S. Imajoh

发表

Limited autolysis of calcium-activated neutral protease (CANP): reduction of the Ca2+-requirement is due to the NH2-terminal processing of the large subunit.

H. Kawasaki, K. Suzuki, S. Imajoh, 1986, Journal of biochemistry.

The amino-terminal hydrophobic region of the small subunit of calcium-activated neutral protease (CANP) is essential for its activation by phosphatidylinositol.

H. Kawasaki, K. Suzuki, S. Imajoh, 1986, Journal of biochemistry.

Complete amino acid sequence of the large subunit of the low‐Ca2+‐requiring form of human Ca2+‐activated neutral protease (μCANP) deduced from its cDNA sequence

K. Suzuki, M. Koike, K. Aoki, 1986, FEBS letters.

A 107-kDa INHIBITOR FOR CALCIUM-ACTIVATED NEUTRAL PROTEASE (CANP): PURIFICATION FROM THE HUMAN LIVER

H. Kawasaki, M. Mukai, Koichi Suzuki, 1984 .

Molecular cloning and sequencing of cDNA for rat cathepsin L

H. Kawasaki, N. Katunuma, E. Kominami, 1987, FEBS letters.

Endogenous inhibitor for calcium-dependent cysteine protease contains four internal repeats that could be responsible for its multiple reactive sites.

K. Imahori, H. Kawasaki, K. Suzuki, 1987, Proceedings of the National Academy of Sciences of the United States of America.

All four repeating domains of the endogenous inhibitor for calcium-dependent protease independently retain inhibitory activity. Expression of the cDNA fragments in Escherichia coli.

H. Kawasaki, K. Suzuki, Y. Emori, 1988, The Journal of biological chemistry.

Calcium-activated neutral protease inhibitor from rabbit erythrocytes lacks the N-terminal region of the liver inhibitor but retains three inhibitory units.

H. Kawasaki, K. Suzuki, Y. Emori, 1987, Biochemical and biophysical research communications.

The COOH-terminal E-F hand structure of calcium-activated neutral protease (CANP) is important for the association of subunits and resulting proteolytic activity.

H. Kawasaki, K. Suzuki, S. Imajoh, 1987, Journal of biochemistry.

Isolation and sequence analyses of cDNA clones for the large subunits of two isozymes of rabbit calcium-dependent protease.

H. Kawasaki, K. Suzuki, Y. Emori, 1986, The Journal of biological chemistry.

Reversible interaction between Ca2+‐activated neutral protease (CANP) and its endogenous inhibitor

K. Suzuki, S. Imajoh, Koichi Suzuki, 1985, FEBS Letters.

Regulation of Plasma Low Density Lipoprotein Levels Biopharmacological Regulation of Protein Phosphorylation Calcium-Activated Neutral Protease Microbial Iron Transport Pharmacokinetic Drug Interactions

H. Kawasaki, K. Suzuki, M. Hagiwara, 1988, Progress in Clinical Biochemistry and Medicine.

Tissue-specific expression of three distinct types of rabbit protein kinase C

H. Kawasaki, H. Hidaka, M. Inagaki, 1987, Nature.

Evolutionary origin of a calcium-dependent protease by fusion of genes for a thiol protease and a calcium-binding protein?

H. Kawasaki, Y. Emori, S. Ohno, 1984, Nature.

Purification and some characteristics of a zinc metalloprotease from the venom of Bothrops jararaca (jararaca).

K. Suzuki, R. Zingali, S. Imajoh, 1989, Toxicon : official journal of the International Society on Toxinology.

Molecular cloning of the cDNA for the large subunit of the high-Ca2+-requiring form of human Ca2+-activated neutral protease.

H. Kawasaki, K. Suzuki, K. Aoki, 1988, Biochemistry.

Fragmentation of an endogenous inhibitor upon complex formation with high- and low-Ca2+-requiring forms of calcium-activated neutral proteases.

M. Nakamura, S. Kawashima, M. Inomata, 1989, Biochemistry.

Fragment of an endogenous inhibitor produced in Escherichia coli for calcium‐activated neutral protease (CANP) retains an inhibitory activity

K. Imahori, H. Kawasaki, Y. Emori, 1987, FEBS letters.

A novel phorbol ester receptor/protein kinase, nPKC, distantly related to the protein kinase C family

S. Ohno, Koichi Suzuki, Y. Akita, 1988, Cell.

The small subunits of calcium dependent proteases with different calcium sensitivities are identical.

H. Kawasaki, K. Suzuki, S. Kawashima, 1986, Journal of biochemistry.

[30] Cloning and evolution of calcium-dependent protease, cDNA cloning of a novel family of calcium-binding proteins

Y. Emori, S. Ohno, Koichi Suzuki, 1987 .

Regulation of activity of calcium activated neutral protease.

H. Kawasaki, K. Suzuki, Y. Emori, 1988, Advances in enzyme regulation.

Calcium‐activated neutral protease and its endogenous inhibitor Activation at the cell membrane and biological function

H. Kawasaki, Y. Emori, Y. Minami, 1987, FEBS letters.

Calcium-Activated Neutral Protease (CANP) and its Biological and Medical Implications

H. Kawasaki, Y. Emori, S. Ohno, 1987 .

Isolation and sequence analysis of cDNA clones for the small subunit of rabbit calcium-dependent protease.

H. Kawasaki, K. Suzuki, Y. Emori, 1986, The Journal of biological chemistry.

The receptor for colicin E3. Isolation and some properties.

K. Imahori, S. Imajoh, Y. Ohno‐Iwashita, 1982, The Journal of biological chemistry.

Structure and Activity-Regulation of Chimeric Proteins a Case Study of Calcium-Activated Neutral Protease

H. Kawasaki, Y. Emori, Y. Minami, 1987 .

IDENTIFICATION AND DISTRIBUTION OF mRNA FOR CALCIUM-ACTIVATED NEUTRAL PROTEASE (CANP)

H. Kawasaki, Y. Emori, S. Ohno, 1988 .

Analysis of calcium-binding sites in calcium-activated neutral protease.

H. Kawasaki, K. Suzuki, Y. Emori, 1989, Advances in experimental medicine and biology.

Molecular cloning and sequencing of cDNA for rat cathepsin H Homology in pro‐peptide regions of cysteine proteinases

H. Kawasaki, N. Katunuma, Y. Emori, 1987, FEBS letters.

Calcium-activated neutral protease (CANP), a putative processing enzyme of the neuropeptide, kyotorphin, in the brain.

Y. Yoshihara, H. Takagi, M. Satoh, 1988, Biochemical and biophysical research communications.

Active-site residues of the transpeptidase domain of penicillin-binding protein 2 from Escherichia coli: similarity in catalytic mechanism to class A beta-lactamases.

H. Matsuzawa, T. Ohta, H. Adachi, 1992, Biochemistry.