ArticleFrontiers in cell and developmental biology2021
Membrane Interactions of the Peroxisomal Proteins PEX5 and PEX14.
Article in Frontiers in cell and developmental biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 31 citations in OpenAlex.
- VdPex30, a peroxisomal membrane protein, is involved in carbon metabolism, stress response, and pathogenicity ofMicrobiology spectrum · 2026Article
- Graphene oxide-microplastic hybrid showcase elicited discrepancy through intrinsic interaction mediated steatosis, and apoptosis in macrophages.Materials today. Bio · 2026Article
- Post-translational modifications of selective autophagy receptors: orchestrating cellular homeostasis, disease pathogenesis, and therapeutic opportunities.Cellular & molecular biology letters · 2026Review
- Evolutionary remodeling of a remnant GET pathway factor into PEX38, an essential peroxin.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- A cryo-electron microscopy structure of yeast Pex5 in complex with a cargo uncovers a novel binding interface.Journal of cell science · 2025Article
- Modular Nanoparticle Platform for Solution-Phase Optical Sensing of Protein-Protein Interactions.ACS applied optical materials · 2025Article
- Detection of a Novel Homozygous PEX5 Stop-Loss Variant Associated with Zellweger Syndrome in a Highly Endogamic Family.The application of clinical genetics · 2025Article
- Towards solving the mystery of peroxisomal matrix protein import.Trends in cell biology · 2024Review
- Modulation of peroxisomal import by the PEX13 SH3 domain and a proximal FxxxF binding motif.Nature communications · 2024Article
- Noncanonical and reversible cysteine ubiquitination prevents the overubiquitination of PEX5 at the peroxisomal membrane.PLoS biology · 2024Article
- Chilling stress response in tobacco seedlings: insights from transcriptome, proteome, and phosphoproteome analyses.Frontiers in plant science · 2024Article
- Article
- Key enzymes involved in the utilization of fatty acids byFrontiers in microbiology · 2023Review
- PEX5 translocation into and out of peroxisomes drives matrix protein import.Molecular cell · 2022Article
- Insights into the Structure and Function of the Pex1/Pex6 AAA-ATPase in Peroxisome Homeostasis.Cells · 2022Review
- Determinants of Peroxisome Membrane Dynamics.Frontiers in physiology · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human PEX5 and PEX14 are essential components of the peroxisomal translocon, which mediates import of cargo enzymes into peroxisomes. PEX5 is a soluble receptor for cargo enzymes comprised of an N-terminal intrinsically disordered domain (NTD) and a C-terminal tetratricopeptide (TPR) domain, which recognizes peroxisomal targeting signal 1 (PTS1) peptide motif in cargo proteins. The PEX5 NTD harbors multiple WF peptide motifs (WxxxF/Y or related motifs) that are recognized by a small globular domain in the NTD of the membrane-associated protein PEX14. How the PEX5 or PEX14 NTDs bind to the peroxisomal membrane and how the interaction between the two proteins is modulated at the membrane is unknown. Here, we characterize the membrane interactions of the PEX5 NTD and PEX14 NTD
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.