Disintegrins: A Family of Integrin Inhibitory Proteins from Viper Venoms

By R. Gould, M. Polokoff, P. Friedman, Tur‐Fu Huang, J. Holt, J. Cook, S. Niewiarowski. 1990

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1. S. Zhong
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8. S. Hackett

Citations in the corpus

• A Disintegrin and Metalloproteinase (ADAM) and ADAM with Thrombospondin Motifs (ADAMTS) Family in Vascular Biology and Disease (2019, background): “The term “disintegrin” was initially assigned to this domain because it is highly similar to RGDcontaining proteins in snake venom, which are highly conservative among different members of the Metzincins superfamily, and are able to adhere to integrins, thus suppressing platelet aggregation and indu”
• A Disintegrin and Metalloprotease (ADAM): Historical Overview of Their Functions (2016, background): “The label “disintegrin” was initially given to describe snake venom cysteine‐rich, RGD‐ containing proteins able to adhere to integrins and inhibit platelet aggregation and cause hemorrhage in snake bite victims [7].”
• An Adam15 amplification loop promotes vascular endothelial growth factor‐induced ocular neovascularization (2008, background): “Disintegrins are protein components of snake venom that contain an RGD sequence that binds platelet integrin IIb 3 and interferes with platelet aggregation (1).”