C
Christopher J. Brandl
Researcher at University of Western Ontario
Publications - 51
Citations - 994
Christopher J. Brandl is an academic researcher from University of Western Ontario. The author has contributed to research in topics: Saccharomyces cerevisiae & Transfer RNA. The author has an hindex of 19, co-authored 51 publications receiving 830 citations.
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Journal ArticleDOI
Pathways to disease from natural variations in human cytoplasmic tRNAs
TL;DR: The unanticipated prevalence of mistranslating tRNA variants in the human population is highlighted and the emerging literature suggests that human diseases may be affected by natural t RNA variants that cause mistranslation or de-regulate tRNA expression and nucleotide modification.
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Discovery and characterization of a nonphosphorylated cyclic peptide inhibitor of the peptidylprolyl isomerase, Pin1.
Kelly E. Duncan,Brian R. Dempsey,Lauren E. Killip,Jarrett Adams,Melanie L. Bailey,Gilles A. Lajoie,David W. Litchfield,Christopher J. Brandl,Gary S. Shaw,Brian H. Shilton +9 more
TL;DR: NMR chemical shift perturbation experiments show that cyclic CRYPEVEIC binds to the active site of Pin1, enabling high affinity binding without the presence of a phosphate group.
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The role of histone ubiquitylation and deubiquitylation in gene expression as determined by the analysis of an HTB1 K123R Saccharomyces cerevisiae strain
A. Irina Mutiu,Stephen M. T. Hoke,Julie Genereaux,Gaoyang Liang,Gaoyang Liang,Christopher J. Brandl +5 more
TL;DR: It is concluded that lysine 123 affects transcription primarily because of it being a site of ubiquitylation.
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The dual histidine motif in the active site of Pin1 has a structural rather than catalytic role.
TL;DR: It is indicated that H59 and H157 are not required for hydrogen bonding within the active site, and in contrast to theActive site C113, they do not participate directly in catalysis.
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Genetic selection for mistranslation rescues a defective co-chaperone in yeast
TL;DR: A strategy that allows mistranslation to suppress deleterious missense Pro mutations in Tti2 is identified, and introduced the same G3:U70 mutation in SUF2 (tRNAProAGG) suppressed a second tti2 allele (tti2L50P).