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Genetic variations in extracellular matrix degradation pathways linking to major depressive disorder: Evidence from a large-scale genetic association study. [PDF]
Biomedicine (Taipei)Zailani H +6 more
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ADAM17 — gatekeeper of the skin barrier
Nature Reviews Immunology, 2012The metalloproteinase ADAM17 maintains the epidermal barrier through basal Notch activation.
Lucy Bird
exaly +3 more sources
The shedding protease ADAM17: Physiology and pathophysiology
Biochimica Et Biophysica Acta - Molecular Cell Research, 2017 The disintegrin metalloprotease ADAM17 has been a matter of intense studies aiming to unravel structure, function and regulation of protease expression, maturation and activity. In this review, we summarize data on the physiological role of ADAM17 in health and disease.
Friederike Zunke, Stefan Rose-John
exaly +3 more sources
ADAM17 Deficiency Protects against Pulmonary Emphysema
American Journal of Respiratory Cell and Molecular Biology, 2021Pulmonary emphysema is the major debilitating component of chronic obstructive pulmonary disease (COPD), which is a leading cause of morbidity and mortality worldwide. The ADAM17 (A disintegrin and metalloproteinase 17) protease mediates inflammation via ectodomain shedding of numerous proinflammatory cytokines, cytokine receptors, and adhesion ...
Mohamed I. Saad +6 more
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HDLs activate ADAM17‐dependent shedding
Journal of Cellular Physiology, 2007AbstractThe tumor necrosis factor‐alpha (TNF) converting enzyme (ADAM17) is a metalloprotease that cleaves several transmembrane proteins, including TNF and its receptors (TNFR1 and TNFR2). We recently showed that the shedding activity of ADAM17 is sequestered in lipid rafts and that cholesterol depletion increased the shedding of ADAM17 substrates ...
Edwige, Tellier +7 more
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The metalloprotease ADAM17 in inflammation and cancer
Pathology Research and Practice, 2019Proteolytic cleavage of transmembrane proteins is an important post-translational modification that regulates the biological function of numerous transmembrane proteins. Among the 560 proteases encoded in the human genome, the metalloprotease A Disintegrin and Metalloprotease 17 (ADAM17) has gained much attention in recent years and has emerged as a ...
Stefan Düsterhöft +2 more
exaly +3 more sources
ADAM17 inhibition effects on Mer shedding
Minerva Biotechnology and Biomolecular Research, 2022Background: Mer belongs to TAM, a tyrosine kinase receptor family with essential roles in the homeostasis of the immune response. Among TA M members, Mer is the less characterized regarding its biological role. Mer is activated by its ligand Gas6, while it is inactivated through proteolytic shedding by the metalloproteinase ADAM17 in response to ...
Salmi L. +5 more
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Inflammatory Bowel Disease andADAM17Deletion
New England Journal of Medicine, 2012To the Editor: Blaydon et al. (Oct. 20 issue)1 identify a loss-of-function mutation in ADAM17 as a cause of inflammatory skin and bowel disease in two of three children born to consanguineous parents. We have previously reported an N-ethyl-Nnitrosourea–induced mutation in Adam17, producing a strong dextran sodium sulfate–induced colitis-susceptibility ...
Katharina, Brandl +2 more
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Degradome of soluble ADAM10 and ADAM17 metalloproteases
Cellular and Molecular Life Sciences, 2019Disintegrin 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.
Franka Scharfenberg +15 more
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