Probe the function of histone lysine 36 methylation using histone H3 lysine 36 to methionine mutant transgene in mammalian cells

References

• Jenuwein T, Allis CD. Translating the Histone Code. Science (80- ) 2001; 293:1074-80; http://dx.doi.org/10.1126/science.1063127
   PubMed Web of Science ®Google Scholar
• Strahl BD, Allis CD. The language of covalent histone modifications. Nature 2000; 403:41-5; PMID:10638745; http://dx.doi.org/10.1038/47412
   PubMed Web of Science ®Google Scholar
• Zhang Y, Reinberg D. Transcription regulation by histone methylation: Interplay between different covalent modifications of the core histone tails. Genes Dev 2001; 15:2343-60; PMID:11562345; http://dx.doi.org/10.1101/gad.927301
   PubMed Web of Science ®Google Scholar
• Deal RB, Henikoff S. Histone variants and modifications in plant gene regulation. Curr. Opin. Plant Biol 2011; 14:116-22; PMID:21159547; http://dx.doi.org/10.1016/j.pbi.2010.11.005
   PubMed Web of Science ®Google Scholar
• Han J, Zhang H, Zhang H, Wang Z, Zhou H, Zhang Z. XA Cul4 E3 ubiquitin ligase regulates histone hand-off during nucleosome assembly. Cell 2013; 155.
   Google Scholar
• Lee JS, Smith E, Shilatifard A. The Language of Histone Crosstalk. Cell 2010; 142:682-5.
   PubMed Web of Science ®Google Scholar
• Burgess RJ, Zhang Z. Histones, histone chaperones and nucleosome assembly. Protein Cell 2010; 1:607-12; PMID:21203931; http://dx.doi.org/10.1007/s13238-010-0086-y
   PubMed Web of Science ®Google Scholar
• Tan M, Luo H, Lee S, Jin F, Yang JS, Montellier E, Buchou T, Cheng Z, Rousseaux S, Rajagopal N, et al. Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification. Cell 2011; 146:1016-28; PMID:21925322; http://dx.doi.org/10.1016/j.cell.2011.08.008
   PubMed Web of Science ®Google Scholar
• Grunstein M. Histone acetylation in chromatin structure and transcription. Nature 1997; 389:349-52; PMID:9311776; http://dx.doi.org/10.1038/38664
   PubMed Web of Science ®Google Scholar
• Weber CM, Henikoff S. Histone variants: dynamic punctuation in transcription. Genes Dev 2014; 28:672-82; PMID:24696452; http://dx.doi.org/10.1101/gad.238873.114
   PubMed Web of Science ®Google Scholar
• Abmayr SM, Workman JL. Holding on through DNA replication: Histone modification or modifier? Cell 2012; 150:875-7; PMID:22939615; http://dx.doi.org/10.1016/j.cell.2012.08.006
   PubMed Web of Science ®Google Scholar
• Han J, Zhou H, Horazdovsky B, Zhang K, Xu R, Zhang Z. Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Sci (New York, NY) 2007; 315:653-5; http://dx.doi.org/10.1126/science.1133234
   Google Scholar
• van Attikum H, Gasser SM. The histone code at DNA breaks: a guide to repair? Nat Rev Mol Cell Biol 2005; 6:757-65; PMID:16167054; http://dx.doi.org/10.1038/nrm1737
   PubMed Web of Science ®Google Scholar
• Jiang Y, Qian X, Shen J, Wang Y, Li X, Liu R, Xia Y, Chen Q, Peng G, Lin S-Y, et al. Local generation of fumarate promotes DNA repair through inhibition of histone H3 demethylation. Nat Cell Biol 2015; 17:1158-68; PMID:26237645; http://dx.doi.org/10.1038/ncb3209
   PubMed Web of Science ®Google Scholar
• Lowndes NF, Toh GWL. DNA repair: The importance of phosphorylating histone H2AX. Curr. Biol 2005; 15.
   Web of Science ®Google Scholar
• Eriksson PR, Ganguli D, Nagarajavel V, Clark DJ. Regulation of histone gene expression in budding yeast. Genetics 2012; 191:7-20; http://dx.doi.org/10.1534/genetics.112.140145
   PubMed Web of Science ®Google Scholar
• Dion MF, Kaplan T, Kim M, Buratowski S, Friedman N, Rando OJ. Dynamics of replication-independent histone turnover in budding yeast. Science (80- ) 2007; 315:1405-8; http://dx.doi.org/10.1126/science.1134053
   PubMed Web of Science ®Google Scholar
• Bernstein BE, Meissner A, Lander ES. The Mammalian Epigenome. Cell 2007; 128:669-81.
   PubMed Web of Science ®Google Scholar
• Etchegaray J, Lee C, Wade P a, Reppert SM. Rhythmic histone acetylation underlies transcription in the mammalian circadian clock. Nature 2003; 421:177-82; PMID:12483227; http://dx.doi.org/10.1038/nature01314
   PubMed Web of Science ®Google Scholar
• Carrozza MJ, Utley RT, Workman JL, Côté J. The diverse functions of histone acetyltransferase complexes. Trends Genet 2003; 19:321-9; PMID:12801725; http://dx.doi.org/10.1016/S0168-9525(03)00115-X
   PubMed Web of Science ®Google Scholar
• Dhalluin C, Carlson JE, Zeng L, He C, Aggarwal a K, Zhou MM. Structure and ligand of a histone acetyltransferase bromodomain. Nature 1999; 399:491-6; PMID:10365964; http://dx.doi.org/10.1038/20974
   PubMed Web of Science ®Google Scholar
• Lee KK, Workman JL. Histone acetyltransferase complexes: one size doesn't fit all. Nat Rev Mol Cell Biol 2007; 8:284-95; PMID:17380162; http://dx.doi.org/10.1038/nrm2145
   PubMed Web of Science ®Google Scholar
• Rea S, Eisenhaber F, O'Carroll D, Strahl BD, Sun ZW, Schmid M, Opravil S, Mechtler K, Ponting CP, Allis CD, et al. Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature 2000; 406:593-9; PMID:10949293; http://dx.doi.org/10.1038/35020506
   PubMed Web of Science ®Google Scholar
• Rice JC, Briggs SD, Ueberheide B, Barber CM, Shabanowitz J, Hunt DF, Shinkai Y, Allis CD. Histone Methyltransferases Direct Different Degrees of Methylation to Define Distinct Chromatin Domains. Mol Cell 2003; 12:1591-8; PMID:14690610; http://dx.doi.org/10.1016/S1097-2765(03)00479-9
   PubMed Web of Science ®Google Scholar
• Trievel RC. Structure and function of histone methyltransferases. Crit Rev Eukaryot Gene Expr 2004; 14:147-69; PMID:15248813; http://dx.doi.org/10.1615/CritRevEukaryotGeneExpr.v14.i3.10
   PubMed Web of Science ®Google Scholar
• Schwartzentruber J, Korshunov A, Liu X-Y, Jones DTW, Pfaff E, Jacob K, Sturm D, Fontebasso AM, Quang D-AK, Tönjes M, et al. Driver mutations in histone H3.3 and chromatin remodelling genes in paediatric glioblastoma. Nature 2012; 482:226-31; PMID:22286061; http://dx.doi.org/10.1038/nature10833
   PubMed Web of Science ®Google Scholar
• Wu G, Broniscer A, McEachron T a, Lu C, Paugh BS, Becksfort J, Qu C, Ding L, Huether R, Parker M, et al. Somatic histone H3 alterations in pediatric diffuse intrinsic pontine gliomas and non-brainstem glioblastomas. Nat. Genet 2012; 44:251-3; PMID:22286216; http://dx.doi.org/10.1038/ng.1102
   PubMed Web of Science ®Google Scholar
• Sturm D, Witt H, Hovestadt V, Khuong-Quang DA, Jones DTW, Konermann C, Pfaff E, Tönjes M, Sill M, Bender S, et al. Hotspot Mutations in H3F3A and IDH1 Define Distinct Epigenetic and Biological Subgroups of Glioblastoma. Cancer Cell 2012; 22:425-37; PMID:23079654; http://dx.doi.org/10.1016/j.ccr.2012.08.024
   PubMed Web of Science ®Google Scholar
• Behjati S, Tarpey PS, Presneau N, Scheipl S, Pillay N, Van Loo P, Wedge DC, Cooke SL, Gundem G, Davies H, et al. Distinct H3F3A and H3F3B driver mutations define chondroblastoma and giant cell tumor of bone. Nat Genet 2013; 45:1479-82; PMID:24162739; http://dx.doi.org/10.1038/ng.2814
   PubMed Web of Science ®Google Scholar
• Szenker E, Ray-Gallet D, Almouzni G. The double face of the histone variant H3.3. Cell Res 2011; 21:421-34; PMID:21263457; http://dx.doi.org/10.1038/cr.2011.14
   PubMed Web of Science ®Google Scholar
• Talbert PB, Henikoff S. Histone variants-ancient wrap artists of the epigenome. Nat Rev Mol Cell Biol 2010; 11:264-75; PMID:20197778; http://dx.doi.org/10.1038/nrm2861
   PubMed Web of Science ®Google Scholar
• Bender S, Tang Y, Lindroth AM, Hovestadt V, Jones DTW, Kool M, Zapatka M, Northcott P a, Sturm D, Wang W, et al. Reduced H3K27me3 and DNA Hypomethylation Are Major Drivers of Gene Expression in K27M Mutant Pediatric High-Grade Gliomas. Cancer Cell 2013; 24(5):660-72.
   PubMed Web of Science ®Google Scholar
• Lewis PW, Muller MM, Koletsky MS, Cordero F, Lin S, Banaszynski LA, Garcia BA, Muir TW, Becher OJ, Allis CD. Inhibition of PRC2 activity by a gain-of-function H3 mutation found in pediatric glioblastoma. Science (80- ) 2013; 340:857-61; http://dx.doi.org/10.1126/science.1232245
   PubMed Web of Science ®Google Scholar
• Chan KM, Han J, Fang D, Gan H, Zhang Z. A lesson learned from the H3.3K27M mutation found in pediatric glioma A new approach to the study of the function of histone modifications in vivo? Cell Cycle 2013; 12:2546-52; PMID:23907119; http://dx.doi.org/10.4161/cc.25625
   PubMed Web of Science ®Google Scholar
• Chan KM, Fang D, Gan H, Hashizume R, Yu C, Schroeder M, Gupta N, Mueller S, David James C, Jenkins R, et al. The histone H3.3K27M mutation in pediatric glioma reprograms H3K27 methylation and gene expression. Genes Dev 2013; 27:985-90; PMID:23603901; http://dx.doi.org/10.1101/gad.217778.113
   PubMed Web of Science ®Google Scholar
• Jiao L, Liu X. Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2. Science 2015; 350:291; http://dx.doi.org/10.1126/science.aab2713
   Web of Science ®Google Scholar
• Justin N, Zhang Y, Tarricone C, Martin SR, Chen S, Underwood E, De Marco V, Haire LF, Walker PA, Reinberg D, et al. Structural basis of oncogenic histone H3K27M inhibition of human polycomb repressive complex 2. Nat Commun 2016; 7:11316; PMID:27121947; http://dx.doi.org/10.1038/ncomms11316
   PubMed Web of Science ®Google Scholar
• Fang D, Gan H, Lee J-H, Han J, Wang Z, Riester SM, Jin L, Chen J, Zhou H, Wang J, et al. The histone H3.3K36M mutation reprograms the epigenome of chondroblastomas. Science (80- ) 2016; 352(6291):1344-8.
   Web of Science ®Google Scholar
• Li J, Moazed D, Gygi SP. Association of the histone methyltransferase Set2 with RNA polymerase II plays a role in transcription elongation. J Biol Chem 2002; 277:49383-8; PMID:12381723; http://dx.doi.org/10.1074/jbc.M209294200
   PubMed Web of Science ®Google Scholar
• Strahl BD, Grant PA, Briggs SD, Sun Z-W, Bone JR, Caldwell JA, Mollah S, Cook RG, Shabanowitz J, Hunt DF, et al. Set2 Is a Nucleosomal Histone H3-Selective Methyltransferase That Mediates Transcriptional Repression. Mol Cell Biol 2002; 22:1298-306; PMID:11839797; http://dx.doi.org/10.1128/MCB.22.5.1298-1306.2002
   PubMed Web of Science ®Google Scholar
• Rayasam GV, Wendling O, Angrand PO, Mark M, Niederreither K, Song L, Lerouge T, Hager GL, Chambon P, Losson R. NSD1 is essential for early post-implantation development and has a catalytically active SET domain. EMBO J 2003; 22:3153-63; PMID:12805229; http://dx.doi.org/10.1093/emboj/cdg288
   PubMed Web of Science ®Google Scholar
• Li Y, Trojer P, Xu CF, Cheung P, Kuo A, Drury WJ, Qiao Q, Neubert TA, Xu RM, Gozani O, et al. The target of the NSD family of histone lysine methyltransferases depends on the nature of the substrate. J Biol Chem 2009; 284:34283-95; PMID:19808676; http://dx.doi.org/10.1074/jbc.M109.034462
   PubMed Web of Science ®Google Scholar
• An S, Yeo KJ, Jeon YH, Song JJ. Crystal structure of the human histone methyltransferase ASH1L catalytic domain and its implications for the regulatory mechanism. J Biol Chem 2011; 286:8369-74; PMID:21239497; http://dx.doi.org/10.1074/jbc.M110.203380
   PubMed Web of Science ®Google Scholar
• Edmunds JW, Mahadevan LC, Clayton AL. Dynamic histone H3 methylation during gene induction: HYPB/Setd2 mediates all H3K36 trimethylation. EMBO J 2008; 27:406-20; PMID:18157086; http://dx.doi.org/10.1038/sj.emboj.7601967
   PubMed Web of Science ®Google Scholar
• Kolasinska-zwierz P, Down T, Latorre I, Liu T, Liu XS, Ahringer J. Differential chromatin marking of introns and expressed exons by H3K36me3. Nat Genet 2009; 41:376-81; PMID:19182803; http://dx.doi.org/10.1038/ng.322
   PubMed Web of Science ®Google Scholar
• Rao B, Shibata Y, Strahl BD, Lieb JD. Dimethylation of histone H3 at lysine 36 demarcates regulatory and nonregulatory chromatin genome-wide. Mol Cell Biol 2005; 25:9447-59; PMID:16227595; http://dx.doi.org/10.1128/MCB.25.21.9447-9459.2005
   PubMed Web of Science ®Google Scholar
• Sen P, Dang W, Donahue G, Dai J, Dorsey J, Cao X, Liu W, Cao K, Perry R, Lee JY, et al. H3K36 methylation promotes longevity by enhancing transcriptional fidelity. Genes Dev 2015; 29:1362-76; PMID:26159996; http://dx.doi.org/10.1101/gad.263707.115
   PubMed Web of Science ®Google Scholar
• de Almeida SF, Grosso AR, Koch F, Fenouil R, Carvalho S, Andrade J, Levezinho H, Gut M, Eick D, Gut I, et al. Splicing enhances recruitment of methyltransferase HYPB/Setd2 and methylation of histone H3 Lys36. Nat Struct Mol Biol 2011; 18:977-83; PMID:21792193; http://dx.doi.org/10.1038/nsmb.2123
   PubMed Web of Science ®Google Scholar
• Luco RF, Pan Q, Tominaga K, Blencowe BJ, Pereira-Smith OM, Misteli T. Regulation of alternative splicing by histone modifications. Science 2010; 327:996-1000; PMID:20133523; http://dx.doi.org/10.1126/science.1184208
   PubMed Web of Science ®Google Scholar
• Pryde F, Jain D, Kerr A, Curley R, Mariotti FR, Vogelauer M. H3 K36 methylation helps determine the timing of Cdc45 association with replication origins. PLoS One 2009; 4(6):e5882.
   PubMed Web of Science ®Google Scholar
• Kim HS, Rhee DK, Jang YK. Methylations of histone H3 lysine 9 and lysine 36 are functionally linked to DNA replication checkpoint control in fission yeast. Biochem Biophys Res Commun 2008; 368:419-25; PMID:18252195; http://dx.doi.org/10.1016/j.bbrc.2008.01.104
   PubMed Web of Science ®Google Scholar
• Wagner EJ, Carpenter PB. Understanding the language of Lys36 methylation at histone H3. Nat Rev Mol Cell Biol 2012; 13:115-26; PMID:22266761; http://dx.doi.org/10.1038/nrm3274
   PubMed Web of Science ®Google Scholar
• Li B, Carey M, Workman JL. The Role of Chromatin during Transcription. Cell 2007; 128:707-19.
   PubMed Web of Science ®Google Scholar
• Dhayalan A, Rajavelu A, Rathert P, Tamas R, Jurkowska RZ, Ragozin S, Jeltsch A. The Dnmt3a PWWP domain reads histone 3 lysine 36 trimethylation and guides DNA methylation. J Biol Chem 2010; 285:26114-20; PMID:20547484; http://dx.doi.org/10.1074/jbc.M109.089433
   PubMed Web of Science ®Google Scholar
• Lucio-Eterovic AK, Singh MM, Gardner JE, Veerappan CS, Rice JC, Carpenter PB. Role for the nuclear receptor-binding SET domain protein 1 (NSD1) methyltransferase in coordinating lysine 36 methylation at histone 3 with RNA polymerase II function. Proc Natl Acad Sci U S A 2010; 107:16952-7; PMID:20837538; http://dx.doi.org/10.1073/pnas.1002653107
   PubMed Web of Science ®Google Scholar
• Fnu S, Williamson EA, De Haro LP, Brenneman M, Wray J, Shaheen M, Radhakrishnan K, Lee S-H, Nickoloff JA, Hromas R. Methylation of histone H3 lysine 36 enhances DNA repair by nonhomologous end-joining. Proc Natl Acad Sci 2011; 108:540-5; PMID:21187428; http://dx.doi.org/10.1073/pnas.1013571108
   PubMed Web of Science ®Google Scholar
• Hudlebusch HR, Santoni-Rugiu E, Simon R, Ralfkiær E, Rossing HH, Johansen JV, Jørgensen M, Sauter G, Helin K. The histone methyltransferase and putative oncoprotein MMSET is overexpressed in a large variety of human tumors. Clin Cancer Res 2011; 17:2919-33; PMID:21385930; http://dx.doi.org/10.1158/1078-0432.CCR-10-1302
   PubMed Web of Science ®Google Scholar
• Duns G, van den Berg E, van Duivenbode I, Osinga J, Hollema H, Hofstra RMW, Kok K. Histone methyltransferase gene SETD2 is a novel tumor suppressor gene in clear cell renal cell carcinoma. Cancer Res 2010; 70:4287-91; PMID:20501857; http://dx.doi.org/10.1158/0008-5472.CAN-10-0120
   PubMed Web of Science ®Google Scholar
• Newbold RF, Mokbel K. Evidence for a tumour suppressor function of SETD2 in human breast cancer: A new hypothesis. Anticancer Res 2010; 30:3309-11; PMID:20944102
   PubMed Web of Science ®Google Scholar
• Kim S, Kim H, Fong N, Erickson B, Bentley DL. Pre-mRNA splicing is a determinant of histone H3K36 methylation. Proc Natl Acad Sci U S A 2011; 108:13564-9; PMID:21807997; http://dx.doi.org/10.1073/pnas.1109475108
   PubMed Web of Science ®Google Scholar
• Goldberg AD, Banaszynski LA, Noh KM, Lewis PW, Elsaesser SJ, Stadler S, Dewell S, Law M, Guo X, Li X, et al. Distinct Factors Control Histone Variant H3.3 Localization at Specific Genomic Regions. Cell 2010; 140:678-91; PMID:20211137; http://dx.doi.org/10.1016/j.cell.2010.01.003
   PubMed Web of Science ®Google Scholar
• Tang Y, Poustovoitov M V, Zhao K, Garfinkel M, Canutescu A, Dunbrack R, Adams PD, Marmorstein R. Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly. Nat Struct Mol Biol 2006; 13:921-9; PMID:16980972; http://dx.doi.org/10.1038/nsmb1147
   PubMed Web of Science ®Google Scholar
• Yamane K, Mizuguchi T, Cui B, Zofall M, Noma KI, Grewal SIS. Asf1/HIRA facilitate global histone deacetylation and associate with HP1 to promote nucleosome occupancy at heterochromatic loci. Mol Cell 2011; 41:56-66; PMID:21211723; http://dx.doi.org/10.1016/j.molcel.2010.12.009
   PubMed Web of Science ®Google Scholar
• Elsässer SJ, Huang H, Lewis PW, Chin JW, Allis CD, Patel DJ. DAXX envelops a histone H3.3-H4 dimer for H3.3-specific recognition. Nature 2012; 491:560-5; PMID:23075851; http://dx.doi.org/10.1038/nature11608
   PubMed Web of Science ®Google Scholar
• Agez M, Chen J, Guerois R, van Heijenoort C, Thuret JY, Mann C, Ochsenbein F. Structure of the Histone Chaperone Asf1 Bound to the Histone H3 C-Terminal Helix and Functional Insights. Structure 2007; 15:191-9; PMID:17292837; http://dx.doi.org/10.1016/j.str.2007.01.002
   PubMed Web of Science ®Google Scholar
• English CM, Adkins MW, Carson JJ, Churchill MEA, Tyler JK. Structural Basis for the Histone Chaperone Activity of Asf1. Cell 2006; 127:495-508; PMID:17081973; http://dx.doi.org/10.1016/j.cell.2006.08.047
   PubMed Web of Science ®Google Scholar
• Duarte LF, Young ARJ, Wang Z, Wu H-A, Panda T, Kou Y, Kapoor A, Hasson D, Mills NR, Ma'ayan A, et al. Histone H3.3 and its proteolytically processed form drive a cellular senescence programme. Nat Commun 2014; 5:5210; PMID:25394905; http://dx.doi.org/10.1038/ncomms6210
   PubMed Web of Science ®Google Scholar
• Mello JA, Silljé HHW, Roche DMJ, Kirschner DB, Nigg EA, Almouzni G. Human Asf1 and CAF-1 interact and synergize in a repair-coupled nucleosome assembly pathway. EMBO Rep 2002; 3:329-34; PMID:11897662; http://dx.doi.org/10.1093/embo-reports/kvf068
   PubMed Web of Science ®Google Scholar
• Bao Y, Shen X. Asf1, a Loveseat for a Histone Couple. Cell 2006; 127:458-60.
   PubMed Web of Science ®Google Scholar
• Cook AJL, Gurard-Levin ZA, Vassias I, Almouzni G. A Specific Function for the Histone Chaperone NASP to Fine-Tune a Reservoir of Soluble H3-H4 in the Histone Supply Chain. Mol Cell 2011; 44:918-27; PMID:22195965; http://dx.doi.org/10.1016/j.molcel.2011.11.021
   PubMed Web of Science ®Google Scholar
• Schmitges FW, Prusty AB, Faty M, Stützer A, Lingaraju GM, Aiwazian J, Sack R, Hess D, Li L, Zhou S, et al. Histone Methylation by PRC2 Is Inhibited by Active Chromatin Marks. Mol Cell 2011; 42:330-41; PMID:21549310; http://dx.doi.org/10.1016/j.molcel.2011.03.025
   PubMed Web of Science ®Google Scholar
• Yuan W, Xu M, Huang C, Liu N, Chen S, Zhu B. H3K36 methylation antagonizes PRC2-mediated H3K27 methylation. J Biol Chem 2011; 286:7983-9; PMID:21239496; http://dx.doi.org/10.1074/jbc.M110.194027
   PubMed Web of Science ®Google Scholar
• Lu C, Jain SU, Hoelper D, Bechet D, Molden RC, Ran L, Murphy D, Venneti S, Hameed M, Pawel BR, et al. Histone H3K36 mutations promote sarcomagenesis through altered histone methylation landscape. Science (80- ) 2016; 352:844-9; http://dx.doi.org/10.1126/science.aac7272
   PubMed Web of Science ®Google Scholar
• Shan C-M, Wang J, Xu K, Chen H, Yue J-X, Andrews S, Moresco JJ, Yates III JR, Nagy PL, Tong L, et al. A histone H3K9M mutation traps histone methyltransferase Clr4 to prevent heterochromatin spreading. Elife 2016; 5:e17903; PMID:27648579
   PubMed Web of Science ®Google Scholar
• De Mattos CBR, Angsanuntsukh C, Arkader A, Dormans JP. Chondroblastoma and chondromyxoid fibroma. J Am Acad Orthop Surg 2013; 21:225-33; PMID:23545728; http://dx.doi.org/10.5435/JAAOS-21-04-225
   PubMed Web of Science ®Google Scholar
• Turcotte RE, Kurt AM, Sim FH, Unni KK, McLeod RA. Chondroblastoma. Hum Pathol 1993; 24:944-9; PMID:8253461; http://dx.doi.org/10.1016/0046-8177(93)90107-R
   PubMed Web of Science ®Google Scholar
• Romeo S, Hogendoorn PCW, Dei Tos AP. Benign cartilaginous tumors of bone: from morphology to somatic and germ-line genetics. Adv Anat Pathol 2009; 16:307-15; PMID:19700940; http://dx.doi.org/10.1097/PAP.0b013e3181b506a1
   PubMed Web of Science ®Google Scholar
• Chan KM, Han J, Fang D, Gan H, Zhang Z. A lesson learned from the H3.3K27M mutation found in pediatric glioma. Cell Cycle 2013; 12:2546-52; PMID:23907119; http://dx.doi.org/10.4161/cc.25625
   PubMed Web of Science ®Google Scholar
• Trapnell C, Williams BA, Pertea G, Mortazavi A, Kwan G, van Baren MJ, Salzberg SL, Wold BJ, Pachter L. Transcript assembly and quantification by RNA-Seq reveals unannotated transcripts and isoform switching during cell differentiation. Nat Biotechnol 2010; 28:511-5; PMID:20436464; http://dx.doi.org/10.1038/nbt.1621
   PubMed Web of Science ®Google Scholar
• Benjamini Y, Speed TP. RSeQC: Quality Control of RNA-seq experiments. Bioinformatics 2012; 40:e72.
   Google Scholar
• Langmead B, Trapnell C, Pop M, Salzberg SL. Ultrafast and memory-efficient alignment of short DNA sequences to the human genome. Genome Biol 2009; 10:R25; PMID:19261174; http://dx.doi.org/10.1186/gb-2009-10-3-r25
   PubMed Web of Science ®Google Scholar