A secreted form of human ADAM9 has an α-secretase activity for APP
- 3 May 2002
- journal article
- Published by Elsevier BV in Biochemical and Biophysical Research Communications
- Vol. 293 (2), 800-805
- https://doi.org/10.1016/s0006-291x(02)00302-9
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- ADAM 12-S Cleaves IGFBP-3 and IGFBP-5 and Is Inhibited by TIMP-3Biochemical and Biophysical Research Communications, 2000
- Regulation of APP cleavage by α‐, β‐ and γ‐secretasesFEBS Letters, 2000
- Functional Analysis of the Domain Structure of Tumor Necrosis Factor-α Converting EnzymePublished by Elsevier BV ,2000
- Isolation of Two Novel Metalloproteinase-Disintegrin (ADAM) cDNAs That Show Testis-Specific Gene ExpressionBiochemical and Biophysical Research Communications, 1999
- Evidence That Tumor Necrosis Factor α Converting Enzyme Is Involved in Regulated α-Secretase Cleavage of the Alzheimer Amyloid Protein PrecursorPublished by Elsevier BV ,1998
- Molecular Cloning of a Gene Encoding a New Type of Metalloproteinase-disintegrin Family Protein with Thrombospondin Motifs as an Inflammation Associated GenePublished by Elsevier BV ,1997
- MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains.The Journal of cell biology, 1996
- ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions.The Journal of cell biology, 1995
- Conventional protein kinase C (PKC)‐α and novel PKCε, but not ‐δ, increase the secretion of an N‐terminal fragment of Alzheimer's disease amyloid precursor protein from PKC cDNA transfected 3Y1 fibroblastsFEBS Letters, 1995
- Human metalloprotease/disintegrin-like (MDC) gene: exon-intron organization and alternative splicingCytogenetic and Genome Research, 1995