Results 281 to 290 of about 10,772,271 (320)

ADAM Family Proteins in the Immune System

Trends in Immunology, 1999
CD156 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.
Masashi Kataoka, Naoki Hijiya, Keiko Matsuura   +2 more
exaly   +3 more sources

Snake Venom Metalloproteinases: Structure, Function and Relevance to the Mammalian ADAM/ADAMTS Family Proteins

Biochimica Et Biophysica Acta - Proteins and Proteomics, 2012
Soichi Takeda, Hiroyuki Takeya, Sadaaki Iwanaga   +2 more
exaly   +2 more sources

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.
Paul Primakoff, Diana G Myles, P Primakoff   +2 more
exaly   +3 more sources

Expression of ADAM-9 mRNA and Protein in Human Breast Cancer [PDF]

International Journal of Cancer, 2003
AbstractThe ADAMs (a disintegrin and metalloprotease) are membrane proteins containing both protease and adhesion domains and thus may be potentially important in cancer invasion and metastasis. The aim of our study was to investigate the distribution and potential clinical significance of ADAM‐9 in breast cancer.
Catherine Duggan, Michael J Duffy, Niall O'Higgins   +2 more
exaly   +4 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

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

Structure-Activity Relationship Studies on ADAM Protein-Integrin Interactions

Cardiovascular and 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
exaly   +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

E-cadherin mechanotransduction activates EGFR-ERK signaling in epithelial monolayers by inducing ADAM-mediated ligand shedding.

Science Signaling
The behavior of cells is governed by signals originating from their local environment, including mechanical forces exerted on the cells. Forces are transduced by mechanosensitive proteins, which can impinge on signaling cascades that are also activated ...
Ronja M. Houtekamer, Mirjam C. van der Net, Marjolein J. Vliem, Tomas E. J. C. Noordzij, L. van Uden, R. V. van Es, J. Sim, Eriko Deguchi, K. Terai, Matthew A Hopcroft, H. Vos, Beth L. Pruitt, M. Matsuda, W. Pannekoek, M. Gloerich   +14 more
semanticscholar   +1 more source