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Quantitative and dynamic expression profile of premature and active forms of the regional ADAM proteins during chicken brain development

Cellular and Molecular Biology Letters, 2011
The ADAM (A Disintegrin and Metalloprotease) family of transmembrane proteins plays important roles in embryogenesis and tissue formation based on their multiple functional domains. In the present study, for the first time, the expression patterns of the
Jiankai Luo
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Crystal structures of catrocollastatin/VAP2B reveal a dynamic, modular architecture of ADAM/adamalysin/reprolysin family proteins

FEBS Letters, 2007
Catrocollastatin/vascular apoptosis-inducing protein (VAP)2B is a metalloproteinase from Crotalus atrox venom, possessing metalloproteinase/disintegrin/cysteine-rich (MDC) domains that bear the typical domain architecture of a disintegrin and ...
Satohiko Araki, Soichi Takeda
exaly   +2 more sources

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ADAM Proteins- Therapeutic Potential in Cancer

Current Cancer Drug Targets, 2008
The A Disintegrin And Metalloprotease (ADAM) proteins belong to the metzincin-superfamily of Zn-dependent metalloproteinases that shed the extracellular domains of membrane-bound growth factors, cytokines and their receptors. The latter play a central role in cell signaling and contribute a potential target in cancer therapy. Of particular interest are
Xinjie, Lu, Dong, Lu, Mike, Scully, Vijay, Kakkar   +3 more
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Shedding of membrane proteins by ADAM family proteases

Essays in Biochemistry, 2002
Many membrane-bound proteins undergo proteolytic release from the membrane, a process known as 'shedding'. Some of the processing events are carried out by enzymes of the ADAM (a disintegrin and metalloproteinase) family, which are also membrane bound.
Marcia L, Moss, Millard H, Lambert
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ADAM proteins, their ligands, and clinical implications

Neurology, 2012
AD= : Alzheimer disease; ADAM= : A disintegrin and metalloproteinase; ADEAF= : autosomal dominant partial epilepsy with auditory features; ADTLE= : autosomal dominant familial temporal lobe epilepsy; APP= : amyloid precursor protein; EPTP= : epitempin; Kv= : voltage-gated potassium; LGI= : leucine-rich, glioma inactivated; LRR= :
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ADAMs family members as amyloid precursor protein α‐secretases

Journal of Neuroscience Research, 2003
AbstractIn the non‐amyloidogenic pathway, the Alzheimer's amyloid precursor protein (APP) is cleaved within the amyloid‐β domain by α‐secretase precluding deposition of intact amyloid‐β peptide. The large ectodomain released from the cell surface by the action of α‐secretase has several neuroprotective properties.
Allinson, Tobias M. J., Parkin, Edward T., Turner, Anthony J., Hooper, Nigel M.   +3 more
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A disintegrin and metalloprotease (ADAM) 33 protein in patients with pulmonary sarcoidosis

Respirology, 2012
ABSTRACTBackground 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.
Shaffiq, Asif, Haitchi, Hans Michael, Pang, Yun Yung, Alangari, Abdullah A., Jones, Mark G., Marshall, Ben G., Howarth, Peter H., Davies, Donna E., O'Reilly, Katherine M.A.   +8 more
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Endothelial metalloprotease-disintegrin protein (ADAM) is implicated in angiogenesis in vitro

Angiogenesis, 1998
Recently 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 ...
V, Trochon, H, Li, M, Vasse, F, Frankenne, A, Thomaidis, J, Soria, H, Lu, C, Gardner, C, Soria   +8 more
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Structure-Activity Relationship Studies on ADAM Protein-Integrin Interactions

Cardiovascular & Hematological Agents in Medicinal Chemistry, 2007
The 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.
X, Lu, D, Lu, M F, Scully, V V, Kakkar
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The ADAM metalloproteinases

Molecular Aspects of Medicine, 2008
The ADAMs (a disintegrin and metalloproteinase) are a fascinating family of transmembrane and secreted proteins with important roles in regulating cell phenotype via their effects on cell adhesion, migration, proteolysis and signalling.
Dylan R Edwards, Caroline J Pennington
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