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Alexander J. Ruthenburg, Ph.D. - Publications

Affiliations: 
2005 Harvard University, Cambridge, MA, United States 
 2010- Molecular Genetics and Cell Biology University of Chicago, Chicago, IL 
Area:
chromatin, biochemistry, chemical biology, structure
Website:
http://mgcb.bsd.uchicago.edu/faculty/ruthenburg/index.html

20 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
2016 Hattori T, Lai D, Dementieva IS, Montaño SP, Kurosawa K, Zheng Y, Akin LR, Świst-Rosowska KM, Grzybowski AT, Koide A, Krajewski K, Strahl BD, Kelleher NL, Ruthenburg AJ, Koide S. Antigen clasping by two antigen-binding sites of an exceptionally specific antibody for histone methylation. Proceedings of the National Academy of Sciences of the United States of America. PMID 26862167 DOI: 10.1073/pnas.1522691113  0.96
2015 Werner MS, Ruthenburg AJ. Nuclear Fractionation Reveals Thousands of Chromatin-Tethered Noncoding RNAs Adjacent to Active Genes. Cell Reports. 12: 1089-98. PMID 26257179 DOI: 10.1016/j.celrep.2015.07.033  0.96
2015 Rothbart SB, Dickson BM, Raab JR, Grzybowski AT, Krajewski K, Guo AH, Shanle EK, Josefowicz SZ, Fuchs SM, Allis CD, Magnuson TR, Ruthenburg AJ, Strahl BD. An Interactive Database for the Assessment of Histone Antibody Specificity. Molecular Cell. 59: 502-11. PMID 26212453 DOI: 10.1016/j.molcel.2015.06.022  0.36
2015 Grzybowski AT, Chen Z, Ruthenburg AJ. Calibrating ChIP-Seq with Nucleosomal Internal Standards to Measure Histone Modification Density Genome Wide. Molecular Cell. 58: 886-99. PMID 26004229 DOI: 10.1016/j.molcel.2015.04.022  0.96
2015 Rothbart SB, Dickson BM, Raab JR, Grzybowski AT, Krajewski K, Guo AH, Shanle EK, Josefowicz SZ, Fuchs SM, Allis CD, Magnuson TR, Ruthenburg AJ, Strahl BD. An Interactive Database for the Assessment of Histone Antibody Specificity Molecular Cell. 59: 502-511. DOI: 10.1016/j.molcel.2015.06.022  0.96
2014 Chen Z, Grzybowski AT, Ruthenburg AJ. Traceless semisynthesis of a set of histone 3 species bearing specific lysine methylation marks. Chembiochem : a European Journal of Chemical Biology. 15: 2071-5. PMID 25155436 DOI: 10.1002/cbic.201402313  0.96
2013 Hattori T, Taft JM, Swist KM, Luo H, Witt H, Slattery M, Koide A, Ruthenburg AJ, Krajewski K, Strahl BD, White KP, Farnham PJ, Zhao Y, Koide S. Recombinant antibodies to histone post-translational modifications. Nature Methods. 10: 992-5. PMID 23955773 DOI: 10.1038/nmeth.2605  0.96
2012 Malecek K, Ruthenburg A. Validation of histone-binding partners by peptide pull-downs and isothermal titration calorimetry Methods in Enzymology. 512: 187-220. PMID 22910208 DOI: 10.1016/B978-0-12-391940-3.00009-3  0.96
2012 Mohrig JR, Beyer BG, Fleischhacker AS, Ruthenburg AJ, John SG, Snyder DA, Nyffeler PT, Noll RJ, Penner ND, Phillips LA, Hurley HL, Jacobs JS, Treitel C, James TL, Montgomery MP. Does activation of the anti proton, rather than concertedness, determine the stereochemistry of base-catalyzed 1,2-elimination reactions? Anti stereospecificity in E1cB eliminations of β-3-trifluoromethylphenoxy esters, thioesters, and ketones. The Journal of Organic Chemistry. 77: 2819-28. PMID 22321002 DOI: 10.1021/jo300053w  0.96
2011 Werner M, Ruthenburg AJ. The United States of histone ubiquitylation and methylation. Molecular Cell. 43: 5-7. PMID 21726805 DOI: 10.1016/j.molcel.2011.06.015  0.96
2011 Ruthenburg AJ, Li H, Milne TA, Dewell S, McGinty RK, Yuen M, Ueberheide B, Dou Y, Muir TW, Patel DJ, Allis CD. Recognition of a mononucleosomal histone modification pattern by BPTF via multivalent interactions. Cell. 145: 692-706. PMID 21596426 DOI: 10.1016/j.cell.2011.03.053  0.96
2010 Milne TA, Kim J, Wang GG, Stadler SC, Basrur V, Whitcomb SJ, Wang Z, Ruthenburg AJ, Elenitoba-Johnson KS, Roeder RG, Allis CD. Multiple interactions recruit MLL1 and MLL1 fusion proteins to the HOXA9 locus in leukemogenesis. Molecular Cell. 38: 853-63. PMID 20541448 DOI: 10.1016/j.molcel.2010.05.011  0.96
2007 Ruthenburg AJ, Li H, Patel DJ, Allis CD. Multivalent engagement of chromatin modifications by linked binding modules. Nature Reviews. Molecular Cell Biology. 8: 983-94. PMID 18037899 DOI: 10.1038/nrm2298  0.96
2007 Taverna SD, Li H, Ruthenburg AJ, Allis CD, Patel DJ. How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers. Nature Structural & Molecular Biology. 14: 1025-40. PMID 17984965 DOI: 10.1038/nsmb1338  0.96
2007 Ruthenburg AJ, Allis CD, Wysocka J. Methylation of lysine 4 on histone H3: intricacy of writing and reading a single epigenetic mark. Molecular Cell. 25: 15-30. PMID 17218268 DOI: 10.1016/j.molcel.2006.12.014  0.96
2006 Dou Y, Milne TA, Ruthenburg AJ, Lee S, Lee JW, Verdine GL, Allis CD, Roeder RG. Regulation of MLL1 H3K4 methyltransferase activity by its core components. Nature Structural & Molecular Biology. 13: 713-9. PMID 16878130 DOI: 10.1038/nsmb1128  0.96
2006 Ruthenburg AJ, Wang W, Graybosch DM, Li H, Allis CD, Patel DJ, Verdine GL. Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex. Nature Structural & Molecular Biology. 13: 704-12. PMID 16829959 DOI: 10.1038/nsmb1119  0.96
2006 Losey HC, Ruthenburg AJ, Verdine GL. Crystal structure of Staphylococcus aureus tRNA adenosine deaminase TadA in complex with RNA. Nature Structural & Molecular Biology. 13: 153-9. PMID 16415880 DOI: 10.1038/nsmb1047  0.96
2005 Wei H, Ruthenburg AJ, Bechis SK, Verdine GL. Nucleotide-dependent domain movement in the ATPase domain of a human type IIA DNA topoisomerase. The Journal of Biological Chemistry. 280: 37041-7. PMID 16100112 DOI: 10.1074/jbc.M506520200  0.96
2005 Ruthenburg AJ, Graybosch DM, Huetsch JC, Verdine GL. A superhelical spiral in the Escherichia coli DNA gyrase A C-terminal domain imparts unidirectional supercoiling bias. The Journal of Biological Chemistry. 280: 26177-84. PMID 15897198 DOI: 10.1074/jbc.M502838200  0.96
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