FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2054266435> ?p ?o ?g. }

• W2054266435 endingPage "110" @default.
• W2054266435 startingPage "90" @default.
• W2054266435 abstract "The binding site for tat protein on TAR RNA has been defined in quantitative terms using an extensive series of mutations. The relative dissociation constants for the mutant TAR RNAs were measured using a dual-label competition filter binding assay in which 35S-labelled wild-type TAR RNA (K1) was competed against 3H-labelled mutant TAR RNA (K2). The error in the self-competition experiment was usually less than 10% (e.g. K2/K1 = 1.07 +/- 0.05, n = 19) and the experimental data accurately matched theoretical curves calculated with fitted dissociation constants. Mutations in U23, a critical residue in the U-rich bulge sequence, or in either of the two base-pairs immediately above the bulge, G26.C39 and A27.U38 reduced that affinity by 8- to 20-fold. Significant contributions to tat binding affinity were also made by the base-pairs located immediately below the bulge. For example, mutation of A22.U40 to U.A reduced tat affinity 5-fold, and mutation of G21.C41 to C.G reduced tat affinity 4-fold. The binding of a series of peptides spanning the basic arginine-rich sequence of tat was examined using both filter-binding and gel mobility shift assays. Each of the peptides showed significantly reduced affinities for wild-type TAR RNA compared to the tat protein. The ADP-2 (residues 43 to 72), ADP-3 (residues 48 to 72) and ADP-5 (residues 49 to 86) peptides were unable to discriminate between wild-type TAR RNA and TAR RNA mutants with the same fidelity as the tat protein. For example, these peptides showed no more than 3-fold reductions in affinity relative to wild-type TAR RNA for the U23-->C mutation in the bulge, or G26.G39-->C.G mutation in the stem of TAR RNA. By contrast, the ADP-I (residues 37 to 72), ADP-4 (residues 32 to 62) and ADP-6 (residues 32 to 72) peptides, which each carry amino acid residues from the core region of the tat protein have binding specificities that more closely resemble the protein. The ADP-4 and ADP-6 peptides showed between 4- and 7-fold reductions in affinity for the U23-->C or G26.C39-->C.G mutations. The ADP-1 peptide most closely resembles the protein in its binding specificity and showed 9-fold and 14-fold reductions in affinity for the two mutants, respectively. Chemical-modification interference assays using diethylpyrocarbonate (DEPC) and ethylnitrosourea (ENU) were also used to compare the binding properties of the tat protein and the tat-derived peptides.(ABSTRACT TRUNCATED AT 400 WORDS)" @default.
• W2054266435 created "2016-06-24" @default.
• W2054266435 creator A5008907883 @default.
• W2054266435 creator A5018652720 @default.
• W2054266435 creator A5032124280 @default.
• W2054266435 creator A5044579516 @default.
• W2054266435 creator A5049581015 @default.
• W2054266435 creator A5054699153 @default.
• W2054266435 creator A5057198168 @default.
• W2054266435 creator A5087082718 @default.
• W2054266435 creator A5090801139 @default.
• W2054266435 date "1993-03-01" @default.
• W2054266435 modified "2023-10-10" @default.
• W2054266435 title "High Affinity Binding of TAR RNA by the Human Immunodeficiency Virus Type-1 tat Protein Requires Base-pairs in the RNA Stem and Amino Acid Residues Flanking the Basic Region" @default.
• W2054266435 doi "https://doi.org/10.1006/jmbi.1993.1128" @default.
• W2054266435 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8450553" @default.
• W2054266435 hasPublicationYear "1993" @default.
• W2054266435 type Work @default.
• W2054266435 sameAs 2054266435 @default.
• W2054266435 citedByCount "269" @default.
• W2054266435 countsByYear W20542664352012 @default.
• W2054266435 countsByYear W20542664352013 @default.
• W2054266435 countsByYear W20542664352014 @default.
• W2054266435 countsByYear W20542664352015 @default.
• W2054266435 countsByYear W20542664352016 @default.
• W2054266435 countsByYear W20542664352017 @default.
• W2054266435 countsByYear W20542664352018 @default.
• W2054266435 countsByYear W20542664352019 @default.
• W2054266435 countsByYear W20542664352020 @default.
• W2054266435 countsByYear W20542664352021 @default.
• W2054266435 countsByYear W20542664352022 @default.
• W2054266435 countsByYear W20542664352023 @default.
• W2054266435 crossrefType "journal-article" @default.
• W2054266435 hasAuthorship W2054266435A5008907883 @default.
• W2054266435 hasAuthorship W2054266435A5018652720 @default.
• W2054266435 hasAuthorship W2054266435A5032124280 @default.
• W2054266435 hasAuthorship W2054266435A5044579516 @default.
• W2054266435 hasAuthorship W2054266435A5049581015 @default.
• W2054266435 hasAuthorship W2054266435A5054699153 @default.
• W2054266435 hasAuthorship W2054266435A5057198168 @default.
• W2054266435 hasAuthorship W2054266435A5087082718 @default.
• W2054266435 hasAuthorship W2054266435A5090801139 @default.
• W2054266435 hasConcept C104317684 @default.
• W2054266435 hasConcept C107824862 @default.
• W2054266435 hasConcept C143065580 @default.
• W2054266435 hasConcept C153911025 @default.
• W2054266435 hasConcept C170493617 @default.
• W2054266435 hasConcept C185592680 @default.
• W2054266435 hasConcept C192643346 @default.
• W2054266435 hasConcept C199360897 @default.
• W2054266435 hasConcept C207583985 @default.
• W2054266435 hasConcept C41008148 @default.
• W2054266435 hasConcept C55493867 @default.
• W2054266435 hasConcept C67705224 @default.
• W2054266435 hasConcept C71240020 @default.
• W2054266435 hasConcept C74998103 @default.
• W2054266435 hasConcept C86803240 @default.
• W2054266435 hasConceptScore W2054266435C104317684 @default.
• W2054266435 hasConceptScore W2054266435C107824862 @default.
• W2054266435 hasConceptScore W2054266435C143065580 @default.
• W2054266435 hasConceptScore W2054266435C153911025 @default.
• W2054266435 hasConceptScore W2054266435C170493617 @default.
• W2054266435 hasConceptScore W2054266435C185592680 @default.
• W2054266435 hasConceptScore W2054266435C192643346 @default.
• W2054266435 hasConceptScore W2054266435C199360897 @default.
• W2054266435 hasConceptScore W2054266435C207583985 @default.
• W2054266435 hasConceptScore W2054266435C41008148 @default.
• W2054266435 hasConceptScore W2054266435C55493867 @default.
• W2054266435 hasConceptScore W2054266435C67705224 @default.
• W2054266435 hasConceptScore W2054266435C71240020 @default.
• W2054266435 hasConceptScore W2054266435C74998103 @default.
• W2054266435 hasConceptScore W2054266435C86803240 @default.
• W2054266435 hasIssue "1" @default.
• W2054266435 hasLocation W20542664351 @default.
• W2054266435 hasLocation W20542664352 @default.
• W2054266435 hasOpenAccess W2054266435 @default.
• W2054266435 hasPrimaryLocation W20542664351 @default.
• W2054266435 hasRelatedWork W2019453585 @default.
• W2054266435 hasRelatedWork W2023513000 @default.
• W2054266435 hasRelatedWork W2025114300 @default.
• W2054266435 hasRelatedWork W2064452889 @default.
• W2054266435 hasRelatedWork W2075018759 @default.
• W2054266435 hasRelatedWork W2077600787 @default.
• W2054266435 hasRelatedWork W2091233792 @default.
• W2054266435 hasRelatedWork W2171963856 @default.
• W2054266435 hasRelatedWork W2918990755 @default.
• W2054266435 hasRelatedWork W2289256138 @default.
• W2054266435 hasVolume "230" @default.
• W2054266435 isParatext "false" @default.
• W2054266435 isRetracted "false" @default.
• W2054266435 magId "2054266435" @default.
• W2054266435 workType "article" @default.