Results 211 to 220 of about 69,298 (248)

The ADAM gene family: surface proteins with adhesion and protease activity

Trends in Genetics, 2000
An 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.
Diana G Myles, D G Myles, P Primakoff
exaly   +3 more sources

Drosophila metalloproteases in development and differentiation: The role of ADAM proteins and their relatives

European Journal of Cell Biology, 2011
ADAM metalloproteases are membrane bound glycoproteins that control many biological processes during development and differentiation, mainly by acting as ectodomain sheddases. The Drosophila genome contains five genes that code for classical ADAM proteins which are characterized by a highly conserved domain structure with the respective catalytic ...
Maik Drechsler, Heiko Meyer, Shuoshuo Wang   +2 more
exaly   +3 more sources

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
openaire   +2 more sources

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
openaire   +2 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= :
openaire   +2 more sources

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

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
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +3 more sources

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
openaire   +2 more sources