Degradome of soluble ADAM10 and ADAM17 metalloproteases

Disintegrin and metalloproteinases (ADAMs) 10 and 17 can release the extracellular part of a variety of membrane-bound proteins via ectodomain shedding important for many biological functions. So far, substrate identification focused exclusively on membrane-anchored ADAM10 and ADAM17. However, besid...

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Veröffentlicht in:	Cellular and molecular life sciences : CMLS 2020-01, Vol.77 (2), p.331-350
Hauptverfasser:	Scharfenberg, Franka, Helbig, Andreas, Sammel, Martin, Benzel, Julia, Schlomann, Uwe, Peters, Florian, Wichert, Rielana, Bettendorff, Maximilian, Schmidt-Arras, Dirk, Rose-John, Stefan, Moali, Catherine, Lichtenthaler, Stefan F., Pietrzik, Claus U., Bartsch, Jörg W., Tholey, Andreas, Becker-Pauly, Christoph
Format:	Artikel
Sprache:	eng
Schlagworte:	ADAM10 Protein - metabolism ADAM17 Protein - metabolism ADAM8 protein Amino acids Amino Acids - metabolism Amyloid Precursor Protein Secretases - metabolism Animals Biochemistry Biochemistry & Molecular Biology Biomedical and Life Sciences Biomedicine Cadherins Cardiomyocytes Cell Behavior Cell Biology Cell Line Cellular Biology Cleavage Cystatin C Fibronectin Genomics HEK293 Cells Humans Life Sciences Life Sciences & Biomedicine Mass spectrometry Mass spectroscopy Membrane Proteins - metabolism Metalloproteases - metabolism Mice Myocytes, Cardiac - metabolism Original Original Article Protease Proteinase Proteins Proteolysis Science & Technology Secretome Shedding Subcellular Processes Substrates
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