Tetraspanin15 regulates cellular trafficking and activity of the ectodomain sheddase ADAM10. (Q47984887)

7 February 2018

title

Tetraspanin15 regulates cellular trafficking and activity of the ectodomain sheddase ADAM10. (English)

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7 February 2018

author

Ralf Schwanbeck

6

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7 February 2018

Michael Schwake

8

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author name string

Johannes Prox

1

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7 February 2018

Michael Willenbrock

2

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Silvio Weber

3

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7 February 2018

Tobias Lehmann

4

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Dirk Schmidt-Arras

5

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Paul Saftig

7

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publication date

25 March 2012

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7 February 2018

Cellular and Molecular Life Sciences

published in

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7 February 2018

volume

69

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issue

17

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page(s)

2919-2932

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7 February 2018

https://scigraph.springernature.com/pub.10.1007/s00018-012-0960-2

exact match

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ADAM10, the rate-limiting protease of regulated intramembrane proteolysis of Notch and other proteins, is processed by ADAMS-9, ADAMS-15, and the gamma-secretase

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Lack of a-disintegrin-and-metalloproteinase ADAM10 leads to intracellular accumulation and loss of shedding of the cellular prion protein in vivo

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Genomic structure and functional characterization of the human ADAM10 promoter

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A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model

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Regulation of the alpha-secretase ADAM10 by its prodomain and proprotein convertases.

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Differential expression of five members of the ADAM family in the developing chicken brain.

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Increased processing of APLP2 and APP with concomitant formation of APP intracellular domains in BDNF and retinoic acid-differentiated human neuroblastoma cells

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Tetraspanins regulate ADAM10-mediated cleavage of TNF-alpha and epidermal growth factor

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Two dileucine motifs mediate late endosomal/lysosomal targeting of transmembrane protein 192 (TMEM192) and a C-terminal cysteine residue is responsible for disulfide bond formation in TMEM192 homodimers

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ADAM10 cleavage of N-cadherin and regulation of cell-cell adhesion and beta-catenin nuclear signalling

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The disintegrin/metalloprotease ADAM 10 is essential for Notch signalling but not for alpha-secretase activity in fibroblasts

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The disintegrin/metalloproteinase ADAM10 is essential for the establishment of the brain cortex

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Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans

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A scan of chromosome 10 identifies a novel locus showing strong association with late-onset Alzheimer disease

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ADAM10 is essential for proteolytic activation of Notch during thymocyte development.

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The "A Disintegrin And Metalloproteases" ADAM10 and ADAM17: novel drug targets with therapeutic potential?

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Proprotein convertase activity contributes to the processing of the Alzheimer's beta-amyloid precursor protein in human cells: evidence for a role of the prohormone convertase PC7 in the constitutive alpha-secretase pathway

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Up-regulation of the alpha-secretase ADAM10 by retinoic acid receptors and acitretin

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12 December 2020

Constitutive activation of metalloproteinase ADAM10 in mantle cell lymphoma promotes cell growth and activates the TNFα/NFκB pathway

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12 December 2020

Synapse-associated protein-97 mediates alpha-secretase ADAM10 trafficking and promotes its activity

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Yeast-based functional genomics and proteomics technologies: the first 15 years and beyond.

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12 December 2020

10.1007/S00018-012-0960-2

Identifiers

DOI

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7 February 2018

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7 February 2018