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

Evaluation of the stability of an SR398/GroES chaperonin complex.

Journal of biochemistry - 1 May 2014

Ishino So, Kawata Yasushi, Ikegami Takahisa, Matsuzaki Katsumi, Hoshino Masaru

Abstract excerpt

The stability of an SR398/GroES chaperonin complex was examined. As was expected, based on the finding of previous studies, the SR398/GroES complex was extremely stable in the presence of an excess amount of free adenosine 5'-[γ-thio]triphosphate (ATPγS) or adenosine 5'-(β,γ-imido)triphosphate (AMPPNP). However, the complex was not stable in the absence of nucleotides. These results indicate that ATPγS and AMPPNP...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Chaperonin 10
Share to Chaperonin 60

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Green Fluorescent Proteins

Share to Molecular Chaperones

Share to Multiprotein Complexes

Share to Nucleotides

Share to Protein Stability

Source

Identifiers

PMID: 24563543
DOI: 10.1093/jb/mvu009

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

Evaluation of the stability of an SR398/GroES chaperonin complex.PMID 24563543Read ↗

Effective ATPase activity and moderate chaperonin-cochaperonin interaction are important for the functional single-ring chaperonin system.Semantic proximity Read ↗

Stimulating the substrate folding activity of a single ring GroEL variant by modulating the cochaperonin GroES.Semantic proximity Read ↗

Characterisation of a GroEL single-ring mutant that supports growth of Escherichia coli and has GroES-dependent ATPase activity.Semantic proximity Read ↗

Creating the Functional Single-Ring GroEL-GroES Chaperonin Systems via Modulating GroEL-GroES Interaction.Semantic proximity Read ↗

GroEL Ring Separation and Exchange in the Chaperonin Reaction.Semantic proximity Read ↗

Triggering protein folding within the GroEL-GroES complex.Semantic proximity Read ↗

The GroEL/GroES cis cavity as a passive anti-aggregation device.Semantic proximity Read ↗

Mapping pathways of allosteric communication in GroEL by analysis of correlated mutations.Semantic proximity Read ↗

TEM and STEM-EDS evaluation of metal nanoparticle encapsulation in GroEL/GroES complexes according to the reaction mechanism of chaperonin.Semantic proximity Read ↗

A kinetic analysis of the nucleotide-induced allosteric transitions in a single-ring mutant of GroEL.Semantic proximity Read ↗

Differential conformational modulations of MreB folding upon interactions with GroEL/ES and TRiC chaperonin components.Semantic proximity Read ↗

Inter-ring communication is dispensable in the reaction cycle of group II chaperonins.Semantic proximity Read ↗

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