Skip to search formSkip to main contentSkip to account menu
You are currently offline. Some features of the site may not work correctly.

Disintegrin Domain

It is an integrin binding domain originally identified in ADAM family proteins. (NCI)
National Institutes of Health

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2006
Highly Cited
2006
We identified a previously unknown integrin, α9β1, on OCLs and their precursors. Antibody to α9 inhibited OCL formation in human… 
Highly Cited
2003
Highly Cited
2003
ADAMTS13 consists of a reprolysin-type metalloprotease domain followed by a disintegrin domain, a thrombospondin type 1 motif… 
Highly Cited
2002
Highly Cited
2002
ADAMs (a disintegrinand metalloprotease domains) are metalloprotease and disintegrin domain-containing transmembrane… 
  • figure 1
  • figure 2
  • figure 3
  • figure 4
  • figure 5
Highly Cited
2001
Highly Cited
2001
ADAM 3 is a sperm surface glycoprotein that has been implicated in sperm-egg adhesion. Because little is known about the adhesive… 
Highly Cited
2000
Highly Cited
2000
Little is yet known about the biological and biochemical properties of the disintegrin-like domains of ADAM (a disintegrin… 
Highly Cited
1999
Highly Cited
1999
ADAM (a disintegrin and metalloprotease) proteins contain structural homology to the P-III class of snake venom metalloproteases… 
Highly Cited
1997
Highly Cited
1997
Sperm–egg plasma membrane fusion is preceded by sperm adhesion to the egg plasma membrane. Cell–cell adhesion frequently involves… 
  • table I
  • figure 2
  • figure 3
  • figure 4
  • figure 5
Highly Cited
1996
Highly Cited
1996
Cellular disintegrins are a family of proteins that are related to snake venom integrin ligands and metalloproteases. We have… 
  • figure 2
  • figure 3
  • figure 5
  • figure 4
Highly Cited
1996
Highly Cited
1996
Cellular disintegrins are a family of membrane-anchored proteins with structural homology to snake venom metalloproteases and… 
Review
1992
Review
1992
Disintegrins are soluble integrin ligands from snake venoms that disrupt cell-matrix interactions. Recently, the nuclear magnetic…