Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Thermodynamic characterization of the interaction between the human Y-box binding protein YB-1 and nucleic acids.

Molecular bioSystems - 1 Sept 2015

Tanabe Yumiko, Nagatoishi Satoru, Tsumoto Kouhei

Abstract excerpt

Y-box binding protein 1 (YB-1) binds to both RNA and DNA to control transcription and translation for the regulation of various cellular systems. YB-1 is overexpressed in some cancer cells and is a potential target for treatment of cancer. Herein, we describe isothermal titration calorimetry analyses of the interaction between a number of recombinant YB-1 domains and nucleic acids to identify the RNA and DNA...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to DNA, Single-Stranded
Share to Nucleic Acids
Share to Protein Interaction Domains and Motifs

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Structure, Secondary

Share to Temperature

Share to Thermodynamics

Share to Y-Box-Binding Protein 1

Source

Identifiers

PMID: 26126888
DOI: 10.1039/c5mb00184f

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Thermodynamic characterization of the interaction between the human Y-box binding protein YB-1 and nucleic acids.PMID 26126888Read ↗

Y box-binding protein-1 binds preferentially to single-stranded nucleic acids and exhibits 3'-->5' exonuclease activity.Semantic proximity Read ↗

Large favorable enthalpy changes drive specific RNA recognition by RNA recognition motif proteins.Semantic proximity Read ↗

DNA plasticity is a key determinant of the energetics of binding of Jun-Fos heterodimeric transcription factor to genetic variants of TGACGTCA motif.Semantic proximity Read ↗

Single nucleotide variants of the TGACTCA motif modulate energetics and orientation of binding of the Jun-Fos heterodimeric transcription factor.Semantic proximity Read ↗

Label-Free Determination of the Dissociation Constant of Small Molecule-Aptamer Interaction by Isothermal Titration Calorimetry.Semantic proximity Read ↗

YB-1 as a cell cycle-regulated transcription factor facilitating cyclin A and cyclin B1 gene expression.Semantic proximity Read ↗

Acquisition of double-stranded DNA-binding ability in a hybrid protein between Escherichia coli CspA and the cold shock domain of human YB-1.Semantic proximity Read ↗

Two distinct DNA sequences recognized by transcription factors represent enthalpy and entropy optimaSemantic proximity Read ↗

Stability and kinetics of c-MYC promoter G-quadruplexes studied by single-molecule manipulation.Semantic proximity Read ↗

[Thermal denaturation of eukaryotic class 1 translation termination factor eRF1. Relationship between stability of the eRF1 molecule and alteration of functional activity of its mutants].Semantic proximity Read ↗

T-rich DNA single strands bind to a preformed site on the bacterial cold shock protein Bs-CspB.Semantic proximity Read ↗

Intermolecular interactions between cysteine and aromatic amino acids with phenyl moiety in the DNA-binding domain of heat shock factor 1 regulate thermal stress-induced trimerizationSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.