Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS)
Type
Research Project (R01)
Project #
1R01AR041161-01A5
Application #
2080523
Study Section
Physical Biochemistry Study Section (PB)
Project Start
1996-04-15
Project End
2000-03-31
Budget Start
1996-04-15
Budget End
1997-03-31
Support Year
1
Fiscal Year
1996
Total Cost
Indirect Cost

  Institution

Name
University of Maryland Baltimore
Department
Biochemistry
Type
Schools of Medicine
DUNS #
003255213
City
Baltimore
State
MD
Country
United States
Zip Code
21201

  Publications

Digel, J; Abugo, O; Kobayashi, T et al. (2001) Calcium- and magnesium-dependent interactions between the C-terminus of troponin I and the N-terminal, regulatory domain of troponin C. Arch Biochem Biophys 387:243-9
Kobayashi, T; Kobayashi, M; Collins, J H (2001) Ca(2+)-dependent, myosin subfragment 1-induced proximity changes between actin and the inhibitory region of troponin I. Biochim Biophys Acta 1549:148-54
Zhao, X; Kobayashi, T; Gryczynski, Z et al. (2000) Calcium-induced flexibility changes in the troponin C-troponin I complex. Biochim Biophys Acta 1479:247-54
Kobayashi, T; Kobayashi, M; Gryczynski, Z et al. (2000) Inhibitory region of troponin I: Ca(2+)-dependent structural and environmental changes in the troponin-tropomyosin complex and in reconstituted thin filaments. Biochemistry 39:86-91
Kobayashi, T; Zhao, X; Wade, R et al. (1999) Involvement of conserved, acidic residues in the N-terminal domain of troponin C in calcium-dependent regulation. Biochemistry 38:5386-91
Khaitlina, S; Antropova, O; Kuznetsova, I et al. (1999) Correlation between polymerizability and conformation in scallop beta-like actin and rabbit skeletal muscle alpha-actin. Arch Biochem Biophys 368:105-11