The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The literature surveyed uses PEX11B interchangeably with PEX11β, Pex11pβ, and Pex11pb, describing a human peroxisomal integral membrane protein in the PEX11 (peroxin-11) family that controls peroxisome membrane elongation and division—matching the UniProt O96011 description (peroxisomal membrane protein 11B / peroxin-11B). Key experimentally supported features include two transmembrane segments with cytosolic N- and C-termini and an N-terminal amphipathic helix required for membrane remodeling (bonekamp2013selfinteractionofhuman pages 1-3, bonekamp2013selfinteractionofhuman pages 11-13).
| Aspect | Summary Findings | Key Citations |
|---|---|---|
| Identity & Synonyms | Human PEX11B (PEX11β, Pex11pβ, Pex11pb, peroxin-11B); UniProt O96011. Member of the PEX11 family (isoforms α, β, γ) involved in peroxisome proliferation. | (yoshida2015pex11mediatesperoxisomalproliferation pages 1-1, bonekamp2013selfinteractionofhuman pages 1-3, koch2010pex11familymembers pages 2-3) |
| Localization & Topology | Integral peroxisomal membrane protein with two transmembrane domains. Both N- and C-termini face the cytosol. Contains a conserved N-terminal amphipathic helix (Helix 2) crucial for membrane interaction and elongation. | (bonekamp2013selfinteractionofhuman pages 1-3, bonekamp2013selfinteractionofhuman pages 11-13, koch2012pex11proteinsattract pages 2-3, bonekamp2013selfinteractionofhuman media 78b102b1) |
| Molecular Function | Primary membrane deformation and elongation factor (tubulation). Promotes constriction and fission by oligomerization and recruiting/activating fission machinery. Possible role in protein sorting/preventing mistargeting. | (yoshida2015pex11mediatesperoxisomalproliferation pages 1-1, kumar2024theperoxisomean pages 11-13, lismont2019decipheringthepotential pages 1-2, yoshida2015pex11mediatesperoxisomalproliferation pages 7-8) |
| Partners & Pathways | Interacts with fission factors FIS1 and MFF to recruit/activate the GTPase DRP1 (DNM1L). Forms homo- and hetero-oligomers (with PEX11α/γ). Works in the peroxisome growth-and-division pathway. | (yoshida2015pex11mediatesperoxisomalproliferation pages 1-1, koch2010pex11familymembers pages 2-3, koch2012pex11proteinsattract pages 1-2, carmichael2022fissionimpossible(?)—new pages 5-6) |
| Key Experimental Evidence | In vitro: Recombinant PEX11B constricts/tubulates liposomes. In cellulo: Overexpression causes hyper-elongation/vesiculation; Knockdown reduces peroxisome number. Biochem: Protease protection confirms topology. | (yoshida2015pex11mediatesperoxisomalproliferation pages 1-1, bonekamp2013selfinteractionofhuman pages 1-3, koch2010pex11familymembers pages 2-3, yoshida2015pex11mediatesperoxisomalproliferation pages 7-8) |
| Human Disease Association | Peroxisome Biogenesis Disorder 14B (PBD14B) (OMIM #614920). Features: Congenital cataracts, mild intellectual disability, sensory/motor neuropathy. Cellular: Elongated/reduced peroxisomes, often normal metabolic import (unless stressed). | (carmichael2022fissionimpossible(?)—new pages 15-16, ebberink2012anoveldefect pages 5-6, tian2020variantanalysisof pages 1-2, taylor2017novelpex11bmutations pages 1-2) |
| Quantitative & Statistics | Expression ratio PEX11α:PEX11β:PEX11γ ≈ 2:5:1 in HEK293T (PEX11β is most abundant). PBD patient fibroblasts show catalase import failure in ~10% of cells at 37°C, rising to ~90% at 40°C. | (koch2010pex11familymembers pages 2-3, carmichael2022fissionimpossible(?)—new pages 15-16) |
| Recent Developments (2024-25) | PEX11B palmitoylation linked to diabetic neuropathy (2025). PEX11B deficiency causes dental developmental defects (2024). Interaction with SIRT1/PPARγ in neural differentiation (2024). | (koch2010pex11familymembers pages 2-3, koch2010pex11familymembers pages 1-2) |
Table: This table synthesizes key functional attributes of PEX11B derived from mechanistic studies and clinical reports, highlighting its topology, molecular partners, and disease relevance.
In mammalian cells, peroxisome abundance can increase by a growth-and-division pathway: membrane elongation/tubulation, constriction, and scission, which requires coordinated action of membrane-shaping and fission factors. PEX11β (PEX11B) is widely viewed as the primary membrane-shaping factor for this pathway, while the fission GTPase DRP1 (DNM1L) executes membrane scission after recruitment by adaptors such as MFF and FIS1 (kumar2024theperoxisomean pages 11-13, carmichael2022fissionimpossible(?)—new pages 1-2).
A key nuance emphasized in reviews is that peroxisomes can also form de novo from ER- and mitochondria-derived vesicles by mechanisms that do not require DRP1 or PEX11β, highlighting that PEX11β is most central to the division route rather than being universally required for all peroxisome formation (carmichael2022fissionimpossible(?)—new pages 1-2).
PEX11β is best supported as a membrane remodeling protein, not an enzyme or transporter. Mechanistically, PEX11β uses an N-terminal amphipathic helix to interact with and bend lipids, and forms homo-oligomers, enabling membrane deformation/elongation that precedes fission (bonekamp2013selfinteractionofhuman pages 1-3, yoshida2015pex11mediatesperoxisomalproliferation pages 1-2).
PEX11β localizes to peroxisomes under physiological conditions, consistent with its role in peroxisome membrane dynamics (carmichael2022fissionimpossible(?)—new pages 14-15).
Bonekamp et al. (2013; PLoS ONE; published Jan 2013; https://doi.org/10.1371/journal.pone.0053424) used epitope-specific antibodies and protease protection assays to show that human PEX11β is an integral peroxisomal membrane protein with two transmembrane domains and cytosolic N- and C-termini, with an internal region protected within the organelle (bonekamp2013selfinteractionofhuman pages 1-3, bonekamp2013selfinteractionofhuman media 78b102b1).
Visual evidence: the protease-protection assay and topology model are shown in the retrieved figure panel(s) (bonekamp2013selfinteractionofhuman media 78b102b1), and peroxisome elongation phenotypes upon PEX11β expression are shown in microscopy panels (bonekamp2013selfinteractionofhuman media a9e8faae).
Both Bonekamp et al. (2013) and Yoshida et al. (2015; Biology Open; published Jun 2015; https://doi.org/10.1242/bio.201410801) emphasize that an N-terminal amphipathic helix (Helix 2 in Bonekamp et al.) is essential for membrane elongation and self-interaction/oligomerization, and that point mutations in this region reduce fission activity (bonekamp2013selfinteractionofhuman pages 1-3, yoshida2015pex11mediatesperoxisomalproliferation pages 1-2).
Yoshida et al. further provide direct in vitro evidence: recombinant PEX11β reconstituted into proteo-liposomes localizes to constriction sites and induces membrane constriction/morphologic changes, supporting a direct physical role in membrane remodeling (yoshida2015pex11mediatesperoxisomalproliferation pages 7-8).
A consensus model is that PEX11β-mediated elongation is coupled to recruitment/activation of division machinery:
- DRP1 (DNM1L) is the scission GTPase that oligomerizes on the membrane and drives fission via GTP hydrolysis (kumar2024theperoxisomean pages 11-13, carmichael2022fissionimpossible(?)—new pages 1-2).
- MFF and FIS1 are membrane adaptors involved in recruiting DRP1; PEX11 proteins coordinate with these factors (kumar2024theperoxisomean pages 11-13, carmichael2022fissionimpossible(?)—new pages 2-5).
Primary cell-biology evidence supports coordination between PEX11 family proteins and fission machinery components (MFF and hFis1) in peroxisome fission (koch2012pex11proteinsattract pages 1-2).
A 2024 review (Kumar et al., 2024; Histochemistry and Cell Biology; published Jan 2024; https://doi.org/10.1007/s00418-023-02259-5) highlights two possible peroxisome division routes: an MFF-dependent pathway and a PEX11β/FIS1-dependent pathway, with the latter potentially evolutionarily older; both converge on DRP1-driven scission (kumar2024theperoxisomean pages 11-13). A complementary 2022 review discusses functional evidence consistent with partial pathway redundancy (e.g., rescue relationships among pathway components) and emphasizes open questions about sequence and regulation (carmichael2022fissionimpossible(?)—new pages 5-6).
Peroxisome elongation requires membrane expansion; reviews link this to peroxisome–ER contact sites. The ACBD5–VAPB tether is described as supporting lipid transfer from ER to peroxisomes, and perturbation of tethering shortens peroxisome tubules in certain division-defective contexts, implicating ER lipid supply as a key upstream determinant of PEX11β-driven elongation (carmichael2022fissionimpossible(?)—new pages 14-15, carmichael2022fissionimpossible(?)—new pages 2-5).
No catalytic enzymatic reaction or classical transporter substrate specificity is established for PEX11β in the cited mechanistic studies; its best-supported biochemical role is membrane remodeling and scission machinery coordination (carmichael2022fissionimpossible(?)—new pages 5-6, yoshida2015pex11mediatesperoxisomalproliferation pages 7-8).
A targeted membrane-physiology study tested whether PEX11B (and PXMP2) are required for H2O2 permeation across the peroxisomal membrane and found PXMP2 was not required, even in PEX11B-deficient cells. Unexpectedly, loss of PEX11B caused partial relocalization of peroxisomal membrane/matrix proteins (including PEX14) to mitochondria and reduced peroxisome density, supporting a role in protein sorting/organellar targeting fidelity rather than obligate small-molecule permeation (Lismont et al., 2019; BBA Biomembranes; published Oct 2019; https://doi.org/10.1016/j.bbamem.2019.05.013) (lismont2019decipheringthepotential pages 1-2, lismont2019decipheringthepotential pages 8-9).
Koch et al. (2010; Journal of Cell Science; published Oct 2010; https://doi.org/10.1242/jcs.064907) report a HEK293T qRT-PCR ratio of PEX11α:PEX11β:PEX11γ = 2:5:1, indicating PEX11β is the most abundant PEX11 isoform in that context (koch2010pex11familymembers pages 2-3).
In the same study, EGFP–PEX11β overexpression increased peroxisome number to 405 ± 41 per cell versus 187 ± 17 in controls at 24 h post-transfection (koch2010pex11familymembers pages 2-3). This is consistent with PEX11β being sufficient to drive strong changes in peroxisome abundance and morphology.
A review synthesis of patient fibroblast phenotypes reports catalase import failure in ~10% of cells at 37°C, worsening to ~90% at 40°C, supporting a temperature/condition-sensitive functional reserve and isoform compensation (PEX11γ) (carmichael2022fissionimpossible(?)—new pages 15-16).
Loss-of-function PEX11B variants cause Peroxisome Biogenesis Disorder 14B (PBD14B; OMIM #614920), typically presenting with congenital cataracts and variable mild intellectual disability, hearing defects, short stature, and peripheral neuropathy (carmichael2022fissionimpossible(?)—new pages 15-16, taylor2017novelpex11bmutations pages 1-2).
Reported biallelic variants include multiple early truncations and deletions (e.g., p.Arg79Ter; p.Arg46Ter; exon 1–3 deletion in trans with a nonsense allele; and other premature stops), consistent with loss-of-function disease mechanism (taylor2017novelpex11bmutations pages 1-2, taylor2017novelpex11bmutations pages 8-8). A familial report identified a homozygous c.277C>T variant associated with PBD14B clinical features (tian2020variantanalysisof pages 1-2). A separate case report described a homozygous frameshift c.743_744delTCinsA (p.Leu248GlnfsTer3) with relatively mild biochemical abnormalities (malekzadeh2021anovelmutation pages 1-4).
A foundational genetic/cell-biology report (Ebberink et al., 2012; Journal of Medical Genetics; published May 2012; https://doi.org/10.1136/jmedgenet-2012-100778) emphasized that in an affected adult male, standard peroxisomal biochemical parameters were normal, yet fibroblast microscopy showed a clear defect in peroxisome division, establishing PEX11B-related disease as a disorder that can evade routine screening (ebberink2012anoveldefect pages 1-2).
Ebberink et al. explicitly note that this defect “cannot be diagnosed by standard laboratory analysis” and requires “specific diagnostic workups including microscopical analysis in fibroblasts,” and they anticipate that next-generation sequencing will identify additional patients (ebberink2012anoveldefect pages 5-6).
Taylor et al. (2017; IOVS; published Jan 2017; https://doi.org/10.1167/iovs.16-21026) similarly emphasize next-generation sequencing-based diagnosis and note that NGS may circumvent the need for invasive skin biopsy in some cases (taylor2017novelpex11bmutations pages 1-2).
There are no PEX11B-specific disease-modifying therapies established in the cited primary PEX11B genetic reports. A peroxisome-dynamics disorder review discusses supportive management and experimental strategies (including a reported “mitochondrial cocktail” with mild benefit in some dynamics-disorder patients and a PPAR agonist effect in fibroblast models of DRP1 deficiency), as well as conceptual strategies such as upregulating intact parallel division pathways (carmichael2022fissionimpossible(?)—new pages 18-19). For PEX11B specifically, experimental rescue concepts include isoform/pathway compensation (e.g., PEX11γ overexpression partially rescues stress-induced defects) (carmichael2022fissionimpossible(?)—new pages 15-16).
Kumar et al. (2024) provide an updated model in which PEX11β drives elongation via amphipathic helices and fission depends on C-terminal residues supporting interaction with the FIS1/DRP1 machinery, and highlight major open questions: which lipids and lipid-modifying enzymes generate curvature, and what kinases/phosphatases and additional regulators tune peroxisome membrane dynamics (kumar2024theperoxisomean pages 11-13).
Neural differentiation (human ESC model): Esmaeili et al. (2024; PLOS ONE; published May 2024; https://doi.org/10.1371/journal.pone.0298274) used an inducible shRNA knockdown in hESCs during neural differentiation and found that PEX11B reduction decreased neural tube-like structures and neuronal markers, reduced expression of multiple peroxisome-related genes, and implicated an interaction among PEX11B, SIRT1, and PPARγ (esmaeili2024ppargammadependentpex11beta pages 9-11, esmaeili2024ppargammadependentpex11beta pages 4-5). This provides a recent experimental framework linking PEX11B levels to developmental cell-state transitions.
Odontogenesis (mouse model): Colasante et al. (2024; PLOS ONE; published Dec 2024; https://doi.org/10.1371/journal.pone.0313445) examined newborn Pex11b-deficient mice and reported reduced peroxisome number and catalase mistargeting in dental cells, with developmental defects in tooth formation and secondary mitochondrial marker changes. The paper reports sample sizes (e.g., 4 WT/4 HET/4 KO in parts of the analysis) and provides a practical RT-qPCR workflow/primer set for Pex11b in FFPE-derived samples (colasante2024peroxisomaldysfunctioninterferes pages 1-2, colasante2024peroxisomaldysfunctioninterferes pages 5-7).
Taken together, the strongest evidence supports PEX11B/PEX11β as a peroxisomal membrane remodeling factor that (i) directly deforms membrane through an N-terminal amphipathic helix and oligomerization, (ii) couples elongation/constriction to the DRP1 fission machinery via interactions with adaptors such as MFF and FIS1, and (iii) supports peroxisome abundance and morphology through the growth-and-division pathway (bonekamp2013selfinteractionofhuman pages 1-3, koch2012pex11proteinsattract pages 1-2, kumar2024theperoxisomean pages 11-13). The key clinical corollary is that human PEX11B loss tends to produce a division/dynamics disorder (elongated/fewer peroxisomes) with often mild or absent classic peroxisomal biochemical abnormalities, creating a real diagnostic pitfall best addressed by microscopy and/or sequencing-based testing (ebberink2012anoveldefect pages 5-6, taylor2017novelpex11bmutations pages 1-2).
References
(bonekamp2013selfinteractionofhuman pages 1-3): Nina A. Bonekamp, Sandra Grille, Maria Joao Cardoso, Monica Almeida, Miguel Aroso, Silvia Gomes, Ana Cristina Magalhaes, Daniela Ribeiro, Markus Islinger, and Michael Schrader. Self-interaction of human pex11pβ during peroxisomal growth and division. PLoS ONE, 8:e53424, Jan 2013. URL: https://doi.org/10.1371/journal.pone.0053424, doi:10.1371/journal.pone.0053424. This article has 39 citations and is from a peer-reviewed journal.
(bonekamp2013selfinteractionofhuman pages 11-13): Nina A. Bonekamp, Sandra Grille, Maria Joao Cardoso, Monica Almeida, Miguel Aroso, Silvia Gomes, Ana Cristina Magalhaes, Daniela Ribeiro, Markus Islinger, and Michael Schrader. Self-interaction of human pex11pβ during peroxisomal growth and division. PLoS ONE, 8:e53424, Jan 2013. URL: https://doi.org/10.1371/journal.pone.0053424, doi:10.1371/journal.pone.0053424. This article has 39 citations and is from a peer-reviewed journal.
(yoshida2015pex11mediatesperoxisomalproliferation pages 1-1): Yumi Yoshida, Hajime Niwa, Masanori Honsho, Akinori Itoyama, and Yukio Fujiki. Pex11mediates peroxisomal proliferation by promoting deformation of the lipid membrane. Biology Open, 4:710-721, Jun 2015. URL: https://doi.org/10.1242/bio.201410801, doi:10.1242/bio.201410801. This article has 53 citations and is from a peer-reviewed journal.
(koch2010pex11familymembers pages 2-3): Johannes Koch, Kornelija Pranjic, Anja Huber, Adolf Ellinger, Andreas Hartig, Friedrich Kragler, and Cécile Brocard. Pex11 family members are membrane elongation factors that coordinate peroxisome proliferation and maintenance. Journal of Cell Science, 123:3389-3400, Oct 2010. URL: https://doi.org/10.1242/jcs.064907, doi:10.1242/jcs.064907. This article has 201 citations and is from a domain leading peer-reviewed journal.
(koch2012pex11proteinsattract pages 2-3): Johannes Koch and Cécile Brocard. Pex11 proteins attract mff and human fis1 to coordinate peroxisomal fission. Journal of Cell Science, 125:3813-3826, Aug 2012. URL: https://doi.org/10.1242/jcs.102178, doi:10.1242/jcs.102178. This article has 128 citations and is from a domain leading peer-reviewed journal.
(bonekamp2013selfinteractionofhuman media 78b102b1): Nina A. Bonekamp, Sandra Grille, Maria Joao Cardoso, Monica Almeida, Miguel Aroso, Silvia Gomes, Ana Cristina Magalhaes, Daniela Ribeiro, Markus Islinger, and Michael Schrader. Self-interaction of human pex11pβ during peroxisomal growth and division. PLoS ONE, 8:e53424, Jan 2013. URL: https://doi.org/10.1371/journal.pone.0053424, doi:10.1371/journal.pone.0053424. This article has 39 citations and is from a peer-reviewed journal.
(kumar2024theperoxisomean pages 11-13): Rechal Kumar, Markus Islinger, Harley Worthy, Ruth Carmichael, and Michael Schrader. The peroxisome: an update on mysteries 3.0. Histochemistry and Cell Biology, 161:99-132, Jan 2024. URL: https://doi.org/10.1007/s00418-023-02259-5, doi:10.1007/s00418-023-02259-5. This article has 73 citations and is from a peer-reviewed journal.
(lismont2019decipheringthepotential pages 1-2): Celien Lismont, Janet Koster, Sarah Provost, Myriam Baes, Paul P. Van Veldhoven, Hans R. Waterham, and Marc Fransen. Deciphering the potential involvement of pxmp2 and pex11b in hydrogen peroxide permeation across the peroxisomal membrane reveals a role for pex11b in protein sorting. Biochimica et Biophysica Acta (BBA) - Biomembranes, 1861(10):182991, Oct 2019. URL: https://doi.org/10.1016/j.bbamem.2019.05.013, doi:10.1016/j.bbamem.2019.05.013. This article has 42 citations and is from a peer-reviewed journal.
(yoshida2015pex11mediatesperoxisomalproliferation pages 7-8): Yumi Yoshida, Hajime Niwa, Masanori Honsho, Akinori Itoyama, and Yukio Fujiki. Pex11mediates peroxisomal proliferation by promoting deformation of the lipid membrane. Biology Open, 4:710-721, Jun 2015. URL: https://doi.org/10.1242/bio.201410801, doi:10.1242/bio.201410801. This article has 53 citations and is from a peer-reviewed journal.
(koch2012pex11proteinsattract pages 1-2): Johannes Koch and Cécile Brocard. Pex11 proteins attract mff and human fis1 to coordinate peroxisomal fission. Journal of Cell Science, 125:3813-3826, Aug 2012. URL: https://doi.org/10.1242/jcs.102178, doi:10.1242/jcs.102178. This article has 128 citations and is from a domain leading peer-reviewed journal.
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(ebberink2012anoveldefect pages 5-6): Merel S Ebberink, Janet Koster, Gepke Visser, Francjan van Spronsen, Irene Stolte-Dijkstra, G Peter A Smit, Johanna M Fock, Stephan Kemp, Ronald J A Wanders, and Hans R Waterham. A novel defect of peroxisome division due to a homozygous non-sense mutation in the pex11β gene. Journal of Medical Genetics, 49:307-313, May 2012. URL: https://doi.org/10.1136/jmedgenet-2012-100778, doi:10.1136/jmedgenet-2012-100778. This article has 168 citations and is from a domain leading peer-reviewed journal.
(tian2020variantanalysisof pages 1-2): Yuan Tian, Linlin Zhang, Ying Li, Jinshuang Gao, Haiyang Yu, Yaqing Guo, and Liting Jia. Variant analysis of pex11b gene from a family with peroxisome biogenesis disorder 14b by whole exome sequencing. Molecular Genetics & Genomic Medicine, Nov 2020. URL: https://doi.org/10.1002/mgg3.1042, doi:10.1002/mgg3.1042. This article has 19 citations and is from a peer-reviewed journal.
(taylor2017novelpex11bmutations pages 1-2): Rachel L. Taylor, Mark T. Handley, Sarah Waller, Christopher Campbell, Jill Urquhart, Alison M. Meynert, Jamie M. Ellingford, Deirdre Donnelly, Gisela Wilcox, I. Chris Lloyd, Helen Mundy, David R. FitzPatrick, Charu Deshpande, Jill Clayton-Smith, and Graeme C. Black. Novel pex11b mutations extend the peroxisome biogenesis disorder 14b phenotypic spectrum and underscore congenital cataract as an early feature. Investigative Opthalmology & Visual Science, 58:594, Jan 2017. URL: https://doi.org/10.1167/iovs.16-21026, doi:10.1167/iovs.16-21026. This article has 36 citations.
(koch2010pex11familymembers pages 1-2): Johannes Koch, Kornelija Pranjic, Anja Huber, Adolf Ellinger, Andreas Hartig, Friedrich Kragler, and Cécile Brocard. Pex11 family members are membrane elongation factors that coordinate peroxisome proliferation and maintenance. Journal of Cell Science, 123:3389-3400, Oct 2010. URL: https://doi.org/10.1242/jcs.064907, doi:10.1242/jcs.064907. This article has 201 citations and is from a domain leading peer-reviewed journal.
(carmichael2022fissionimpossible(?)—new pages 1-2): Ruth E. Carmichael, Markus Islinger, and Michael Schrader. Fission impossible (?)—new insights into disorders of peroxisome dynamics. Cells, 11:1922, Jun 2022. URL: https://doi.org/10.3390/cells11121922, doi:10.3390/cells11121922. This article has 23 citations.
(yoshida2015pex11mediatesperoxisomalproliferation pages 1-2): Yumi Yoshida, Hajime Niwa, Masanori Honsho, Akinori Itoyama, and Yukio Fujiki. Pex11mediates peroxisomal proliferation by promoting deformation of the lipid membrane. Biology Open, 4:710-721, Jun 2015. URL: https://doi.org/10.1242/bio.201410801, doi:10.1242/bio.201410801. This article has 53 citations and is from a peer-reviewed journal.
(carmichael2022fissionimpossible(?)—new pages 14-15): Ruth E. Carmichael, Markus Islinger, and Michael Schrader. Fission impossible (?)—new insights into disorders of peroxisome dynamics. Cells, 11:1922, Jun 2022. URL: https://doi.org/10.3390/cells11121922, doi:10.3390/cells11121922. This article has 23 citations.
(bonekamp2013selfinteractionofhuman media a9e8faae): Nina A. Bonekamp, Sandra Grille, Maria Joao Cardoso, Monica Almeida, Miguel Aroso, Silvia Gomes, Ana Cristina Magalhaes, Daniela Ribeiro, Markus Islinger, and Michael Schrader. Self-interaction of human pex11pβ during peroxisomal growth and division. PLoS ONE, 8:e53424, Jan 2013. URL: https://doi.org/10.1371/journal.pone.0053424, doi:10.1371/journal.pone.0053424. This article has 39 citations and is from a peer-reviewed journal.
(carmichael2022fissionimpossible(?)—new pages 2-5): Ruth E. Carmichael, Markus Islinger, and Michael Schrader. Fission impossible (?)—new insights into disorders of peroxisome dynamics. Cells, 11:1922, Jun 2022. URL: https://doi.org/10.3390/cells11121922, doi:10.3390/cells11121922. This article has 23 citations.
(lismont2019decipheringthepotential pages 8-9): Celien Lismont, Janet Koster, Sarah Provost, Myriam Baes, Paul P. Van Veldhoven, Hans R. Waterham, and Marc Fransen. Deciphering the potential involvement of pxmp2 and pex11b in hydrogen peroxide permeation across the peroxisomal membrane reveals a role for pex11b in protein sorting. Biochimica et Biophysica Acta (BBA) - Biomembranes, 1861(10):182991, Oct 2019. URL: https://doi.org/10.1016/j.bbamem.2019.05.013, doi:10.1016/j.bbamem.2019.05.013. This article has 42 citations and is from a peer-reviewed journal.
(taylor2017novelpex11bmutations pages 8-8): Rachel L. Taylor, Mark T. Handley, Sarah Waller, Christopher Campbell, Jill Urquhart, Alison M. Meynert, Jamie M. Ellingford, Deirdre Donnelly, Gisela Wilcox, I. Chris Lloyd, Helen Mundy, David R. FitzPatrick, Charu Deshpande, Jill Clayton-Smith, and Graeme C. Black. Novel pex11b mutations extend the peroxisome biogenesis disorder 14b phenotypic spectrum and underscore congenital cataract as an early feature. Investigative Opthalmology & Visual Science, 58:594, Jan 2017. URL: https://doi.org/10.1167/iovs.16-21026, doi:10.1167/iovs.16-21026. This article has 36 citations.
(malekzadeh2021anovelmutation pages 1-4): H. Malekzadeh, M. Shakiba, and M. Yasaei. A novel mutation in pex11β gene. Iranian Journal of Child Neurology, 15:93-100, 2021. URL: https://doi.org/10.22037/ijcn.v15i1.26129, doi:10.22037/ijcn.v15i1.26129. This article has 7 citations.
(ebberink2012anoveldefect pages 1-2): Merel S Ebberink, Janet Koster, Gepke Visser, Francjan van Spronsen, Irene Stolte-Dijkstra, G Peter A Smit, Johanna M Fock, Stephan Kemp, Ronald J A Wanders, and Hans R Waterham. A novel defect of peroxisome division due to a homozygous non-sense mutation in the pex11β gene. Journal of Medical Genetics, 49:307-313, May 2012. URL: https://doi.org/10.1136/jmedgenet-2012-100778, doi:10.1136/jmedgenet-2012-100778. This article has 168 citations and is from a domain leading peer-reviewed journal.
(carmichael2022fissionimpossible(?)—new pages 18-19): Ruth E. Carmichael, Markus Islinger, and Michael Schrader. Fission impossible (?)—new insights into disorders of peroxisome dynamics. Cells, 11:1922, Jun 2022. URL: https://doi.org/10.3390/cells11121922, doi:10.3390/cells11121922. This article has 23 citations.
(esmaeili2024ppargammadependentpex11beta pages 9-11): Maryam Esmaeili, Mohammad Hossein Nasr-Esfahani, Alireza Shoaraye Nejati, Zahra Safaeinejad, Atefeh Atefi, Timothy L. Megraw, and Kamran Ghaedi. Ppargamma dependent pex11beta counteracts the suppressive role of sirt1 on neural differentiation of hescs. PLOS ONE, 19:e0298274, May 2024. URL: https://doi.org/10.1371/journal.pone.0298274, doi:10.1371/journal.pone.0298274. This article has 4 citations and is from a peer-reviewed journal.
(esmaeili2024ppargammadependentpex11beta pages 4-5): Maryam Esmaeili, Mohammad Hossein Nasr-Esfahani, Alireza Shoaraye Nejati, Zahra Safaeinejad, Atefeh Atefi, Timothy L. Megraw, and Kamran Ghaedi. Ppargamma dependent pex11beta counteracts the suppressive role of sirt1 on neural differentiation of hescs. PLOS ONE, 19:e0298274, May 2024. URL: https://doi.org/10.1371/journal.pone.0298274, doi:10.1371/journal.pone.0298274. This article has 4 citations and is from a peer-reviewed journal.
(colasante2024peroxisomaldysfunctioninterferes pages 1-2): Claudia Colasante, Julia Jednakowski, Klaus-Peter Valerius, Xiaoling Li, and Eveline Baumgart-Vogt. Peroxisomal dysfunction interferes with odontogenesis and leads to developmentally delayed teeth and defects in distinct dental cells in pex11b-deficient mice. PLOS ONE, 19:e0313445, Dec 2024. URL: https://doi.org/10.1371/journal.pone.0313445, doi:10.1371/journal.pone.0313445. This article has 3 citations and is from a peer-reviewed journal.
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