A secreted form of human ADAM9 has an alpha-secretase activity for APP (Q24299257)

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Hisashi Koike

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Noboru Sasagawa

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Shoichi Ishiura

Biochemical and Biophysical Research Communications

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language of work or name

English

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publication date

3 May 2002

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published in

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volume

293

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page(s)

800-5

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issue

2

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cites work

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MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains

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Metalloprotease-disintegrin MDC9: intracellular maturation and catalytic activity

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Cloning and expression in Pichia pastoris of metalloprotease domain of ADAM 9 catalytically active against fibronectin

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A metalloprotease-disintegrin, MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor.

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Regulation of APP cleavage by alpha-, beta- and gamma-secretases

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Alzheimer's amyloid precursor protein alpha-secretase is inhibited by hydroxamic acid-based zinc metalloprotease inhibitors: similarities to the angiotensin converting enzyme secretase

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Conventional protein kinase C (PKC)-alpha and novel PKC epsilon, but not -delta, increase the secretion of an N-terminal fragment of Alzheimer's disease amyloid precursor protein from PKC cDNA transfected 3Y1 fibroblasts

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Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1

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Isolation of two novel metalloproteinase-disintegrin (ADAM) cDNAs that show testis-specific gene expression

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ADAM 12-S cleaves IGFBP-3 and IGFBP-5 and is inhibited by TIMP-3

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Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS family

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ADAMTS-1 is an active metalloproteinase associated with the extracellular matrix

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