Disintegrins represent a family of low-molecular weight, cysteine-rich, RGD-containing peptides
that inhibit fibrinogen binding to glycoprotein IIb/IIIa complex as well as binding of other …

The term “disintegrin” was first used in 1990 to describe a group of viper venom-derived,
nonenzymatic small proteins that shared numerous structural and functional properties. These …

There are key differences between the amino acid residues of the RGD loops and the C
termini of echistatin, a potent antagonist of α IIb β 3 , α v β 3 and α 5 β 1 , and eristostatin, a …

Echistatin is a viper venom disintegrin containing RGD loop maintained by disulfide bridges.
It binds with a high affinity to αvβ3 and αIIbβ3 and it induces extensive conformational …

The inhibitory capacities of six different disintegrins and one related neurotoxin analogue for
the binding of RGD-dependent integrins to either fibrinogen, vitronectin or fibronectin were …

… McLane: Structural requirements of echistatin for the recognition of alpha (v)beta (3) and …
Galileo and MA McLane: Inhibition of melanoma cell motility by the snake venom disintegrin …

Disintegrins are low molecular weight proteins (4–15kDa) with an RGD binding region at
their binding loop. Disintegrin and disintegrin-like proteins are found in the venom of four …

Echistatin and eristostatin are structurally homologous disintegrins which exhibit significant
functional differences in interaction with various integrins. We hypothesized that this may …

Eristostatin, an RGD-containing disintegrin isolated from the venom of Eristicophis macmahoni,
inhibits lung or liver colonization of melanoma cells in a mouse model. In this study, …

The disulphide bond pattern of the long disintegrin bitistatin (83 amino acids, 14 cysteines)
was established using structural information gathered by amino acid analysis, N-terminal …