Agency
National Institute of Health (NIH)
Institute
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Type
Research Project (R01)
Project #
5R01DK050074-02
Application #
2151069
Study Section
Biochemistry Study Section (BIO)
Project Start
1995-08-01
Project End
1998-07-31
Budget Start
1996-08-01
Budget End
1997-07-31
Support Year
2
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Mount Sinai School of Medicine
Department
Biochemistry
Type
Schools of Medicine
DUNS #
City
New York
State
NY
Country
United States
Zip Code
10029
Till, J H; Ablooglu, A J; Frankel, M et al. (2001) Crystallographic and solution studies of an activation loop mutant of the insulin receptor tyrosine kinase: insights into kinase mechanism. J Biol Chem 276:10049-55
Ablooglu, A J; Kohanski, R A (2001) Activation of the insulin receptor's kinase domain changes the rate-determining step of substrate phosphorylation. Biochemistry 40:504-13
Ablooglu, A J; Till, J H; Kim, K et al. (2000) Probing the catalytic mechanism of the insulin receptor kinase with a tetrafluorotyrosine-containing peptide substrate. J Biol Chem 275:30394-8
Bishop, S M; Ross, J B; Kohanski, R A (1999) Autophosphorylation dependent destabilization of the insulin receptor kinase domain: tryptophan-1175 reports changes in the catalytic cleft. Biochemistry 38:3079-89
Frankel, M; Bishop, S M; Ablooglu, A J et al. (1999) Conformational changes in the activation loop of the insulin receptor's kinase domain. Protein Sci 8:2158-65
Wang, R; Chait, B T; Wolf, I et al. (1999) Lysozyme degradation by the bovine multicatalytic proteinase complex (proteasome): evidence for a nonprocessive mode of degradation. Biochemistry 38:14573-81
Cann, A D; Bishop, S M; Ablooglu, A J et al. (1998) Partial activation of the insulin receptor kinase domain by juxtamembrane autophosphorylation. Biochemistry 37:11289-300
Cardozo, C; Kohanski, R A (1998) Altered properties of the branched chain amino acid-preferring activity contribute to increased cleavages after branched chain residues by the ""immunoproteasome"". J Biol Chem 273:16764-70
Chen, J; Sadowski, H B; Kohanski, R A et al. (1997) Stat5 is a physiological substrate of the insulin receptor. Proc Natl Acad Sci U S A 94:2295-300
Cann, A D; Wolf, I; Kohanski, R A (1997) A tyrosine kinase assay using reverse-phase high-performance liquid chromatography. Anal Biochem 247:327-32

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