Giebeler, Nives and Zigrino, Paola ORCID: 0000-0002-7470-0064 (2016). A Disintegrin and Metalloprotease (ADAM): Historical Overview of Their Functions. Toxins, 8 (4). BASEL: MDPI. ISSN 2072-6651

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Abstract

Since the discovery of the first disintegrin protein from snake venom and the following identification of a mammalian membrane-anchored metalloprotease-disintegrin implicated in fertilization, almost three decades of studies have identified additional members of these families and several biochemical mechanisms regulating their expression and activity in the cell. Most importantly, new in vivo functions have been recognized for these proteins including cell partitioning during development, modulation of inflammatory reactions, and development of cancers. In this review, we will overview the a disintegrin and metalloprotease (ADAM) family of proteases highlighting some of the major research achievements in the analysis of ADAMs' function that have underscored the importance of these proteins in physiological and pathological processes over the years.

Item Type: Journal Article
Creators:
CreatorsEmailORCIDORCID Put Code
Giebeler, NivesUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Zigrino, PaolaUNSPECIFIEDorcid.org/0000-0002-7470-0064UNSPECIFIED
URN: urn:nbn:de:hbz:38-280776
DOI: 10.3390/toxins8040122
Journal or Publication Title: Toxins
Volume: 8
Number: 4
Date: 2016
Publisher: MDPI
Place of Publication: BASEL
ISSN: 2072-6651
Language: English
Faculty: Unspecified
Divisions: Unspecified
Subjects: no entry
Uncontrolled Keywords:
KeywordsLanguage
NECROSIS-FACTOR-ALPHA; REGULATED INTRAMEMBRANE PROTEOLYSIS; EGF RECEPTOR TRANSACTIVATION; CONVERTING-ENZYME TACE; CELL-CELL ADHESION; SNAKE-VENOM; TNF-ALPHA; DISINTEGRIN/METALLOPROTEINASE ADAM10; PATHOLOGICAL NEOVASCULARIZATION; DOMAIN ARCHITECTUREMultiple languages
Food Science & Technology; ToxicologyMultiple languages
Refereed: Yes
URI: http://kups.ub.uni-koeln.de/id/eprint/28077

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