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- W1969134675 abstract "Human T-cell leukemia virus type 1 (HTLV-1) is a type C human retrovirus and is the causative agent of adult T-cell leukemia and other diseases. The enzymatic and structural proteins of HTLV-I are synthesized as part of a Gag-Pro-Pol precursor polyprotein, and the mature proteins are released by proteolytic processing catalyzed by HTLV-I protease. The locations of most of the proteolytic cleavage sites are known, however, the site that creates the N-terminus of HTLV-1 integrase has not been previously identified. A 15 residue peptide corresponding to junction of the C-terminus of RNaseH and N-terminus of integrase (DALLITPVLQLSPAF-OH) was incubated with HTLV-1 protease. Analysis of the cleavage products by LC-MS revealed fragments Ac-DALLITPVLQL-OH and H(2)N-SPAF-OH were produced, indicating cleavage between the leucine and serine. This is the first physical identification of the N-terminal amino acid sequence of the integrase of HTLV-1." @default.
- W1969134675 created "2016-06-24" @default.
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- W1969134675 date "2003-01-01" @default.
- W1969134675 modified "2023-09-27" @default.
- W1969134675 title "Identification of the RT–RH/IN cleavage site of HTLV-I" @default.
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- W1969134675 doi "https://doi.org/10.1016/s0006-291x(02)02848-6" @default.
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