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ADAM family proteins in the immune system
Immunology Today, 1999CD156 is a member of a family proteins characterized by a disintegrin and a metalloprotease domain (ADAM). These molecules are phylogenically conserved but have individual roles in a variety of cells. Here, Shunsuke Yamamoto and colleagues discuss data suggesting that ADAM family proteins have important roles in the immune system.
Eiichi Shimizu+6 more
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ADAM Proteins- Therapeutic Potential in Cancer
Current Cancer Drug Targets, 2008The 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
Vijay V. Kakkar+3 more
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Sexual Selection and the Molecular Evolution of ADAM Proteins
Journal of Molecular Evolution, 2010Rapid evolution has been identified for many reproductive genes and recent studies have combined phylogenetic tests and information on species mating systems to test sexual selection. Here we examined the molecular evolution of the ADAM gene family, a diverse group of 35 proteins capable of adhesion to and cleavage of other proteins, using sequence ...
Scott Finn, Alberto Civetta
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Shedding of membrane proteins by ADAM family proteases
Essays in Biochemistry, 2002Many 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.
Millard H. Lambert, Marcia L. Moss
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ADAMs family members as amyloid precursor protein α‐secretases
Journal of Neuroscience Research, 2003AbstractIn 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.+3 more
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Altered cell-matrix associated ADAM proteins in Alzheimer disease
Journal of Neuroscience Research, 2000Alterations 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 ...
Smith, MA+8 more
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Journal of Clinical Neuroscience, 2004
ADAM proteins are a family of metalloproteinases with a disintegrin domain. They have proteolytic as well as adhesive functions and can be involved in cell fusion events. Some ADAM proteins are expressed in a highly tissue restricted fashion, whereas others are expressed quite ubiquitously. In the brain, ADAM proteins have a role in neural development,
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ADAM proteins are a family of metalloproteinases with a disintegrin domain. They have proteolytic as well as adhesive functions and can be involved in cell fusion events. Some ADAM proteins are expressed in a highly tissue restricted fashion, whereas others are expressed quite ubiquitously. In the brain, ADAM proteins have a role in neural development,
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ADAM proteins, their ligands, and clinical implications
Neurology, 2012AD= : 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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The ADAM gene family: surface proteins with adhesion and protease activity
Trends in Genetics, 2000An ADAM is a transmembrane protein that contains a disintegrin and metalloprotease domain and, therefore, it potentially has both cell adhesion and protease activities. Currently, the ADAM gene family has 29 members, although the function of most ADAM gene products is unknown.
Paul Primakoff, Diana G. Myles
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