 10.1016/0309-1651(80)90045-4
    • Wheatley DN, Giddings MR, Inglis MS (1980) Kinetics of degradation of "short-" and "long-lived" proteins in cultured mammalian cells. Cell Biol Int Rep 4: 1081-1090. doi: 10.1016/0309-1651(80)90045-4. (Pubitemid 11221748)
    • (1980) Cell Biology International Reports , vol.4 , Issue.12 , pp. 1081-1090
    • Wheatley, D.N.1    Giddings, M.R.2    Inglis, M.S.3
  • 11
    • 60849097304 scopus 로고    scopus 로고
    • Turnover of the human proteome: Determination of protein intracellular stability by dynamic SILAC
    • doi: 10.1021/pr800641v
    • Doherty MK, Hammond DE, Clague MJ, Gaskell SJ, Beynon RJ (2009) Turnover of the human proteome: determination of protein intracellular stability by dynamic SILAC. J Proteome Res 8: 104-112. doi: 10.1021/pr800641v.
    • (2009) J Proteome Res , vol.8 , pp. 104-112
    • Doherty, M.K.1    Hammond, D.E.2    Clague, M.J.3    Gaskell, S.J.4    Beynon, R.J.5
  • 12
    • 84857963102 scopus 로고    scopus 로고
    • A quantitative spatial proteomics analysis of proteome turnover in human cells
    • doi: 10.1074/mcp.M111.011429
    • Boisvert FM, Ahmad Y, Gierlinski M, Charriere F, Lamont D, et al. (2012) A quantitative spatial proteomics analysis of proteome turnover in human cells. Mol Cell Proteomics 11: M111011429. doi: 10.1074/mcp.M111.011429.
    • (2012) Mol Cell Proteomics , vol.11
    • Boisvert, F.M.1    Ahmad, Y.2    Gierlinski, M.3    Charriere, F.4    Lamont, D.5
  • 13
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair A, Finley D, Varshavsky A (1986) In vivo half-life of a protein is a function of its amino-terminal residue. Science 234: 179-186. doi: 10.1126/science.3018930. (Pubitemid 17186094)
    • (1986) Science , vol.234 , Issue.4773 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 14
    • 0034703437 scopus 로고    scopus 로고
    • Detecting and measuring cotranslational protein degradation in vivo
    • doi: 10.1126/science.289.5487.2117
    • Turner GC, Varshavsky A (2000) Detecting and measuring cotranslational protein degradation in vivo. Science 289: 2117-2120. doi: 10.1126/science.289. 5487.2117.
    • (2000) Science , vol.289 , pp. 2117-2120
    • Turner, G.C.1    Varshavsky, A.2
  • 15
    • 0028352233 scopus 로고
    • An RNA heresy in the fifties
    • doi: 10.1016/0968-0004(94)90011-6
    • Harris H (1994) An RNA heresy in the fifties. Trends Biochem Sci 19: 303-305. doi: 10.1016/0968-0004(94)90011-6.
    • (1994) Trends Biochem Sci , vol.19 , pp. 303-305
    • Harris, H.1
  • 17
    • 84881225582 scopus 로고    scopus 로고
    • Metabolic labeling with noncanonical amino acids and visualization by chemoselective fluorescent tagging
    • doi: 10.1002/0471143030.cb0711s56
    • Tom Dieck S, Muller A, Nehring A, Hinz FI, Bartnik I, et al. (2012) Metabolic labeling with noncanonical amino acids and visualization by chemoselective fluorescent tagging. Curr Protoc Cell Biol 7: 11. doi: 10.1002/0471143030.cb0711s56.
    • (2012) Curr Protoc Cell Biol , vol.7 , pp. 11
    • Tom Dieck, S.1    Muller, A.2    Nehring, A.3    Hinz, F.I.4    Bartnik, I.5
  • 18
    • 84856064801 scopus 로고    scopus 로고
    • Non-canonical amino acid labeling in vivo to visualize and affinity purify newly synthesized proteins in larval zebrafish
    • doi: 10.1021/cn2000876
    • Hinz FI, Dieterich DC, Tirrell DA, Schuman EM (2012) Non-canonical amino acid labeling in vivo to visualize and affinity purify newly synthesized proteins in larval zebrafish. ACS Chem Neurosci 3: 40-49. doi: 10.1021/cn2000876.
    • (2012) ACS Chem Neurosci , vol.3 , pp. 40-49
    • Hinz, F.I.1    Dieterich, D.C.2    Tirrell, D.A.3    Schuman, E.M.4
  • 20
    • 0038013670 scopus 로고    scopus 로고
    • Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit
    • DOI 10.1016/S0022-2836(03)00668-5
    • Hansen JL, Moore PB, Steitz TA (2003) Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit. J Mol Biol 330: 1061-1075. doi: 10.1016/s0022-2836(03)00668-5. (Pubitemid 36818903)
    • (2003) Journal of Molecular Biology , vol.330 , Issue.5 , pp. 1061-1075
    • Hansen, J.L.1    Moore, P.B.2    Steitz, T.A.3
  • 21
    • 0028884942 scopus 로고
    • A regulatory mechanism that detects premature nonsense codons in T-cell receptor transcripts in vivo is reversed by protein synthesis inhibitors in vitro
    • doi: 10.1074/jbc.270.48.28995
    • Carter MS, Doskow J, Morris JP, Li S, Nhim RP, et al. (1995) A regulatory mechanism that detects premature nonsense codons in T-cell receptor transcripts in vivo is reversed by protein synthesis inhibitors in vitro. J Biol Chem 270: 28995-29003. doi: 10.1074/jbc.270.48.28995.
    • (1995) J Biol Chem , vol.270 , pp. 28995-29003
    • Carter, M.S.1    Doskow, J.2    Morris, J.P.3    Li, S.4    Nhim, R.P.5
  • 22
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB
    • DOI 10.1016/S0092-8674(94)90482-0
    • Palombella VJ, Rando OJ, Goldberg AL, Maniatis T (1994) The ubiquitinproteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB. Cell 78: 773-785. doi: 10.1016/s0092-8674(94)90482-0. (Pubitemid 24294453)
    • (1994) Cell , vol.78 , Issue.5 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 24
    • 0019301036 scopus 로고
    • Evidence for control of protein synthesis in HeLa cells via the elongation rate
    • DOI 10.1002/jcp.1041040302
    • Nielsen PJ, McConkey EH (1980) Evidence for control of protein synthesis in HeLa cells via the elongation rate. J Cell Physiol 104: 269-281. doi: 10.1002/jcp.1041040302. (Pubitemid 11127505)
    • (1980) Journal of Cellular Physiology , vol.104 , Issue.3 , pp. 269-281
    • Nielsen, P.J.1    McConkey, E.H.2
  • 25
    • 63949084607 scopus 로고    scopus 로고
    • SUnSET, a nonradioactive method to monitor protein synthesis
    • doi: 10.1038/nmeth.1314
    • Schmidt EK, Clavarino G, Ceppi M, Pierre P (2009) SUnSET, a nonradioactive method to monitor protein synthesis. Nat Methods 6: 275-277. doi: 10.1038/nmeth.1314.
    • (2009) Nat Methods , vol.6 , pp. 275-277
    • Schmidt, E.K.1    Clavarino, G.2    Ceppi, M.3    Pierre, P.4
  • 26
    • 0013936848 scopus 로고
    • Vectorial discharge of peptides released by puromycin from attached ribosomes
    • doi: 10.1073/pnas.56.2.608
    • Redman CM, Sabatini DD (1966) Vectorial discharge of peptides released by puromycin from attached ribosomes. Proc Natl Acad Sci USA 56: 608-615. doi: 10.1073/pnas.56.2.608.
    • (1966) Proc Natl Acad Sci USA , vol.56 , pp. 608-615
    • Redman, C.M.1    Sabatini, D.D.2
  • 27
    • 0019420560 scopus 로고
    • Very low density lipoprotein synthesis and secretion. Extrusion of apoprotein B nascent chains through the membrane of the endoplasmic reticulum without protein synthesis
    • Siuta-Mangano P, Lane MD (1981) Very low density lipoprotein synthesis and secretion. Extrusion of apoprotein B nascent chains through the membrane of the endoplasmic reticulum without protein synthesis. J Biol Chem 256: 2094-2097. (Pubitemid 11151461)
    • (1981) Journal of Biological Chemistry , vol.256 , Issue.5 , pp. 2094-2097
    • Siuta-Mangano, P.1    Lane, M.D.2
  • 28
    • 67650315227 scopus 로고    scopus 로고
    • Advances in imaging secondary ion mass spectrometry for biological samples
    • doi: 10.1146/annurev.biophys.050708.133634
    • Boxer SG, Kraft ML, Weber PK (2009) Advances in imaging secondary ion mass spectrometry for biological samples. Annu Rev Biophys 38: 53-74. doi: 10.1146/annurev.biophys.050708.133634.
    • (2009) Annu Rev Biophys , vol.38 , pp. 53-74
    • Boxer, S.G.1    Kraft, M.L.2    Weber, P.K.3
  • 30
    • 44149106396 scopus 로고    scopus 로고
    • Similar active genes cluster in specialized transcription factories
    • DOI 10.1083/jcb.200710053
    • Xu M, Cook PR (2008) Similar active genes cluster in specialized transcription factories. J Cell Biol 181: 615-623. doi: 10.1083/jcb.200710053. (Pubitemid 351717509)
    • (2008) Journal of Cell Biology , vol.181 , Issue.4 , pp. 615-623
    • Xu, M.1    Cook, P.R.2
  • 31
    • 1642303746 scopus 로고    scopus 로고
    • Molecular cross-talk between the transcription, translation, and nonsense-mediated decay machineries
    • DOI 10.1242/jcs.00933
    • Iborra FJ, Escargueil AE, Kwek KY, Akoulitchev A, Cook PR (2004) Molecular cross-talk between the transcription, translation, and nonsense-mediated decay machineries. J Cell Sci 117: 899-906. doi: 10.1242/jcs.00933. (Pubitemid 38386947)
    • (2004) Journal of Cell Science , vol.117 , Issue.6 , pp. 899-906
    • Iborra, F.J.1    Escargueil, A.E.2    Kwek, K.Y.3    Akoulitchev, A.4    Cook, P.R.5
  • 32
    • 84890016562 scopus 로고    scopus 로고
    • Genome-wide map of nuclear protein degradation shows NCoR1 turnover as a key to mitochondrial gene regulation
    • doi: 10.1016/j.cell.2013.11.016
    • Catic A, Suh CY, Hill CT, Daheron L, Henkel T, et al. (2013) Genome-wide map of nuclear protein degradation shows NCoR1 turnover as a key to mitochondrial gene regulation. Cell 155: 1380-1395. doi: 10.1016/j.cell.2013.11. 016.
    • (2013) Cell , vol.155 , pp. 1380-1395
    • Catic, A.1    Suh, C.Y.2    Hill, C.T.3    Daheron, L.4    Henkel, T.5
  • 33
    • 0033525169 scopus 로고    scopus 로고
    • A perfect message: RNA surveillance and nonsense-mediated decay
    • DOI 10.1016/S0092-8674(00)80542-5
    • Hentze MW, Kulozik AE (1999) A perfect message: RNA surveillance and nonsense-mediated decay. Cell 96: 307-310. doi: 10.1016/s0092-8674(00)80542-5. (Pubitemid 29077583)
    • (1999) Cell , vol.96 , Issue.3 , pp. 307-310
    • Hentze, M.W.1    Kulozik, A.E.2
  • 35
    • 9244234513 scopus 로고    scopus 로고
    • Biosynthesis of nonribosomal peptides
    • DOI 10.1146/annurev.micro.58.030603.123615
    • Finking R, Marahiel MA (2004) Biosynthesis of nonribosomal peptides. Annu Rev Microbiol 58: 453-488. doi: 10.1146/annurev.micro.58.030603.123615. (Pubitemid 39551994)
    • (2004) Annual Review of Microbiology , vol.58 , pp. 453-488
    • Finking, R.1    Marahiel, M.A.2
  • 36
    • 79958766636 scopus 로고    scopus 로고
    • Translating DRiPs: Progress in understanding viral and cellular sources of MHC class I peptide ligands
    • doi: 10.1007/s00018-011-0656-z
    • Dolan BP, Bennink JR, Yewdell JW (2011) Translating DRiPs: progress in understanding viral and cellular sources of MHC class I peptide ligands. Cell Mol Life Sci 68: 1481-1489. doi: 10.1007/s00018-011-0656-z.
    • (2011) Cell Mol Life Sci , vol.68 , pp. 1481-1489
    • Dolan, B.P.1    Bennink, J.R.2    Yewdell, J.W.3
  • 37
    • 84985240052 scopus 로고
    • Comparison of the abilities of trichloroacetic, picric, sulfosalicylic, and tungstic acids to precipitate protein hydrolysates and proteins
    • doi: 10.1111/j.1365-2621.1979.tb08487.x
    • Greenberg NA, Shipe WF (1979) Comparison of the abilities of trichloroacetic, picric, sulfosalicylic, and tungstic acids to precipitate protein hydrolysates and proteins. J Food Sci 44: 735-737. doi: 10.1111/j.1365-2621.1979.tb08487.x.
    • (1979) J Food Sci , vol.44 , pp. 735-737
    • Greenberg, N.A.1    Shipe, W.F.2
  • 38
    • 33745833084 scopus 로고    scopus 로고
    • The DRiP hypothesis decennial: Support, controversy, refinement and extension
    • DOI 10.1016/j.it.2006.06.008, PII S1471490606001785
    • Yewdell JW, Nicchitta CV (2006) The DRiP hypothesis decennial: support, controversy, refinement and extension. Trends Immunol 27: 368-373. doi: 10.1016/j.it.2006.06.008. (Pubitemid 44038666)
    • (2006) Trends in Immunology , vol.27 , Issue.8 , pp. 368-373
    • Yewdell, J.W.1    Nicchitta, C.V.2
  • 39
    • 84856815566 scopus 로고    scopus 로고
    • The role of mRNA translation in direct MHC class I antigen presentation
    • doi: 10.1016/j.coi.2012.01.007
    • Apcher S, Manoury B, Fahraeus R (2012) The role of mRNA translation in direct MHC class I antigen presentation. Curr Opin Immunol 24: 71-76. doi: 10.1016/j.coi.2012.01.007.
    • (2012) Curr Opin Immunol , vol.24 , pp. 71-76
    • Apcher, S.1    Manoury, B.2    Fahraeus, R.3
  • 40
    • 66149123741 scopus 로고    scopus 로고
    • Direct detection of abortive RNA transcripts in vivo
    • doi: 10.1126/science.1169237
    • Goldman SR, Ebright RH, Nickels BE (2009) Direct detection of abortive RNA transcripts in vivo. Science 324: 927-928. doi: 10.1126/science.1169237.
    • (2009) Science , vol.324 , pp. 927-928
    • Goldman, S.R.1    Ebright, R.H.2    Nickels, B.E.3
  • 41
    • 57849140661 scopus 로고    scopus 로고
    • Divergent transcription from active promoters
    • doi: 10.1126/science.1162253
    • Seila AC, Calabrese JM, Levine SS, Yeo GW, Rahl PB, et al. (2008) Divergent transcription from active promoters. Science 322: 1849-1851. doi: 10.1126/science.1162253.
    • (2008) Science , vol.322 , pp. 1849-1851
    • Seila, A.C.1    Calabrese, J.M.2    Levine, S.S.3    Yeo, G.W.4    Rahl, P.B.5
  • 42
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • doi: 10.1038/nrm2838
    • Jackson RJ, Hellen CU, Pestova TV (2010) The mechanism of eukaryotic translation initiation and principles of its regulation. Nat Rev Mol Cell Biol 11: 113-127. doi: 10.1038/nrm2838.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.2    Pestova, T.V.3
  • 43
    • 81055155799 scopus 로고    scopus 로고
    • Ribosome profiling of mouse embryonic stem cells reveals the complexity and dynamics of mammalian proteomes
    • doi: 10.1016/j.cell.2011.10.002
    • Ingolia NT, Lareau LF, Weissman JS (2011) Ribosome profiling of mouse embryonic stem cells reveals the complexity and dynamics of mammalian proteomes. Cell 147: 789-802. doi: 10.1016/j.cell.2011.10.002.
    • (2011) Cell , vol.147 , pp. 789-802
    • Ingolia, N.T.1    Lareau, L.F.2    Weissman, J.S.3
  • 44
    • 84868315457 scopus 로고    scopus 로고
    • Genome-wide search for novel human uORFs and N-terminal protein extensions using ribosomal footprinting
    • doi: 10.1101/gr.139568.112
    • Fritsch C, Herrmann A, Nothnagel M, Szafranski K, Huse K, et al. (2012) Genome-wide search for novel human uORFs and N-terminal protein extensions using ribosomal footprinting. Genome Res 22: 2208-2218. doi: 10.1101/gr.139568.112.
    • (2012) Genome Res , vol.22 , pp. 2208-2218
    • Fritsch, C.1    Herrmann, A.2    Nothnagel, M.3    Szafranski, K.4    Huse, K.5
  • 45
    • 66149118241 scopus 로고    scopus 로고
    • Upstream open reading frames cause widespread reduction of protein expression and are polymorphic among humans
    • doi: 10.1073/pnas.0810916106
    • Calvo SE, Pagliarini DJ, Mootha VK (2009) Upstream open reading frames cause widespread reduction of protein expression and are polymorphic among humans. Proc Natl Acad Sci USA 106: 7507-7512. doi: 10.1073/pnas.0810916106.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 7507-7512
    • Calvo, S.E.1    Pagliarini, D.J.2    Mootha, V.K.3
  • 46
    • 84866267681 scopus 로고    scopus 로고
    • Global mapping of translation initiation sites in mammalian cells at single-nucleotide resolution
    • doi: 10.1073/pnas.1207846109
    • Lee S, Liu B, Lee S, Huang SX, Shen B, et al. (2012) Global mapping of translation initiation sites in mammalian cells at single-nucleotide resolution. Proc Natl Acad Sci USA 109: E2424-E2432. doi: 10.1073/pnas.1207846109.
    • (2012) Proc Natl Acad Sci USA , vol.109
    • Lee, S.1    Liu, B.2    Lee, S.3    Huang, S.X.4    Shen, B.5
  • 47
    • 84870238817 scopus 로고    scopus 로고
    • Dark matter RNA: Existence, function, and controversy
    • doi: 10.3389/fgene.2012.00060
    • Kapranov P, St Laurent G (2012) Dark matter RNA: existence, function, and controversy. Front Genet 3: 60. doi: 10.3389/fgene.2012.00060.
    • (2012) Front Genet , vol.3 , pp. 60
    • Kapranov, P.1    St Laurent, G.2
  • 49
    • 78650590308 scopus 로고    scopus 로고
    • Cleavable biotin probes for labeling biomolecules via azide-alkyne cycloaddition
    • doi: 10.1021/ja1083909
    • Szychowski J, Mahdavi A, Hodas JJ, Bagert JD, Ngo JT, et al. (2010) Cleavable biotin probes for labeling biomolecules via azide-alkyne cycloaddition. J Am Chem Soc 132: 18351-18360. doi: 10.1021/ja1083909.
    • (2010) J Am Chem Soc , vol.132 , pp. 18351-18360
    • Szychowski, J.1    Mahdavi, A.2    Hodas, J.J.3    Bagert, J.D.4    Ngo, J.T.5
  • 50
    • 77955047663 scopus 로고    scopus 로고
    • Active RNA polymerases: Mobile or immobile molecular machines?
    • doi: 10.1371/journal.pbio.1000419
    • Papantonis A, Larkin JD, Wada Y, Ohta Y, Ihara S, et al. (2010) Active RNA polymerases: mobile or immobile molecular machines? PLoS Biol 8: e1000419. doi: 10.1371/journal.pbio.1000419.
    • (2010) PLoS Biol , vol.8
    • Papantonis, A.1    Larkin, J.D.2    Wada, Y.3    Ohta, Y.4    Ihara, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.