Affinage

PEX14

Peroxisomal membrane protein PEX14 · UniProt O75381

Length
377 aa
Mass
41.2 kDa
Annotated
2026-06-10
45 papers in source corpus 22 papers cited in narrative 22 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PEX14 is an intrinsic peroxisomal membrane protein that functions as the central docking platform of the matrix protein import machinery, required for import of both PTS1- and PTS2-targeted proteins (PMID:9009266, PMID:15146459). It adopts an Nin-Cout topology, with the conserved three-helical N-terminal domain (NTD) and the C-terminus exposed to the cytosol (PMID:30414318, PMID:19197237). The NTD is the principal receptor-binding surface: it engages the cycling import receptor PEX5 with low-nanomolar affinity through PEX5's reiterated di-aromatic WxxxF/Y pentapeptide motifs and a kinetically distinct LVXEF motif, both of which dock as amphipathic helices via conserved aromatic anchors (PMID:10026185, PMID:11438541, PMID:24235149). The same NTD surface binds the PEX19 F/YFxxxF motif competitively, coupling receptor docking to PEX14 membrane targeting (PMID:19197237). Beyond receptor capture, PEX14 mediates cargo release, disrupting the PEX5-catalase complex to participate in matrix protein delivery (PMID:21976670), and organizes the translocation complex by binding PEX13 through both an SH3-domain site and a second intraperoxisomal site (PMID:15798189). The receptor cycle is regulated downstream by AAA+ ATPase-driven, ubiquitination-dependent topological remodeling of the PEX14 N-terminus controlled by PEX6/PEX26 (PMID:41581879), while the cytosolic C-terminal domain undergoes phase separation into condensates that recruit PEX5-cargo complexes to drive import (PMID:40555785). PEX14 carries additional, separable functions: its NTD binds β-tubulin to anchor peroxisomes to microtubules for motility, a contact competitively displaced by PEX5 to couple import state to organelle movement (PMID:21525035, PMID:33484719); phosphorylation at Ser232 upon H2O2 stress selectively blocks catalase import to redistribute catalase to the cytosol (PMID:32831175); and it serves as the membrane docking site for the autophagy receptor optineurin, enabling pexophagy (PMID:41071103, PMID:17921697). Loss-of-function mutation (p.Q185X) causes Zellweger syndrome, defining PEX14 as a peroxisome biogenesis disorder gene (PMID:15146459).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 1997 High

    Established that Pex14 is a peroxisomal membrane protein essential for matrix protein import, and that its abundance relative to other biogenesis components must be tightly controlled.

    Evidence Gene disruption, complementation, fractionation and EM in H. polymorpha

    PMID:9009266

    Open questions at the time
    • Molecular partners and mechanism of import not defined
    • Topology unknown
  2. 1999 High

    Identified PEX14 as a high-affinity PEX5 receptor docking partner, answering how the cycling receptor engages the membrane.

    Evidence SPR and in vitro binding with recombinant human PEX5 and PEX14-(1-78)

    PMID:10026185

    Open questions at the time
    • Structural basis of binding not resolved
    • Stoichiometry not determined
  3. 2001 High

    Defined the molecular determinant of docking, showing seven di-aromatic pentapeptide repeats in PEX5 each bind the PEX14 NTD via conserved aromatic anchors.

    Evidence Two-hybrid, mutagenesis, and SPR in mammalian/in vitro systems

    PMID:11438541

    Open questions at the time
    • Atomic structure of the complex still lacking
    • Why seven repeats unclear
  4. 2005 High

    Showed PEX14 organizes the translocon by binding PEX13 through two distinct sites, with PEX5 contributing, defining how the docking complex is assembled and how PTS1 vs PTS2 import depend on these contacts.

    Evidence Combinatorial mutagenesis, co-purification, and oleic-acid growth assays in yeast

    PMID:15798189

    Open questions at the time
    • Quantitative complex architecture not resolved
    • Dynamics during the import cycle unknown
  5. 2009 High

    Resolved the three-helical PEX14 NTD fold and revealed competitive, oppositely oriented binding of PEX5 and PEX19 ligand helices, linking receptor docking to PEX14 membrane targeting; SAXS established a 1:6 PEX5:PEX14 stoichiometry.

    Evidence NMR structure, mutagenesis, in vivo localization; SAXS solution model

    PMID:19197237 PMID:19584060

    Open questions at the time
    • High-resolution structure of the full complex absent
    • Functional meaning of 1:6 ratio in vivo unclear
  6. 2011 High

    Uncovered two distinct PEX14 functions beyond docking: facilitating cargo release by disrupting the PEX5-catalase complex, and anchoring peroxisomes to microtubules via direct tubulin binding through the NTD.

    Evidence In vitro reconstitution and domain deletion; affinity purification, in vitro binding, and live-cell motility assays in PEX14-deficient cells

    PMID:21525035 PMID:21976670

    Open questions at the time
    • Mechanism coupling docking surface to two ligand classes not fully resolved
    • In vivo balance between motility and import unknown
  7. 2013 High

    Identified the LVXEF motif as a second class of PEX5 docking sequence with faster dissociation kinetics, refining the model of how receptor engagement and release are kinetically tuned.

    Evidence Peptide library screen, NMR structure, SPR kinetics, and in vivo import assays

    PMID:24235149

    Open questions at the time
    • Functional division of labor between WxxxF/Y and LVXEF motifs in vivo unclear
  8. 2018 High

    Defined PEX14 as an Nin-Cout intrinsic membrane protein, fixing the topological framework for interpreting which domain faces the cytosol versus lumen.

    Evidence Protease-protection assays in proteoliposomes and native rat liver peroxisomes

    PMID:30414318

    Open questions at the time
    • Membrane integration mechanism not addressed
    • Topological dynamics during import not tested here
  9. 2020 High

    Showed PEX14 is a regulatory node coupling oxidative stress to selective import: Ser232 phosphorylation specifically suppresses catalase import to redistribute catalase to the cytosol and confer H2O2 resistance.

    Evidence Phosphoproteomics, S232D phosphomimetic mutant, in vivo and in vitro import/binding assays

    PMID:32831175

    Open questions at the time
    • Kinase responsible for Ser232 phosphorylation not identified
    • Physiological signaling context incompletely mapped
  10. 2021 High

    Mapped the tubulin-binding interface to two β-tubulin C-terminal motifs and demonstrated PEX5 competes for this site, providing a mechanistic switch linking import state to organelle motility; also showed PEX5 docking is preserved at the membrane.

    Evidence NMR mapping, ITC, and competition binding with bicelles/nanodiscs

    PMID:33484719 PMID:33937250

    Open questions at the time
    • In vivo regulation of the motility/import switch not established
    • Membrane association role of NTD surface unresolved
  11. 2025 High

    Revealed two new layers of import organization: phase separation of the PEX14 C-terminal domain into condensates that recruit PEX5-cargo, and PEX14 acting as the optineurin docking site for pexophagy, unifying biogenesis and turnover at one protein.

    Evidence In vitro phase separation, tetramer structural analysis, and domain swaps; proximity labeling, Co-IP, domain mapping, and LC3 colocalization

    PMID:40555785 PMID:41071103

    Open questions at the time
    • In vivo relevance of condensates not fully established
    • Optineurin interaction is a single-lab finding without reciprocal cross-validation
    • Trigger for PEX14-mediated pexophagy unclear
  12. 2026 Medium

    Demonstrated that the PEX14 N-terminus undergoes ATP- and ubiquitination-dependent topological reorientation driven by PEX6/PEX26, connecting receptor recycling to dynamic remodeling of the docking platform.

    Evidence Protease protection, immunofluorescence, AAA+ ATPase and ubiquitin pathway inhibition

    PMID:41581879

    Open questions at the time
    • Direct demonstration of N-terminal movement at single-molecule level lacking
    • Functional consequence of reorientation for import cycle not quantified
    • Single-lab study

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the docking, cargo-release, condensate, motility, and pexophagy functions of PEX14 are temporally and spatially coordinated within a single import/turnover cycle remains unresolved.
  • No integrated structural model of the assembled translocon in the membrane
  • Kinase and upstream signals controlling Ser232 phosphorylation unknown
  • Interplay between condensate formation and topological remodeling untested

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 4 GO:0008092 cytoskeletal protein binding 2 GO:0038024 cargo receptor activity 2
Localization
GO:0005777 peroxisome 3
Pathway
R-HSA-1852241 Organelle biogenesis and maintenance 2 R-HSA-9609507 Protein localization 2 R-HSA-9612973 Autophagy 2
Partners
OPTNPEX13PEX19PEX26PEX5PEX6TUBB
Complex memberships
peroxisomal docking/translocation complex

Evidence

Reading pass · 22 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1999 Human PEX5 binds the N-terminal fragment of PEX14-(1-78) with very high affinity in the low nanomolar range, as measured by surface plasmon resonance. PEX5 possesses multiple binding sites for PEX14 distributed throughout its N-terminal half, and a pentapeptide motif reiterated seven times in PEX5 was identified as the determinant for interaction with PEX14. Surface plasmon resonance, in vitro binding assay with recombinant proteins, sizing chromatography The Journal of biological chemistry High 10026185
1997 H. polymorpha Pex14p is a peroxisomal membrane protein essential for import of matrix proteins; loss of Pex14p results in peroxisomal membrane remnants containing only small amounts of matrix proteins (AO, catalase, DHAS), with the bulk mislocalized to the cytosol. Overproduction of Pex14p causes a peroxisome-deficient phenotype with numerous small vesicles lacking matrix proteins, indicating stoichiometry of Pex14p relative to other biogenesis components is critical. Genetic complementation, biochemical fractionation, electron microscopy, gene disruption The EMBO journal High 9009266
2001 The seven di-aromatic pentapeptide repeat motifs (WX(E/D/Q/A/S)(E/D/Q)(F/Y)) of human PEX5 each independently bind to the same site in the N-terminus of PEX14 with equilibrium dissociation constants in the low nanomolar range. Mutational analysis showed the conserved aromatic amino acids at positions 1 and 5 of the motif are essential for high affinity binding, proposed to form hydrophobic anchors via an amphipathic alpha-helix. Two-hybrid analysis in mammalian cells, in vitro binding assays, mutational analysis, surface plasmon resonance The Journal of biological chemistry High 11438541
2009 The N-terminal domain of Pex14 (Pex14-N) adopts a three-helical fold. Both PEX5 and PEX19 ligand helices bind competitively to the same surface of Pex14-N, but with opposite directionality. The Pex5 WxxxF/Y motif and a newly identified F/YFxxxF sequence in Pex19 mediate this recognition through conserved aromatic side chains. Mutations of Pex14 residues in the Pex5/Pex19 binding region disrupt binding in vitro and impair peroxisomal membrane localization of Pex14 in vivo. NMR structure determination, in vitro binding assays, site-directed mutagenesis, in vivo localization The EMBO journal High 19197237
2011 Human PEX14 interacts directly with tubulin, and this binding is mediated by the conserved N-terminal domain of PEX14. PEX14-deficient cells lose the ability of peroxisomal remnants to move along microtubules, establishing PEX14 as the membrane anchor linking peroxisomes to microtubules for motility. Affinity purification of native PEX14 complexes, mass spectrometry, size-exclusion chromatography, in vitro binding, live cell imaging, PEX14-deficient cell analysis Journal of cell science High 21525035
2011 PEX5 binds monomeric catalase and potently inhibits its tetramerization; no such complex was detected with tetrameric catalase. The N-terminal domain of PEX14 disrupts the PEX5-catalase interaction, with one or two of the seven PEX14-binding diaromatic motifs of PEX5 involved, indicating PEX14 participates in the cargo protein release step. In vitro binding assays, biochemical reconstitution, domain deletion analysis The Journal of biological chemistry High 21976670
2013 A novel PEX5-PEX14 interaction site in PEX5 with the sequence LVAEF (consensus LVXEF) was identified. NMR structure of the Pex5-(57-71)/Pex14-NTD complex showed this motif binds in a similar alpha-helical orientation as the WxxxF/Y motif but with the tryptophan pocket occupied by leucine. The LVXEF motif has 33-fold faster dissociation from PEX14 than WxxxF/Y motifs, and alanine substitution of LVAEF strongly impairs peroxisomal matrix protein import in vivo. Peptide library ligand blot screening, NMR structure determination, surface plasmon resonance, mutagenesis, in vivo import assays The Journal of biological chemistry High 24235149
2020 Pex14 is phosphorylated at Ser232 in response to H2O2-induced oxidative stress in mammalian cells. This phosphorylation suppresses peroxisomal import of catalase specifically (but not canonical PTS1 proteins) by selectively impairing the interaction of catalase with the Pex14-Pex5 complex in vitro. A phosphomimetic Pex14-S232D mutant elevates cytosolic catalase and confers higher cell resistance to H2O2. Phosphoproteomics, site-directed mutagenesis (S232D phosphomimetic), in vivo import assays, in vitro binding assays eLife High 32831175
2007 Hansenula polymorpha Pex14 has a unique dual function: it is required both for matrix protein import into peroxisomes and for selective autophagic degradation of peroxisomes (pexophagy). Other components of the peroxisomal translocon (Pex2, Pex10, Pex12, Pex13, Pex17) are not required for pexophagy, making Pex14 the sole peroxisomal translocon component with this dual function. Genetic epistasis analysis with multiple pex deletion mutants, pexophagy assays Autophagy Medium 17921697
2005 Pex13 binds Pex14 via two sites: its SH3 domain and a novel intraperoxisomal site. Pex5 also contributes to the association of Pex13 with Pex14. Combining mutations in the novel Pex14-interaction site of Pex13 with a non-Pex13-interacting Pex5(W204A) mutant severely compromised PTS1-dependent import; additionally blocking the SH3-Pex14 interaction completely abrogated PTS2-dependent import and dissociated Pex13 from the docking complex. In vitro binding assays, genetic epistasis with combined mutants, co-purification, growth assays on oleic acid Molecular and cellular biology High 15798189
2000 In H. polymorpha Δpex14 cells, overproduction of the PTS1 receptor Pex5p leads to enhanced import of PTS1 proteins AO and DHAS but not PTS2 protein amine oxidase, and not catalase. Pex5p localizes to the cytosol and outer peroxisomal membrane surface in Δpex14 cells, indicating that Pex5p can bind the peroxisomal membrane and mediate partial import of certain PTS1 proteins in the absence of Pex14p. Genetic overexpression in pex14 null mutant, subcellular fractionation, immunofluorescence The Journal of biological chemistry Medium 10777551
2018 PEX14 is a bona fide intrinsic membrane protein with Nin-Cout topology (N-terminus facing the peroxisomal lumen, C-terminus facing the cytosol), as determined in proteoliposomes and purified rat liver peroxisomes. Protease-protection assays on proteoliposomes and native peroxisomes, mass spectrometry, Edman degradation, western blotting with domain-specific antibodies The FEBS journal High 30414318
2021 The PEX14 N-terminal domain (NTD) binds to microtubular filaments in vitro with nanomolar affinity, interacting with two motifs in the C-terminal region of human β-tubulin. PEX5 competes with β-tubulin for binding to PEX14-NTD, such that PEX5 binding to PEX14 can prevent peroxisome anchoring to microtubules, providing a mechanistic link between peroxisomal protein import and motility. In vitro binding assays, NMR spectroscopy, competition binding experiments, dissociation constant measurement Journal of molecular biology High 33484719
2021 The PEX14 NTD weakly interacts with membrane-mimicking bicelles via a surface that partially overlaps with the WxxxF/Y binding site. The PEX5-PEX14 NTD interaction is largely unaffected by the presence of membranes, with reduced binding enthalpy compensated by reduced entropy loss, indicating docking of PEX5 to PEX14 at the membrane does not reduce overall binding affinity. NMR spectroscopy with bicelles and nanodiscs, isothermal titration calorimetry (ITC) Frontiers in cell and developmental biology Medium 33937250
2017 Small molecules disrupting the Trypanosoma PEX14-PEX5 protein-protein interaction cause mislocalization of glycosomal enzymes, metabolic catastrophe, and parasite death. High-resolution X-ray crystal structures of inhibitors bound to TbPEX14 were obtained, revealing the structural basis for blocking PEX14-PEX5 interaction as a drug target. X-ray crystallography of inhibitor-PEX14 complexes, NMR binding studies, cell-based trypanocidal assays Science High 28360328
2003 T. brucei PEX14 is associated with glycosomes and its N-terminal part binds specifically to TbPEX5. RNAi-mediated depletion of TbPEX14 causes mislocalization of glycosomal proteins (PTS1, PTS2, and internal I-PTS-containing) to the cytosol and is essential for survival of both bloodstream-form and procyclic trypanosomes. Subcellular fractionation, in vitro binding with recombinant proteins, RNA interference, immunofluorescence European journal of biochemistry High 12709066
2004 Human PEX14 is required for both PTS1- and PTS2-dependent peroxisomal matrix protein import in human cells. Loss-of-function (nonsense mutation p.Q185X) causes Zellweger syndrome; transfection with wild-type PEX14 rescued import in patient fibroblasts, establishing PEX14 as the 13th complementation group gene for peroxisome biogenesis disorders. Genetic complementation in patient fibroblasts, immunocytochemistry, mutational analysis Human mutation Medium 15146459
2009 Solution structure of the human Pex5-Pex14-PTS1 complex determined by small angle X-ray scattering reveals a 1:6 stoichiometry for the Pex5-Pex14 complex. The N-terminus of Pex5 remains extended in the presence of cargo and Pex14, with Pex14 significantly intermingled with the Pex5 moiety. Small angle X-ray scattering (SAXS), static light scattering, titration studies The Journal of biological chemistry Medium 19584060
2025 The C-terminal domain (CTD) of human PEX14 undergoes phase separation in vitro, forming condensates that recruit PEX5-cargo complexes carrying PTS1 or PTS2 signals. hPEX14 forms tetramers, and hPEX14 and hPEX13 form immiscible condensates. Replacing hPEX14 CTD with other phase-separating polypeptides partially restores peroxisomal import; electrostatic interactions and the specific CTD sequence are essential for import. In vitro phase separation assays, structural analysis of PEX14 tetramer, domain replacement experiments, cargo recruitment assays Nature structural & molecular biology High 40555785
2025 PEX14 acts as a docking site for the autophagy receptor optineurin (OPTN) on the peroxisomal membrane, enabling OPTN-mediated pexophagy. PEX14 and OPTN interact through their coiled-coil and ubiquitin-binding domains, respectively. PEX14-OPTN complexes colocalize with LC3, and bafilomycin A1 suppresses OPTN-mediated peroxisome degradation. Proximity labeling, co-immunoprecipitation, domain mapping, fluorescence microscopy, autophagy inhibitor treatment The Journal of cell biology Medium 41071103
2026 The N-terminal domain of Pex14 undergoes ATP- and ubiquitination-dependent topological remodeling regulated by the AAA+ ATPase Pex6 and its membrane-recruiting partner Pex26. Under normal conditions, the Pex14 N-terminus is oriented toward the peroxisomal lumen; deficiency of Pex6 or Pex26, or pharmacological inhibition of AAA+ ATPases, causes the N-terminus to become exposed to the cytoplasm. Inhibition of ubiquitin activation blocks this reorientation, likely by preventing Pex5 ubiquitination and extraction. Immunofluorescence microscopy, protease protection assays, pharmacological inhibition of AAA+ ATPases, ubiquitin pathway inhibition The Journal of biological chemistry Medium 41581879
2005 In procyclic T. brucei, RNAi knockdown of PEX14 causes mislocalization of glycosomal enzymes and cell death that is triggered by glucose or fructose, but not in the absence of sugars. Double RNAi of PEX14 and hexokinase rescued cells from glucose toxicity even though glycosomal proteins remained mislocalized, establishing that the toxicity of PEX14 depletion in glucose is due to unregulated cytosolic glycolysis. RNA interference (single and double knockdown), genetic epistasis, cell viability assays with different carbon sources The Journal of biological chemistry Medium 15637070

Source papers

Stage 0 corpus · 45 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1999 Recombinant human peroxisomal targeting signal receptor PEX5. Structural basis for interaction of PEX5 with PEX14. The Journal of biological chemistry 154 10026185
1997 The Hansenula polymorpha PEX14 gene encodes a novel peroxisomal membrane protein essential for peroxisome biogenesis. The EMBO journal 116 9009266
2001 The di-aromatic pentapeptide repeats of the human peroxisome import receptor PEX5 are separate high affinity binding sites for the peroxisomal membrane protein PEX14. The Journal of biological chemistry 101 11438541
2011 PEX5 protein binds monomeric catalase blocking its tetramerization and releases it upon binding the N-terminal domain of PEX14. The Journal of biological chemistry 74 21976670
2009 Structural basis for competitive interactions of Pex14 with the import receptors Pex5 and Pex19. The EMBO journal 73 19197237
2000 Overproduction of Pex5p stimulates import of alcohol oxidase and dihydroxyacetone synthase in a Hansenula polymorpha Pex14 null mutant. The Journal of biological chemistry 73 10777551
2011 PEX14 is required for microtubule-based peroxisome motility in human cells. Journal of cell science 64 21525035
2020 The peroxisome counteracts oxidative stresses by suppressing catalase import via Pex14 phosphorylation. eLife 59 32831175
2004 Identification of a new complementation group of the peroxisome biogenesis disorders and PEX14 as the mutated gene. Human mutation 59 15146459
2007 Pex14 is the sole component of the peroxisomal translocon that is required for pexophagy. Autophagy 57 17921697
2013 The biogenesis protein PEX14 is an optimal marker for the identification and localization of peroxisomes in different cell types, tissues, and species in morphological studies. Histochemistry and cell biology 54 23959168
2013 A novel Pex14 protein-interacting site of human Pex5 is critical for matrix protein import into peroxisomes. The Journal of biological chemistry 50 24235149
2017 Inhibitors of PEX14 disrupt protein import into glycosomes and kill Trypanosoma parasites. Science (New York, N.Y.) 49 28360328
2003 Characterization of Trypanosoma brucei PEX14 and its role in the import of glycosomal matrix proteins. European journal of biochemistry 48 12709066
2005 Probing the role of compartmentation of glycolysis in procyclic form Trypanosoma brucei: RNA interference studies of PEX14, hexokinase, and phosphofructokinase. The Journal of biological chemistry 45 15637070
2007 The peroxin PEX14 of Neurospora crassa is essential for the biogenesis of both glyoxysomes and Woronin bodies. Traffic (Copenhagen, Denmark) 42 17461798
2005 Identification of a novel, intraperoxisomal pex14-binding site in pex13: association of pex13 with the docking complex is essential for peroxisomal matrix protein import. Molecular and cellular biology 41 15798189
2018 Membrane topologies of PEX13 and PEX14 provide new insights on the mechanism of protein import into peroxisomes. The FEBS journal 38 30414318
2016 Pex14/17, a filamentous fungus-specific peroxin, is required for the import of peroxisomal matrix proteins and full virulence of Magnaporthe oryzae. Molecular plant pathology 36 27571711
2010 Penicillium chrysogenum Pex14/17p--a novel component of the peroxisomal membrane that is important for penicillin production. The FEBS journal 35 20597979
2009 Solution structure of human Pex5.Pex14.PTS1 protein complexes obtained by small angle X-ray scattering. The Journal of biological chemistry 35 19584060
2002 Peroxisomal targeting protein 14 (PEX14) from Leishmania donovani. Molecular, biochemical, and immunocytochemical characterization. Molecular and biochemical parasitology 33 12387850
2019 Pex13 and Pex14, the key components of the peroxisomal docking complex, are required for peroxisome formation, host infection and pathogenicity-related morphogenesis in Magnaporthe oryzae. Virulence 30 30905264
2021 Membrane Interactions of the Peroxisomal Proteins PEX5 and PEX14. Frontiers in cell and developmental biology 23 33937250
2008 Identification of a novel PEX14 mutation in Zellweger syndrome. Journal of medical genetics 21 18285423
2023 Peroxin Pex14/17 Is Required for Trap Formation, and Plays Pleiotropic Roles in Mycelial Development, Stress Response, and Secondary Metabolism in Arthrobotrys oligospora. mSphere 19 36786584
2021 Competitive Microtubule Binding of PEX14 Coordinates Peroxisomal Protein Import and Motility. Journal of molecular biology 13 33484719
2020 Structure-Activity Relationship in Pyrazolo[4,3-c]pyridines, First Inhibitors of PEX14-PEX5 Protein-Protein Interaction with Trypanocidal Activity. Journal of medicinal chemistry 13 31860309
2023 Autosomal dominant Zellweger spectrum disorder caused by de novo variants in PEX14 gene. Genetics in medicine : official journal of the American College of Medical Genetics 7 37493040
2022 Distinct conformational and energetic features define the specific recognition of (di)aromatic peptide motifs by PEX14. Biological chemistry 6 36437542
2024 Peroxisome biogenesis factor PEX14 is crucial for survival and fecundity of female brown planthopper, Nilaparvata lugens (Stål). Insect biochemistry and molecular biology 5 38815735
2022 Structure-based design, synthesis and evaluation of a novel family of PEX5-PEX14 interaction inhibitors against Trypanosoma. European journal of medicinal chemistry 5 36194937
2021 Computer-Aided Design and Synthesis of a New Class of PEX14 Inhibitors: Substituted 2,3,4,5-Tetrahydrobenzo[F][1,4]oxazepines as Potential New Trypanocidal Agents. Journal of chemical information and modeling 5 34597510
2015 First Japanese case of Zellweger syndrome with a mutation in PEX14. Pediatrics international : official journal of the Japan Pediatric Society 5 26627464
2011 Molecular characterization of the PEX14 gene from the methylotrophic yeast Pichia methanolica. Journal of bioscience and bioengineering 5 21317032
2023 Development of novel PEX5-PEX14 protein-protein interaction (PPI) inhibitors based on an oxopiperazine template. European journal of medicinal chemistry 4 37406382
2009 Identification of a novel PEX14 mutation in Zellweger syndrome. BMJ case reports 4 21686775
2025 PEX14 condensates recruit receptor and cargo pairs for peroxisomal protein import. Nature structural & molecular biology 3 40555785
2025 PEX14 acts as a molecular link between optineurin and the autophagic machinery to induce pexophagy. The Journal of cell biology 3 41071103
2020 The coiled-coil domain of glycosomal membrane-associated Leishmania donovani PEX14: cloning, overexpression, purification and preliminary crystallographic analysis. Acta crystallographica. Section F, Structural biology communications 2 33006573
2025 Unveiling the roles of PEX16 in female reproductive capacity and lifespan of brown planthopper, Nilaparvata lugens (Stål), in relation to PEX14. Pest management science 1 40928320
2026 Pex6 and ubiquitination regulate topological remodeling of the peroxisomal membrane protein Pex14. The Journal of biological chemistry 0 41581879
2026 Loss of peroxisomal membrane proteins PEX13 and PEX14 disrupts fatty acid oxidation and drives lipid imbalance. Bioscience reports 0 41860470
2025 Quantum mechanics-driven structure-activity relationship study of PEX5-PEX14 protein-protein interaction inhibitors based on a dibenzo[b,e]azepin-6(6H)-one scaffold. European journal of medicinal chemistry 0 40749258
2025 PEX14 powers OPTN (optineurin) to drive peroxisome turnover. Autophagy 0 41474135

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