Agency
National Institute of Health (NIH)
Institute
National Heart, Lung, and Blood Institute (NHLBI)
Type
Research Project (R01)
Project #
5R01HL038412-08
Application #
2218830
Study Section
Biochemistry Study Section (BIO)
Project Start
1986-09-01
Project End
1998-03-31
Budget Start
1996-04-01
Budget End
1997-03-31
Support Year
8
Fiscal Year
1996
Total Cost
Indirect Cost
Name
University of Missouri Kansas City
Department
Anatomy/Cell Biology
Type
Schools of Medicine
DUNS #
800772162
City
Kansas City
State
MO
Country
United States
Zip Code
64110
Mattingly Jr, J R; Yanez, A J; Martinez-Carrion, M (2000) The folding of nascent mitochondrial aspartate aminotransferase synthesized in a cell-free extract can be assisted by GroEL and GroES. Arch Biochem Biophys 382:113-22
Artigues, A; Crawford, D L; Iriarte, A et al. (1998) Divergent Hsc70 binding properties of mitochondrial and cytosolic aspartate aminotransferase. Implications for their segregation to different cellular compartments. J Biol Chem 273:33130-4
Torella, C; Mattingly Jr, J R; Artigues, A et al. (1998) Insight into the conformation of protein folding intermediate(s) trapped by GroEL. J Biol Chem 273:3915-25
Lain, B; Yanez, A; Iriarte, A et al. (1998) Aminotransferase variants as probes for the role of the N-terminal region of a mature protein in mitochondrial precursor import and processing. J Biol Chem 273:4406-15
Donate, F; Artigues, A; Iriarte, A et al. (1998) Opposite behavior of two isozymes when refolding in the presence of non-ionic detergents. Protein Sci 7:1811-20
Artigues, A; Iriarte, A; Martinez-Carrion, M (1997) Refolding intermediates of acid-unfolded mitochondrial aspartate aminotransferase bind to hsp70. J Biol Chem 272:16852-61
Mattingly Jr, J R; Iriarte, A; Martinez-Carrion, M (1995) Homologous proteins with different affinities for groEL. The refolding of the aspartate aminotransferase isozymes at varying temperatures. J Biol Chem 270:1138-48
Lain, B; Iriarte, A; Mattingly Jr, J R et al. (1995) Structural features of the precursor to mitochondrial aspartate aminotransferase responsible for binding to hsp70. J Biol Chem 270:24732-9
Reyes, A M; Iriarte, A; Martinez-Carrion, M (1993) Refolding of the precursor and mature forms of mitochondrial aspartate aminotransferase after guanidine hydrochloride denaturation. J Biol Chem 268:22281-91
Mattingly Jr, J R; Iriarte, A; Martinez-Carrion, M (1993) Structural features which control folding of homologous proteins in cell-free translation systems. The effect of a mitochondrial-targeting presequence on aspartate aminotransferase. J Biol Chem 268:26320-7

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