The fungal‐resistance factors BmSPI38 and BmSPI39 predominantly exist as tetramers, not monomers, in Bombyx mori
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DOI: 10.1111/imb.12504
Abstract: Previous studies have indicated that trypsin inhibitor‐like cysteine‐rich domain (TIL)‐type protease inhibitors, BmSPI38 and BmSPI39, suppress conidial germination and integument penetration of entomopathogenic fungi by inhibiting their cuticle‐degrading proteases and might functions as fungal‐resistance factors… read more here.
Keywords: resistance factors; bombyx mori; fungal resistance; bmspi38 bmspi39 ... See more keywords
Amino Acid Substitutions at P1 Position Change the Inhibitory Activity and Specificity of Protease Inhibitors BmSPI38 and BmSPI39 from Bombyx mori
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DOI: 10.3390/molecules28052073
Abstract: It was found that silkworm serine protease inhibitors BmSPI38 and BmSPI39 were very different from typical TIL-type protease inhibitors in sequence, structure, and activity. BmSPI38 and BmSPI39 with unique structure and activity may be good… read more here.
Keywords: bmspi38 bmspi39; activity; protease inhibitors; inhibitory ... See more keywords