Results 251 to 260 of about 68,067 (282)

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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Altered cell-matrix associated ADAM proteins in Alzheimer disease

Journal of Neuroscience Research, 2000
Alterations in cell-matrix 'contact' are often related to a disruption of cell cycle regulation and, as such, occur variously in neoplasia. Given the recent findings showing cell cycle alterations in Alzheimer disease, we undertook a study of ADAM-1 and 2 (A Disintegrin And Metalloprotease), developmentally-regulated, integrin-binding, membrane-bound ...
Ibrahim Pirim, Sandra Siedlak, Robert B Petersen   +2 more
exaly   +4 more sources

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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ADAMs as mediators of EGF receptor transactivation by G protein-coupled receptors

American Journal of Physiology-Cell Physiology, 2006
A 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, Peter J, Dempsey, Satoru, Eguchi   +2 more
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Snake venom metalloproteinases: Structure, function and relationship to the ADAMs family of proteins

Toxicon, 1996
A 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.
L G, Jia, K, Shimokawa, J B, Bjarnason, J W, Fox   +3 more
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