Browse our anti-ADAM10 (ADAM10) Antibodies

Mouse (Murine) ADAM Metallopeptidase Domain 10 (ADAM10) interaction partners

1. In the present study, we report that Nrxn3beta is processed by the metalloproteases ADAM10, ADAM17 (show ADAM17 Antibodies), and by the intramembrane-cleaving protease gamma-secretase, producing secreted neurexin3beta (sNrxn3beta) and a single intracellular domain (Nrxn3beta-ICD). Thea (show ACOT11 Antibodies) authors show that sNrxn3beta produced by the cells of the dentate gyrus increases the spine density of newborn neurons.

2. the synaptic localization of APP (show APP Antibodies), ADAM10, and BACE1 (show BACE Antibodies) in the mouse cerebral cortex, was examined.

3. Pharmacological inhibition of ADAM10 reduces sEphrin-B2 levels in bronchoalveolar lavage and prevents lung fibrosis in mice. Consistent with the mouse data, ADAM10-sEphrin-B2 signaling is upregulated in fibroblasts from human subjects with idiopathic pulmonary fibrosis.

4. Xenoestrogens biphenol-A and nonylphenol stimulate the release of EGFR (show EGFR Antibodies)-ligands by differentially activating ADAM17 (show ADAM17 Antibodies) or ADAM10.

5. study confirms the importance of ICOSL (show ICOSLG Antibodies) shedding in ICOS (show ICOS Antibodies)/ICOSL (show ICOSLG Antibodies) function and expression and it identifies ADAM10 as the most important sheddase for controlling ICOSL (show ICOSLG Antibodies) levels

6. Tspan3 (show TSPAN3 Antibodies) is a central endocytic membrane component regulating the expression of ADAM10, presenilin and the amyloid precursor protein (show APP Antibodies).

7. these results show that ADAM10-Notch (show NOTCH1 Antibodies) signaling in ovarian somatic cells governs the primordial follicle formation by controlling the development of ovarian pregranulosa cells.

8. Findings provide evidence that ADAM10, and not ADAM17 (show ADAM17 Antibodies), is indispensable for proper retinal development as a regulator of NOTCH (show NOTCH1 Antibodies) signaling.

9. this study shows that during positive selection in the spleen, B-cell receptor signaling causes immature type 1 transitional B cells to become receptive to Notch (show NOTCH1 Antibodies) ligands via Taok3 (show TAOK3 Antibodies)-mediated surface expression of ADAM10

10. Thus, Leda-1/Pianp (show C12orf53 Antibodies) is constitutively processed by proprotein convertases, sheddases including MMPs and ADAM10/17 and intramembrane protease gamma-secretase.

Human ADAM Metallopeptidase Domain 10 (ADAM10) interaction partners

1. mechanistic experiments revealed that ADAM10-RNAi resulted in an increase in E-cadherin (show CDH1 Antibodies) and a decrease in N-cadherin (show CDH2 Antibodies) and vimentin (show VIM Antibodies) expression. Our study implies that high expression of ADAM10 promotes the proliferation and migration of hypopharyngeal squamous cell carcinoma (HSCC). These findings may help to provide a method for treatment of HSCC

2. Notch (show NOTCH1 Antibodies) is ligand activated and undergoes DTX4 (show DTX4 Antibodies)-mediated ubiquitylation and bilateral endocytosis before ADAM10 processing

3. therapies against ADAM10 and ADAM17 (show ADAM17 Antibodies) may promote cancer stem cell migration away from the tumourigenic niche resulting in a differentiated phenotype that is more susceptible to treatment.

4. Presence of anti-ADAM10 auto-Antibodies seems to reflect the increased tumor expression of the immunogenic immature-ADAM10 in a group of Colorectal cancer patients, and is associated with a favourable prognosis in patients at stage III of the disease.

5. ADAM10 and ADAM17 (show ADAM17 Antibodies) are the best characterized members of the ADAM (A Disintegrin and Metalloproteinase) - family of transmembrane proteases. Both are involved diverse physiological and pathophysiological processes.For ADAM17 (show ADAM17 Antibodies) phosphatidylserine exposure is required to then induce its shedding function.

6. A better understanding of the regulatory mechanisms controlling the expression, subcellular localization and activity of ADAM10 will likely uncover suitable drug targets which will allow a more specific and fine-tuned modulation of its proteolytic activity

7. In the present study, the authors show that deletion of a triple serine (3S) motif (Ser (show SIGLEC1 Antibodies)-359 to Ser (show SIGLEC1 Antibodies)-361) adjacent to the cleavage site is sufficient to prevent IL-6R cleavage by ADAM17 (show ADAM17 Antibodies), but not ADAM10. We find that the impaired shedding is caused by the reduced distance between the cleavage site and the plasma membrane.

8. Here, I review some of the proposed functions of ADAM10 associated with intestinal crypt homeostasis and tumorigenesis within the gastrointestinal tract in vivo.

9. Study reports the structure of the ADAM10 ectodomain, providing fundamental insights into how substrate selectivity and regulation of catalytic activity is achieved in this important representative of the ADAM family of metalloproteases.

10. Data suggest that ADAM10 associates directly with all members of a subgroup of tetraspanins having eight cysteines in the large extracellular domain ('TspanC8'): Tspan5 (show TSPAN5 Antibodies), Tspan10, Tspan14, Tspan15 (show TSPAN15 Antibodies), Tspan17, and Tspan33 (show TSPAN33 Antibodies). [REVIEW]

Xenopus laevis ADAM Metallopeptidase Domain 10 (ADAM10) interaction partners

1. A dramatic decline in ephrinB2 (show EFNB2 Antibodies) protein levels on the absence of flotillin-1 (show FLOT1 Antibodies) expression is specific, and is partly the result of an increased susceptibility to cleavage by the metalloprotease ADAM10.

Pig (Porcine) ADAM Metallopeptidase Domain 10 (ADAM10) interaction partners

1. significantly increased expression of ADAM10 in the ISR versus non-ISR segment in diabetic minipigs

Cow (Bovine) ADAM Metallopeptidase Domain 10 (ADAM10) interaction partners

1. Data show that ADAM10 and APLP2 (show APLP2 Antibodies) are expressed in proximal tubule cells, and that ADAM10 activity has a pronounced effect on expression of specific brush-border proteins.

2. Intracellular trafficking of ADAM10 critically requires a novel sorting signal within its cytoplasmic domain.

3. N-glycosylation is crucial for ADAM10 processing and resistance to proteolysis, and results suggest that it is required for full-enzyme activity.