Agency
National Institute of Health (NIH)
Institute
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Type
Research Project (R01)
Project #
3R01DK018849-10S1
Application #
3226158
Study Section
Biochemistry Study Section (BIO)
Project Start
1976-05-01
Project End
1989-06-30
Budget Start
1986-02-15
Budget End
1986-06-30
Support Year
10
Fiscal Year
1986
Total Cost
Indirect Cost
Name
Purdue University
Department
Type
Earth Sciences/Resources
DUNS #
072051394
City
West Lafayette
State
IN
Country
United States
Zip Code
47907
Banerjee, Sourav; Ji, Chenggong; Mayfield, Joshua E et al. (2018) Ancient drug curcumin impedes 26S proteasome activity by direct inhibition of dual-specificity tyrosine-regulated kinase 2. Proc Natl Acad Sci U S A 115:8155-8160
Zhang, Hui; Zhu, Qinyu; Cui, Jixin et al. (2018) Structure and evolution of the Fam20 kinases. Nat Commun 9:1218
Qiu, Yimin; Poppleton, Erik; Mekkat, Arya et al. (2018) Enzymatic Phosphorylation of Ser in a Type I Collagen Peptide. Biophys J 115:2327-2335
Pollak, Adam J; Haghighi, Kobra; Kunduri, Swati et al. (2017) Phosphorylation of serine96 of histidine-rich calcium-binding protein by the Fam20C kinase functions to prevent cardiac arrhythmia. Proc Natl Acad Sci U S A 114:9098-9103
Cui, Jixin; Zhu, Qinyu; Zhang, Hui et al. (2017) Structure of Fam20A reveals a pseudokinase featuring a unique disulfide pattern and inverted ATP-binding. Elife 6:
Wang, Xiaorong; Cimermancic, Peter; Yu, Clinton et al. (2017) Molecular Details Underlying Dynamic Structures and Regulation of the Human 26S Proteasome. Mol Cell Proteomics 16:840-854
Nguyen, Kim B; Sreelatha, Anju; Durrant, Eric S et al. (2016) Phosphorylation of spore coat proteins by a family of atypical protein kinases. Proc Natl Acad Sci U S A 113:E3482-91
Guo, Xing; Wang, Xiaorong; Wang, Zhiping et al. (2016) Site-specific proteasome phosphorylation controls cell proliferation and tumorigenesis. Nat Cell Biol 18:202-12
Tagliabracci, Vincent S; Wiley, Sandra E; Guo, Xiao et al. (2015) A Single Kinase Generates the Majority of the Secreted Phosphoproteome. Cell 161:1619-32
He, Yantao; Guo, Xing; Yu, Zhi-Hong et al. (2015) A potent and selective inhibitor for the UBLCP1 proteasome phosphatase. Bioorg Med Chem 23:2798-809

Showing the most recent 10 out of 83 publications