ArticleThe Biochemical journal2000
Alanine mutagenesis of high-mobility-group-protein-1 box B (HMG1-B).
Article in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed, 12 citations in OpenAlex.
- Interaction of HMG proteins and H1 with hybrid PNA-DNA junctions.Protein science : a publication of the Protein Society · 2013Article
- Heparan sulfate is essential for high mobility group protein 1 (HMGB1) signaling by the receptor for advanced glycation end products (RAGE).The Journal of biological chemistry · 2011Article
- Interactions of recombinant HMGB proteins with branched RNA substrates.Biochemical and biophysical research communications · 2008Article
- Mechanism of high-mobility group protein B enhancement of progesterone receptor sequence-specific DNA binding.Nucleic acids research · 2008Article
- The role of intercalating residues in chromosomal high-mobility-group protein DNA binding, bending and specificity.Nucleic acids research · 2003Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We have generated a set of alanine-scanning substitutions in high-mobility-group protein 1 box B (HMG1-B; the second domain of the HMG1 nuclear protein from the rat) in order to explore the influence of specific surface side chains on its function and folding. Guanidine hydrochloride and thermal unfolding studies have been carried out to investigate the effect of substituted residues on the folding pathway. Binding to four-way junction and linear-duplex DNA has been assayed to determine which residues play an important role in DNA binding. We have identified several mutants that are more stable or bind more tightly to the junction than the wild-type, including the particular phenylalanine side chain that is thought to intercalate into the DNA. Thus the interaction between HMG1-B and branched DNA substrates should exhibit differences from present models based on the structure of the complexes that have been solved to date.
Indexed as
Identifiers
10769186PMC1221019W2009889319What OpenQuestion holds
Registered trials
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.