Year |
Citation |
Score |
2020 |
Sanderson MR, Badior KE, Fahlman RP, Wevrick R. The necdin interactome: evaluating the effects of amino acid substitutions and cell stress using proximity-dependent biotinylation (BioID) and mass spectrometry. Human Genetics. PMID 32529326 DOI: 10.1007/S00439-020-02193-9 |
0.314 |
|
2020 |
Eldeeb M, Esmaili M, Fahlman R. Degradation of proteins with N-terminal glycine. Nature Structural & Molecular Biology. 26: 761-763. PMID 31477902 DOI: 10.1038/S41594-019-0291-1 |
0.339 |
|
2019 |
McRae EKS, Dupas SJ, Booy EP, Piragasam RS, Fahlman RP, McKenna SA. An RNA guanine quadruplex regulated pathway to TRAIL-sensitization by DDX21. Rna (New York, N.Y.). PMID 31653714 DOI: 10.1261/Rna.072199.119 |
0.333 |
|
2019 |
Eldeeb MA, Fahlman RP, Ragheb MA, Esmaili M. Does N-Terminal Protein Acetylation Lead to Protein Degradation? Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology. e1800167. PMID 31549739 DOI: 10.1002/Bies.201800167 |
0.346 |
|
2019 |
Eldeeb MA, Piragasam RS, Ragheb MA, Esmaili M, Salla M, Fahlman RP. A molecular toolbox for studying protein degradation in mammalian cells. Journal of Neurochemistry. PMID 31357232 DOI: 10.1111/Jnc.14838 |
0.325 |
|
2019 |
Eldeeb MA, Fahlman RP, Esmaili M, Fon EA. Formylation of Eukaryotic Cytoplasmic Proteins: Linking Stress to Degradation. Trends in Biochemical Sciences. PMID 30661830 DOI: 10.1016/J.Tibs.2018.12.008 |
0.343 |
|
2018 |
Eldeeb MA, Fahlman RP, Esmaili M, Ragheb MA. Regulating Apoptosis by Degradation: The N-End Rule-Mediated Regulation of Apoptotic Proteolytic Fragments in Mammalian Cells. International Journal of Molecular Sciences. 19. PMID 30384441 DOI: 10.3390/Ijms19113414 |
0.34 |
|
2017 |
Eldeeb MA, Leitao LCA, Fahlman RP. Emerging Branches of the N-End Rule Pathways are Revealing the Sequence Complexities of N-Termini Dependent Protein Degradation. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. PMID 29253354 DOI: 10.1139/Bcb-2017-0274 |
0.361 |
|
2017 |
Li L, Poon HY, Hildebrandt MR, Monckton EA, Germain DR, Fahlman RP, Godbout R. Role for RIF1-interacting partner DDX1 in BLM recruitment to DNA double-strand breaks. Dna Repair. 55: 47-63. PMID 28544931 DOI: 10.1016/J.Dnarep.2017.05.001 |
0.337 |
|
2017 |
Reimer KA, Stark MR, Aguilar LC, Stark SR, Burke RD, Moore J, Fahlman RP, Yip CK, Kuroiwa H, Oeffinger M, Rader SD. The sole LSm complex in Cyanidioschyzon merolae associates with pre-mRNA splicing and mRNA degradation factors. Rna (New York, N.Y.). PMID 28325844 DOI: 10.1261/Rna.058487.116 |
0.333 |
|
2016 |
Eldeeb MA, Fahlman RP. Phosphorylation Impacts N-End Rule Degradation of the Proteolytically Activated Form of BMX Kinase. The Journal of Biological Chemistry. PMID 27601470 DOI: 10.1074/Jbc.M116.737387 |
0.334 |
|
2016 |
Eldeeb M, Fahlman R. The-N-End Rule: The Beginning Determines the End. Protein and Peptide Letters. 23: 343-8. PMID 26743630 DOI: 10.2174/0929866523666160108115809 |
0.375 |
|
2015 |
Fung AW, Payoe R, Fahlman RP. Perspectives and Insights into the Competition for Aminoacyl-tRNAs between the Translational Machinery and for tRNA Dependent Non-Ribosomal Peptide Bond Formation. Life (Basel, Switzerland). 6. PMID 26729173 DOI: 10.3390/Life6010002 |
0.324 |
|
2015 |
Khan SR, Aljuhani N, Morgan AG, Baghdasarian A, Fahlman RP, Siraki AG. Cytoprotective effect of isoniazid against H2O2 derived injury in HL-60 cells. Chemico-Biological Interactions. PMID 26658028 DOI: 10.1016/J.Cbi.2015.11.026 |
0.307 |
|
2015 |
Lopez-Orozco J, Pare JM, Holme AL, Chaulk SG, Fahlman RP, Hobman TC. Functional analyses of phosphorylation events in human Argonaute 2. Rna (New York, N.Y.). 21: 2030-8. PMID 26443379 DOI: 10.1261/Rna.053207.115 |
0.302 |
|
2015 |
Khan SR, Baghdasarian A, Nagar PH, Fahlman R, Jurasz P, Michail K, Aljuhani N, Siraki AG. Proteomic profile of aminoglutethimide-induced apoptosis in HL-60 cells: Role of myeloperoxidase and arylamine free radicals. Chemico-Biological Interactions. PMID 26102013 DOI: 10.1016/J.Cbi.2015.06.020 |
0.306 |
|
2015 |
Fung AW, Fahlman RP. The molecular basis for the post-translational addition of amino acids by L/F transferase in the N-end rule pathway. Current Protein & Peptide Science. 16: 163-80. PMID 25692952 DOI: 10.2174/1389203716666150112095726 |
0.358 |
|
2014 |
Fung AW, Leung CC, Fahlman RP. The determination of tRNALeu recognition nucleotides for Escherichia coli L/F transferase. Rna (New York, N.Y.). 20: 1210-22. PMID 24935875 DOI: 10.1261/Rna.044529.114 |
0.312 |
|
2014 |
Eldeeb MA, Fahlman RP. The anti-apoptotic form of tyrosine kinase Lyn that is generated by proteolysis is degraded by the N-end rule pathway. Oncotarget. 5: 2714-22. PMID 24798867 DOI: 10.18632/Oncotarget.1931 |
0.314 |
|
2014 |
Fung AW, Ebhardt HA, Krishnakumar KS, Moore J, Xu Z, Strazewski P, Fahlman RP. Probing the leucyl/phenylalanyl tRNA protein transferase active site with tRNA substrate analogues. Protein and Peptide Letters. 21: 603-14. PMID 24521222 DOI: 10.2174/0929866521666140212110639 |
0.316 |
|
2014 |
Fahlman RP, Chen W, Overall CM. Absolute proteomic quantification of the activity state of proteases and proteolytic cleavages using proteolytic signature peptides and isobaric tags. Journal of Proteomics. 100: 79-91. PMID 24060996 DOI: 10.1016/J.Jprot.2013.09.006 |
0.327 |
|
2012 |
Xu Z, Payoe R, Fahlman RP. The C-terminal proteolytic fragment of the breast cancer susceptibility type 1 protein (BRCA1) is degraded by the N-end rule pathway. The Journal of Biological Chemistry. 287: 7495-502. PMID 22262859 DOI: 10.1074/Jbc.M111.301002 |
0.308 |
|
2011 |
Fung AW, Ebhardt HA, Abeysundara H, Moore J, Xu Z, Fahlman RP. An alternative mechanism for the catalysis of peptide bond formation by L/F transferase: substrate binding and orientation. Journal of Molecular Biology. 409: 617-29. PMID 21530538 DOI: 10.1016/J.Jmb.2011.04.033 |
0.327 |
|
2011 |
Payoe R, Fahlman RP. Dependence of RelA-mediated (p)ppGpp formation on tRNA identity. Biochemistry. 50: 3075-83. PMID 21410133 DOI: 10.1021/Bi1015309 |
0.316 |
|
2009 |
Ebhardt HA, Xu Z, Fung AW, Fahlman RP. Quantification of the post-translational addition of amino acids to proteins by MALDI-TOF mass spectrometry. Analytical Chemistry. 81: 1937-43. PMID 19186990 DOI: 10.1021/Ac802423D |
0.333 |
|
2009 |
Dale T, Fahlman RP, Olejniczak M, Uhlenbeck OC. Specificity of the ribosomal A site for aminoacyl-tRNAs. Nucleic Acids Research. 37: 1202-10. PMID 19129224 DOI: 10.1093/Nar/Gkn1040 |
0.313 |
|
2004 |
Fahlman RP, Dale T, Uhlenbeck OC. Uniform binding of aminoacylated transfer RNAs to the ribosomal A and P sites. Molecular Cell. 16: 799-805. PMID 15574334 DOI: 10.1016/J.Molcel.2004.10.030 |
0.318 |
|
2003 |
Fahlman RP, Hsing M, Sporer-Tuhten CS, Sen D. Duplex pinching: A structural switch suitable for contractile DNA nanoconstructions Nano Letters. 3: 1073-1078. DOI: 10.1021/Nl034267I |
0.52 |
|
2002 |
Fahlman RP, Sharma RD, Sen D. The charge conduction properties of DNA holliday junctions depend critically on the identity of the tethered photooxidant. Journal of the American Chemical Society. 124: 12477-85. PMID 12381189 DOI: 10.1021/Ja020495N |
0.503 |
|
2002 |
Fahlman RP, Sen D. DNA conformational switches as sensitive electronic sensors of analytes. Journal of the American Chemical Society. 124: 4610-6. PMID 11971708 DOI: 10.1021/ja012618u |
0.442 |
|
1999 |
Fahlman RP, Sen D. 'Synapsable' DNA double helices: Self-selective modules for assembling DNA superstructures Journal of the American Chemical Society. 121: 11079-11085. DOI: 10.1021/Ja992574D |
0.508 |
|
1998 |
Fahlman RP, Sen D. Cation-regulated self-association of "synapsable" DNA duplexes. Journal of Molecular Biology. 280: 237-44. PMID 9654448 DOI: 10.1006/Jmbi.1998.1875 |
0.51 |
|
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