Adam Frankel, Ph.D. - Publications

Affiliations: 
2001 University of California, Los Angeles, Los Angeles, CA 
Area:
macromolecular repair for DNA and proteins

31 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any innacuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2017 Vhuiyan MI, Pak ML, Park MA, Thomas D, Lakowski TM, Chalfant CE, Frankel A. PRMT2 interacts with splicing factors and regulates the alternative splicing of BCL-X. Journal of Biochemistry. PMID 28057797 DOI: 10.1093/jb/mvw102  0.4
2015 Lakowski TM, Pak ML, Szeitz A, Thomas D, Vhuiyan MI, Clement B, Frankel A. Arginine methylation in yeast proteins during stationary-phase growth and heat shock. Amino Acids. PMID 26189025 DOI: 10.1007/s00726-015-2047-5  0.4
2014 Thomas D, Koopmans T, Lakowski TM, Kreinin H, Vhuiyan MI, Sedlock SA, Bui JM, Martin NI, Frankel A. Protein arginine N-methyltransferase substrate preferences for different nη-substituted arginyl peptides. Chembiochem : a European Journal of Chemical Biology. 15: 1607-13. PMID 25044481 DOI: 10.1002/cbic.201402045  0.4
2013 Vhuiyan M, Thomas D, Hossen F, Frankel A. Targeting protein arginine N-methyltransferases with peptide-based inhibitors: opportunities and challenges. Future Medicinal Chemistry. 5: 2199-206. PMID 24261895 DOI: 10.4155/fmc.13.184  0.4
2013 Lakowski TM, Szeitz A, Pak ML, Thomas D, Vhuiyan MI, Kotthaus J, Clement B, Frankel A. MS³ fragmentation patterns of monomethylarginine species and the quantification of all methylarginine species in yeast using MRM³. Journal of Proteomics. 80: 43-54. PMID 23333926 DOI: 10.1016/j.jprot.2013.01.003  0.4
2012 Frankel A. Inconvenient truths for PRMT6 kinetic studies. The Journal of Biological Chemistry. 287: 9512; author reply 9. PMID 22427433 DOI: 10.1074/jbc.L111.333609  0.4
2012 T Hart P, Thomas D, Van Ommeren R, Lakowski TM, Frankel A, Martin NI. Analogues of the HIV-Tat peptide containing Nη-modified arginines as potent inhibitors of protein arginine N-methyltransferases Medchemcomm. 3: 1235-1244. DOI: 10.1039/c2md20161e  0.4
2011 Pak ML, Lakowski TM, Thomas D, Vhuiyan MI, Hüsecken K, Frankel A. A protein arginine N-methyltransferase 1 (PRMT1) and 2 heteromeric interaction increases PRMT1 enzymatic activity. Biochemistry. 50: 8226-40. PMID 21851090 DOI: 10.1021/bi200644c  0.4
2011 Pless SA, Galpin JD, Frankel A, Ahern CA. Molecular basis for class Ib anti-arrhythmic inhibition of cardiac sodium channels. Nature Communications. 2: 351. PMID 21673672 DOI: 10.1038/ncomms1351  0.4
2011 't Hart P, Lakowski TM, Thomas D, Frankel A, Martin NI. Peptidic partial bisubstrates as inhibitors of the protein arginine N-methyltransferases. Chembiochem : a European Journal of Chemical Biology. 12: 1427-32. PMID 21560220 DOI: 10.1002/cbic.201100074  0.4
2010 Thomas D, Lakowski TM, Pak ML, Kim JJ, Frankel A. Förster resonance energy transfer measurements of cofactor-dependent effects on protein arginine N-methyltransferase homodimerization. Protein Science : a Publication of the Protein Society. 19: 2141-51. PMID 20812326 DOI: 10.1002/pro.492  0.4
2010 Lakowski TM, 't Hart P, Ahern CA, Martin NI, Frankel A. Nη-substituted arginyl peptide inhibitors of protein arginine N-methyltransferases. Acs Chemical Biology. 5: 1053-63. PMID 20701328 DOI: 10.1021/cb100161u  0.4
2010 Lakowski TM, Zurita-Lopez C, Clarke SG, Frankel A. Approaches to measuring the activities of protein arginine N-methyltransferases. Analytical Biochemistry. 397: 1-11. PMID 19761747 DOI: 10.1016/j.ab.2009.09.021  0.4
2010 Lakowski TM, Frankel A. Sources of S-adenosyl-L-homocysteine background in measuring protein arginine N-methyltransferase activity using tandem mass spectrometry. Analytical Biochemistry. 396: 158-60. PMID 19733141 DOI: 10.1016/j.ab.2009.08.043  0.4
2009 Lakowski TM, Frankel A. Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4. The Biochemical Journal. 421: 253-61. PMID 19405910 DOI: 10.1042/BJ20090268  0.4
2008 Lakowski TM, Frankel A. A kinetic study of human protein arginine N-methyltransferase 6 reveals a distributive mechanism. The Journal of Biological Chemistry. 283: 10015-25. PMID 18263580 DOI: 10.1074/jbc.M710176200  0.4
2006 Miranda TB, Sayegh J, Frankel A, Katz JE, Miranda M, Clarke S. Yeast Hsl7 (histone synthetic lethal 7) catalyses the in vitro formation of omega-N(G)-monomethylarginine in calf thymus histone H2A. The Biochemical Journal. 395: 563-70. PMID 16426232 DOI: 10.1042/BJ20051771  0.4
2004 Singh V, Miranda TB, Jiang W, Frankel A, Roemer ME, Robb VA, Gutmann DH, Herschman HR, Clarke S, Newsham IF. DAL-1/4.1B tumor suppressor interacts with protein arginine N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and in vivo. Oncogene. 23: 7761-71. PMID 15334060 DOI: 10.1038/sj.onc.1208057  0.4
2004 Miranda TB, Miranda M, Frankel A, Clarke S. PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity. The Journal of Biological Chemistry. 279: 22902-7. PMID 15044439 DOI: 10.1074/jbc.M312904200  0.4
2003 Frankel A, Millward SW, Roberts RW. Encodamers: unnatural peptide oligomers encoded in RNA. Chemistry & Biology. 10: 1043-50. PMID 14652071 DOI: 10.1016/j.chembiol.2003.11.004  0.4
2003 Xia T, Frankel A, Takahashi TT, Ren J, Roberts RW. Context and conformation dictate function of a transcription antitermination switch. Nature Structural Biology. 10: 812-9. PMID 14502268 DOI: 10.1038/nsb983  0.4
2003 Frankel A, Li S, Starck SR, Roberts RW. Unnatural RNA display libraries. Current Opinion in Structural Biology. 13: 506-12. PMID 12948781 DOI: 10.1016/S0959-440X(03)00110-6  0.4
2003 Xia T, Becker HC, Wan C, Frankel A, Roberts RW, Zewail AH. The RNA-protein complex: direct probing of the interfacial recognition dynamics and its correlation with biological functions. Proceedings of the National Academy of Sciences of the United States of America. 100: 8119-23. PMID 12815093 DOI: 10.1073/pnas.1433099100  0.4
2003 Frankel A, Roberts RW. In vitro selection for sense codon suppression. Rna (New York, N.Y.). 9: 780-6. PMID 12810911 DOI: 10.1261/rna.5350303  0.4
2002 Frankel A, Yadav N, Lee J, Branscombe TL, Clarke S, Bedford MT. The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity. The Journal of Biological Chemistry. 277: 3537-43. PMID 11724789 DOI: 10.1074/jbc.M108786200  0.4
2001 Branscombe TL, Frankel A, Lee JH, Cook JR, Yang ZH, Pestka S, Clarke S. PRMT5 (Janus Kinase-binding Protein 1) Catalyzes the Formation of Symmetric Dimethylarginine Residues in Proteins Journal of Biological Chemistry. 276: 32971-32976. DOI: 10.1074/jbc.M105412200  0.4
2000 Frankel A, Clarke S. PRMT3 is a distinct member of the protein arginine N-methyltransferase family: Conferral of substrate specificity by a zinc-finger domain Journal of Biological Chemistry. 275: 32974-32982. PMID 10931850  0.4
2000 Bedford MT, Frankel A, Yaffe MB, Clarke S, Leder P, Richard S. Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains. The Journal of Biological Chemistry. 275: 16030-6. PMID 10748127 DOI: 10.1074/jbc.M909368199  0.4
2000 Tang J, Frankel A, Cook RJ, Kim S, Paik WK, Williams KR, Clarke S, Herschman HR. PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells. The Journal of Biological Chemistry. 275: 7723-30. PMID 10713084 DOI: 10.1074/jbc.275.11.7723  0.4
1999 Poon WW, Barkovich RJ, Hsu AY, Frankel A, Lee PT, Shepherd JN, Myles DC, Clarke CF. Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis. The Journal of Biological Chemistry. 274: 21665-72. PMID 10419476 DOI: 10.1074/jbc.274.31.21665  0.4
1999 Frankel A, Clarke S. RNase treatment of yeast and mammalian cell extracts affects in vitro substrate methylation by Type I protein arginine N-methyltransferases Biochemical and Biophysical Research Communications. 259: 391-400. PMID 10362520 DOI: 10.1006/bbrc.1999.0779  0.4
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