Caspase-3 binds diverse P4 residues in peptides as revealed by crystallography and structural modeli...
Caspase-3 binds diverse P4 residues in peptides as revealed by crystallography and structural modeling
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New York: Boston : Springer US
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Language
English
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New York: Boston : Springer US
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Contents
Caspase-3 recognition of various P4 residues in its numerous protein substrates was investigated by crystallography, kinetics, and calculations on model complexes. Asp is the most frequent P4 residue in peptide substrates, although a wide variety of P4 residues are found in the cellular proteins cleaved by caspase-3. The binding of peptidic inhibit...
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Full title
Caspase-3 binds diverse P4 residues in peptides as revealed by crystallography and structural modeling
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TN_cdi_osti_scitechconnect_1005536
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_osti_scitechconnect_1005536
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ISSN
1360-8185
E-ISSN
1573-675X
DOI
10.1007/s10495-009-0333-y
