Eukaryotic and retroviral aspartic proteases: similarities and differences
نویسندگان
چکیده
منابع مشابه
Avian retroviral protease and cellular aspartic proteases are distinguished by activities on peptide substrates.
The avian sarcoma/leukemia virus protease (PR), purified from avian myeloblastosis virus has a native molecular mass of 26 kDa, suggesting a dimer structure. The enzymatic activity of PR has been characterized using synthetic peptide substrates. PR is most active at pH 5.5, 35 degrees C and 2-3 M NaCl. Under these conditions PR cleaves decapeptides which are resistant in low ionic strength. Thi...
متن کاملStructural and biochemical studies of retroviral proteases.
Retroviral proteases form a unique subclass of the family of aspartic proteases. These homodimeric enzymes from a number of viral sources have by now been extensively characterized, both structurally and biochemically. The importance of such knowledge to the development of new drugs against AIDS has been, to a large extent, the driving force behind this progress. High-resolution structures are ...
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Background and purpose: The boundary between bipolar disorder and borderline personality disorder has always been a matter of debate. Despite the importance of this issue, only a few studies have directly compared these two groups. The main purpose of this study was to compare the cognitive profile of patients with bipolar disorder and borderline personality disorder in terms of attentional bia...
متن کاملThe eukaryotic translation initiation factor 4GI is cleaved by different retroviral proteases.
The initiation factor eIF4G plays a central role in the regulation of translation. In picornaviruses, as well as in human immunodeficiency virus type 1 (HIV-1), cleavage of eIF4G by the viral protease leads to inhibition of protein synthesis directed by capped cellular mRNAs. In the present work, cleavage of both eIF4GI and eIF4GII has been analyzed by employing the proteases encoded within the...
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ژورنال
عنوان ژورنال: The FASEB Journal
سال: 2008
ISSN: 0892-6638,1530-6860
DOI: 10.1096/fasebj.22.1_supplement.606.2