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ADAM15 gene
Known as:
A Disintegrin and Metalloproteinase Domain 15 Gene
, ADAM15
, METARGIDIN
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This gene is involved in the restructuring of the mesangial matrix.
National Institutes of Health
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Related topics
Related topics
5 relations
ADAM15 protein, human
Cell Adhesion
Hydrolysis
Integrin Binding
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Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2008
Highly Cited
2008
The Ectodomain Shedding of E-cadherin by ADAM15 Supports ErbB Receptor Activation*
Abdo J. Najy
,
K. Day
,
M. Day
Journal of Biological Chemistry
2008
Corpus ID: 45203354
The zinc-dependent disintegrin metalloproteinases (a disintegrin and metalloproteinases (ADAMs) have been implicated in several…
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Highly Cited
2007
Highly Cited
2007
Proteolytic Processing of Delta-like 1 by ADAM Proteases*
Emilia Dyczynska
,
Danqiong Sun
,
Haiqing Yi
,
A. Sehara-Fujisawa
,
C. Blobel
,
A. Zolkiewska
Journal of Biological Chemistry
2007
Corpus ID: 10607223
Delta-like 1 (Dll1) is a mammalian ligand for Notch receptors. Interactions between Dll1 and Notch in trans activate the Notch…
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Highly Cited
2005
Highly Cited
2005
The disintegrin-metalloproteinases ADAM9, ADAM12, and ADAM15 are upregulated in gastric cancer.
S. Carl‐McGrath
,
U. Lendeckel
,
M. Ebert
,
A. Roessner
,
C. Röcken
International Journal of Oncology
2005
Corpus ID: 39045298
The ADAMs (A disintegrin and metalloproteinase) are a family of cell-surface membrane glycoproteins, whose multidomain structure…
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Highly Cited
2005
Highly Cited
2005
Homeostatic effects of the metalloproteinase disintegrin ADAM15 in degenerative cartilage remodeling.
B. Böhm
,
T. Aigner
,
B. Roy
,
T. Brodie
,
C. Blobel
,
H. Burkhardt
Arthritis & Rheumatism
2005
Corpus ID: 9638280
OBJECTIVE The membrane-anchored metalloproteinase disintegrin ADAM15 is up-regulated in osteoarthritis and has been implicated in…
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Highly Cited
2004
Highly Cited
2004
Evidence of Antiangiogenic and Antimetastatic Activities of the Recombinant Disintegrin Domain of Metargidin
V. Trochon-Joseph
,
D. Martel-Renoir
,
+11 authors
He Lu
Cancer Research
2004
Corpus ID: 1528019
Metargidin, a transmembrane protein of the adamalysin family, and integrins, e.g., α5β1 and αv, are preferentially expressed on…
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Highly Cited
2003
Highly Cited
2003
Catalytic Activity of ADAM8, ADAM15, and MDC-L (ADAM28) on Synthetic Peptide Substrates and in Ectodomain Cleavage of CD23*
A. Fourie
,
F. Coles
,
Veronica Moreno
,
L. Karlsson
Journal of Biological Chemistry
2003
Corpus ID: 20815224
The ADAM family of disintegrin metalloproteases plays important roles in “ectodomain shedding,” the process by which biologically…
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Highly Cited
2002
Highly Cited
2002
Phosphorylation-dependent Interactions between ADAM15 Cytoplasmic Domain and Src Family Protein-tyrosine Kinases*
Zaruhi Poghosyan
,
S. Robbins
,
M. Houslay
,
A. Webster
,
G. Murphy
,
D. Edwards
Journal of Biological Chemistry
2002
Corpus ID: 170827
The adamalysins (ADAMs) are transmembrane glycoproteins involved in cell adhesion and proteolytic ectodomain processing of…
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Review
2001
Review
2001
Fertilin β and other ADAMs as integrin ligands: insights into cell adhesion and fertilization
J. Evans
Bioessays
2001
Corpus ID: 23712246
One of the most important cell–cell interactions is that of the sperm with the egg. This interaction, which begins with cell…
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Highly Cited
1999
Highly Cited
1999
Interaction of metargidin (ADAM-15) with alphavbeta3 and alpha5beta1 integrins on different haemopoietic cells.
D. Nath
,
P. Slocombe
,
+5 authors
G. Murphy
Journal of Cell Science
1999
Corpus ID: 36010679
Metargidin (ADAM-15) is a type I transmembrane glycoprotein belonging to the ADAM (A Disintegrin and Metalloprotease Domain…
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Highly Cited
1998
Highly Cited
1998
Intracellular Maturation of the Mouse Metalloprotease Disintegrin MDC15*
L. Lum
,
Martha S. Reid
,
C. Blobel
Journal of Biological Chemistry
1998
Corpus ID: 30093257
Metalloprotease disintegrins are a family of membrane-anchored glycoproteins that play a role in fertilization, myoblast fusion…
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