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References:

ExPASy PeptideCutter tool:
Gasteiger E., Hoogland C., Gattiker A., Duvaud S., Wilkins M.R., Appel R.D., Bairoch A.;
Protein Identification and Analysis Tools on the ExPASy Server;
(In) John M. Walker (ed): The Proteomics Protocols Handbook, Humana Press (2005).
Full text - Copyright Humana Press.

Proteases:

Barrett A., Rawlings N.D., Woessner J.F.
Handbook of proteolytic enzymes.
Academic Press (1998)

Birktoft J.J., Breddam K.
Glutamyl endopeptidases.
Methods of Enzymology (1994) 244: 114-126.

Bornstein P., Balian G.
Cleavage at Asn-Gly bonds with hydroxylamine.
Methods in Enzymology (1977) 47: 132- 144

Degani Y., Patchornik A.
Cyanylation of sulfhydryl groups by 2-nitro-5-thiocyanobenzoic acid. High-yield modification and cleavage of peptides at cysteine residues.
Biochemistry (1974) 13: 1-11.

Earnshaw W.C., Martins L.M., Kaufmann S.H.
Mammalian caspases: Structure, activation, substrates, and functions during apoptosis.
Annual Review of Biochemistry (1999) 68: 383-424.

Fulop V., Bocskei Z., Polgar L.
Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis
Cell (1998) 94: 161-170.

Fujikawa K., Titani K., Davie E.W.
Activation of bovine factor X (Stuart factor): conversion of factor Xa alpha to factor Xa beta.
Proceedings of the National Academy of Science of the United States of America. (1975) 72: 3359-3363.

Houmard J., Drapeau G.R.
Staphylococcal protease: a proteolytic enzyme specific for glutamoyl bonds.
Proceedings of the National Academy of Science of the United States of America (1972) 69: 3506-3509.
Han, K.K et al.
Current developments in chemical cleavage of proteins.
International Journal of Biochemistry (1983) 15(7): 875-884.

Keil, B.
Proteolysis Data Bank: specificity of alpha-chymotrypsin from computation of protein cleavages.
Protein Sequence Data Analysis (1987 ) 1: 13-21.

Keil, B.
Specificity of proteolysis.
Springer-Verlag Berlin-Heidelberg-NewYork, pp.335. (1992)

Keil, B., Tong T.N.
LYSIS.
Springer-Verlag Berlin-Heidelberg-NewYork, diskette set. (1992)

Li, A. et al.
Chemical cleavage at aspartyl residues for protein identification.
Anal Chem. (2001) 73: 5395-5402

Roche
Product description, version 3, October 1999
http://www.roche-applied-science.com/pack-insert/1334115a.pdf

Schechter I. & Berger A.
On the size of the active site in proteases. I. Papain.
Biochemical and Biophysical Research Communication (1967) 27: 157.

Schechter I. & Berger A.
On the active site of proteases. 3. Mapping the active site of papain; specific peptide inhibitors of papain.
Biochemical and Biophysical Research Communication (1968) 32: 898.

Schroeder W.A., Shelton J.B., Shelton J.R.
An examination of conditions for the cleavage of polypeptide chains with cyanogen bromide: application to catalase.
Archives of Biochemistry and Biophysics (1969) 130: 551-556.

Stennicke H.R., Renatus M., Meldal M., Salvesen G.S.
Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1,3,6,7 and 8.
Biochem. J. (2000) 350: 563-568.

Talanian R.V., Quinlan C., Trautz S., Hackett M.C., Mankovich J.A., Banach D., Ghayur T., Brady K.D., Wong W.W.
Substrate specificities of caspase family proteases.
Journal of Biological Chemistry (1997) 272: 9677- 9682.
Thornberry N.A., Rano T.A., Peterson E.P., Rasper D.M., Timkey T. et al.
A combinatorial approach defines specificities of members of the caspase family and Granzyme B.
Journal of Biological Chemistry (1997) 272: 17907- 17911.

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