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Adam Frankel, Ph.D. - Publications

Affiliations: 
2001 University of California, Los Angeles, Los Angeles, CA 
Area:
macromolecular repair for DNA and proteins
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38 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, 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
2024 Hendrickson-Rebizant T, Sudhakar SRN, Rowley MJ, Frankel A, Davie JR, Lakowski TM. Structure, Function, and Activity of Small Molecule and Peptide Inhibitors of Protein Arginine Methyltransferase 1. Journal of Medicinal Chemistry. PMID 39250434 DOI: 10.1021/acs.jmedchem.4c00490  0.342
2023 Rowley MJ, Prout-Holm RA, Liu RW, Hendrickson-Rebizant T, Ige OO, Lakowski TM, Frankel A. Protein arginine N-methyltransferase 2 (PRMT2) plays a noncatalytic role in the histone methylation activity of PRMT1. The Journal of Biological Chemistry. 105360. PMID 37863263 DOI: 10.1016/j.jbc.2023.105360  0.458
2022 Rowley MJ, Taylor SA, Frankel A. Protein arginine N-methyltransferase activity determination with filter binding and phosphor screening (FBAPS) assay. Analytical Biochemistry. 653: 114778. PMID 35709928 DOI: 10.1016/j.ab.2022.114778  0.333
2020 Frankel A. Biological and chemical approaches to understanding protein arginine methylation. Methods (San Diego, Calif.). PMID 32032700 DOI: 10.1016/J.Ymeth.2020.02.001  0.473
2019 Silva ACE, Wu CY, Citadin CT, Clemons GA, Possoit HE, Grames MS, Lien CF, Minagar A, Lee RH, Frankel A, Lin HW. Protein Arginine Methyltransferases in Cardiovascular and Neuronal Function. Molecular Neurobiology. PMID 31823198 DOI: 10.1007/S12035-019-01850-Z  0.374
2019 Brown JI, Page BDG, Frankel A. The application of differential scanning fluorimetry in exploring bisubstrate binding to protein arginine N-methyltransferase 1. Methods (San Diego, Calif.). PMID 31726226 DOI: 10.1016/J.Ymeth.2019.11.004  0.498
2018 Frankel A, Brown JI. Evaluation of kinetic data: What the numbers tell us about PRMTs. Biochimica Et Biophysica Acta. Proteins and Proteomics. PMID 30342239 DOI: 10.1016/J.Bbapap.2018.10.010  0.394
2017 Brown JI, Koopmans T, van Strien J, Martin NI, Frankel A. Kinetic analysis of PRMT1 reveals multifactorial processivity and a sequential ordered mechanism. Chembiochem : a European Journal of Chemical Biology. PMID 29112789 DOI: 10.1002/Cbic.201700521  0.473
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  0.36
2016 Wu H, Zheng W, Eram MS, Vhuiyan M, Dong A, Zeng H, He H, Brown P, Frankel A, Vedadi M, Luo M, Min J. Structural basis of arginine asymmetrical dimethylation by PRMT6. The Biochemical Journal. PMID 27480107 DOI: 10.1042/Bcj20160537  0.479
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  0.38
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  0.589
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  0.412
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  0.421
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  0.414
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  0.44
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  0.523
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  0.443
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  0.491
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  0.479
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  0.738
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  0.427
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  0.52
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  0.553
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  0.684
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  0.752
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  0.773
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  0.355
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  0.374
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  0.361
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  0.38
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  0.67
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  0.667
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 DOI: 10.1074/Jbc.M006445200  0.671
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  0.592
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  0.656
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  0.314
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  0.702
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