Two disintegrins with a high degree of amino acid sequence similarity, echistatin and
eristostatin, showed a low level of interaction with Chinese hamster ovary (CHO) cells, but …

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

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 integrin αvβ3 is the major receptor mediating the attachment of osteoclasts to the
extracellular matrix in bone and plays a critical role in bone resorption and bone remodeling …

A mutant of echistatin, a disintegrin with a high affinity for the integrins, was constructed by
substituting RGD for RGD in the Arg‐Gly‐Asp (RGD) region. The mutant was chemically …

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 …

Echistatin is a 49-amino-acid peptide belonging to the family of disintegrins that are derived
from snake venoms and are potent inhibitors of platelet aggregation and cell adhesion …

Viper venom disintegrins contain the RGD/KGD motif. They inhibit platelet aggregation and
cell adhesion, but show structural and functional heterogeneity. We investigated the …

Peptides containing the integrin recognition sequence, RGD, can inhibit experimental
metastasis of mouse melanoma cells, but the integrin (s) affected in these experiments is …