Year |
Citation |
Score |
2022 |
Karaj E, Sindi SH, Kuganesan N, Koranne RA, Knoff JR, James AW, Fu Y, Kotsull LN, Pflum MK, Shah Z, Taylor WR, Tillekeratne LMV. First-in-Class Dual Mechanism Ferroptosis-HDAC Inhibitor Hybrids. Journal of Medicinal Chemistry. PMID 36306372 DOI: 10.1021/acs.jmedchem.2c01276 |
0.304 |
|
2019 |
Tillekeratne LMV, Al-Hamashi AA, Dlamini S, Taylor W, Koranne R, Pflum MK, Negmeldin AT, Knoff J. In Search of Selectivity: Design, Synthesis, and Biological Evaluation of New Classes of HDAC Inhibitors Proceedings. 22: 63. DOI: 10.3390/PROCEEDINGS2019022063 |
0.436 |
|
2017 |
Nalawansha DA, Gomes ID, Wambua MK, Pflum MK. HDAC Inhibitor-Induced Mitotic Arrest Is Mediated by Eg5/KIF11 Acetylation. Cell Chemical Biology. PMID 28392145 DOI: 10.1016/J.Chembiol.2017.03.008 |
0.808 |
|
2017 |
Negmeldin AT, Padige G, Bieliauskas AV, Pflum MK. Structural Requirements of HDAC Inhibitors: SAHA Analogues Modified at the C2 Position Display HDAC6/8 Selectivity. Acs Medicinal Chemistry Letters. 8: 281-286. PMID 28337317 DOI: 10.1021/Acsmedchemlett.6B00124 |
0.824 |
|
2017 |
Nalawansha DA, Pflum MK. LSD1 Substrate Binding and Gene Expression Are Affected by HDAC1-Mediated Deacetylation. Acs Chemical Biology. 12: 254-264. PMID 27977115 DOI: 10.1021/Acschembio.6B00776 |
0.539 |
|
2017 |
Embogama DM, Pflum MK. K-BILDS: A Kinase Substrate Discovery Tool. Chembiochem : a European Journal of Chemical Biology. 18: 136-141. PMID 27860220 DOI: 10.1002/Cbic.201600511 |
0.421 |
|
2016 |
Almaliti J, Al-Hamashi AA, Negmeldin AT, Hanigan CL, Perera L, Pflum MK, Casero RA, Tillekeratne LM. Largazole Analogues Embodying Radical Changes in the Depsipeptide Ring: Development of a More Selective and Highly Potent Analogue. Journal of Medicinal Chemistry. PMID 27809521 DOI: 10.1021/Acs.Jmedchem.6B01271 |
0.445 |
|
2016 |
Dedigama-Arachchige PM, Pflum MK. K-CLASP: A Tool to Identify Phosphosite Specific Kinases and Interacting Proteins. Acs Chemical Biology. 11: 3251-3255. PMID 27726338 DOI: 10.1021/Acschembio.6B00289 |
0.412 |
|
2016 |
Bieliauskas AV, Weerasinghe SV, Negmeldin AT, Pflum MK. Structural Requirements of Histone Deacetylase Inhibitors: SAHA Analogs Modified on the Hydroxamic Acid. Archiv Der Pharmazie. PMID 27062198 DOI: 10.1002/Ardp.201500472 |
0.802 |
|
2016 |
Senevirathne C, Embogama DM, Anthony TA, Fouda AE, Pflum MK. The generality of kinase-catalyzed biotinylation. Bioorganic & Medicinal Chemistry. 24: 12-9. PMID 26672511 DOI: 10.1016/J.Bmc.2015.11.029 |
0.403 |
|
2015 |
Padige G, Negmeldin AT, Pflum MK. Development of an ELISA-Based HDAC Activity Assay for Characterization of Isoform-Selective Inhibitors. Journal of Biomolecular Screening. 20: 1277-85. PMID 26232305 DOI: 10.1177/1087057115598118 |
0.604 |
|
2015 |
Fouda AE, Pflum MK. A Cell-Permeable ATP Analogue for Kinase-Catalyzed Biotinylation. Angewandte Chemie (International Ed. in English). 54: 9618-21. PMID 26119262 DOI: 10.1002/Anie.201503041 |
0.36 |
|
2014 |
Garre S, Senevirathne C, Pflum MK. A comparative study of ATP analogs for phosphorylation-dependent kinase-substrate crosslinking. Bioorganic & Medicinal Chemistry. 22: 1620-5. PMID 24529309 DOI: 10.1016/J.Bmc.2014.01.034 |
0.408 |
|
2014 |
Wambua MK, Nalawansha DA, Negmeldin AT, Pflum MK. Mutagenesis studies of the 14 Å internal cavity of histone deacetylase 1: insights toward the acetate-escape hypothesis and selective inhibitor design. Journal of Medicinal Chemistry. 57: 642-50. PMID 24405391 DOI: 10.1021/Jm401837E |
0.803 |
|
2013 |
Senevirathne C, Pflum MK. Biotinylated phosphoproteins from kinase-catalyzed biotinylation are stable to phosphatases: implications for phosphoproteomics. Chembiochem : a European Journal of Chemical Biology. 14: 381-7. PMID 23335220 DOI: 10.1002/Cbic.201200626 |
0.449 |
|
2012 |
Senevirathne C, Green KD, Pflum MK. Kinase-Catalyzed Biotinylation. Current Protocols in Chemical Biology. 4: 83-100. PMID 25177527 DOI: 10.1002/9780470559277.Ch110228 |
0.624 |
|
2012 |
Suwal S, Senevirathne C, Garre S, Pflum MK. Structural analysis of ATP analogues compatible with kinase-catalyzed labeling. Bioconjugate Chemistry. 23: 2386-91. PMID 23116557 DOI: 10.1021/Bc300404S |
0.781 |
|
2012 |
Choi SE, Pflum MK. The structural requirements of histone deacetylase inhibitors: suberoylanilide hydroxamic acid analogs modified at the C6 position. Bioorganic & Medicinal Chemistry Letters. 22: 7084-6. PMID 23089527 DOI: 10.1016/J.Bmcl.2012.09.093 |
0.524 |
|
2011 |
Choi SE, Weerasinghe SV, Pflum MK. The structural requirements of histone deacetylase inhibitors: Suberoylanilide hydroxamic acid analogs modified at the C3 position display isoform selectivity. Bioorganic & Medicinal Chemistry Letters. 21: 6139-42. PMID 21889343 DOI: 10.1016/J.Bmcl.2011.08.027 |
0.814 |
|
2010 |
Weerasinghe SV, Wambua M, Pflum MK. A histone deacetylase-dependent screen in yeast. Bioorganic & Medicinal Chemistry. 18: 7586-92. PMID 20863708 DOI: 10.1016/J.Bmc.2010.08.045 |
0.77 |
|
2010 |
Suwal S, Pflum MK. Phosphorylation-dependent kinase-substrate cross-linking. Angewandte Chemie (International Ed. in English). 49: 1627-30. PMID 20108289 DOI: 10.1002/Anie.200905244 |
0.775 |
|
2009 |
Green KD, Pflum MK. Exploring kinase cosubstrate promiscuity: monitoring kinase activity through dansylation. Chembiochem : a European Journal of Chemical Biology. 10: 234-7. PMID 19107758 DOI: 10.1002/Cbic.200800393 |
0.644 |
|
2008 |
Weerasinghe SV, Estiu G, Wiest O, Pflum MK. Residues in the 11 A channel of histone deacetylase 1 promote catalytic activity: implications for designing isoform-selective histone deacetylase inhibitors. Journal of Medicinal Chemistry. 51: 5542-51. PMID 18729444 DOI: 10.1021/Jm800081J |
0.793 |
|
2008 |
Bieliauskas AV, Pflum MK. Isoform-selective histone deacetylase inhibitors. Chemical Society Reviews. 37: 1402-13. PMID 18568166 DOI: 10.1039/B703830P |
0.818 |
|
2008 |
Mohrig JR, Alberg DG, Cartwright CH, Pflum MK, Aldrich JS, Anderson JK, Anderson SR, Fimmen RL, Snover AK. Stereochemistry of 1,2-elimination reactions at the E2-E1cB interface--tert-butyl 3-tosyloxybutanoate and its thioester. Organic & Biomolecular Chemistry. 6: 1641-6. PMID 18421398 DOI: 10.1039/b801592a |
0.718 |
|
2008 |
Singh EK, Ravula S, Pan CM, Pan PS, Vasko RC, Lapera SA, Weerasinghe SV, Pflum MK, McAlpine SR. Synthesis and biological evaluation of histone deacetylase inhibitors that are based on FR235222: a cyclic tetrapeptide scaffold. Bioorganic & Medicinal Chemistry Letters. 18: 2549-54. PMID 18381239 DOI: 10.1016/J.Bmcl.2008.03.047 |
0.819 |
|
2007 |
Karwowska-Desaulniers P, Ketko A, Kamath N, Pflum MK. Histone deacetylase 1 phosphorylation at S421 and S423 is constitutive in vivo, but dispensable in vitro. Biochemical and Biophysical Research Communications. 361: 349-55. PMID 17643391 DOI: 10.1016/J.Bbrc.2007.06.167 |
0.789 |
|
2007 |
Bieliauskas AV, Weerasinghe SV, Pflum MK. Structural requirements of HDAC inhibitors: SAHA analogs functionalized adjacent to the hydroxamic acid. Bioorganic & Medicinal Chemistry Letters. 17: 2216-9. PMID 17307359 DOI: 10.1016/J.Bmcl.2007.01.117 |
0.788 |
|
2007 |
Green KD, Pflum MK. Kinase-catalyzed biotinylation for phosphoprotein detection. Journal of the American Chemical Society. 129: 10-1. PMID 17199263 DOI: 10.1021/Ja066828O |
0.636 |
|
2006 |
Warthaka M, Karwowska-Desaulniers P, Pflum MK. Phosphopeptide modification and enrichment by oxidation-reduction condensation. Acs Chemical Biology. 1: 697-701. PMID 17184134 DOI: 10.1021/Cb6003564 |
0.749 |
|
2006 |
Kamath N, Karwowska-Desaulniers P, Pflum MK. Limited proteolysis of human histone deacetylase 1. Bmc Biochemistry. 7: 22. PMID 17022812 DOI: 10.1186/1471-2091-7-22 |
0.793 |
|
2004 |
Pflum MK. Grafting miniature DNA binding proteins. Chemistry & Biology. 11: 3-4. PMID 15112983 DOI: 10.1016/J.Chembiol.2004.01.010 |
0.324 |
|
2001 |
Pflum MK, Tong JK, Lane WS, Schreiber SL. Histone deacetylase 1 phosphorylation promotes enzymatic activity and complex formation. The Journal of Biological Chemistry. 276: 47733-41. PMID 11602581 DOI: 10.1074/Jbc.M105590200 |
0.807 |
|
2001 |
Pflum MK, Schneider TL, Hall D, Schepartz A. Hepatitis B virus X protein activates transcription by bypassing CREB phosphorylation, not by stabilizing bZIP-DNA complexes. Biochemistry. 40: 693-703. PMID 11170386 DOI: 10.1021/Bi0011936 |
0.727 |
|
Low-probability matches (unlikely to be authored by this person) |
2006 |
Pflum MK. H-NS gives invading DNA the silent treatment. Nature Chemical Biology. 2: 400-1. PMID 16850014 DOI: 10.1038/Nchembio0806-400 |
0.235 |
|
2006 |
Flammer JR, Popova KN, Pflum MK. Cyclic AMP response element-binding protein (CREB) and CAAT/enhancer-binding protein beta (C/EBPbeta) bind chimeric DNA sites with high affinity. Biochemistry. 45: 9615-23. PMID 16878996 DOI: 10.1021/bi052521a |
0.146 |
|
Hide low-probability matches. |