FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2000747180> ?p ?o ?g. }

• W2000747180 endingPage "709" @default.
• W2000747180 startingPage "693" @default.
• W2000747180 abstract "The mammalian heterogeneous ribonucleoprotein (hnRNP) A1 and its constituent N-terminal domain, termed UP1, have been studied by steady-state and dynamic fluorimetry, as well as phosphorescence and optically detected magnetic resonance (ODMR) spectroscopy at cryogenic temperatures. The results of these diverse techniques coincide in assigning the site of the single tryptophan residue of A1, located in the UP1 domain, to a partially solvent-exposed site distal to the protein's nucleic acid binding surface. In contrast, tyrosine fluorescence is significantly perturbed when either protein associates with single-stranded polynucleotides. Tyr to Trp energy transfer at the singlet level is found for both UP1 and A1 proteins. Single-stranded polynucleotide binding induces a quenching of their intrinsic fluorescence emission, which can be attributed to a significant reduction (>50%) of the Tyr contribution, while Trp emission is only quenched by ∼ 15%. Tyrosine quenching effects of similar magnitude are seen upon polynucleotide binding by either UP1 (1 Trp, 4 Tyr) or A1 (1 Trp, 12 Tyr), strongly suggesting that Tyr residues in both the N-terminal and C-terminal domain of A1 are involved in the binding process. Tyr phosphorescence emission was strongly quenched in the complexes of UP1 with various polynucleotides, and was attributed to triplet state energy transfer to nucleic acid bases located in the close vicinity of the fluorophore. These results are consistent with stacking of the tyrosine residues with the nucleic acid bases. While the UP1 Tyr phosphorescence lifetime is drastically shortened in the polynucleotide complex, no change of phosphorescence emission maximum, phosphorescence decay lifetime or ODMR transition frequencies were observed for the single Trp residue. The results of dynamic anisotropy measurements of the Trp fluorescence have been interpreted as indicative of significant internal flexibility in both UP1 and A1, suggesting a flexible linkage connecting the two sub-domains in UP1. Theoretical calculations based on amino acid sequence for chain flexibility and other secondary structural parameters are consistent with this observation, and suggest that flexible linkages between sub-domains may exist in other RNA binding proteins. While the dynamic anisotropy data are consistent with simultaneous binding of both the C-terminal and the N-terminal domains to the nucleic acid lattice, no evidence for simultaneous binding of both UP1 sub-domains was found." @default.
• W2000747180 created "2016-06-24" @default.
• W2000747180 creator A5019500830 @default.
• W2000747180 creator A5045523035 @default.
• W2000747180 creator A5048254108 @default.
• W2000747180 creator A5049702210 @default.
• W2000747180 creator A5084688805 @default.
• W2000747180 date "1991-09-01" @default.
• W2000747180 modified "2023-09-23" @default.
• W2000747180 title "Physical studies of tyrosine and tryptophan residues in mammalian A1 heterogeneous nuclear ribonucleoprotein Support for a segmented structure" @default.
• W2000747180 cites W1481260212 @default.
• W2000747180 cites W1485677996 @default.
• W2000747180 cites W1500915551 @default.
• W2000747180 cites W1503517711 @default.
• W2000747180 cites W1526839960 @default.
• W2000747180 cites W1550600895 @default.
• W2000747180 cites W1555057470 @default.
• W2000747180 cites W1563007775 @default.
• W2000747180 cites W1582560650 @default.
• W2000747180 cites W1589353440 @default.
• W2000747180 cites W1603523537 @default.
• W2000747180 cites W1605966225 @default.
• W2000747180 cites W1936434484 @default.
• W2000747180 cites W1967482997 @default.
• W2000747180 cites W1973558926 @default.
• W2000747180 cites W1974407488 @default.
• W2000747180 cites W1974824041 @default.
• W2000747180 cites W1975304761 @default.
• W2000747180 cites W1981587090 @default.
• W2000747180 cites W1987203170 @default.
• W2000747180 cites W1992681071 @default.
• W2000747180 cites W1998172963 @default.
• W2000747180 cites W1998736146 @default.
• W2000747180 cites W2009310436 @default.
• W2000747180 cites W2013824759 @default.
• W2000747180 cites W2018543221 @default.
• W2000747180 cites W2019801529 @default.
• W2000747180 cites W2023941617 @default.
• W2000747180 cites W2024061796 @default.
• W2000747180 cites W2024187343 @default.
• W2000747180 cites W2031416144 @default.
• W2000747180 cites W2031804200 @default.
• W2000747180 cites W2034890717 @default.
• W2000747180 cites W2041553172 @default.
• W2000747180 cites W2047188621 @default.
• W2000747180 cites W2048797088 @default.
• W2000747180 cites W2049695588 @default.
• W2000747180 cites W2059364771 @default.
• W2000747180 cites W2060788948 @default.
• W2000747180 cites W2069453874 @default.
• W2000747180 cites W2078188479 @default.
• W2000747180 cites W2081284538 @default.
• W2000747180 cites W2087202599 @default.
• W2000747180 cites W2094285422 @default.
• W2000747180 cites W2095450147 @default.
• W2000747180 cites W2119144097 @default.
• W2000747180 cites W2134524888 @default.
• W2000747180 cites W2197691169 @default.
• W2000747180 cites W2211367741 @default.
• W2000747180 cites W3004635462 @default.
• W2000747180 doi "https://doi.org/10.1016/0022-2836(91)80081-5" @default.
• W2000747180 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1656054" @default.
• W2000747180 hasPublicationYear "1991" @default.
• W2000747180 type Work @default.
• W2000747180 sameAs 2000747180 @default.
• W2000747180 citedByCount "17" @default.
• W2000747180 countsByYear W20007471802012 @default.
• W2000747180 countsByYear W20007471802019 @default.
• W2000747180 crossrefType "journal-article" @default.
• W2000747180 hasAuthorship W2000747180A5019500830 @default.
• W2000747180 hasAuthorship W2000747180A5045523035 @default.
• W2000747180 hasAuthorship W2000747180A5048254108 @default.
• W2000747180 hasAuthorship W2000747180A5049702210 @default.
• W2000747180 hasAuthorship W2000747180A5084688805 @default.
• W2000747180 hasConcept C111921641 @default.
• W2000747180 hasConcept C121332964 @default.
• W2000747180 hasConcept C121745418 @default.
• W2000747180 hasConcept C12554922 @default.
• W2000747180 hasConcept C181817918 @default.
• W2000747180 hasConcept C185592680 @default.
• W2000747180 hasConcept C2776165026 @default.
• W2000747180 hasConcept C2776706248 @default.
• W2000747180 hasConcept C2777337673 @default.
• W2000747180 hasConcept C515207424 @default.
• W2000747180 hasConcept C55493867 @default.
• W2000747180 hasConcept C62520636 @default.
• W2000747180 hasConcept C86803240 @default.
• W2000747180 hasConcept C91881484 @default.
• W2000747180 hasConcept C96305047 @default.
• W2000747180 hasConceptScore W2000747180C111921641 @default.
• W2000747180 hasConceptScore W2000747180C121332964 @default.
• W2000747180 hasConceptScore W2000747180C121745418 @default.
• W2000747180 hasConceptScore W2000747180C12554922 @default.
• W2000747180 hasConceptScore W2000747180C181817918 @default.
• W2000747180 hasConceptScore W2000747180C185592680 @default.
• W2000747180 hasConceptScore W2000747180C2776165026 @default.
• W2000747180 hasConceptScore W2000747180C2776706248 @default.
• W2000747180 hasConceptScore W2000747180C2777337673 @default.

• next