Imajoh S - Search Results

1

Regulation of activity of calcium activated neutral protease.

Suzuki K, Imajoh S, Emori Y, Kawasaki H, Minami Y, Ohno S. Suzuki K, et al. Among authors: imajoh s. Adv Enzyme Regul. 1988;27:153-69. doi: 10.1016/0065-2571(88)90015-5. Adv Enzyme Regul. 1988. PMID: 2854947

2

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

Nakamura M, Inomata M, Imajoh S, Suzuki K, Kawashima S. Nakamura M, et al. Among authors: imajoh s. Biochemistry. 1989 Jan 24;28(2):449-55. doi: 10.1021/bi00428a007. Biochemistry. 1989. PMID: 2540798

3

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

Suzuki K, Minami Y, Emori Y, Imajoh S, Kawasaki H. Suzuki K, et al. Among authors: imajoh s. Adv Exp Med Biol. 1989;255:173-83. doi: 10.1007/978-1-4684-5679-0_19. Adv Exp Med Biol. 1989. PMID: 2559595 No abstract available.

4

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

Emori Y, Kawasaki H, Imajoh S, Minami Y, Suzuki K. Emori Y, et al. Among authors: imajoh s. J Biol Chem. 1988 Feb 15;263(5):2364-70. J Biol Chem. 1988. PMID: 2828366 Free article.

We have already determined the primary structure of the endogenous inhibitor for calcium-dependent protease (CANP inhibitor, calpastatin) from the cDNA sequence and revealed that the CANP inhibitor contains four internally repeating units which could be responsible for its multip …

We have already determined the primary structure of the endogenous inhibitor for calcium-dependent protease (CANP inhibitor, calpastatin) fr …

5

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

Imajoh S, Aoki K, Ohno S, Emori Y, Kawasaki H, Sugihara H, Suzuki K. Imajoh S, et al. Biochemistry. 1988 Oct 18;27(21):8122-8. doi: 10.1021/bi00421a022. Biochemistry. 1988. PMID: 2852952

6

A fragment of an endogenous inhibitor produced in Escherichia coli for calcium-activated neutral protease (CANP) retains an inhibitory activity.

Imajoh S, Kawasaki H, Emori Y, Ishiura S, Minami Y, Sugita H, Imahori K, Suzuki K. Imajoh S, et al. FEBS Lett. 1987 May 11;215(2):274-8. doi: 10.1016/0014-5793(87)80161-8. FEBS Lett. 1987. PMID: 3034666 Free article.

7

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

Imajoh S, Kawasaki H, Suzuki K. Imajoh S, et al. J Biochem. 1987 Feb;101(2):447-52. doi: 10.1093/oxfordjournals.jbchem.a121930. J Biochem. 1987. PMID: 3034871 Free article.

8

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

Emori Y, Kawasaki H, Imajoh S, Imahori K, Suzuki K. Emori Y, et al. Among authors: imajoh s. Proc Natl Acad Sci U S A. 1987 Jun;84(11):3590-4. doi: 10.1073/pnas.84.11.3590. Proc Natl Acad Sci U S A. 1987. PMID: 3035539 Free PMC article.

9

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

Suzuki K, Imajoh S, Emori Y, Kawasaki H, Minami Y, Ohno S. Suzuki K, et al. Among authors: imajoh s. FEBS Lett. 1987 Aug 17;220(2):271-7. doi: 10.1016/0014-5793(87)80828-1. FEBS Lett. 1987. PMID: 3038617 Free article. Review.

10

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

Imajoh S, Kawasaki H, Emori Y, Suzuki K. Imajoh S, et al. Biochem Biophys Res Commun. 1987 Jul 31;146(2):630-7. doi: 10.1016/0006-291x(87)90575-4. Biochem Biophys Res Commun. 1987. PMID: 3039985

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