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

INTERMEDIATE CLEAVAGE PEPTIDASE55 Modifies Enzyme Amino Termini and Alters Protein Stability in Arabidopsis Mitochondria.

Plant physiology - 1 Jun 2015

Huang Shaobai, Nelson Clark J, Li Lei, Taylor Nicolas L, Ströher Elke, Peteriet Jakob, Millar A Harvey

Abstract excerpt

Precursor proteins containing mitochondrial peptide signals are cleaved after import by a mitochondrial processing peptidase. In yeast (Saccharomyces cerevisiae) and human (Homo sapiens), intermediate cleavage peptidase55 (ICP55) plays a role in stabilizing mitochondrial proteins by the removal of single amino acids from mitochondrial processing peptidase-processed proteins. We have investigated the role of a...

Read the complete abstract on PubMed

Topics

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

Share to Metalloproteases
Share to Mitochondrial Proteins

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

Share to Mutagenesis, Insertional

Share to Plant Development

Share to Protein Stability

Share to Protein Transport

Share to Proteolysis

Share to Subcellular Fractions

Source

Open in PubMed Open full text

Identifiers

PMID: 25862457
DOI: 10.1104/pp.15.00300
PMCID: PMC4453787

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

INTERMEDIATE CLEAVAGE PEPTIDASE55 Modifies Enzyme Amino Termini and Alters Protein Stability in Arabidopsis Mitochondria.PMID 25862457Read ↗

Two novel targeting peptide degrading proteases, PrePs, in mitochondria and chloroplasts, so similar and still different.Semantic proximity Read ↗

Quantitative Profiling for Substrates of the Mitochondrial Presequence Processing Protease Reveals a Set of Nonsubstrate Proteins Increased upon Proteotoxic Stress.Semantic proximity Read ↗

Functional coupling of presequence processing and degradation in human mitochondria.Semantic proximity Read ↗

Mammalian mitochondrial intermediate peptidase: structure/function analysis of a new homologue from Schizophyllum commune and relationship to thimet oligopeptidases.Semantic proximity Read ↗

tRNA-Dependent Import of a Transit Sequence-Less Aminoacyl-tRNA Synthetase (LeuRS2) into the Mitochondria of Arabidopsis.Semantic proximity Read ↗

Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences.Semantic proximity Read ↗

m-AAA Complexes Are Not Crucial for the Survival of Arabidopsis Under Optimal Growth Conditions Despite Their Importance for Mitochondrial Translation.Semantic proximity Read ↗

The plant i-AAA protease controls the turnover of an essential mitochondrial protein import component.Semantic proximity Read ↗

ClpS1 is a conserved substrate selector for the chloroplast Clp protease system in Arabidopsis.Semantic proximity Read ↗

Targeting capacity and conservation of PreP homologues localization in mitochondria of different species.Semantic proximity Read ↗

Tripeptidyl peptidase II. An oligomeric protease complex from Arabidopsis.Semantic proximity Read ↗

Structure of the human aminopeptidase XPNPEP3 and comparison of its in vitro activity with Icp55 orthologs: Insights into diverse cellular processes.Semantic proximity Read ↗

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