Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Institutional National Research Service Award (T32)
Project #
5T32CA009363-14
Application #
2085369
Study Section
Cancer Institutional Fellowship Review Committee (CT)
Project Start
1980-07-01
Project End
1996-06-30
Budget Start
1994-07-01
Budget End
1995-06-30
Support Year
14
Fiscal Year
1994
Total Cost
Indirect Cost
Name
University of Rochester
Department
Internal Medicine/Medicine
Type
Schools of Dentistry
DUNS #
208469486
City
Rochester
State
NY
Country
United States
Zip Code
14627
Gleghorn, Michael L; Zhao, Jianbo; Turner, Douglas H et al. (2016) Crystal structure of a poly(rA) staggered zipper at acidic pH: evidence that adenine N1 protonation mediates parallel double helix formation. Nucleic Acids Res 44:8417-24
Guy, Michael P; Phizicky, Eric M (2015) Conservation of an intricate circuit for crucial modifications of the tRNAPhe anticodon loop in eukaryotes. RNA 21:61-74
McCall, Matthew N; McMurray, Helene R; Land, Hartmut et al. (2014) On non-detects in qPCR data. Bioinformatics 30:2310-6
Gleghorn, Michael L; Maquat, Lynne E (2014) 'Black sheep' that don't leave the double-stranded RNA-binding domain fold. Trends Biochem Sci 39:328-40
Haider, Baqer A; Baras, Alexander S; McCall, Matthew N et al. (2014) A critical evaluation of microRNA biomarkers in non-neoplastic disease. PLoS One 9:e89565
McCall, Matthew N; Jaffee, Harris A; Zelisko, Susan J et al. (2014) The Gene Expression Barcode 3.0: improved data processing and mining tools. Nucleic Acids Res 42:D938-43
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Barone, Maria Cecilia; Bohmann, Dirk (2013) Assessing neurodegenerative phenotypes in Drosophila dopaminergic neurons by climbing assays and whole brain immunostaining. J Vis Exp :e50339
Gleghorn, Michael L; Gong, Chenguang; Kielkopf, Clara L et al. (2013) Staufen1 dimerizes through a conserved motif and a degenerate dsRNA-binding domain to promote mRNA decay. Nat Struct Mol Biol 20:515-24
Park, Eonyoung; Gleghorn, Michael L; Maquat, Lynne E (2013) Staufen2 functions in Staufen1-mediated mRNA decay by binding to itself and its paralog and promoting UPF1 helicase but not ATPase activity. Proc Natl Acad Sci U S A 110:405-12

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