ArticleBiochemical and biophysical research communications2008
Transient HMGB protein interactions with B-DNA duplexes and complexes.
Article in Biochemical and biophysical research communications, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
- Single-molecule tracking reveals that the nucleoid-associated protein HU plays a dual role in maintaining proper nucleoid volume through differential interactions with chromosomal DNA.Molecular microbiology · 2021Article
- How do DNA-bound proteins leave their binding sites? The role of facilitated dissociation.Current opinion in chemical biology · 2019Review
- Evidence for a bind-then-bend mechanism for architectural DNA binding protein yNhp6A.Nucleic acids research · 2019Article
- Single-molecule studies of high-mobility group B architectural DNA bending proteins.Biophysical reviews · 2017Review
- The HMGB1 C-Terminal Tail Regulates DNA Bending.Journal of molecular biology · 2016Article
- DNA-Segment-Facilitated Dissociation of Fis and NHP6A from DNA Detected via Single-Molecule Mechanical Response.Journal of molecular biology · 2015Article
- HMGB1 in health and disease.Molecular aspects of medicine · 2014Review
- Single-molecule kinetics reveal microscopic mechanism by which High-Mobility Group B proteins alter DNA flexibility.Nucleic acids research · 2013Article
- Role of the acidic tail of high mobility group protein B1 (HMGB1) in protein stability and DNA bending.PloS one · 2013Article
- Single-molecule FRET analysis of DNA binding and bending by yeast HMGB protein Nhp6A.Nucleic acids research · 2013Article
- Understanding apparent DNA flexibility enhancement by HU and HMGB architectural proteins.Journal of molecular biology · 2011Article
- Concentration-dependent exchange accelerates turnover of proteins bound to double-stranded DNA.Nucleic acids research · 2011Article
- DNA stretching as a probe for nucleic acid interactions: Reply to Comments on "Biophysical characterization of DNA binding from single molecule force measurements" by Kathy R. Chaurasiya, Thayaparan Paramanathan, Micah J. McCauley, Mark C. Williams.Physics of life reviews · 2010Article
- Enhancement of DNA flexibility in vitro and in vivo by HMGB box A proteins carrying box B residues.Biochemistry · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
HMGB proteins are abundant, non-histone proteins in eukaryotic chromatin. HMGB proteins contain one or two conserved "HMG boxes" and can be sequence-specific or nonspecific in their DNA binding. HMGB proteins cause strong DNA bending and bind preferentially to deformed DNAs. We wish to understand how HMGB proteins increase the apparent flexibility of non-distorted B-form DNA. We test the hypothesis that HMGB proteins bind transiently, creating an ensemble of distorted DNAs with rapidly interconverting conformations. We show that binding of B-form DNA by HMGB proteins is both weak and transient under conditions where DNA cyclization is strongly enhanced. We also detect novel complexes in which HMGB proteins simultaneously bind more than one DNA duplex.
Indexed as
Identifiers
What 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.