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Titlebook: Retroviral Proteases; Control of maturatio Laurence H. Pearl Textbook 1990Latest edition Macmillan Publishers Limited 1990 AIDS.biology.evo

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發(fā)表于 2025-3-21 19:41:08 | 只看該作者 |倒序瀏覽 |閱讀模式
書目名稱Retroviral Proteases
副標題Control of maturatio
編輯Laurence H. Pearl
視頻videohttp://file.papertrans.cn/830/829284/829284.mp4
圖書封面Titlebook: Retroviral Proteases; Control of maturatio Laurence H. Pearl Textbook 1990Latest edition Macmillan Publishers Limited 1990 AIDS.biology.evo
描述This volume describes the state-of-the-art of our understanding of the structure and function of retroviral proteases, and their substrates, the viral polyproteins, described by the leading workers in the field. The contributions range from detailed biochemical and structural characterisation of several retroviral proteases including that from HIV-1, through the analysis of the proteolytic processing of the viral polyproteins, to the structure of the viral capsids formed by the action of the protease, and is essential reading for anyone interested in the molecular biology of AIDS.
出版日期Textbook 1990Latest edition
關鍵詞AIDS; biology; evolution; gene; HIV; insects; molecular biology; morphogenesis; protein; proteins; replication
版次1
doihttps://doi.org/10.1007/978-1-349-11907-3
copyrightMacmillan Publishers Limited 1990
The information of publication is updating

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發(fā)表于 2025-3-21 22:57:25 | 只看該作者
Characterisation and Inhibition of the Retroviral HIV-Protease,particles (Kohl, ., 1988). Retroviral proteases appear to have a highly specific relation to their virus encoded substrate (Dittmar and Moelling, 1978; Khan and Stephenson, 1979; Yoshinaka ., 1985; Kr?usslich and von der Helm, 1987). Examination of the amino acid sequences of retroviral proteases in
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Cleavage of RT/RNase H by HIV-1 Protease and Analysis of Substrate Cleavage Sites ,ge of denatured ovalbumin, of the MS2. fusion protein or synthetic peptides. Several synthetic peptides representing various poten tial protease cleavage sites and modifications thereof were analyzed . . for their efficiency of cleavage by the protease. One synthetic peptide representing the natural
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Functional Characterisation of HIV-1 , Fusion Protein,ypeptide composed of a C-terminal-truncated . peptide and the entire . peptide. The second stage involves the proteolytic processing of this fusion protein to generate mature structural and functional viral components (Debouck ., 1987; Lillehoj ., 1988). An HIV-specific protease cleaves the fusion p
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Biosynthesis and Processing of the , and , Polyproteins of Human Immunodeficiency Virus Type 1 in , (Farmerie ., 1987; Graves ., 1988). There are at least seven protease cleavage sites in the . and . polyprotein precursors (Darke ., 1988), as depicted in Figure 1. The numbering of amino acid residues at the cleavage sites is based on the amino acid sequence predicted from the nucleotide sequence
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Expression of HIV-1 , and , Gene Products using Recombinant Baculoviruses,oduce some ten different recombinant baculoviruses expressing various gene products encoded by both HIV-1 and HIV-2. Here we describe four of these recombinant viruses that produce products encoded by the gag and . genes of HIV-1. We show that a feature of gag and . translation in HIV-1 infected cel
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Mei-Huei T. Lai,Albert G. Dee,Peter H. Zervos,William F. Heath Jr,Maurice E. Scheetz
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