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

Intramolecular disulfide bond of Tim22 protein maintains integrity of the TIM22 complex in the mitochondrial inner membrane.

The Journal of biological chemistry - 21 Feb 2014

Okamoto Hiroaki, Miyagawa Akiko, Shiota Takuya, Tamura Yasushi, Endo Toshiya

Abstract excerpt

Mitochondrial proteins require protein machineries called translocators in the outer and inner membranes for import into and sorting to their destination submitochondrial compartments. Among them, the TIM22 complex mediates insertion of polytopic membrane proteins into the inner membrane, and Tim22 constitutes its central insertion channel. Here we report that the conserved Cys residues of Tim22 form an...

Read the complete abstract on PubMed

Topics

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

Share to Antiporters
Share to Disulfides

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Mitochondrial Membrane Transport Proteins

Share to Mitochondrial Membranes

Share to Mitochondrial Precursor Protein Import Complex Proteins

Share to Multiprotein Complexes

Share to Protein Stability

Share to Proteolysis

Source

Open in PubMed Open full text

Identifiers

PMID: 24385427
DOI: 10.1074/jbc.M113.543264
PMCID: PMC3931045

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Intramolecular disulfide bond of Tim22 protein maintains integrity of the TIM22 complex in the mitochondrial inner membrane.PMID 24385427Read ↗

Mitochondrial protein import: Mia40 facilitates Tim22 translocation into the inner membrane of mitochondria.Semantic proximity Read ↗

Role of Tim17 Transmembrane Regions in Regulating the Architecture of Presequence Translocase and Mitochondrial DNA Stability.Semantic proximity Read ↗

The Tim54p-Tim22p complex mediates insertion of proteins into the mitochondrial inner membrane.Semantic proximity Read ↗

Biogenesis of Tim23 and Tim17, integral components of the TIM machinery for matrix‐targeted preproteinsSemantic proximity Read ↗

InVivo Dissection of the Intrinsically Disordered Receptor Domain of Tim23.Semantic proximity Read ↗

Juxtaposition of the two distal CX3C motifs via intrachain disulfide bonding is essential for the folding of Tim10.Semantic proximity Read ↗

The channel-forming Sym1 protein is transported by the TIM23 complex in a presequence-independent manner.Semantic proximity Read ↗

Mitochondrial Tim9 protects Tim10 from degradation by the protease Yme1.Semantic proximity Read ↗

Pam17 and Tim44 act sequentially in protein import into the mitochondrial matrix.Semantic proximity Read ↗

The divergent N-terminal domain of Tim17 is critical for its assembly in the TIM complex in Trypanosoma brucei.Semantic proximity Read ↗

Biogenesis of Tim Proteins of the Mitochondrial Carrier Import Pathway: Differential Targeting Mechanisms and Crossing Over with the Main Import PathwaySemantic proximity Read ↗

The J-related segment of tim44 is essential for cell viability: a mutant Tim44 remains in the mitochondrial import site, but inefficiently recruits mtHsp70 and impairs protein translocation.Semantic proximity Read ↗

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