Literature for inhibitor I25.001: cystatin A
(References are filtered for relevance to Structure. To remove the filter click here. See explanation.)
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Renko,M., Pozgan,U., Majera,D. and Turk,D.
Stefin A displaces the occluding loop of cathepsin B only by as much as required to bind to the active site cleft
FEBS J277, 4338-4345. PubMed Europe PubMed DOI S -
[YEAR:21-2-2003]Jenko,S., Dolenc,I., Guncar,G., Dobersek,A., Podobnik,M. and Turk,D.
Crystal structure of stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases
J Mol Biol326, 875-885. PubMed Europe PubMed DOI S -
Shimba,N., Kariya,E., Tate,S., Kaji,H. and Kainosho,M.
Structural comparison between wild-type and P25S human cystatin A by NMR spectroscopy. Does this mutation affect the alpha-helix conformation?
J Struct Funct Genomics1, 26-42. PubMed Europe PubMed S -
Martin,J.R., Craven,C.J., Jerala,R., Kroon-Zitko,L., Zerovnik,E., Turk,V. and Waltho,J.P.
The three-dimensional solution structure of human stefin A
J Mol Biol246, 331-343. PubMed Europe PubMed DOI S
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