Michael P. Guy, Ph.D.
Affiliations: | 2008 | University of Wisconsin, Madison, Madison, WI |
Area:
BiochemistryGoogle:
"Michael Guy"Parents
Sign in to add mentorPaul D. Friesen | grad student | 2008 | UW Madison | |
(The reactive site loop cleavage motif of baculovirus P49 determines its caspase target.) |
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Publications
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Funk HM, Brooks JH, Detmer AE, et al. (2024) Identification of Amino Acids in Trm734 Required for 2'--Methylation of the tRNA Wobble Residue. Acs Omega. 9: 25063-25072 |
Funk HM, DiVita DJ, Sizemore HE, et al. (2022) Identification of a Trm732 Motif Required for 2'--methylation of the tRNA Anticodon Loop by Trm7. Acs Omega. 7: 13667-13675 |
Han L, Guy MP, Kon Y, et al. (2018) Lack of 2'-O-methylation in the tRNA anticodon loop of two phylogenetically distant yeast species activates the general amino acid control pathway. Plos Genetics. 14: e1007288 |
Shaheen R, Abdel-Salam GM, Guy MP, et al. (2015) Mutation in WDR4 impairs tRNA m(7)G46 methylation and causes a distinct form of microcephalic primordial dwarfism. Genome Biology. 16: 210 |
Guy MP, Shaw M, Weiner CL, et al. (2015) Defects in tRNA Anticodon Loop 2'-O-Methylation Are Implicated in Nonsyndromic X-Linked Intellectual Disability due to Mutations in FTSJ1. Human Mutation. 36: 1176-87 |
Payea MJ, Guy MP, Phizicky EM. (2015) Methodology for the High-Throughput Identification and Characterization of tRNA Variants That Are Substrates for a tRNA Decay Pathway. Methods in Enzymology. 560: 1-17 |
Guy MP, Phizicky EM. (2015) Conservation of an intricate circuit for crucial modifications of the tRNAPhe anticodon loop in eukaryotes. Rna (New York, N.Y.). 21: 61-74 |
Guy MP, Phizicky EM. (2014) Two-subunit enzymes involved in eukaryotic post-transcriptional tRNA modification. Rna Biology. 11: 1608-18 |
Guy MP, Young DL, Payea MJ, et al. (2014) Identification of the determinants of tRNA function and susceptibility to rapid tRNA decay by high-throughput in vivo analysis. Genes & Development. 28: 1721-32 |
Guy MP, Podyma BM, Preston MA, et al. (2012) Yeast Trm7 interacts with distinct proteins for critical modifications of the tRNAPhe anticodon loop. Rna (New York, N.Y.). 18: 1921-33 |