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- W1494051330 endingPage "131" @default.
- W1494051330 startingPage "99" @default.
- W1494051330 abstract "Epidermal growth factor (EGF) has been the prototype growth-stimulating peptide for many years. It has a characteristic structure with three disulfide bridges, which is essential for its activity. However, many other proteins, including both growth factors and proteins with unrelated functions, have similar EGF-like domains. This indicates that besides a characteristic conformation provided by the EGF-like domain, specific amino acids are required to provide specificity in protein functioning. Currently, more than 10 different growth factors with an EGF-like domain have been characterized which all exert their action by binding to the four members of the erbB family of receptors. In this review, studies are described on the structure-function relationship of these EGF-like growth factor molecules in an attempt to analyze the individual amino acids that determine their binding specificity to the individual members of the erbB family." @default.
- W1494051330 created "2016-06-24" @default.
- W1494051330 creator A5023507947 @default.
- W1494051330 creator A5035312473 @default.
- W1494051330 creator A5048297189 @default.
- W1494051330 creator A5052940933 @default.
- W1494051330 date "2000-01-01" @default.
- W1494051330 modified "2023-09-25" @default.
- W1494051330 title "The EGF domain: Requirements for binding to receptors of the ErbB family" @default.
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