ArticleJournal of biomolecular NMR1998
Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by the three amino-terminal zinc finger domains from transcription factor IIIA.
Article in Journal of biomolecular NMR, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 114 citations in OpenAlex.
- Conformational dynamics in specialized CProtein science : a publication of the Protein Society · 2025Article
- Structural characterization of PHOX2B and its DNA interaction shed light on the molecular basis of the +7Ala variant pathogenicity in CCHS.Chemical science · 2024Article
- Electrostatic complementarity at the interface drives transient protein-protein interactions.Scientific reports · 2023Article
- DNA binding induces aProceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Connector Domain of Vesicular Stomatitis Virus Large Protein Interacts with the Viral Phosphoprotein.Journal of virology · 2020Article
- Identification and characterization of a factor Va-binding site on human prothrombin fragment 2.Scientific reports · 2019Article
- Structural analyses reveal the mechanism of inhibition of influenza virus NS1 by two antiviral compounds.The Journal of biological chemistry · 2018Article
- The zinc fingers of YY1 bind single-stranded RNA with low sequence specificity.Nucleic acids research · 2016Article
- Structural Basis for a Novel Interaction between the NS1 Protein Derived from the 1918 Influenza Virus and RIG-I.Structure (London, England : 1993) · 2015Article
- Thermodynamic Switch in Binding of Adhesion/Growth Regulatory Human Galectin-3 to Tumor-Associated TF Antigen (CD176) and MUC1 Glycopeptides.Biochemistry · 2015Article
- Structural and functional studies of Stf76 from the Sulfolobus islandicus plasmid-virus pSSVx: a novel peculiar member of the winged helix-turn-helix transcription factor family.Nucleic acids research · 2014Article
- An introduction to biological NMR spectroscopy.Molecular & cellular proteomics : MCP · 2013Review
- Drug-induced conformational and dynamical changes of the S31N mutant of the influenza M2 proton channel investigated by solid-state NMR.Journal of the American Chemical Society · 2013Article
- Exploring the reactivity of flavonoid compounds with metal-associated amyloid-β species.Dalton transactions (Cambridge, England : 2003) · 2012Article
- Development of bifunctional stilbene derivatives for targeting and modulating metal-amyloid-β species.Inorganic chemistry · 2011Article
- Purification of proteins containing zinc finger domains using immobilized metal ion affinity chromatography.Protein expression and purification · 2011Article
- Solution structure and backbone dynamics of the DNA-binding domain of FOXP1: insight into its domain swapping and DNA binding.Protein science : a publication of the Protein Society · 2011Article
- Mechanism for pH-dependent gene regulation by amino-terminus-mediated homooligomerization of Bacillus subtilis anti-trp RNA-binding attenuation protein.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Structural determination of biomolecular interfaces by nuclear magnetic resonance of proteins with reduced proton density.Journal of biomolecular NMR · 2010Article
- Solution structure and backbone dynamics of streptopain: insight into diverse substrate specificity.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
We report the NMR resonance assignments for a macromolecular protein/DNA complex containing the three amino-terminal zinc fingers (92 amino acid residues) of Xenopus laevis TFIIIA (termed zf1-3) bound to the physiological DNA target (15 base pairs), and for the free DNA. Comparisons are made of the chemical shifts of protein backbone 1HN, 15N, 13C alpha and 13C beta and DNA base and sugar protons of the free and bound species. Chemical shift changes are analyzed in the context of the structures of the zf1-3/DNA complex to assess the utility of chemical shift change as a probe of molecular interfaces. Chemical shift perturbations that occur upon binding in the zf1-3/DNA complex do not correspond directly to the structural interface, but rather arise from a number of direct and indirect structural and dynamic effects.
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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.