1. Kim S, Paik WK. Studies on the origin of epsilon-N-methyl-L-lysine in protein. J Biol Chem. 1965; 240:4629–4634.
2. Schoenheimer R, Ratner S, Rittenberg D. Studies on protein metabolism: VII. The metabolism of tyrosine. J Biol Chem. 1939; 127:333–344.
3. Neuberger A, Sanger F. The availability of in-acetyl-d-lysine and in-methyl-dl-lysine for growth. Biochem J. 1944; 38:125–129.
4. Ambler RP, Rees MW. Epsilon-N-methyl-lysine in bacterial flagellar protein. Nature. 1959; 184:56–57.
5. Murray K. The occurence of epsilon-N-methyl lysine in histones. Biochemistry. 1964; 3:10–15.
6. Huang RC, Bonner J. Histone, a suppressor of chromosomal RNA synthesis. Proc Natl Acad Sci U S A. 1962; 48:1216–1222.
![crossref](/image/icon/bnr_ref_cross.gif)
7. Allfrey VG, Faulkner R, Mirsky AE. Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc Natl Acad Sci U S A. 1964; 51:786–794.
![crossref](/image/icon/bnr_ref_cross.gif)
8. Paik WK, Bloch-Frankenthal L, Birnbaum SM, Winitz M, Greenstein JP. Eepsilon-lysine acylase. Arch Biochem Biophys. 1957; 69:56–66.
9. Kim S, Benoiton L, Paik WK. On the metabolism of epsilon-N-methyl-L-lysine by rat-kidney homogenate. Biochim Biophys Acta. 1963; 71:745–747.
10. Kim S, Benoition L, Paik WK. Epsilon-alkyllysinase. Purification and properties of the enzyme. J Biol Chem. 1964; 239:3790–3796.
11. Paik WK, Kim S. Epsilon-alkyllysinase. New assay method, purification, and biological significance. Arch Biochem Biophys. 1974; 165:369–378.
![crossref](/image/icon/bnr_ref_cross.gif)
12. Mosammaparast N, Shi Y. Reversal of histone methylation: biochemical and molecular mechanisms of histone demethylases. Annu Rev Biochem. 2010; 79:155–179.
![crossref](/image/icon/bnr_ref_cross.gif)
13. Paik WK, Kim S. ε-N-dimethyllysine in histones. Biochem Biophys Res Commun. 1967; 27:216–220.
14. Hempel K, Lange HW, Birkofer L. [Epsilon-N-trimethyllysine, a new amino acid in histones]. Naturwissenschaften. 1968; 55:37.
15. Takemoto T, Daigo K, Takagi N. [Studies on the hypotensive constituents of marine algae. I. a new basic amino acid "laminine" and the other basic constituents isolated from laminaria angustata]. Yakugaku Zasshi. 1964; 84:1176–1179.
![crossref](/image/icon/bnr_ref_cross.gif)
16. Paik WK, Kim S. Protein methylase I. Purification and properties of the enzyme. J Biol Chem. 1968; 243:2108–2114.
17. Kakimoto Y, Akazawa S. Isolation and identification of N-G,N-G- and N-G,N'-G-dimethyl-arginine, N-epsilon-mono-, di-, and trimethyllysine, and glucosylgalactosyl- and galactosyl-delta-hydroxylysine from human urine. J Biol Chem. 1970; 245:5751–5758.
![crossref](/image/icon/bnr_ref_cross.gif)
18. Baldwin GS, Carnegie PR. Specific enzymic methylation of an arginine in the experimental allergic encephalomyelitis protein from human myelin. Science. 1971; 171:579–581.
![crossref](/image/icon/bnr_ref_cross.gif)
19. Brostoff S, Eylar EH. Localization of methylated arginine in the A1 protein from myelin. Proc Natl Acad Sci U S A. 1971; 68:765–769.
![crossref](/image/icon/bnr_ref_cross.gif)
20. Rajpurohit R, Lee SO, Park JO, Paik WK, Kim S. Enzymatic methylation of recombinant heterogeneous nuclear RNP protein A1. Dual substrate specificity for S-adenosylmethionine:histone-arginine N-methyltransferase. J Biol Chem. 1994; 269:1075–1082.
![crossref](/image/icon/bnr_ref_cross.gif)
21. Ghosh SK, Paik WK, Kim S. Purification and molecular identification of two protein methylases I from calf brain. Myelin basic protein- and histone-specific enzyme. J Biol Chem. 1988; 263:19024–19033.
![crossref](/image/icon/bnr_ref_cross.gif)
22. Wang YC, Li C. Evolutionarily conserved protein arginine methyltransferases in non-mammalian animal systems. FEBS J. 2012; 279:932–945.
![crossref](/image/icon/bnr_ref_cross.gif)
23. Kim S, Paik WK. Purification and properties of protein methylase II. J Biol Chem. 1970; 245:1806–1813.
![crossref](/image/icon/bnr_ref_cross.gif)
24. Liss M, Edelstein LM. Evidence for the enzymatic methylation of crystalline ovalbumin preparations. Biochem Biophys Res Commun. 1967; 26:497–504.
![crossref](/image/icon/bnr_ref_cross.gif)
25. Axelrod J, Daly J. Pituitary gland: enzymic formation of methanol from S-adenosylmethionine. Science. 1965; 150:892–893.
![crossref](/image/icon/bnr_ref_cross.gif)
26. Springer MS, Goy MF, Adler J. Protein methylation in behavioural control mechanisms and in signal transduction. Nature. 1979; 280:279–284.
![crossref](/image/icon/bnr_ref_cross.gif)
27. Clarke S. Aging as war between chemical and biochemical processes: protein methylation and the recognition of age-damaged proteins for repair. Ageing Res Rev. 2003; 2:263–285.
![crossref](/image/icon/bnr_ref_cross.gif)
28. Paik WK, Kim S. Solubilization and partial purification of protein methylase 3 from calf thymus nuclei. J Biol Chem. 1970; 245:6010–6015.
![crossref](/image/icon/bnr_ref_cross.gif)
29. Paik WK, Kim S. Protein methylation. Science. 1971; 174:114–119.
![crossref](/image/icon/bnr_ref_cross.gif)
30. Martin C, Zhang Y. The diverse functions of histone lysine methylation. Nat Rev Mol Cell Biol. 2005; 6:838–849.
![crossref](/image/icon/bnr_ref_cross.gif)
31. Fackelmayer FO. Protein arginine methyltransferases: guardians of the Arg? Trends Biochem Sci. 2005; 30:666–671.
![crossref](/image/icon/bnr_ref_cross.gif)
32. Pahlich S, Zakaryan RP, Gehring H. Protein arginine methylation: Cellular functions and methods of analysis. Biochim Biophys Acta. 2006; 1764:1890–1903.
![crossref](/image/icon/bnr_ref_cross.gif)
33. Lee DY, Teyssier C, Strahl BD, Stallcup MR. Role of protein methylation in regulation of transcription. Endocr Rev. 2005; 26:147–170.
![crossref](/image/icon/bnr_ref_cross.gif)
34. Bedford MT, Richard S. Arginine methylation an emerging regulator of protein function. Mol Cell. 2005; 18:263–272.
35. Shi Y, Lan F, Matson C, Mulligan P, Whetstine JR, Cole PA, et al. Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell. 2004; 119:941–953.
![crossref](/image/icon/bnr_ref_cross.gif)
36. Wang Y, Wysocka J, Sayegh J, Lee YH, Perlin JR, Leonelli L, et al. Human PAD4 regulates histone arginine methylation levels via demethylimination. Science. 2004; 306:279–283.
![crossref](/image/icon/bnr_ref_cross.gif)
37. Cuthbert GL, Daujat S, Snowden AW, Erdjument-Bromage H, Hagiwara T, Yamada M, et al. Histone deimination antagonizes arginine methylation. Cell. 2004; 118:545–553.
![crossref](/image/icon/bnr_ref_cross.gif)
38. Teyssier C, Le Romancer M, Sentis S, Jalaguier S, Corbo L, Cavaillès V. Protein arginine methylation in estrogen signaling and estrogen-related cancers. Trends Endocrinol Metab. 2010; 21:181–189.
![crossref](/image/icon/bnr_ref_cross.gif)
39. Yang Y, Bedford MT. Protein arginine methyltransferases and cancer. Nat Rev Cancer. 2013; 13:37–50.
![crossref](/image/icon/bnr_ref_cross.gif)
40. Blackwell E, Ceman S. Arginine methylation of RNA-binding proteins regulates cell function and differentiation. Mol Reprod Dev. 2012; 79:163–175.
![crossref](/image/icon/bnr_ref_cross.gif)
41. Ahmad A, Cao X. Plant PRMTs broaden the scope of arginine methylation. J Genet Genomics. 2012; 39:195–208.
![crossref](/image/icon/bnr_ref_cross.gif)
42. Fisk JC, Read LK. Protein arginine methylation in parasitic protozoa. Eukaryot Cell. 2011; 10:1013–1022.
![crossref](/image/icon/bnr_ref_cross.gif)
43. Parry RV, Ward SG. Protein arginine methylation: a new handle on T lymphocytes? Trends Immunol. 2010; 31:164–169.
![crossref](/image/icon/bnr_ref_cross.gif)
44. Kim S, Lim IK, Park GH, Paik WK. Biological methylation of myelin basic protein: enzymology and biological significance. Int J Biochem Cell Biol. 1997; 29:743–751.
![crossref](/image/icon/bnr_ref_cross.gif)
45. An W, Kim J, Roeder RG. Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53. Cell. 2004; 117:735–748.
![crossref](/image/icon/bnr_ref_cross.gif)
46. Leiper J, Nandi M. The therapeutic potential of targeting endogenous inhibitors of nitric oxide synthesis. Nat Rev Drug Discov. 2011; 10:277–291.
![crossref](/image/icon/bnr_ref_cross.gif)
47. Moncada S, Palmer RM, Higgs EA. Nitric oxide: physiology, pathophysiology, and pharmacology. Pharmacol Rev. 1991; 43:109–142.
48. Tsukada Y, Fang J, Erdjument-Bromage H, Warren ME, Borchers CH, Tempst P, et al. Histone demethylation by a family of JmjC domain-containing proteins. Nature. 2006; 439:811–816.
![crossref](/image/icon/bnr_ref_cross.gif)
49. Yamane K, Toumazou C, Tsukada Y, Erdjument-Bromage H, Tempst P, Wong J, et al. JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor. Cell. 2006; 125:483–495.
![crossref](/image/icon/bnr_ref_cross.gif)
50. Whetstine JR, Nottke A, Lan F, Huarte M, Smolikov S, Chen Z, et al. Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases. Cell. 2006; 125:467–481.
![crossref](/image/icon/bnr_ref_cross.gif)
51. Paik WK, Kim S. Protein methylation. Boca Raton, FL: CRC Press;1990.
52. Raunser S, Magnani R, Huang Z, Houtz RL, Trievel RC, Penczek PA, et al. Rubisco in complex with Rubisco large subunit methyltransferase. Proc Natl Acad Sci U S A. 2009; 106:3160–3165.
![crossref](/image/icon/bnr_ref_cross.gif)
53. Greer EL, Shi Y. Histone methylation: a dynamic mark in health, disease and inheritance. Nat Rev Genet. 2012; 13:343–357.
![crossref](/image/icon/bnr_ref_cross.gif)
54. Yap KL, Zhou MM. Structure and mechanisms of lysine methylation recognition by the chromodomain in gene transcription. Biochemistry. 2011; 50:1966–1980.
![crossref](/image/icon/bnr_ref_cross.gif)
55. Beck DB, Oda H, Shen SS, Reinberg D. PR-Set7 and H4K20me1: at the crossroads of genome integrity, cell cycle, chromosome condensation, and transcription. Genes Dev. 2012; 26:325–337.
![crossref](/image/icon/bnr_ref_cross.gif)
56. Han S, Brunet A. Histone methylation makes its mark on longevity. Trends Cell Biol. 2012; 22:42–49.
![crossref](/image/icon/bnr_ref_cross.gif)
57. Sen GL. Remembering one's identity: the epigenetic basis of stem cell fate decisions. FASEB J. 2011; 25:2123–2128.
![crossref](/image/icon/bnr_ref_cross.gif)
58. Miller D, Brinkworth M, Iles D. Paternal DNA packaging in spermatozoa: more than the sum of its parts? DNA, histones, protamines and epigenetics. Reproduction. 2010; 139:287–301.
![crossref](/image/icon/bnr_ref_cross.gif)
59. Wagner EJ, Carpenter PB. Understanding the language of Lys36 methylation at histone H3. Nat Rev Mol Cell Biol. 2012; 13:115–126.
![crossref](/image/icon/bnr_ref_cross.gif)
60. Holec S, Berger F. Polycomb group complexes mediate developmental transitions in plants. Plant Physiol. 2012; 158:35–43.
![crossref](/image/icon/bnr_ref_cross.gif)
61. Thorstensen T, Grini PE, Aalen RB. SET domain proteins in plant development. Biochim Biophys Acta. 2011; 1809:407–420.
![crossref](/image/icon/bnr_ref_cross.gif)
62. Keating ST, El-Osta A. Chromatin modifications associated with diabetes. J Cardiovasc Transl Res. 2012; 5:399–412.
![crossref](/image/icon/bnr_ref_cross.gif)
63. Imai K, Ochiai K. Role of histone modification on transcriptional regulation and HIV-1 gene expression: possible mechanisms of periodontal diseases in AIDS progression. J Oral Sci. 2011; 53:1–13.
![crossref](/image/icon/bnr_ref_cross.gif)
64. Peter CJ, Akbarian S. Balancing histone methylation activities in psychiatric disorders. Trends Mol Med. 2011; 17:372–379.
![crossref](/image/icon/bnr_ref_cross.gif)
65. Paik WK, Nochumson S, Kim S. Carnitine biosynthesis via protein methylation. Trens Biochem Sci. 1977; 2:159–161.
![crossref](/image/icon/bnr_ref_cross.gif)
66. Matsuda S, Rouault J, Magaud J, Berthet C. In search of a function for the TIS21/PC3/BTG1/TOB family. FEBS Lett. 2001; 497:67–72.
![crossref](/image/icon/bnr_ref_cross.gif)
67. Buanne P, Corrente G, Micheli L, Palena A, Lavia P, Spadafora C, et al. Cloning of PC3B, a novel member of the PC3/BTG/TOB family of growth inhibitory genes, highly expressed in the olfactory epithelium. Genomics. 2000; 68:253–263.
![crossref](/image/icon/bnr_ref_cross.gif)
68. Guéhenneux F, Duret L, Callanan MB, Bouhas R, Hayette S, Berthet C, et al. Cloning of the mouse BTG3 gene and definition of a new gene family (the BTG family) involved in the negative control of the cell cycle. Leukemia. 1997; 11:370–375.
![crossref](/image/icon/bnr_ref_cross.gif)
69. Fletcher BS, Lim RW, Varnum BC, Kujubu DA, Koski RA, Herschman HR. Structure and expression of TIS21, a primary response gene induced by growth factors and tumor promoters. J Biol Chem. 1991; 266:14511–14518.
![crossref](/image/icon/bnr_ref_cross.gif)
70. Bradbury A, Possenti R, Shooter EM, Tirone F. Molecular cloning of PC3, a putatively secreted protein whose mRNA is induced by nerve growth factor and depolarization. Proc Natl Acad Sci U S A. 1991; 88:3353–3357.
![crossref](/image/icon/bnr_ref_cross.gif)
71. Konrad MA, Zúñiga-Pflücker JC. The BTG/TOB family protein TIS21 regulates stage-specific proliferation of developing thymocytes. Eur J Immunol. 2005; 35:3030–3042.
![crossref](/image/icon/bnr_ref_cross.gif)
72. Kim BC, Ryu MS, Oh SP, Lim IK. TIS21/(BTG2) negatively regulates estradiol-stimulated expansion of hematopoietic stem cells by derepressing Akt phosphorylation and inhibiting mTOR signal transduction. Stem Cells. 2008; 26:2339–2348.
![crossref](/image/icon/bnr_ref_cross.gif)
73. Ryu MS, Lee MS, Hong JW, Hahn TR, Moon E, Lim IK. TIS21/BTG2/PC3 is expressed through PKC-delta pathway and inhibits binding of cyclin B1-Cdc2 and its activity, independent of p53 expression. Exp Cell Res. 2004; 299:159–170.
![crossref](/image/icon/bnr_ref_cross.gif)
74. Guardavaccaro D, Corrente G, Covone F, Micheli L, D'Agnano I, Starace G, et al. Arrest of G(1)-S progression by the p53-inducible gene PC3 is Rb dependent and relies on the inhibition of cyclin D1 transcription. Mol Cell Biol. 2000; 20:1797–1815.
![crossref](/image/icon/bnr_ref_cross.gif)
75. Lim IK, Lee MS, Ryu MS, Park TJ, Fujiki H, Eguchi H, et al. Induction of growth inhibition of 293 cells by downregulation of the cyclin E and cyclin-dependent kinase 4 proteins due to overexpression of TIS21. Mol Carcinog. 1998; 23:25–35.
![crossref](/image/icon/bnr_ref_cross.gif)
76. Hong JW, Ryu MS, Lim IK. Phosphorylation of serine 147 of tis21/BTG2/pc3 by p-Erk1/2 induces Pin-1 binding in cytoplasm and cell death. J Biol Chem. 2005; 280:21256–21263.
![crossref](/image/icon/bnr_ref_cross.gif)
77. Lim YB, Park TJ, Lim IK. B cell translocation gene 2 enhances susceptibility of HeLa cells to doxorubicin-induced oxidative damage. J Biol Chem. 2008; 283:33110–33118.
![crossref](/image/icon/bnr_ref_cross.gif)
78. Corrente G, Guardavaccaro D, Tirone F. PC3 potentiates NGF-induced differentiation and protects neurons from apoptosis. Neuroreport. 2002; 13:417–422.
![crossref](/image/icon/bnr_ref_cross.gif)
79. Farioli-Vecchioli S, Saraulli D, Costanzi M, Leonardi L, Cinà I, Micheli L, et al. Impaired terminal differentiation of hippocampal granule neurons and defective contextual memory in PC3/Tis21 knockout mice. PLoS One. 2009; 4:e8339.
![crossref](/image/icon/bnr_ref_cross.gif)
80. Passeri D, Marcucci A, Rizzo G, Billi M, Panigada M, Leonardi L, et al. Btg2 enhances retinoic acid-induced differentiation by modulating histone H4 methylation and acetylation. Mol Cell Biol. 2006; 26:5023–5032.
![crossref](/image/icon/bnr_ref_cross.gif)
81. Imran M, Park TJ, Lim IK. TIS21/BTG2/PC3 enhances downregulation of c-Myc during differentiation of HL-60 cells by activating Erk1/2 and inhibiting Akt in response to all-trans-retinoic acid. Eur J Cancer. 2012; 48:2474–2485.
![crossref](/image/icon/bnr_ref_cross.gif)
82. Tirone F. The gene PC3(TIS21/BTG2), prototype member of the PC3/BTG/TOB family: regulator in control of cell growth, differentiation, and DNA repair? J Cell Physiol. 2001; 187:155–165.
![crossref](/image/icon/bnr_ref_cross.gif)
83. Choi KS, Kim JY, Lim SK, Choi YW, Kim YH, Kang SY, et al. TIS21(/BTG2/PC3) accelerates the repair of DNA double strand breaks by enhancing Mre11 methylation and blocking damage signal transfer to the Chk2(T68)-p53(S20) pathway. DNA Repair (Amst). 2012; 11:965–975.
![crossref](/image/icon/bnr_ref_cross.gif)
84. Lim SK, Choi YW, Lim IK, Park TJ. BTG2 suppresses cancer cell migration through inhibition of Src-FAK signaling by downregulation of reactive oxygen species generation in mitochondria. Clin Exp Metastasis. 2012; 29:901–913.
![crossref](/image/icon/bnr_ref_cross.gif)
85. Karve TM, Rosen EM. B-cell translocation gene 2 (BTG2) stimulates cellular antioxidant defenses through the antioxidant transcription factor NFE2L2 in human mammary epithelial cells. J Biol Chem. 2012; 287:31503–31514.
![crossref](/image/icon/bnr_ref_cross.gif)
86. Herschman HR. Primary response genes induced by growth factors and tumor promoters. Annu Rev Biochem. 1991; 60:281–319.
![crossref](/image/icon/bnr_ref_cross.gif)
87. Imran M, Lim IK. Regulation of Btg2(/TIS21/PC3) expression via reactive oxygen species-protein kinase C-NFκB pathway under stress conditions. Cell Signal. 2013; 25:2400–2412.
![crossref](/image/icon/bnr_ref_cross.gif)
88. Lin WJ, Gary JD, Yang MC, Clarke S, Herschman HR. The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase. J Biol Chem. 1996; 271:15034–15044.
![crossref](/image/icon/bnr_ref_cross.gif)
89. Berthet C, Guéhenneux F, Revol V, Samarut C, Lukaszewicz A, Dehay C, et al. Interaction of PRMT1 with BTG/TOB proteins in cell signalling: molecular analysis and functional aspects. Genes Cells. 2002; 7:29–39.
![crossref](/image/icon/bnr_ref_cross.gif)
90. Lim IK, Park TJ, Kim S, Lee HW, Paik WK. Enzymatic methylation of recombinant TIS21 protein-arginine residues. Biochem Mol Biol Int. 1998; 45:871–878.
![crossref](/image/icon/bnr_ref_cross.gif)
91. Bakker WJ, Blázquez-Domingo M, Kolbus A, Besooyen J, Steinlein P, Beug H, et al. FoxO3a regulates erythroid differentiation and induces BTG1, an activator of protein arginine methyl transferase 1. J Cell Biol. 2004; 164:175–184.
![crossref](/image/icon/bnr_ref_cross.gif)
92. Miyata S, Mori Y, Tohyama M. PRMT1 and Btg2 regulates neurite outgrowth of Neuro2a cells. Neurosci Lett. 2008; 445:162–165.
![crossref](/image/icon/bnr_ref_cross.gif)
93. Hata K, Nishijima K, Mizuguchi J. Role for Btg1 and Btg2 in growth arrest of WEHI-231 cells through arginine methylation following membrane immunoglobulin engagement. Exp Cell Res. 2007; 313:2356–2366.
![crossref](/image/icon/bnr_ref_cross.gif)
94. Zhang J, Tsaprailis G, Bowden GT. Nucleolin stabilizes Bcl-X L messenger RNA in response to UVA irradiation. Cancer Res. 2008; 68:1046–1054.
![crossref](/image/icon/bnr_ref_cross.gif)
95. Mauxion F, Faux C, Séraphin B. The BTG2 protein is a general activator of mRNA deadenylation. EMBO J. 2008; 27:1039–1048.
![crossref](/image/icon/bnr_ref_cross.gif)
96. Rouault JP, Prévôt D, Berthet C, Birot AM, Billaud M, Magaud JP, et al. Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex. J Biol Chem. 1998; 273:22563–22569.
![crossref](/image/icon/bnr_ref_cross.gif)
97. Robin-Lespinasse Y, Sentis S, Kolytcheff C, Rostan MC, Corbo L, Le Romancer M. hCAF1, a new regulator of PRMT1-dependent arginine methylation. J Cell Sci. 2007; 120(Pt 4):638–647.
![crossref](/image/icon/bnr_ref_cross.gif)
98. Collart MA, Panasenko OO. The Ccr4--not complex. Gene. 2012; 492:42–53.
![crossref](/image/icon/bnr_ref_cross.gif)
99. Boisvert FM, Déry U, Masson JY, Richard S. Arginine methylation of MRE11 by PRMT1 is required for DNA damage checkpoint control. Genes Dev. 2005; 19:671–676.
![crossref](/image/icon/bnr_ref_cross.gif)
100. Stracker TH, Petrini JH. The MRE11 complex: starting from the ends. Nat Rev Mol Cell Biol. 2011; 12:90–103.
![crossref](/image/icon/bnr_ref_cross.gif)
101. Déry U, Coulombe Y, Rodrigue A, Stasiak A, Richard S, Masson JY. A glycine-arginine domain in control of the human MRE11 DNA repair protein. Mol Cell Biol. 2008; 28:3058–3069.
![crossref](/image/icon/bnr_ref_cross.gif)
102. Yu Z, Vogel G, Coulombe Y, Dubeau D, Spehalski E, Hébert J, et al. The MRE11 GAR motif regulates DNA double-strand break processing and ATR activation. Cell Res. 2012; 22:305–320.
![crossref](/image/icon/bnr_ref_cross.gif)
103. Chrzanowska KH, Gregorek H, Dembowska-Bagińska B, Kalina MA, Digweed M. Nijmegen breakage syndrome (NBS). Orphanet J Rare Dis. 2012; 7:13.
![crossref](/image/icon/bnr_ref_cross.gif)
104. Lehninger AL. Biochemistry: The molecular basis of cell structure and function. New York, NY: Worth Publisher;1970.