Associated Papers
NMR and crystallographic structural studies of the extremely stable monomeric variant of human cystatin C with single amino acid substitution.
Maszota-Zieleniak M et al.
The Febs Journal, 2020
Wild-type and met-65-->Leu variants of human cystatin A are functionally and structurally identical.
Craven CJ et al.
Biochemistry, 2000
Structural comparison between wild-type and P25S human cystatin A by NMR spectroscopy. Does this mutation affect the alpha-helix conformation?
Shimba N et al.
Journal of Structural and Functional Genomics, 2000
Hydrophobic sequences can substitute for the wild-type N-terminal sequence of cystatin A (stefin A) in tight binding to cysteine proteinases selection of high-affinity N-terminal region variants by phage display.
Ylinenjärvi K et al.
European Journal of Biochemistry, 1999
Solution structure of a human cystatin A variant, cystatin A2-98 M65L, by NMR spectroscopy. A possible role of the interactions between the N- and C-termini to maintain the inhibitory active form of cystatin A.
Tate S et al.
Biochemistry, 1995
Human cystatin A is inactivated by engineered truncation. The NH2-terminal region of the cysteine proteinase inhibitor is essential for expression of its inhibitory activity.
Shibuya K et al.
Biochemistry, 1995
Significance of the highly conserved Gly-4 residue in human cystatin A.
Shibuya K et al.
Journal of Biochemistry, 1995
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