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Volumn 7, Issue 1, 2014, Pages

Phosphorylation and arginine methylation mark histone H2A prior to deposition during Xenopus laevis development

Author keywords

Early development; H2A; Histone arginine methylation; Histone deposition; Histone phosphorylation; Histones; Xenopus laevis

Indexed keywords

ARGININE; HISTONE H2A; HISTONE H2AX; HISTONE H4; SERINE;

EID: 84907985742     PISSN: None     EISSN: 17568935     Source Type: Journal    
DOI: 10.1186/1756-8935-7-22     Document Type: Article
Times cited : (23)

References (50)
  • 1
    • 84884665362 scopus 로고    scopus 로고
    • Histone modifications and mitosis: Countermarks, landmarks, and bookmarks
    • 23246430
    • Histone modifications and mitosis: countermarks, landmarks, and bookmarks. Wang F, Higgins JM, Trends Cell Biol 2013 23 175 184 10.1016/j.tcb.2012.11.005 23246430
    • (2013) Trends Cell Biol , vol.23 , pp. 175-184
    • Wang, F.1    Higgins, J.M.2
  • 2
    • 84877815977 scopus 로고    scopus 로고
    • Genetic and epigenetic determinants of DNA replication origins, position and activation
    • 23541525
    • Genetic and epigenetic determinants of DNA replication origins, position and activation. Mechali M, Yoshida K, Coulombe P, Pasero P, Curr Opin Genet Dev 2013 23 124 131 10.1016/j.gde.2013.02.010 23541525
    • (2013) Curr Opin Genet Dev , vol.23 , pp. 124-131
    • Mechali, M.1    Yoshida, K.2    Coulombe, P.3    Pasero, P.4
  • 3
    • 35848961668 scopus 로고    scopus 로고
    • How chromatin-binding modules interpret histone modifications: Lessons from professional pocket pickers
    • 17984965
    • How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers. Taverna S, Li H, Ruthenburg A, Allis C, Patel D, Nat Struct Mol Biol 2007 14 1025 1040 10.1038/nsmb1338 17984965
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 1025-1040
    • Taverna, S.1    Li, H.2    Ruthenburg, A.3    Allis, C.4    Patel, D.5
  • 4
    • 36448949026 scopus 로고    scopus 로고
    • Multivalent engagement of chromatin modifications by linked binding modules
    • 18037899
    • Multivalent engagement of chromatin modifications by linked binding modules. Ruthenburg A, Li H, Patel D, Allis C, Nat Rev Mol Cell Biol 2007 8 983 994 10.1038/nrm2298 18037899
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 983-994
    • Ruthenburg, A.1    Li, H.2    Patel, D.3    Allis, C.4
  • 6
    • 59449108085 scopus 로고    scopus 로고
    • Analysis of histones in Xenopus laevis. I. A distinct index of enriched variants and modifications exists in each cell type and is remodeled during developmental transitions
    • 18957438
    • Analysis of histones in Xenopus laevis. I. A distinct index of enriched variants and modifications exists in each cell type and is remodeled during developmental transitions. Shechter D, Nicklay JJ, Chitta RK, Shabanowitz J, Hunt DF, Allis CD, J Biol Chem 2009 284 1064 1074 10.1074/jbc.M807273200 18957438
    • (2009) J Biol Chem , vol.284 , pp. 1064-1074
    • Shechter, D.1    Nicklay, J.J.2    Chitta, R.K.3    Shabanowitz, J.4    Hunt, D.F.5    Allis, C.D.6
  • 7
    • 0033200205 scopus 로고    scopus 로고
    • The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSK1 as a potential histone H3/HMG-14 kinase
    • 10469656
    • The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSK1 as a potential histone H3/HMG-14 kinase. Thomson S, Clayton AL, Hazzalin CA, Rose S, Barratt MJ, Mahadevan LC, EMBO J 1999 18 4779 4793 10.1093/emboj/18.17.4779 10469656
    • (1999) EMBO J , vol.18 , pp. 4779-4793
    • Thomson, S.1    Clayton, A.L.2    Hazzalin, C.A.3    Rose, S.4    Barratt, M.J.5    Mahadevan, L.C.6
  • 8
    • 2542440487 scopus 로고    scopus 로고
    • Phosphorylation of histone H2A inhibits transcription on chromatin templates
    • 15010469
    • Phosphorylation of histone H2A inhibits transcription on chromatin templates. Zhang Y, Griffin K, Mondal N, Parvin JD, J Biol Chem 2004 279 21866 21872 10.1074/jbc.M400099200 15010469
    • (2004) J Biol Chem , vol.279 , pp. 21866-21872
    • Zhang, Y.1    Griffin, K.2    Mondal, N.3    Parvin, J.D.4
  • 10
    • 77955810447 scopus 로고    scopus 로고
    • Genome-wide mapping of histone H4 serine-1 phosphorylation during sporulation in Saccharomyces cerevisiae
    • 20375100
    • Genome-wide mapping of histone H4 serine-1 phosphorylation during sporulation in Saccharomyces cerevisiae. Govin J, Schug J, Krishnamoorthy T, Dorsey J, Khochbin S, Berger SL, Nucleic Acids Res 2010 38 4599 4606 10.1093/nar/gkq218 20375100
    • (2010) Nucleic Acids Res , vol.38 , pp. 4599-4606
    • Govin, J.1    Schug, J.2    Krishnamoorthy, T.3    Dorsey, J.4    Khochbin, S.5    Berger, S.L.6
  • 11
    • 0035980018 scopus 로고    scopus 로고
    • PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins
    • 11413150
    • PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins. Branscombe TL, Frankel A, Lee JH, Cook JR, Yang Z, Pestka S, Clarke S, J Biol Chem 2001 276 32971 32976 10.1074/jbc.M105412200 11413150
    • (2001) J Biol Chem , vol.276 , pp. 32971-32976
    • Branscombe, T.L.1    Frankel, A.2    Lee, J.H.3    Cook, J.R.4    Yang, Z.5    Pestka, S.6    Clarke, S.7
  • 12
    • 0033615656 scopus 로고    scopus 로고
    • The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity
    • 10531356
    • The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity. Pollack BP, Kotenko SV, He W, Izotova LS, Barnoski BL, Pestka S, J Biol Chem 1999 274 31531 31542 10.1074/jbc.274.44.31531 10531356
    • (1999) J Biol Chem , vol.274 , pp. 31531-31542
    • Pollack, B.P.1    Kotenko, S.V.2    He, W.3    Izotova, L.S.4    Barnoski, B.L.5    Pestka, S.6
  • 13
    • 58149295717 scopus 로고    scopus 로고
    • Protein arginine methylation in mammals: Who, what, and why
    • 19150423
    • Protein arginine methylation in mammals: who, what, and why. Bedford MT, Clarke SG, Mol Cell 2009 33 1 13 10.1016/j.molcel.2008.12.013 19150423
    • (2009) Mol Cell , vol.33 , pp. 1-13
    • Bedford, M.T.1    Clarke, S.G.2
  • 14
    • 79960696358 scopus 로고    scopus 로고
    • Stage-specific histone modification profiles reveal global transitions in the Xenopus embryonic epigenome
    • 21814581
    • Stage-specific histone modification profiles reveal global transitions in the Xenopus embryonic epigenome. Schneider TD, Arteaga-Salas JM, Mentele E, David R, Nicetto D, Imhof A, Rupp RA, PLoS One 2011 6 22548 10.1371/journal.pone.0022548 21814581
    • (2011) PLoS One , vol.6 , pp. 522548
    • Schneider, T.D.1    Arteaga-Salas, J.M.2    Mentele, E.3    David, R.4    Nicetto, D.5    Imhof, A.6    Rupp, R.A.7
  • 15
    • 58849129850 scopus 로고    scopus 로고
    • A distinct H2A.X isoform is enriched in Xenopus laevis eggs and early embryos and is phosphorylated in the absence of a checkpoint
    • 19131518
    • A distinct H2A.X isoform is enriched in Xenopus laevis eggs and early embryos and is phosphorylated in the absence of a checkpoint. Shechter D, Chitta RK, Xiao A, Shabanowitz J, Hunt DF, Allis CD, Proc Natl Acad Sci U S A 2009 106 749 754 10.1073/pnas.0812207106 19131518
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 749-754
    • Shechter, D.1    Chitta, R.K.2    Xiao, A.3    Shabanowitz, J.4    Hunt, D.F.5    Allis, C.D.6
  • 17
    • 77951877310 scopus 로고    scopus 로고
    • Analysis of histones and chromatin in Xenopus laevis egg and oocyte extracts
    • 20051265
    • Analysis of histones and chromatin in Xenopus laevis egg and oocyte extracts. Banaszynski LA, Allis CD, Shechter D, Methods 2010 51 3 10 10.1016/j.ymeth.2009.12.014 20051265
    • (2010) Methods , vol.51 , pp. 3-10
    • Banaszynski, L.A.1    Allis, C.D.2    Shechter, D.3
  • 18
    • 0031922636 scopus 로고    scopus 로고
    • Control of gene expression in Xenopus early development
    • 9581284
    • Control of gene expression in Xenopus early development. Hair A, Prioleau MN, Vassetzky Y, Mechali M, Dev Genet 1998 22 122 131 10.1002/(SICI)1520-6408(1998)22:2<122::AID-DVG2>3.0.CO;2-8 9581284
    • (1998) Dev Genet , vol.22 , pp. 122-131
    • Hair, A.1    Prioleau, M.N.2    Vassetzky, Y.3    Mechali, M.4
  • 19
    • 0032511148 scopus 로고    scopus 로고
    • Geminin, an inhibitor of DNA replication, is degraded during mitosis
    • Geminin, an inhibitor of DNA replication, is degraded during mitosis. McGarry TJ, Kirschner MW, Cell 1998 93 1043 1053 10.1016/S0092-8674(00)81209-X 9635433
    • (1998) Cell , vol.93 , pp. 1043-1053
    • McGarry, T.J.1    Kirschner, M.W.2
  • 20
    • 0032560517 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 at serine 10 is correlated with chromosome condensation during mitosis and meiosis in Tetrahymena
    • 9636175
    • Phosphorylation of histone H3 at serine 10 is correlated with chromosome condensation during mitosis and meiosis in Tetrahymena. Wei Y, Mizzen CA, Cook RG, Gorovsky MA, Allis CD, Proc Natl Acad Sci U S A 1998 95 7480 7484 10.1073/pnas.95.13.7480 9636175
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 7480-7484
    • Wei, Y.1    Mizzen, C.A.2    Cook, R.G.3    Gorovsky, M.A.4    Allis, C.D.5
  • 21
    • 0033515426 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 is required for proper chromosome condensation and segregation
    • 10199406
    • Phosphorylation of histone H3 is required for proper chromosome condensation and segregation. Wei Y, Yu L, Bowen J, Gorovsky MA, Allis CD, Cell 1999 97 99 109 10.1016/S0092-8674(00)80718-7 10199406
    • (1999) Cell , vol.97 , pp. 99-109
    • Wei, Y.1    Yu, L.2    Bowen, J.3    Gorovsky, M.A.4    Allis, C.D.5
  • 22
    • 18144370095 scopus 로고    scopus 로고
    • Serine 31 phosphorylation of histone variant H3.3 is specific to regions bordering centromeres in metaphase chromosomes
    • 15851689
    • Serine 31 phosphorylation of histone variant H3.3 is specific to regions bordering centromeres in metaphase chromosomes. Hake S, Garcia B, Kauer M, Baker S, Shabanowitz J, Hunt D, Allis C, Proc Natl Acad Sci U S A 2005 102 6344 6349 10.1073/pnas.0502413102 15851689
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 6344-6349
    • Hake, S.1    Garcia, B.2    Kauer, M.3    Baker, S.4    Shabanowitz, J.5    Hunt, D.6    Allis, C.7
  • 24
    • 84870352601 scopus 로고    scopus 로고
    • Vertebrate nucleoplasmin and NASP: Egg histone storage proteins with multiple
    • 22968912
    • Vertebrate nucleoplasmin and NASP: egg histone storage proteins with multiple. Finn RM, Ellard K, Eirin-Lopez JM, Ausio J, FASEB J 2012 26 4788 4804 10.1096/fj.12-216663 22968912
    • (2012) FASEB J , vol.26 , pp. 4788-4804
    • Finn, R.M.1    Ellard, K.2    Eirin-Lopez, J.M.3    Ausio, J.4
  • 25
    • 79955029493 scopus 로고    scopus 로고
    • Epigenetic reprogramming and development: A unique heterochromatin organization in the preimplantation mouse embryo
    • 21186177
    • Epigenetic reprogramming and development: a unique heterochromatin organization in the preimplantation mouse embryo. Burton A, Torres-Padilla ME, Brief Funct Genomics 2010 9 444 454 10.1093/bfgp/elq027 21186177
    • (2010) Brief Funct Genomics , vol.9 , pp. 444-454
    • Burton, A.1    Torres-Padilla, M.E.2
  • 26
    • 33846226977 scopus 로고    scopus 로고
    • Histone arginine methylation regulates pluripotency in the early mouse embryo
    • 17215844
    • Histone arginine methylation regulates pluripotency in the early mouse embryo. Torres-Padilla ME, Parfitt DE, Kouzarides T, Zernicka-Goetz M, Nature 2007 445 214 218 10.1038/nature05458 17215844
    • (2007) Nature , vol.445 , pp. 214-218
    • Torres-Padilla, M.E.1    Parfitt, D.E.2    Kouzarides, T.3    Zernicka-Goetz, M.4
  • 27
    • 78650212707 scopus 로고    scopus 로고
    • Prmt5 is essential for early mouse development and acts in the cytoplasm to maintain ES cell pluripotency
    • 21159818
    • Prmt5 is essential for early mouse development and acts in the cytoplasm to maintain ES cell pluripotency. Tee WW, Pardo M, Theunissen TW, Yu L, Choudhary JS, Hajkova P, Surani MA, Genes Dev 2010 24 2772 2777 10.1101/gad.606110 21159818
    • (2010) Genes Dev , vol.24 , pp. 2772-2777
    • Tee, W.W.1    Pardo, M.2    Theunissen, T.W.3    Yu, L.4    Choudhary, J.S.5    Hajkova, P.6    Surani, M.A.7
  • 28
    • 59449086329 scopus 로고    scopus 로고
    • Analysis of histones in Xenopus laevis. II. Mass spectrometry reveals an index of cell type-specific modifications on H3 and H4
    • 18957437
    • Analysis of histones in Xenopus laevis. II. mass spectrometry reveals an index of cell type-specific modifications on H3 and H4. Nicklay JJ, Shechter D, Chitta RK, Garcia BA, Shabanowitz J, Allis CD, Hunt DF, J Biol Chem 2009 284 1075 1085 10.1074/jbc.M807274200 18957437
    • (2009) J Biol Chem , vol.284 , pp. 1075-1085
    • Nicklay, J.J.1    Shechter, D.2    Chitta, R.K.3    Garcia, B.A.4    Shabanowitz, J.5    Allis, C.D.6    Hunt, D.F.7
  • 30
    • 34248577604 scopus 로고    scopus 로고
    • Chemical derivatization of histones for facilitated analysis by mass spectrometry
    • 17446892
    • Chemical derivatization of histones for facilitated analysis by mass spectrometry. Garcia B, Mollah S, Ueberheide B, Busby S, Muratore T, Shabanowitz J, Hunt D, Nat Protoc 2007 2 933 938 10.1038/nprot.2007.106 17446892
    • (2007) Nat Protoc , vol.2 , pp. 933-938
    • Garcia, B.1    Mollah, S.2    Ueberheide, B.3    Busby, S.4    Muratore, T.5    Shabanowitz, J.6    Hunt, D.7
  • 31
    • 29144491494 scopus 로고    scopus 로고
    • Resetting the epigenetic histone code in the MRL-lpr/lpr mouse model of lupus by histone deacetylase inhibition
    • Resetting the epigenetic histone code in the MRL-lpr/lpr mouse model of lupus by histone deacetylase inhibition. Garcia B, Busby S, Shabanowitz J, Hunt D, Mishra N, J Proteome Res 2005 4 2032 2042 10.1021/pr050188r 16335948
    • (2005) J Proteome Res , vol.4 , pp. 2032-2042
    • Garcia, B.1    Busby, S.2    Shabanowitz, J.3    Hunt, D.4    Mishra, N.5
  • 32
    • 84867183192 scopus 로고    scopus 로고
    • Histone phosphorylation: A chromatin modification involved in diverse nuclear events
    • 22948226
    • Histone phosphorylation: a chromatin modification involved in diverse nuclear events. Rossetto D, Avvakumov N, Cote J, Epigenetics 2012 7 1098 1108 10.4161/epi.21975 22948226
    • (2012) Epigenetics , vol.7 , pp. 1098-1108
    • Rossetto, D.1    Avvakumov, N.2    Cote, J.3
  • 34
    • 84868689206 scopus 로고    scopus 로고
    • A histone arginine methylation localizes to nucleosomes in satellite II and III DNA sequences in the human genome
    • 23153121
    • A histone arginine methylation localizes to nucleosomes in satellite II and III DNA sequences in the human genome. Capurso D, Xiong H, Segal MR, BMC Genomics 2012 13 630 10.1186/1471-2164-13-630 23153121
    • (2012) BMC Genomics , vol.13 , pp. 630
    • Capurso, D.1    Xiong, H.2    Segal, M.R.3
  • 35
    • 84875204948 scopus 로고    scopus 로고
    • Dynamic alterations in the paternal epigenetic landscape following fertilization
    • 23024648
    • Dynamic alterations in the paternal epigenetic landscape following fertilization. Jenkins TG, Carrell DT, Front Genet 2012 3 143 23024648
    • (2012) Front Genet , vol.3 , pp. 143
    • Jenkins, T.G.1    Carrell, D.T.2
  • 37
    • 83255193432 scopus 로고    scopus 로고
    • Dramatic replacement of histone variants during genome remodeling in nuclear-transferred embryos
    • 22139579
    • Dramatic replacement of histone variants during genome remodeling in nuclear-transferred embryos. Nashun B, Akiyama T, Suzuki MG, Aoki F, Epigenetics 2011 6 1489 1497 10.4161/epi.6.12.18206 22139579
    • (2011) Epigenetics , vol.6 , pp. 1489-1497
    • Nashun, B.1    Akiyama, T.2    Suzuki, M.G.3    Aoki, F.4
  • 39
    • 0023663912 scopus 로고
    • Two complexes that contain histones are required for nucleosome assembly in vitro: Role of nucleoplasmin and N1 in Xenopus egg extracts
    • 3690659
    • Two complexes that contain histones are required for nucleosome assembly in vitro: role of nucleoplasmin and N1 in Xenopus egg extracts. Dilworth SM, Black SJ, Laskey RA, Cell 1987 51 1009 1018 10.1016/0092-8674(87)90587-3 3690659
    • (1987) Cell , vol.51 , pp. 1009-1018
    • Dilworth, S.M.1    Black, S.J.2    Laskey, R.A.3
  • 40
    • 20444411909 scopus 로고    scopus 로고
    • Nucleosome assembly protein-1 is a linker histone chaperone in Xenopus eggs
    • 15928086
    • Nucleosome assembly protein-1 is a linker histone chaperone in Xenopus eggs. Shintomi K, Iwabuchi M, Saeki H, Ura K, Kishimoto T, Ohsumi K, Proc Natl Acad Sci U S A 2005 102 8210 8215 10.1073/pnas.0500822102 15928086
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 8210-8215
    • Shintomi, K.1    Iwabuchi, M.2    Saeki, H.3    Ura, K.4    Kishimoto, T.5    Ohsumi, K.6
  • 41
    • 17644391390 scopus 로고    scopus 로고
    • Linker histone variants control chromatin dynamics during early embryogenesis
    • 15821029
    • Linker histone variants control chromatin dynamics during early embryogenesis. Saeki H, Ohsumi K, Aihara H, Ito T, Hirose S, Ura K, Kaneda Y, Proc Natl Acad Sci U S A 2005 102 5697 5702 10.1073/pnas.0409824102 15821029
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 5697-5702
    • Saeki, H.1    Ohsumi, K.2    Aihara, H.3    Ito, T.4    Hirose, S.5    Ura, K.6    Kaneda, Y.7
  • 42
    • 82755176334 scopus 로고    scopus 로고
    • Protein arginine methyltransferase Prmt5-Mep50 methylates histones H2A and H4 and the histone chaperone nucleoplasmin in Xenopus laevis eggs
    • 22009756
    • Protein arginine methyltransferase Prmt5-Mep50 methylates histones H2A and H4 and the histone chaperone nucleoplasmin in Xenopus laevis eggs. Wilczek C, Chitta R, Woo E, Shabanowitz J, Chait BT, Hunt DF, Shechter D, J Biol Chem 2011 286 42221 42231 10.1074/jbc.M111.303677 22009756
    • (2011) J Biol Chem , vol.286 , pp. 42221-42231
    • Wilczek, C.1    Chitta, R.2    Woo, E.3    Shabanowitz, J.4    Chait, B.T.5    Hunt, D.F.6    Shechter, D.7
  • 43
    • 3242670803 scopus 로고    scopus 로고
    • ATR and ATM regulate the timing of DNA replication origin firing
    • 15220931
    • ATR and ATM regulate the timing of DNA replication origin firing. Shechter D, Costanzo V, Gautier J, Nat Cell Biol 2004 6 648 655 10.1038/ncb1145 15220931
    • (2004) Nat Cell Biol , vol.6 , pp. 648-655
    • Shechter, D.1    Costanzo, V.2    Gautier, J.3
  • 44
    • 3042824849 scopus 로고    scopus 로고
    • A neutral loss activation method for improved phosphopeptide sequence analysis by quadrupole ion trap mass spectrometry
    • 15228329
    • A neutral loss activation method for improved phosphopeptide sequence analysis by quadrupole ion trap mass spectrometry. Schroeder MJ, Shabanowitz J, Schwartz JC, Hunt DF, Coon JJ, Anal Chem 2004 76 3590 3598 10.1021/ac0497104 15228329
    • (2004) Anal Chem , vol.76 , pp. 3590-3598
    • Schroeder, M.J.1    Shabanowitz, J.2    Schwartz, J.C.3    Hunt, D.F.4    Coon, J.J.5
  • 45
    • 0034665968 scopus 로고    scopus 로고
    • Subfemtomole MS and MS/MS peptide sequence analysis using nano-HPLC micro-ESI fourier transform ion cyclotron resonance mass spectrometry
    • Subfemtomole MS and MS/MS peptide sequence analysis using nano-HPLC micro-ESI fourier transform ion cyclotron resonance mass spectrometry. Martin SE, Shabanowitz J, Hunt DF, Marto JA, Anal Chem 2000 72 4266 4274 10.1021/ac000497v 11008759
    • (2000) Anal Chem , vol.72 , pp. 4266-4274
    • Martin, S.E.1    Shabanowitz, J.2    Hunt, D.F.3    Marto, J.A.4
  • 46
    • 58749083921 scopus 로고    scopus 로고
    • Methods for analyzing peptides and proteins on a chromatographic timescale by electron-transfer dissociation mass spectrometry
    • 18927556
    • Methods for analyzing peptides and proteins on a chromatographic timescale by electron-transfer dissociation mass spectrometry. Udeshi ND, Compton PD, Shabanowitz J, Hunt DF, Rose KL, Nat Protoc 2008 3 1709 1717 10.1038/nprot.2008.159 18927556
    • (2008) Nat Protoc , vol.3 , pp. 1709-1717
    • Udeshi, N.D.1    Compton, P.D.2    Shabanowitz, J.3    Hunt, D.F.4    Rose, K.L.5
  • 47
    • 84856690645 scopus 로고    scopus 로고
    • Optimization of electron transfer dissociation via informed selection of reagents and operating parameters
    • Optimization of electron transfer dissociation via informed selection of reagents and operating parameters. Compton PD, Strukl JV, Bai DL, Shabanowitz J, Hunt DF, Anal Chem 2012 84 1781 1785 10.1021/ac202807h 22182179
    • (2012) Anal Chem , vol.84 , pp. 1781-1785
    • Compton, P.D.1    Strukl, J.V.2    Bai, D.L.3    Shabanowitz, J.4    Hunt, D.F.5
  • 49
    • 34247396011 scopus 로고    scopus 로고
    • A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC)
    • 17406521
    • A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC). Ong SE, Mann M, Nat Protoc 2006 1 2650 2660 17406521
    • (2006) Nat Protoc , vol.1 , pp. 2650-2660
    • Ong, S.E.1    Mann, M.2
  • 50
    • 10944227347 scopus 로고    scopus 로고
    • NAD + -dependent modulation of chromatin structure and transcription by nucleosome binding properties of PARP-1
    • 15607977
    • NAD + -dependent modulation of chromatin structure and transcription by nucleosome binding properties of PARP-1. Kim MY, Mauro S, Gevry N, Lis JT, Kraus WL, Cell 2004 119 803 814 10.1016/j.cell.2004.11.002 15607977
    • (2004) Cell , vol.119 , pp. 803-814
    • Kim, M.Y.1    Mauro, S.2    Gevry, N.3    Lis, J.T.4    Kraus, W.L.5


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