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Structure-Activity Relationship Studies on ADAM Protein-Integrin Interactions
Cardiovascular & Hematological Agents in Medicinal Chemistry, 2007The ADAM (a disintegrin and metalloprotease) family of proteins possess multi-domain structures composed of a signal peptide, a prodomain, a metalloprotease domain, a disintegrin-like domain, a cysteine rich domain, an epidermal growth factor-like domain, a transmembrane domain and cytoplasmic tail.
D. Lu, X. Lu, M. F. Scully, V. V. Kakkar
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A disintegrin and metalloprotease (ADAM) 33 protein in patients with pulmonary sarcoidosis
Respirology, 2012ABSTRACTBackground and objective: A disintegrin and metalloproteinase (ADAM) 33 is a susceptibility gene associated with inflammatory lung and skin diseases. It is selectively expressed in mesenchymal cells, and its metalloprotease activity has been linked to angiogenesis and tissue remodelling.
Ben G. Marshall +11 more
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ADAMs as mediators of EGF receptor transactivation by G protein-coupled receptors
American Journal of Physiology-Cell Physiology, 2006A disintegrin and metalloprotease (ADAM) is a membrane-anchored metalloprotease implicated in the ectodomain shedding of cell surface proteins, including the ligands for epidermal growth factor (EGF) receptors (EGFR)/ErbB. It has been well documented that the transactivation of the EGFR plays critical roles for many cellular functions, such as ...
Haruhiko Ohtsu +2 more
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The ADAMs family of proteins: from basic studies to potential clinical applications
Thrombosis and Haemostasis, 2003SummaryThe ADAMs are a family of membrane proteins possessing a disintegrin and metalloprotease domain. Currently,34 members are known to exist. Approximately 50% of the ADAMs contain a metalloprotease-like domain and some of these have been shown to possess protease activity.
Caroline O'Shea +3 more
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Snake venom metalloproteinases: Structure, function and relationship to the ADAMs family of proteins
Toxicon, 1996A large number of zinc metalloproteinases of varying mol. wts and biological functions has been isolated from crotalid and viperid venoms. Over the past few years, structural studies on these proteinases have suggested their organization into four classes, P-I to P-IV.
Li-Guo Jia +3 more
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Protein synthesis during germination of Peronospora tabacina (Adam) conidia
Archives of Biochemistry and Biophysics, 1971The characteristics of an in vitro amino acid-incorporating system prepared from germinated Peronospora tabacina conidia are described. Material sedimenting at 20,000 g and at 117,000 g was found to possess significant amino acid-incorporating activity. Although germination is accompanied by an increase in the activity of both these fractions, if
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Endothelial metalloprotease-disintegrin protein (ADAM) is implicated in angiogenesis in vitro.
Angiogenesis, 1998Recently two metalloproteinase, disintegrin, cysteine proteins (MDCs), also called ADAMs were identified on endothelial cells. However the role of these ADAMs are not defined on these cells. In order to elucidate whether ADAMs associated with endothelial cells could be involved in angiogenesis, we have tested the effect of an inhibitor of ADAM (GL ...
Annick Thomaidis +8 more
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Biochemical Journal, 2010
The ADAM disintegrin metalloproteinases (where ADAM is ‘a disintegrin and metalloproteinase’) are a family of transmembrane cell-surface proteins with essential roles in adhesion and proteolytic processing in all animals. The archetypal family member is ADAM17 {also known as TACE [TNFα (tumour necrosis factor α)-converting enzyme]}, which is involved ...
Bass, Rosemary, Edwards, Dylan R.
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The ADAM disintegrin metalloproteinases (where ADAM is ‘a disintegrin and metalloproteinase’) are a family of transmembrane cell-surface proteins with essential roles in adhesion and proteolytic processing in all animals. The archetypal family member is ADAM17 {also known as TACE [TNFα (tumour necrosis factor α)-converting enzyme]}, which is involved ...
Bass, Rosemary, Edwards, Dylan R.
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2003
Publisher Summary Since their discovery about a decade ago, some very intriguing insights into the function of a few Anchored Metalloprotease-Disintegrin Proteins (ADAMs) have emerged. They have been linked to a role in cell–cell interactions as potential integrin ligands and in the cleavage and release and, in several cases, activation of membrane ...
J. David Becherer, Carl P. Blobel
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Publisher Summary Since their discovery about a decade ago, some very intriguing insights into the function of a few Anchored Metalloprotease-Disintegrin Proteins (ADAMs) have emerged. They have been linked to a role in cell–cell interactions as potential integrin ligands and in the cleavage and release and, in several cases, activation of membrane ...
J. David Becherer, Carl P. Blobel
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Inflammation Research, 2002
Proteolysis on the cell surface and in the extracellular matrix is essential for normal cellular functions during development and in the adult, but it may also have undesirable consequences by promoting diseases such as cancer, arthritis, and Alzheimer's disease.
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Proteolysis on the cell surface and in the extracellular matrix is essential for normal cellular functions during development and in the adult, but it may also have undesirable consequences by promoting diseases such as cancer, arthritis, and Alzheimer's disease.
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