PEX5 Antibody

1. these findings lend credit to the idea that inefficient catalase import, when coupled with the role of PEX5 as a redox-regulated import receptor, constitutes a cellular defense mechanism to combat oxidative insults of extra-peroxisomal origin. PMID: 28760655
2. TRIM37-mediated ubiquitylation stabilizes PEX5 and promotes peroxisomal matrix protein import, suggesting that mulibrey nanism is a new peroxisomal biogenesis disorder. PMID: 28724525
3. Data suggest that soluble/cytosolic PEX5 interacts with PEX14/PEX13 complex, a model for the docking/translocation module (DTM) of the peroxisomal matrix protein translocon; PEX14/PEX13 complex appears to function in peroxisomal membrane as large cavity into which cytosolic PEX5 can enter to release its cargo. (PEX = peroxisomal biogenesis factor) PMID: 28765278
4. data reveal subpopulations of peroxisomes showing only weak colocalization between PEX14 and PEX5 or PEX11 but at the same time a clear compartmentalized organization. This compartmentalization, which was less evident in cases of strong colocalization, indicates dynamic protein reorganization linked to changes occurring in the peroxisomes. PMID: 27311714
5. our data suggest that insertion of the trimeric PEX5-PEX7-PTS2 protein complex into the DTM is probably accompanied by conformational alterations in PEX5 to allow release of the PTS2 protein into the organelle matrix PMID: 26138649
6. Our data suggest that the functional polymorphism rs3814058C>T in 3'-UTR of PXR may be a functional biomarker to predict risk of colorectal cancer PMID: 26547791
7. PEX5 encodes two isoforms, PEX5L & PEX5S, & a homozygous frame shift mutation c.722dupA (p.Val242Glyfs( *)33), located in the PEX5L-specific exon 9, results in loss of PEX5L only. Loss of PEX5L results in deficient import of PTS2-tagged proteins PMID: 26220973
8. bulky side chain within the recognition motif, which blocks contraction of the PEX5 binding cavity PMID: 25369882
9. Data show that ataxia-telangiectasia mutated (ATM) phosphorylates peroxisomal biogenesis factor 5 (PEX5) at serine 141 in response to reactive oxygen species. PMID: 26344566
10. the molecular recognition of PTS1 cargo proteins by Pex5p PMID: 25689234
11. ubiquitination of peroxisome-targeting signal type 1 (PTS1) receptor Pex5p regulating PTS1 protein import PMID: 24662292
12. PEX5 has a role in regulating peroxisome numbers by signaling to mediate pexophagy PMID: 24453954
13. Cys11 in PEX5 serves as a functional redox switch regulating the peroxisomal/cytosolic localization of peroxisomal proteins. PMID: 24118911
14. The novel Pex14-binding site may represent the initial tethering site of Pex5 from which the cargo-loaded receptor is further processed in a sequential manner. PMID: 24235149
15. Translocation of proteins across the organelle membrane occurs downstream of a reversible docking step and upstream of the first cytosolic ATP-dependent step, i.e. before ubiquitination of PEX5. PMID: 23963456
16. The molecular mechanism of recognition by the peroxisomal receptor Pex5p, in complex with alanine-glyoxylate aminotransferase revealed by X-ray crystallography. PMID: 22529745
17. Our results suggest that ubiquitin-specific protease 9X (USP9X) is by far the most active deubiquitinase acting on Ub-PEX5, both in female rat liver and HeLa cells. PMID: 22371489
18. interaction of PEX5 with catalase and PEX14 PMID: 21976670
19. The Peroxisomal targeting signal 1 in Scp2 is autonomous and is essential for binding to pex5. PMID: 21375735
20. the affinities of the PTS1-containing peptides from 42 proteins from the human proteome for Pex5p PMID: 20178365
21. Data suggest that translocation of PTS1-containing proteins across the peroxisomal membrane occurs concomitantly with formation of the Pex5p-Pex14p membrane complex and that this is probably the site from which Pex5p leaves the peroxisomal compartment. PMID: 12411433
22. binds the PTS1 independently of Hsp70 and the peroxin PEX12 PMID: 12456682
23. Binding energy threshold data have been generated for PTS1 pentapeptides containing different C-terminal tripeptide sequences to determine the functionality of specific PTS1 sequences. PMID: 12578380
24. concluded that the PTS1 domain of SR-BI is functional and can mediate peroxisomal interaction via Pex5p, in vitro PMID: 14652019
25. the N terminus of Pex5p is required for redirecting the peroxisome-associated peroxin back to the cytosol PMID: 15328363
26. Pex5p is a monomeric protein with an abnormal shape PMID: 15866874
27. Pex5 most likely enters peroxisomes, changes its interacting partners, and then exits using ATP energy. PMID: 16314507
28. Results indicate that the N-terminal half of Pex5p is best described as a natively unfolded pre-molten globule-like domain. PMID: 16403517
29. study shows mutation-dependent, gain-of-function association between myocilin & PTS1R; there was correlation between glaucoma phenotype & specific MYOC mutations, with more severe early-onset POAG mutations having higher degree of association with PTS1R PMID: 17317787
30. Results describe the affinities of mutated forms of Pex5p for a series of peroxisomal targeting signal type-1 (PTS1) peptides and conclude that PTS1-affinity reductions are correlated with Zellweger disease severity and cell biological phenotype. PMID: 17399738
31. A previously unobserved conformation for PEX5 suggests roles for intrinsic flexibility and rigid domain motions in ligand binding. PMID: 17428317
32. E2D1/2/3 (UbcH5a/b/c) are the mammalian functional counterparts of yeast/plant Pex4p PMID: 18359941
33. The location of the different mutations within the PEX5 amino acid sequence correlates rather well with the peroxisomal protein import defect observed in the cell lines. PMID: 18712838
34. Results describe the properties of the soluble and membrane-bound monoubiquitinated Pex5p species (Ub-Pex5p). PMID: 19208625
35. analysis of the human Pex5.Pex14.PTS1 protein complex structure obtained by small angle X-ray scattering PMID: 19584060
36. the step of protein translocation across the peroxisomal membrane into the PEX5 cycling pathway PMID: 19632994

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HGNC: 9719

OMIM: 202370

KEGG: hsa:5830

STRING: 9606.ENSP00000407401

UniGene: Hs.567327