Agency
National Institute of Health (NIH)
Institute
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Type
Method to Extend Research in Time (MERIT) Award (R37)
Project #
3R37DK013149-23S1
Application #
3482994
Study Section
Endocrinology Study Section (END)
Project Start
1977-01-01
Project End
1991-12-31
Budget Start
1990-01-01
Budget End
1990-12-31
Support Year
23
Fiscal Year
1990
Total Cost
Indirect Cost
Name
University of California San Diego
Department
Type
Schools of Medicine
DUNS #
077758407
City
La Jolla
State
CA
Country
United States
Zip Code
92093
Yeo, Michele; Lin, Patrick S (2007) Functional characterization of small CTD phosphatases. Methods Mol Biol 365:335-46
Lee, Soo-Kyung; Jurata, Linda W; Nowak, Roberta et al. (2005) The LIM domain-only protein LMO4 is required for neural tube closure. Mol Cell Neurosci 28:205-14
Yeo, Michele; Lee, Soo-Kyung; Lee, Bora et al. (2005) Small CTD phosphatases function in silencing neuronal gene expression. Science 307:596-600
Yeo, Michele; Lin, Patrick S; Dahmus, Michael E et al. (2003) A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5. J Biol Chem 278:26078-85
Gill, Gordon N (2003) Decoding the LIM development code. Trans Am Clin Climatol Assoc 114:179-89
Thaler, Joshua P; Lee, Soo-Kyung; Jurata, Linda W et al. (2002) LIM factor Lhx3 contributes to the specification of motor neuron and interneuron identity through cell-type-specific protein-protein interactions. Cell 110:237-49
van Meyel, D J; O'Keefe, D D; Thor, S et al. (2000) Chip is an essential cofactor for apterous in the regulation of axon guidance in Drosophila. Development 127:1823-31
Edwards, D C; Sanders, L C; Bokoch, G M et al. (1999) Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Nat Cell Biol 1:253-9
van Meyel, D J; O'Keefe, D D; Jurata, L W et al. (1999) Chip and apterous physically interact to form a functional complex during Drosophila development. Mol Cell 4:259-65
Klingbeil, C K; Gill, G N (1999) A basic residue, Lys 782, composes part of the ATP-binding site on the epidermal growth factor receptor tyrosine kinase. Arch Biochem Biophys 363:27-32

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