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pro vyhledávání: '"C. L. DiIanni"'
Autor:
C L DiIanni, W K Herber, Richard A. F. Dixon, Lenora Davis, Paul L. Darke, Nancy E. Kohl, M K Holloway
Publikováno v:
Journal of Biological Chemistry. 265:17348-17354
The pepsin-like aspartyl proteases consist of a single polypeptide chain with topologically similar amino- and carboxyl-terminal domains, each of which contributes 1 aspartic acid residue to the active site. This structure has been proposed to have e
Autor:
C. L. DiIanni, C. A. Meyers, Jonglin Tsao, Donald R. O'Boyle, D. A. Drier, J T Stevens, Claudio Mapelli, S P Weinheimer
Publikováno v:
Peptides 1994 ISBN: 9789072199218
Peptides 1994
Peptides 1994
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eadbc758c45a0ba904db13eafd0eece5
https://doi.org/10.1007/978-94-011-1468-4_359
https://doi.org/10.1007/978-94-011-1468-4_359
Publikováno v:
The Journal of biological chemistry. 269(17)
Herpes simplex virus type 1 (HSV-1) encodes a protease that is essential for proteolytic processing of itself and of the nucleocapsid-associated protein, ICP35 (infected cell protein 35) (Liu, F., and Roizman, B. (1991) J. Virol. 65, 5149-5156). Inhi
Autor:
C L, DiIanni, C, Mapelli, D A, Drier, J, Tsao, S, Natarajan, D, Riexinger, S M, Festin, M, Bolgar, G, Yamanaka, S P, Weinheimer
Publikováno v:
The Journal of biological chemistry. 268(34)
Herpes simplex virus type-1 (HSV-1) protease is responsible for proteolytic processing of itself and the virus assembly protein ICP35 (infected cell protein 35). Two proteolytic processing sites within the protease have recently been identified betwe
Autor:
C L, DiIanni, D A, Drier, I C, Deckman, P J, McCann, F, Liu, B, Roizman, R J, Colonno, M G, Cordingley
Publikováno v:
The Journal of biological chemistry. 268(3)
Herpes simplex virus type-1 (HSV-1) encodes a protease responsible for proteolytic processing of the virus assembly protein, ICP35 (infected cell protein 35). The coding region of ICP35 is contained within the gene that encodes the protease, and ICP3
Publikováno v:
The Journal of biological chemistry. 265(28)
The pepsin-like aspartyl proteases consist of a single polypeptide chain with topologically similar amino- and carboxyl-terminal domains, each of which contributes 1 aspartic acid residue to the active site. This structure has been proposed to have e