Freund, J. and Kellner, R. and Konvalinka, J. and Wolber, V. and Kräusslich, H. G. and Kalbitzer, Hans Robert (1994) A possible regulation of negative factor (Nef) activity of human immunodeficiency virus type 1 by the viral protease. European journal of biochemistry: EJB(= the FEBS journal) 223 (2), pp. 589-593.
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Negative factor (Nef) protein from human immunodeficiency virus type 1 (HIV-1) is cleaved into two well-defined domains by the HIV-1-encoded protease. The cleavage site is located between Trp57 and Leu58 and is well conserved. The two domains are stable in the presence of protease for more than 48 h. The C-terminal core domain contains a well-conserved well-folded region. The cleavage releases the core domain from the myristoylated membrane anchor domain. As is the case for other HIV proteins, cleavage of Nef could be crucial for correct biological function.
|Institutions:||Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer|
|Subjects:||500 Science > 570 Life sciences|
|Created at the University of Regensburg:||Unknown|
|Deposited On:||08 Sep 2010 10:10|
|Last Modified:||08 Sep 2010 10:10|
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