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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
Human EFR3A (EFR3 homolog A; KIAA0143; UniProt Q14156) is correctly identified and is not ambiguous in the literature reviewed. It is distinct from the related human paralog EFR3B/KIAA0953. EFR3A is a nonenzymatic, ARM/HEAT-like helical scaffold and peripheral protein on the cytoplasmic face of the plasma membrane. Its best-established primary function is to anchor the PI4KA–TTC7–FAM126 phosphatidylinositol 4-kinase complex at that membrane. Thus, EFR3A has no catalytic reaction or substrate specificity of its own; it spatially positions PI4KA, whose substrate is phosphatidylinositol and whose product is plasma-membrane phosphatidylinositol 4-phosphate, PI4P. (trybus2025efr3aanintriguing pages 1-3, trybus2025efr3aanintriguing pages 6-8, suresh2024molecularbasisfor pages 2-4, suresh2024molecularbasisfor pages 1-2)
The most important recent advance is a December 2024 cryo-EM study that resolved how the EFR3A C terminus binds both TTC7B and FAM126A with nanomolar affinity and demonstrated that disrupting this interface reduces PI4KA recruitment to the plasma membrane. A separate October 2023 study proposed an additional role in flotillin-associated, cholesterol-sensitive membrane organization, but this remains less firmly established than the PI4KA-anchor function. (trybus2023efr3aanew pages 1-2, suresh2024molecularbasisfor pages 2-4, suresh2024molecularbasisfor pages 4-7, suresh2024molecularbasisfor pages 1-2)
The supplied target is confirmed as follows:
The Q14156-linked AlphaFold model is AF-Q14156-F1. Vertebrate EFR3A and EFR3B representative isoforms have approximately 64% sequence identity and 78% similarity, explaining both their shared function and potential experimental redundancy. The reviewed literature’s ARM/HEAT-like, predominantly α-helical superstructure agrees with the supplied InterPro/Pfam annotations—ARM-type fold, EFR3-like ARM, EFR3 homolog and EFR3 ARM. No conflicting same-symbol protein from another organism was substituted in this report. (trybus2025efr3aanintriguing pages 1-3, trybus2025efr3aanintriguing pages 6-8, marekbukowiec2025apotentialrole pages 3-4)
EFR3A is an approximately 821-residue, 92.9-kDa adapter/scaffold in a commonly studied isoform. Its N-terminal two-thirds are predicted or structurally inferred to form an elongated superhelical rod assembled from ARM and HEAT-like α-helical repeats. A reported ARM region encompasses approximately residues 48–144, while the extreme C terminus contains a conserved three-helix interaction module. Earlier descriptions suggesting multiple transmembrane helices are inconsistent with modern structural models and experimental localization; EFR3A is instead a lipidated peripheral membrane protein. (trybus2025efr3aanintriguing pages 6-8, trybus2023efr3aanew pages 1-2, marekbukowiec2025apotentialrole pages 3-4)
This architecture is functionally appropriate for a scaffold: the N terminus mediates membrane association, whereas the C terminus docks the soluble PI4KA regulatory assembly. The protein therefore bridges a lipid bilayer and a large enzyme complex without itself spanning the membrane or catalyzing lipid phosphorylation. (trybus2025efr3aanintriguing pages 8-10, suresh2024molecularbasisfor pages 2-4, suresh2024molecularbasisfor pages 1-2)
EFR3A’s central function is to recruit and stabilize the class IIIα phosphatidylinositol 4-kinase complex at the plasma membrane. PI4KA normally associates with TTC7A/B and FAM126A/B. PI4KA dimerization yields a dimer of heterotrimers with an overall mass near 750 kDa; incorporation of membrane-bound EFR3 creates a membrane-tethered dimeric assembly. (suresh2024molecularbasisfor pages 2-4, suresh2024molecularbasisfor pages 1-2)
The mechanistic division of labor is:
Notably, the 2024 structure detected no direct EFR3A–PI4KA contact and no major EFR3A-induced PI4KA conformational change. EFR3A therefore acts mainly as a localization scaffold rather than an allosteric kinase activator, although localization itself is essential for productive catalysis on membrane-embedded substrate. (suresh2024molecularbasisfor pages 2-4, suresh2025molecularmechanismsinvolved pages 61-65)
Suresh and colleagues reconstituted an EFR3A-bound PI4KA complex and solved its structure at 3.65 Å nominal resolution. The biochemical construct encompassed EFR3A residues 721–791, with residues 724–787 resolved. This segment undergoes a disorder-to-order transition and forms a V-shaped three-α-helix structure on binding TTC7B–FAM126A. The interface buries approximately 1,500 Ų, including about 800 Ų against TTC7B. Biolayer interferometry measured a dissociation constant of K_D = 23.5 ± 2 nM, consistent with a stable recruitment interaction. The study was published in Science Advances in December 2024: https://doi.org/10.1126/sciadv.adp6660. (suresh2024molecularbasisfor pages 2-4, suresh2024molecularbasisfor pages 1-2, suresh2025molecularmechanismsinvolved pages 65-69)
EFR3A α1 residues 728–735 form an amphipathic interface with TTC7B helices spanning residues 599–616, 690–707 and 712–723. EFR3A residues 741–775 additionally contact FAM126A helices 53–66 and 97–117. HDX-MS independently detected protection in FAM126A residues 89–102, TTC7B residues 539–544 and all three EFR3A helices. Thus, cryo-EM, solution dynamics and binding assays converge on a composite TTC7B–FAM126A docking site. (suresh2024molecularbasisfor pages 2-4, suresh2024molecularbasisfor pages 4-7, suresh2025molecularmechanismsinvolved pages 61-65, suresh2025molecularmechanismsinvolved pages 65-69)
Interface substitutions EFR3A F728A, L731A, K732E and A734R reduced binding, with L731A having the strongest effect in that group. EFR3A F755A and I763A disrupted the FAM126-facing interface; TTC7B A702R and FAM126A F61A/A103R were also disruptive. Live-cell BRET and confocal microscopy showed reduced PI4KA plasma-membrane recruitment when EFR3, TTC7B or FAM126A interfaces were disrupted. These experiments establish causality from atomic interface to cellular localization rather than relying solely on structural inference. (suresh2025molecularmechanismsinvolved pages 69-73, suresh2024molecularbasisfor pages 4-7, suresh2025molecularmechanismsinvolved pages 65-69)
EFR3A operates principally on the cytoplasmic surface of the plasma membrane. Its N-terminal cysteine-rich motif is palmitoylated and is required for membrane association. A 37-residue N-terminal EFR3A fragment can redirect GFP to membranes, although the fragment accumulates in Golgi membranes, indicating that lipidation is necessary but additional EFR3A sequences or trafficking interactions contribute to selective plasma-membrane localization. Some isoforms may differ: a reported isoform 2 lacks the N-terminal cysteine cluster and may consequently have altered membrane targeting. (trybus2025efr3aanintriguing pages 8-10, trybus2025efr3aanintriguing pages 1-3, marekbukowiec2025apotentialrole pages 3-4)
A conserved basic N-terminal patch may also interact electrostatically with acidic phosphoinositides. Nevertheless, palmitoylation is the experimentally supported primary targeting mechanism. Specific palmitoylation-dependent partitioning patterns are better established for EFR3B than EFR3A, so EFR3B’s exact “palmitoylation code” should not automatically be assigned to Q14156. (trybus2025efr3aanintriguing pages 6-8, trybus2025efr3aanintriguing pages 11-13)
PI4KA is the major source of plasma-membrane PI4P. By positioning PI4KA, EFR3A sustains a lipid pool that has both direct functions and serves as precursor for PI(4,5)P2. PI(4,5)P2 in turn supports phospholipase C signaling, ion-channel regulation, actin–membrane interactions and receptor trafficking, and is a substrate for class I PI3K production of PIP3. Plasma-membrane PI4P also contributes to phosphatidylserine transport and membrane lipid asymmetry. Consequently, EFR3A loss can affect many pathways indirectly through altered lipid composition; such effects should not all be interpreted as direct EFR3A interactions. (trybus2025efr3aanintriguing pages 10-11, suresh2025molecularmechanismsinvolved pages 46-49)
EFR3 proteins influence GPCR responsiveness by maintaining the phosphoinositide environment required for receptor signaling and resensitization. Combined loss of EFR3A and EFR3B in HEK293 cells caused angiotensin II receptor type 1 hyperphosphorylation and accelerated desensitization. Because both paralogs were removed, this establishes an EFR3-family role more strongly than an EFR3A-exclusive role. (marekbukowiec2025apotentialrole pages 3-4)
The 2023 Trybus study identified EFR3A as a flotillin-2 partner using affinity purification–mass spectrometry, followed by immunoblotting, co-immunoprecipitation and recombinant overlay assays. EFR3A occurred in detergent-resistant fractions of HeLa cells, and cholesterol depletion reduced that association. siRNA depletion lowered membrane order in live cells and giant plasma-membrane vesicles, changed raft-probe mobility and altered EGF-induced EGFR and PLCγ1 phosphorylation and cytosolic Ca²⁺ responses. The work was published in Cellular & Molecular Biology Letters in October 2023: https://doi.org/10.1186/s11658-023-00497-y. (trybus2023efr3aanew pages 1-2, trybus2025efr3aanintriguing pages 11-13, trybus2025efr3aanintriguing pages 13-15)
These results support a potential role in cholesterol-sensitive nanodomain organization. However, detergent-resistant membrane fractionation is an operational assay rather than direct proof of a physiological “raft,” and it remains unresolved whether the membrane-order phenotype reflects direct flotillin scaffolding, altered PI4P/PI(4,5)P2 metabolism, or both. Recent expert reviews accordingly describe the raft-organizer model as intriguing but still requiring reconstitution and structural validation. (trybus2025efr3aanintriguing pages 13-15)
A 2014 case-control study assessed rare EFR3A variation in 2,196 autism-spectrum-disorder cases and 3,389 controls. Novel nonsynonymous singleton variants occurred in 16 cases (0.73%) and 12 controls (0.35%). The overall approximately twofold enrichment did not remain significant after correction for testing two genes: OR 2.065, 95% CI 0.924–4.652, P=0.084. More selective analyses found enrichment at conserved positions (10,000-permutation P=0.0077) and six structurally predicted deleterious variants in cases versus one in controls (OR 9.282, P=0.017), but with a very wide confidence interval. The paper was published in Molecular Autism in April 2014: https://doi.org/10.1186/2040-2392-5-31. (gupta2014raredeleteriousmutations pages 1-2, gupta2014raredeleteriousmutations pages 7-9)
EFR3A was expressed in developing and adult human cortical neurons, including pyramidal neurons, and strongly co-expressed with an autism-associated transcriptional module (P<2.2×10⁻16). Nevertheless, some variants were inherited from unaffected relatives, an overall burden signal was weak and loss-of-function observations did not establish Mendelian causation. The evidence therefore supports EFR3A as a possible incompletely penetrant risk modifier, not a proven monogenic autism gene. (gupta2014raredeleteriousmutations pages 7-9, gupta2014raredeleteriousmutations pages 9-11)
PI4KA-complex disruption can lower plasma-membrane PI4P and phosphatidylserine, displace oncogenic KRAS from the membrane and reduce proliferation signaling and colony formation. Genetic EFR3A/EFR3B loss and PI4KA inhibition produced related phenotypes in cancer models. EFR3A amplification has also been reported in nearly 12% of pancreatic ductal adenocarcinomas, with associations to poorer outcome. These observations make the EFR3–PI4KA membrane-recruitment axis a potential therapeutic vulnerability in KRAS-dependent cancers. (trybus2025efr3aanintriguing pages 6-8, trybus2025efr3aanintriguing pages 10-11)
However, EFR3A and EFR3B redundancy complicates paralog-selective targeting, and PI4KA/PI4P biology is essential in normal cells. Reported compounds such as Compound 7 and simeprevir target PI4KA-related signaling rather than being validated EFR3A drugs. No established EFR3A-directed treatment, diagnostic test or clinically validated biomarker was identified. (trybus2025efr3aanintriguing pages 10-11)
Open Targets lists low-to-moderate association scores for phenotypes including alcohol drinking, stroke, liver disorder, prostate carcinoma and rosacea, with scores around 0.24–0.29 in the retrieved results. These database associations are hypothesis-generating and should not be treated as proof of molecular causality or clinical actionability. (OpenTargets Search: -EFR3A)
The following table separates established molecular facts from emerging and association-only findings.
| Question/aspect | Current conclusion | Strongest evidence/method | Confidence/caveat |
|---|---|---|---|
| Identity and paralog | Q14156 is human EFR3A/KIAA0143, an EFR3-family protein distinct from EFR3B/KIAA0953; the paralogs share about 64% sequence identity and 78% similarity. (trybus2025efr3aanintriguing pages 1-3, trybus2025efr3aanintriguing pages 6-8, marekbukowiec2025apotentialrole pages 3-4) | UniProt-linked structural review, nomenclature comparison, and sequence analysis | High. Correct human target verified; paralog redundancy can obscure EFR3A-specific phenotypes. |
| Architecture | EFR3A is a nonenzymatic, predominantly α-helical ARM/HEAT-like superhelical scaffold, not a transmembrane enzyme. (trybus2025efr3aanintriguing pages 1-3, trybus2025efr3aanintriguing pages 6-8, gupta2014raredeleteriousmutations pages 7-9) | Homology modeling, structural analysis, AlphaFold model AF-Q14156-F1, and cryo-EM | High for scaffold architecture; precise boundaries outside the resolved C terminus remain partly model-based. |
| Membrane localization | EFR3A is a peripheral cytosolic-face plasma-membrane protein. Palmitoylation of its N-terminal cysteine-rich motif drives membrane association; a 37-residue N-terminal segment targets GFP to membranes but alone shows Golgi retention. (trybus2025efr3aanintriguing pages 8-10, marekbukowiec2025apotentialrole pages 3-4) | Lipidation/mutational targeting experiments and fluorescence localization | High for palmitoylation-dependent targeting; isoform 2 lacks the cysteine cluster, so localization may be isoform-dependent. |
| PI4KA-complex interface | EFR3A residues 724–787 become an ordered, V-shaped three-helix element that contacts TTC7B and FAM126A, burying about 1,500 Ų; affinity is K_D = 23.5 ± 2 nM. (suresh2024molecularbasisfor pages 2-4, suresh2024molecularbasisfor pages 1-2, suresh2025molecularmechanismsinvolved pages 65-69) | 3.65 Å cryo-EM, HDX-MS, BLI, and interface mutagenesis; disruptive substitutions included EFR3A L731A and F755A, TTC7B A702R, and FAM126A A103R | Very high. Direct structural and orthogonal biochemical evidence; the resolved construct was EFR3A 721–791 rather than full-length protein. |
| Primary molecular function | EFR3A is a membrane anchor/adaptor that recruits the dimeric PI4KA–TTC7–FAM126 assembly to the plasma membrane; it does not catalyze a reaction and does not directly contact PI4KA in the resolved structure. (suresh2024molecularbasisfor pages 2-4, suresh2024molecularbasisfor pages 1-2, suresh2025molecularmechanismsinvolved pages 61-65) | Reconstituted complex, cryo-EM, HDX-MS, live-cell BRET, confocal microscopy, and recruitment-defective mutants | Very high. This is the best-established primary function; EFR3B can compensate in some systems. |
| Biochemical pathway | By positioning PI4KA, EFR3A supports plasma-membrane PI4P, the precursor pool for PI(4,5)P₂ and downstream PLC, GPCR, ion-channel, lipid-transport, and PI3K signaling. (marekbukowiec2025apotentialrole pages 3-4, trybus2025efr3aanintriguing pages 10-11, suresh2025molecularmechanismsinvolved pages 46-49) | Lipid measurements, genetic disruption of complex components, and established phosphoinositide biochemistry | High for PI4P maintenance; many downstream effects are indirect consequences of altered lipid homeostasis. |
| Flotillin/raft role | A 2023 study proposed that EFR3A binds flotillin-2 and helps maintain cholesterol-sensitive membrane order and EGF–EGFR–PLCγ–Ca²⁺ signaling. (trybus2023efr3aanew pages 1-2, trybus2025efr3aanintriguing pages 11-13, trybus2025efr3aanintriguing pages 13-15) | Affinity purification–mass spectrometry, recombinant overlay, co-immunoprecipitation, detergent-resistant fractions, siRNA, FLIM, and spot-variation FCS | Moderate/emerging. Supported in cultured cells, but detergent-resistant fractions are operational proxies and a direct raft-organizing mechanism remains unproven. |
| Autism relevance | Rare nonsynonymous variants occurred in 16/2,196 cases (0.73%) versus 12/3,389 controls (0.35%); overall burden was not significant after correction (OR 2.065, P=0.084), although structurally predicted deleterious variants were enriched (6 versus 1; OR 9.282, P=0.017). (gupta2014raredeleteriousmutations pages 1-2, gupta2014raredeleteriousmutations pages 7-9) | Case-control sequencing, conservation tests, structural modeling, inheritance analysis, and human-brain expression networks | Association only. Small counts, wide confidence intervals, inherited variants, incomplete penetrance, and no proof that EFR3A variants independently cause autism. |
| Cancer/KRAS relevance | EFR3A/B loss or PI4KA inhibition lowers PI4P/phosphatidylserine, mislocalizes oncogenic KRAS, and reduces proliferation signaling and colony formation; EFR3A amplification has been reported in nearly 12% of pancreatic ductal adenocarcinomas. (trybus2025efr3aanintriguing pages 6-8, trybus2025efr3aanintriguing pages 10-11) | Cancer-cell knockout/knockdown, lipid and localization assays, colony formation, inhibitor studies, and tumor-genomic association | Preclinical/associative. Mechanistically plausible but not established clinical causality; no validated EFR3A-directed therapy or clinical biomarker currently exists. |
Table: Evidence-tier summary of the verified identity, structure, localization, primary scaffolding function, pathways, and disease relevance of human EFR3A (Q14156). It distinguishes established molecular mechanisms from emerging or association-only findings.
Current practical use of EFR3A is primarily as a mechanistic research target rather than a clinical target:
The evidence supports a high-confidence annotation of EFR3A as a palmitoylated plasma-membrane adaptor for PI4KA, not as an enzyme, transporter or integral membrane protein. The December 2024 work upgrades this annotation from a general recruitment model to a residue-level mechanism supported by cryo-EM, HDX-MS, nanomolar binding measurements, mutagenesis and live-cell validation. (suresh2024molecularbasisfor pages 2-4, suresh2024molecularbasisfor pages 4-7, suresh2024molecularbasisfor pages 1-2, suresh2025molecularmechanismsinvolved pages 65-69)
Important gaps remain. The extent of EFR3A versus EFR3B functional specialization is unclear; full-length EFR3A has not been resolved atomically; isoform-specific localization is insufficiently characterized; regulation by the reported phosphorylation sites and palmitoylation dynamics is largely unresolved; and the flotillin/raft function has not yet been mechanistically connected to PI4KA recruitment. Disease associations—especially autism and cancer amplification—are biologically plausible but do not yet establish EFR3A-specific clinical causality. (trybus2025efr3aanintriguing pages 8-10, trybus2025efr3aanintriguing pages 1-3, trybus2025efr3aanintriguing pages 13-15, suresh2024molecularbasisfor pages 1-2, gupta2014raredeleteriousmutations pages 9-11)
References
(trybus2025efr3aanintriguing pages 1-3): Magdalena Trybus, Anita Hryniewicz-Jankowska, Aleksander Czogalla, and Aleksander F. Sikorski. Efr3a, an intriguing gene, and protein with a scaffolding function. Cells, Mar 2025. URL: https://doi.org/10.3390/cells14060445, doi:10.3390/cells14060445. This article has 6 citations.
(trybus2025efr3aanintriguing pages 6-8): Magdalena Trybus, Anita Hryniewicz-Jankowska, Aleksander Czogalla, and Aleksander F. Sikorski. Efr3a, an intriguing gene, and protein with a scaffolding function. Cells, Mar 2025. URL: https://doi.org/10.3390/cells14060445, doi:10.3390/cells14060445. This article has 6 citations.
(suresh2024molecularbasisfor pages 2-4): Sushant Suresh, Alexandria L. Shaw, Joshua G. Pemberton, Mackenzie K. Scott, Noah J. Harris, Matthew A. H. Parson, Meredith L. Jenkins, Pooja Rohilla, Alejandro Alvarez-Prats, Tamas Balla, Calvin K. Yip, and John E. Burke. Molecular basis for plasma membrane recruitment of pi4ka by efr3. Science Advances, Dec 2024. URL: https://doi.org/10.1126/sciadv.adp6660, doi:10.1126/sciadv.adp6660. This article has 25 citations and is from a highest quality peer-reviewed journal.
(suresh2024molecularbasisfor pages 1-2): Sushant Suresh, Alexandria L. Shaw, Joshua G. Pemberton, Mackenzie K. Scott, Noah J. Harris, Matthew A. H. Parson, Meredith L. Jenkins, Pooja Rohilla, Alejandro Alvarez-Prats, Tamas Balla, Calvin K. Yip, and John E. Burke. Molecular basis for plasma membrane recruitment of pi4ka by efr3. Science Advances, Dec 2024. URL: https://doi.org/10.1126/sciadv.adp6660, doi:10.1126/sciadv.adp6660. This article has 25 citations and is from a highest quality peer-reviewed journal.
(trybus2023efr3aanew pages 1-2): Magdalena Trybus, Anita Hryniewicz-Jankowska, Karolina Wójtowicz, Tomasz Trombik, Aleksander Czogalla, and Aleksander F. Sikorski. Efr3a: a new raft domain organizing protein? Cellular & Molecular Biology Letters, Oct 2023. URL: https://doi.org/10.1186/s11658-023-00497-y, doi:10.1186/s11658-023-00497-y. This article has 9 citations and is from a peer-reviewed journal.
(suresh2024molecularbasisfor pages 4-7): Sushant Suresh, Alexandria L. Shaw, Joshua G. Pemberton, Mackenzie K. Scott, Noah J. Harris, Matthew A. H. Parson, Meredith L. Jenkins, Pooja Rohilla, Alejandro Alvarez-Prats, Tamas Balla, Calvin K. Yip, and John E. Burke. Molecular basis for plasma membrane recruitment of pi4ka by efr3. Science Advances, Dec 2024. URL: https://doi.org/10.1126/sciadv.adp6660, doi:10.1126/sciadv.adp6660. This article has 25 citations and is from a highest quality peer-reviewed journal.
(marekbukowiec2025apotentialrole pages 3-4): Karolina Marek-Bukowiec, Magdalena Trybus, Anita Hryniewicz-Jankowska, Aleksander Czogalla, and Aleksander F. Sikorski. A potential role of efr3a in human disease states. Biomolecules, 15:466, Mar 2025. URL: https://doi.org/10.3390/biom15040466, doi:10.3390/biom15040466. This article has 0 citations.
(trybus2025efr3aanintriguing pages 8-10): Magdalena Trybus, Anita Hryniewicz-Jankowska, Aleksander Czogalla, and Aleksander F. Sikorski. Efr3a, an intriguing gene, and protein with a scaffolding function. Cells, Mar 2025. URL: https://doi.org/10.3390/cells14060445, doi:10.3390/cells14060445. This article has 6 citations.
(suresh2025molecularmechanismsinvolved pages 61-65): S Suresh. Molecular mechanisms involved in the regulation of phosphatidylinositol 4-kinase iii α (pi4kiiiα/pi4ka). Unknown journal, 2025.
(suresh2025molecularmechanismsinvolved pages 65-69): S Suresh. Molecular mechanisms involved in the regulation of phosphatidylinositol 4-kinase iii α (pi4kiiiα/pi4ka). Unknown journal, 2025.
(suresh2025molecularmechanismsinvolved pages 69-73): S Suresh. Molecular mechanisms involved in the regulation of phosphatidylinositol 4-kinase iii α (pi4kiiiα/pi4ka). Unknown journal, 2025.
(trybus2025efr3aanintriguing pages 11-13): Magdalena Trybus, Anita Hryniewicz-Jankowska, Aleksander Czogalla, and Aleksander F. Sikorski. Efr3a, an intriguing gene, and protein with a scaffolding function. Cells, Mar 2025. URL: https://doi.org/10.3390/cells14060445, doi:10.3390/cells14060445. This article has 6 citations.
(trybus2025efr3aanintriguing pages 10-11): Magdalena Trybus, Anita Hryniewicz-Jankowska, Aleksander Czogalla, and Aleksander F. Sikorski. Efr3a, an intriguing gene, and protein with a scaffolding function. Cells, Mar 2025. URL: https://doi.org/10.3390/cells14060445, doi:10.3390/cells14060445. This article has 6 citations.
(suresh2025molecularmechanismsinvolved pages 46-49): S Suresh. Molecular mechanisms involved in the regulation of phosphatidylinositol 4-kinase iii α (pi4kiiiα/pi4ka). Unknown journal, 2025.
(trybus2025efr3aanintriguing pages 13-15): Magdalena Trybus, Anita Hryniewicz-Jankowska, Aleksander Czogalla, and Aleksander F. Sikorski. Efr3a, an intriguing gene, and protein with a scaffolding function. Cells, Mar 2025. URL: https://doi.org/10.3390/cells14060445, doi:10.3390/cells14060445. This article has 6 citations.
(gupta2014raredeleteriousmutations pages 1-2): Abha R Gupta, Michelle Pirruccello, Feng Cheng, Hyo Kang, Thomas V Fernandez, Jeremy M Baskin, Murim Choi, Li Liu, Adife Ercan-Sencicek, John D Murdoch, Lambertus Klei, Benjamin M Neale, Daniel Franjic, Mark J Daly, Richard P Lifton, Pietro De Camilli, Hongyu Zhao, Nenad Šestan, and Matthew W State. Rare deleterious mutations of the gene efr3a in autism spectrum disorders. Molecular Autism, 5:31-31, Apr 2014. URL: https://doi.org/10.1186/2040-2392-5-31, doi:10.1186/2040-2392-5-31. This article has 39 citations and is from a peer-reviewed journal.
(gupta2014raredeleteriousmutations pages 7-9): Abha R Gupta, Michelle Pirruccello, Feng Cheng, Hyo Kang, Thomas V Fernandez, Jeremy M Baskin, Murim Choi, Li Liu, Adife Ercan-Sencicek, John D Murdoch, Lambertus Klei, Benjamin M Neale, Daniel Franjic, Mark J Daly, Richard P Lifton, Pietro De Camilli, Hongyu Zhao, Nenad Šestan, and Matthew W State. Rare deleterious mutations of the gene efr3a in autism spectrum disorders. Molecular Autism, 5:31-31, Apr 2014. URL: https://doi.org/10.1186/2040-2392-5-31, doi:10.1186/2040-2392-5-31. This article has 39 citations and is from a peer-reviewed journal.
(gupta2014raredeleteriousmutations pages 9-11): Abha R Gupta, Michelle Pirruccello, Feng Cheng, Hyo Kang, Thomas V Fernandez, Jeremy M Baskin, Murim Choi, Li Liu, Adife Ercan-Sencicek, John D Murdoch, Lambertus Klei, Benjamin M Neale, Daniel Franjic, Mark J Daly, Richard P Lifton, Pietro De Camilli, Hongyu Zhao, Nenad Šestan, and Matthew W State. Rare deleterious mutations of the gene efr3a in autism spectrum disorders. Molecular Autism, 5:31-31, Apr 2014. URL: https://doi.org/10.1186/2040-2392-5-31, doi:10.1186/2040-2392-5-31. This article has 39 citations and is from a peer-reviewed journal.
(OpenTargets Search: -EFR3A): Open Targets Query (-EFR3A, 5 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.