ArticleMolecular and cellular biochemistry2005
In-vitro dual binding activity of a evolutionarily related subgroup of hnRNP proteins.
Article in Molecular and cellular biochemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 7 citations in OpenAlex.
- The citrullinated/native index of autoantibodies against hnRNP-DL predicts an individual "window of treatment success" in RA patients.Arthritis research & therapy · 2021Article
- NRF IRES activity is mediated by RNA binding protein JKTBP1 and a 14-nt RNA element.RNA (New York, N.Y.) · 2007Article
- Telomere dynamics: the means to an end.Cell proliferation · 2007Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The wide family of heterogeneous nuclear ribonucleoproteins (hnRNPs) comprises members that interact with single-stranded nucleic acids. On the basis of their structure, some of them are characterised by a tandem RNA-binding domain (RBD) and a glycine-rich C-terminus, showing a high degree of homology. Recently, we have isolated some proteins belonging to this group that interact with single-stranded cytosine-block telomeric DNA. The aim of the present investigation is to better characterise the relationship of some structural features shared by these proteins and their in-vitro interaction with the telomeric type sequences. We analysed the in-vitro binding properties of some of these components toward both single-stranded telomeric motifs. Using deletion mutants, the relationship between cytosine-rich motif binding activity and the structural features of one of these proteins is further characterized. This binding activity appears to be related to a subgroup of the 2xRBD+Glycine rich hnRNP, suggesting functionally distinct properties of these proteins, in agreement with their evolutionary relationship.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.