Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM040602-09
Application #
2180472
Study Section
Physical Biochemistry Study Section (PB)
Project Start
1988-07-01
Project End
1997-06-30
Budget Start
1996-07-01
Budget End
1997-06-30
Support Year
9
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Duke University
Department
Biochemistry
Type
Schools of Medicine
DUNS #
071723621
City
Durham
State
NC
Country
United States
Zip Code
27705
CastaƱeda, Carol Ann; Wolfson, Noah A; Leng, Katherine R et al. (2017) HDAC8 substrate selectivity is determined by long- and short-range interactions leading to enhanced reactivity for full-length histone substrates compared with peptides. J Biol Chem 292:21568-21577
Niu, Shuai; Kim, Byung Chul; Fierke, Carol A et al. (2017) Ion Mobility-Mass Spectrometry Reveals Evidence of Specific Complex Formation between Human Histone Deacetylase 8 and Poly-r(C)-binding Protein 1. Int J Mass Spectrom 420:9-15
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Bergom, Carmen; Hauser, Andrew D; Rymaszewski, Amy et al. (2016) The tumor-suppressive small GTPase DiRas1 binds the noncanonical guanine nucleotide exchange factor SmgGDS and antagonizes SmgGDS interactions with oncogenic small GTPases. J Biol Chem 291:10948
Temple, Kayla J; Wright, Elia N; Fierke, Carol A et al. (2016) Synthesis of Non-natural, Frame-Shifted Isoprenoid Diphosphate Analogues. Org Lett 18:6038-6041
Temple, Kayla J; Wright, Elia N; Fierke, Carol A et al. (2016) Exploration of GGTase-I substrate requirements. Part 2: Synthesis and biochemical analysis of novel saturated geranylgeranyl diphosphate analogs. Bioorg Med Chem Lett 26:3503-7
Bergom, Carmen; Hauser, Andrew D; Rymaszewski, Amy et al. (2016) The Tumor-suppressive Small GTPase DiRas1 Binds the Noncanonical Guanine Nucleotide Exchange Factor SmgGDS and Antagonizes SmgGDS Interactions with Oncogenic Small GTPases. J Biol Chem 291:6534-45

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