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B96Bom encodes a Bombyx mori tyramine receptor negatively coupled to adenylate cyclase
Findings indicate that the B96Bom receptor is a B. mori TA receptor, which is negatively coupled to adenylate cyclase, and the use of this expression system should facilitate physiological studies of TA receptors as well as structure–activity studies ofTA receptor ligands.
Amino Acid Residue Penultimate to the Amino-terminal Gly Residue Strongly Affects Two Cotranslational Protein Modifications, N-Myristoylation andN-Acetylation*
- T. Utsumi, M. Sato, K. Nakano, D. Takemura, H. Iwata, R. Ishisaka
- Biology, ChemistryThe Journal of Biological Chemistry
- 30 March 2001
The amino acid residue penultimate to the N-terminal Gly residue strongly affected two cotranslational protein modifications, N-myristoylation andN-acetylation, and the amino acid requirements at this position for these two modifications were significantly affected by downstream residues.
Induction and mechanism of apoptotic cell death by propofol in HL‐60 cells
It is of both clinical interest and biomedical importance to investigate and clarify the effect and mechanism of propofol upon the intracellular reactions underlying apoptotic cell death.
C‐terminal 15 kDa fragment of cytoskeletal actin is posttranslationally N‐myristoylated upon caspase‐mediated cleavage and targeted to mitochondria
Vertical-scanning mutagenesis of amino acids in a model N-myristoylation motif reveals the major amino-terminal sequence requirements for protein N-myristoylation.
The amino acid requirements found in this study were fully consistent with the N-terminal sequence of 78 N- myristoylated proteins in which N-myristoylation was experimentally verified and strongly indicate that the combination of amino acids at position 3, 6 and 7 is a major determinant for protein N-Myristoylations.
Amino acid residues involved in interaction with tyramine in the Bombyx mori tyramine receptor
It is confirmed that at least three amino acid residues play key roles in interaction with tyramine (TA) in the BmTA receptor.
Participation of a cathepsin L-type protease in the activation of caspase-3.
Results suggested that a cathepsin L-type protease activity might participate in the activation mechanism of caspase-3 in the presence of the supernatant of the digitonin-treated ML.
Oxidative Stress Underlies the Mechanism for Ca2+-induced Permeability Transition of Mitochondria
Results indicate that Ca2+ increases the generation of ROS which oxidize the free thiol groups in mitochondrial ANT, thereby inducing MPT to release cytochrome c.
Activation of caspase‐3‐like protease by digitonin‐treated lysosomes