Zobrazeno 1 - 4
of 4
pro vyhledávání: '"C A Veloski"'
Autor:
Robert L. Lafemina, Bohdan S. Wolanski, A I Marcy, B Pramanik, W J Long, Daria J. Hazuda, K Bakshi, C A Veloski
Publikováno v:
Journal of Virology. 70:4819-4824
The human cytomegalovirus (HCMV) protease is a potential target for antiviral chemotherapeutics; however, autoprocessing at internal sites, particularly at positions 143 and 209, hinders the production of large quantities of stable enzyme for either
Autor:
Robert L. Lafemina, C A Veloski, Jules A. Shafer, Paul L. Darke, Elizabeth Chen, Dawn L. Hall, Lawrence Kuo, Mohinder K. Sardana
Publikováno v:
Journal of Biological Chemistry. 269:18708-18711
Assembly of viral capsids for replication of herpes simplex virus requires the proteolytic processing of the assembly protein ICP35. The protease responsible for this process is encoded within the 635-amino acid open reading frame of the UL26 gene of
Autor:
C A Veloski, W J Long, K LeGrow, J A Wolfgang, V V Sardana, Bohdan S. Wolanski, Emilio A. Emini, Robert L. Lafemina
Publikováno v:
Journal of Biological Chemistry. 269:14337-14340
The human cytomegalovirus UL80 gene encodes an 80-kDa precursor polyprotein whose N-terminal 256-amino acid domain is a protease. This enzyme cleaves a specific peptide bond that results in its own release from the precursor, as well as a peptide bon
Autor:
V V, Sardana, J A, Wolfgang, C A, Veloski, W J, Long, K, LeGrow, B, Wolanski, E A, Emini, R L, LaFemina
Publikováno v:
The Journal of biological chemistry. 269(20)
The human cytomegalovirus UL80 gene encodes an 80-kDa precursor polyprotein whose N-terminal 256-amino acid domain is a protease. This enzyme cleaves a specific peptide bond that results in its own release from the precursor, as well as a peptide bon