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To confirm the binding mode between c-MET II and HGF I as shown in our structure, we introduced three point mutations in the K1 domain of HGF, including E159R, E195R, and R197E, to disrupt this interface, and examined the effects of these mutations on c-MET activation

Numerical claims, including wait intervals and channel-closure ranges, were cross-checked for internal consistency across the matrix, the mechanism sections, the protocol, the quick answers, the FAQs, and the key takeaways before publication

Identification of MNPs in human thrombi samples and their possible association with disease severity

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doi:10.1093/BMB/LDR030 6