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Structure—function relationships in the receptor for urokinase‐type plasminogen activator Comparison to other members of the Ly‐6 family and snake venom α‐neurotoxins

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Ploug, Michael, Ellis, Vincent·1994·FEBS Letters

Abstract

Plasminogen activation is regulated by the interaction between urokinase‐type plasminogen activator (uPA) and its specific glycolipid‐anchored cell surface receptor (uPAR). uPAR is composed of three homologous domains and is the only multi‐domain member of the Ly‐6 family of glycolipid‐anchored membrane proteins. Recent evidence has highlighted similarities between the individual domains of uPAR and the large family of secreted, single domain snake venom α‐neurotoxins, suggesting that uPAR may adopt the same gross folding pattern as these structurally well characterized proteins. Structural aspects of the binding between α‐neurotoxins and the acetylcholine receptor may have a major influence on future studies of the interaction between uPA and uPAR.

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Metadata

Authors
Ploug, M., & Ellis, V.
Venue
FEBS Letters
Publisher
Wiley
Published
1994-08
Volume
349
Issue
2
Pages
163-168
ISSN
  • 0014-5793 (ISSN-L)
  • 1873-3468
OpenAlex
W2131307163
Cited by
246
References
0
FWCI
4.15
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Structure—function relationships in the receptor for urokinase‐type plasminogen activator Comparison to other members of the Ly‐6 family and snake venom α‐neurotoxins. https://app.cochat.ai/papers/10.1016/0014-5793(94)00674-1
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Ploug, M., & Ellis, V. (1994). Structure—function relationships in the receptor for urokinase‐type plasminogen activator Comparison to other members of the Ly‐6 family and snake venom α‐neurotoxins. FEBS Letters. https://doi.org/10.1016/0014-5793(94)00674-1

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