Genetic Mapping and Exome Sequencing Identify Variants Associated with Five Novel Diseases
- E. Puffenberger, R. N. Jinks, K. Strauss
- BiologyPLoS ONE
- 17 January 2012
The results reveal the power of coupling new genotyping technologies to population-specific genetic knowledge and robust clinical data and show evidence to strongly support the pathogenicity of variants identified in TUBGCP6, BRAT1, SNIP1, CRADD, and HARS.
Transfer RNA and human disease
- Jamie A. Abbott, C. Francklyn, Susan M Robey-Bond
- BiologyFrontiers in Genetics
- 3 June 2014
This chapter will review recent literature on the relation of mitochondrial and cytoplasmic tRNA, and enzymes that process tRNAs, to human disease and explore the mechanisms involved in the clinical presentation of these various diseases with an emphasis on neurological disease.
Germ-line variant of human NTH1 DNA glycosylase induces genomic instability and cellular transformation
- H. Galick, Scott D. Kathe, J. Sweasy
- BiologyProceedings of the National Academy of Sciences
- 12 August 2013
It is demonstrated that expression of the D239Y variant in cells also expressing wild-type NTH1 leads to genomic instability and cellular transformation as assessed by anchorage-independent growth, focus formation, invasion, and chromosomal aberrations, and the data suggest that individuals possessing the D 239Y variant are at risk for genomic stability and cancer.
Clostridium acetobutylicum 8-oxoguanine DNA glycosylase (Ogg) differs from eukaryotic Oggs with respect to opposite base discrimination.
- Susan M Robey-Bond, Ramiro Barrantes-Reynolds, J. Bond, S. Wallace, V. Bandaru
- BiologyBiochemistry
- 22 July 2008
The first characterization of a bacterial Ogg, Clostridium acetobutylicum Ogg (CacOgg), is reported, which shows unambiguous qualitative functional differences in vitro between hOGG1 and both hOGg1 and EcoFpg and is consistent with the idea that evolution of Ogg function is based on kinetic control of repair.
Structural characterization of Clostridium acetobutylicum 8-oxoguanine DNA glycosylase in its apo form and in complex with 8-oxodeoxyguanosine.
- F. Faucher, Susan M Robey-Bond, S. Wallace, S. Doublié
- Chemistry, BiologyJournal of Molecular Biology
- 3 April 2009
Substrate specificity and catalysis by the editing active site of Alanyl-tRNA synthetase from Escherichia coli.
- Z. Pasman, Susan M Robey-Bond, A. Mirando, Gregory J. Smith, Astrid Lague, C. Francklyn
- Biology, ChemistryBiochemistry
- 8 March 2011
Deacylation activities of the wild type and five different Escherichia coli AlaRS editing site substitution mutants were characterized, providing the only example of a true reversal of substrate specificity and highlighting a potential role of the coordinated zinc in editing substrate specificity.
The Usher Syndrome Type IIIB Histidyl-tRNA Synthetase Mutation Confers Temperature Sensitivity.
- Jamie A. Abbott, E. Guth, Susan M Robey-Bond
- BiologyBiochemistry
- 7 July 2017
The results demonstrate that the Y454S substitution leaves HARS amino acid activation, aminoacylation, and tRNAHis binding functions largely intact compared with those of WT HARS, and the mutant enzyme dimerizes like the wild type does.