The metalloproteinase ADAM10 requires its activity to sustain surface expression

The metalloprotease ADAM10 (a disintegrin and metalloprotease 10) undergoes rapid, postlysis autocatalytic degradation

(2018) Tobias Brummer et al.   FASEB JOURNAL

Synthesis and in vitro Evaluation of ADAM10 and ADAM17 Highly Selective Bioimaging Probes

(2018) Caterina Camodeca et al.   ChemMedChem

ADAM10-mediated ephrin-B2 shedding promotes myofibroblast activation and organ fibrosis

(2017) David Lagares et al.   NATURE MEDICINE

Proteolytic Origin of the Soluble Human IL-6R In Vivo and a Decisive Role of N-Glycosylation

(2017) Steffen Riethmueller et al.   PLOS BIOLOGY

Stimulated release and functional activity of surface expressed metalloproteinase ADAM17 in exosomes

(2016) Esther Groth et al.   BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH

ADAM10-Dependent Signaling Through Notch1 and Notch4 Controls Development of Organ-Specific Vascular BedsNovelty and Significance

(2016) Rolake O. Alabi et al.   CIRCULATION RESEARCH

Discovery of a new selective inhibitor of A Disintegrin And Metalloprotease 10 (ADAM-10) able to reduce the shedding of NKG2D ligands in Hodgkin's lymphoma cell models

(2016) Caterina Camodeca et al.   EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY

An activated form of ADAM10 is tumor selective and regulates cancer stem-like cells and tumor growth

(2016) Lakmali Atapattu et al.   JOURNAL OF EXPERIMENTAL MEDICINE

Control of ADAM17 activity by regulation of its cellular localisation

(2016) Inken Lorenzen et al.   Scientific Reports

TspanC8 tetraspanins differentially regulate the cleavage of ADAM10 substrates, Notch activation and ADAM10 membrane compartmentalization

(2015) Stéphanie Jouannet et al.   CELLULAR AND MOLECULAR LIFE SCIENCES

TspanC8 Tetraspanins and A Disintegrin and Metalloprotease 10 (ADAM10) Interact via Their Extracellular Regions

(2015) Peter J. Noy et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The alpha secretase ADAM10: A metalloprotease with multiple functions in the brain

(2015) Paul Saftig et al.   PROGRESS IN NEUROBIOLOGY

Leukocytes require ADAM10 but not ADAM17 for their migration and inflammatory recruitment into the alveolar space

(2014) J. Pruessmeyer et al.   BLOOD

A Disintegrin and Metalloprotease 17 Dynamic Interaction Sequence, the Sweet Tooth for the Human Interleukin 6 Receptor

(2014) Stefan Düsterhöft et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Surface expression and limited proteolysis of ADAM10 are increased by a dominant negative inhibitor of dynamin

(2011) Robyn M Carey et al.   BMC CELL BIOLOGY

The disintegrin/metalloproteinase Adam10 is essential for epidermal integrity and Notch-mediated signaling

(2011) S. Weber et al.   DEVELOPMENT

A Staphylococcus aureus pore-forming toxin subverts the activity of ADAM10 to cause lethal infection in mice

(2011) Ichiro Inoshima et al.   NATURE MEDICINE

Distinct role of the intracellular C-terminus for subcellular expression, shedding and function of the murine transmembrane chemokine CX3CL1

(2010) Michael G. Andrzejewski et al.   BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

The Disintegrin/Metalloproteinase ADAM10 Is Essential for the Establishment of the Brain Cortex

(2010) E. Jorissen et al.   JOURNAL OF NEUROSCIENCE

Active-site determinants of substrate recognition by the metalloproteinases TACE and ADAM10

(2009) Cristina I. Caescu et al.   BIOCHEMICAL JOURNAL

ADAM10, the Rate-limiting Protease of Regulated Intramembrane Proteolysis of Notch and Other Proteins, Is Processed by ADAMS-9, ADAMS-15, and the γ-Secretase

(2009) Thomas Tousseyn et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

A Disintegrin and Metalloproteinase 17 (ADAM17) Mediates Inflammation-induced Shedding of Syndecan-1 and -4 by Lung Epithelial Cells

(2009) Jessica Pruessmeyer et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

ADAM10 Regulates Endothelial Permeability and T-Cell Transmigration by Proteolysis of Vascular Endothelial Cadherin

(2008) Beate Schulz et al.   CIRCULATION RESEARCH