The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Fragments of the HIV-1 Tat Protein Specifically Biand TAR RNA
Abstract
Proteolytically produced carboxyl-terminal fragments of the human immunodeficiency virus type-1 (HIV-1) Tat protein that include a conserved region rich in arginine and lysine bind specifically to transactivation response RNA sequences (TAR). A chemically synthesized 14-residue peptide spanning the basic subdomain also recognizes TAR, identifying this subdomain as central for RNA interaction. TAR RNA forms a stable hairpin that includes a six-residue loop, a trinucleotide pyrimidine bulge, and extensive duplex structure. Competition and interference experiments show that the Tat-derived fragments bind to double-stranded RNA and interact specifically at the pyrimidine bulge and adjacent duplex of TAR.
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Cites
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Metadata
- Authors
- Weeks, K. M., Ampe, C., Schultz, S. C., Steitz, T. A., & Crothers, D. M.
- Venue
- Science
- Published
- 1990-09-14
- Volume
- 249
- Issue
- 4974
- Pages
- 1281-1285
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2074225638
- Cited by
- 444
- References
- 35
- FWCI
- 15.40
- Type
- journal article
- Language
- en
- Open access
- closed
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- Weeks, K. M., Ampe, C., Schultz, S. C., Steitz, T. A., & Crothers, D. M. (1990). Fragments of the HIV-1 Tat Protein Specifically Biand TAR RNA. Science. https://doi.org/10.1126/science.2205002
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
