Arginine-rich peptides that translocate through cell membranes.
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Accession number;02A0304378
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| Title;Arginine-rich peptides that translocate through cell membranes. |
| Author;
FUTAKI SHIRO
(Inst. for Chem. Res., Kyoto Univ.)
SUZUKI TOMOKI
(Inst. for Chem. Res., Kyoto Univ.)
NAKASE IKUHIKO
(Inst. for Chem. Res., Kyoto Univ.)
NIWA MIKI
(Inst. for Chem. Res., Kyoto Univ.)
OHASHI WAKANA
(Inst. for Chem. Res., Kyoto Univ.)
SUGIURA YUKIO
(Inst. for Chem. Res., Kyoto Univ.)
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Journal Title;Abstracts. Symposium on Biofunctional Chemistry
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Journal Code:L0836A
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ISSN:
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VOL.16th;NO.;PAGE.44-45(2001)
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| Figure&Table&Reference; |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;A basic peptide derived from human immunodeficiency virus(HIV)-1 Tat protein (positions 48-60) has been reported to have the ability to translocate through the cell membranes and accumulate in the nucleus, the characteristics of which are utilized for the delivery of exogenous proteins into cells. Based on the fluorescence microscopic observations of mouse macrophage RAW264.7 cells, we found that various arginine-rich peptides have a translocation activity very similar to Tat-(48-60). These included the RNA-binding peptides derived from virus proteins, such as HIV-1 Rev, and flock house virus(FHV) coat proteins, and the DNA binding segments of leucine zipper proteins, such as cancer-related proteins cFos, and cJun, and the yeast transcription factor GCN4. Using (Arg)n (n=4-16) peptides, we also demonstrated that there would be an optimal number of arginine residues (n-8) for the efficient translocation. Branched-chain arginine peptides also showed efficient translocation. (author abst.) |
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