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

Crystal structure analysis, overexpression and refolding behaviour of a DING protein with single mutation.

Journal of synchrotron radiation - 1 Nov 2013

Gai Zuoqi, Nakamura Akiyoshi, Tanaka Yoshikazu, Hirano Nagisa, Tanaka Isao, Yao Min

Abstract excerpt

After crystallization of a certain protein-RNA complex, well diffracting crystals were obtained. However, the asymmetric unit of the crystal was too small to locate any components. Mass spectrometry and X-ray crystal structure analysis showed that it was a member of the DING protein family (HPBP). Surprisingly, the structure of HPBP reported previously was also determined accidentally as a contaminant, suggesting...

Read the complete abstract on PubMed

Topics

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

Share to Crystallography, X-Ray
Share to Electrophoresis, Polyacrylamide Gel

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli Proteins

Share to Mass Spectrometry

Share to Models, Molecular

Share to Mutation

Share to Protein Folding

Source

Open in PubMed Open full text

Identifiers

PMID: 24121327
DOI: 10.1107/S0909049513020694
PMCID: PMC3795543

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

Crystal structure analysis, overexpression and refolding behaviour of a DING protein with single mutation.PMID 24121327Read ↗

BIOMEDICINE: One Misfolded Protein Allows Others to Sneak By.Semantic proximity Read ↗

YrhB is a highly stable small protein with unique chaperone-like activity in Escherichia coli BL21(DE3).Semantic proximity Read ↗

The biomedical potential of tardigrade proteins: A reviewSemantic proximity Read ↗

Protein misfolding and disease: from the test tube to the organismSemantic proximity Read ↗

Protein misfolding in endoplasmic reticulum stress with applications to renal diseases.Semantic proximity Read ↗

Current updates on computer aided protein modeling and designing.Semantic proximity Read ↗

The prefoldin complex stabilizes the von Hippel-Lindau protein against aggregation and degradation.Semantic proximity Read ↗

Human mitochondrial NDUFS3 protein bearing Leigh syndrome mutation is more prone to aggregation than its wild-type.Semantic proximity Read ↗

Homo-oligomer models prediction, functional characterization, and Ab initio docking analysis of hypothetical protein HP33 from Vibrio harveyi strainSemantic proximity Read ↗

Emergence of de novo proteins from 'dark genomic matter' by 'grow slow and moult'.Semantic proximity Read ↗

Structure, Folding and Stability of Nucleoside Diphosphate Kinases.Semantic proximity Read ↗

A general method for rapid and nondenaturing purification of RNAs.Semantic proximity Read ↗

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