Human Cytomegalovirus Protease Complexes Its Substrate Recognition Sequences in an Extended Peptide Conformation†,‡

Biochemistry ◽  
1998 ◽  
Vol 37 (27) ◽  
pp. 9793-9801 ◽  
Author(s):  
Steven R. LaPlante ◽  
Norman Aubry ◽  
Pierre R. Bonneau ◽  
Dale R. Cameron ◽  
Lisette Lagacé, ◽  
...  
10.1038/1860 ◽  
1998 ◽  
Vol 5 (9) ◽  
pp. 819-826 ◽  
Author(s):  
Liang Tong ◽  
Chungeng Qian ◽  
Marie-Josée Massariol ◽  
Robert Déziel ◽  
Christiane Yoakim ◽  
...  

1987 ◽  
Vol 57 (01) ◽  
pp. 017-019 ◽  
Author(s):  
Magda M W Ulrich ◽  
Berry A M Soute ◽  
L Johan M van Haarlem ◽  
Cees Vermeer

SummaryDecarboxylated osteocalcins were prepared and purified from bovine, chicken, human and monkey bones and assayed for their ability to serve as a substrate for vitamin K-dependent carboxylase from bovine liver. Substantial differences were observed, especially between bovine and monkey d-osteocalcin. Since these substrates differ only in their amino acid residues 3 and 4, it seems that these residues play a role in the recognition of a substrate by hepatic carboxylase.


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