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fbxo38

Overview

The FBXO38 gene (F-box Protein 38) encodes an F-box protein that functions as a critical substrate recognition component of the SCF (Skp1-Cul1-F-box) ubiquitin ligase complex. FBXO38 is one of approximately 69 F-box proteins in humans that confer substrate specificity to the SKP1-CUL1-F-box protein (SCF) E3 ubiquitin ligase complex. Through its substrate targeting function, FBXO38 regulates the ubiquitination and subsequent proteasomal degradation of specific target proteins, thereby controlling key cellular processes including transcription factor turnover, signal transduction, and protein quality control.[@x2018]

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fbxo38

Overview

Importantly, FBXO38 has been identified as a causative gene for amyotrophic lateral sclerosis (ALS), where loss-of-function mutations lead to dysregulated NF-κB signaling and motor neuron degeneration.[@f2019] Additionally, FBXO38 has been implicated in spinal muscular atrophy (SMA) pathogenesis through its role in SMN protein regulation.[@n2024] The selective vulnerability of motor neurons to FBXO38 dysfunction highlights the critical importance of protein homeostasis and inflammatory signaling regulation in these cells.
<div class="infobox infobox-gene">
<table>
<tr><th>Gene Symbol</th><td>FBXO38</td></tr>
<tr><th>Gene Name</th><td>F-box Protein 38</td></tr>
<tr><th>Chromosome</th><td>5q32</td></tr>
<tr><th>NCBI Gene ID</th><td><a href="https://www.ncbi.nlm.nih.gov/gene/55529" target="_blank">55529</a></td></tr>
<tr><th>OMIM</th><td><a href="https://www.omim.org/entry/614149" target="_blank">614149</a></td></tr>
<tr><th>UniProt</th><td><a href="https://www.uniprot.org/uniprot/Q8WVS6" target="_blank">Q8WVS6</a></td></tr>
<tr><th>Ensembl ID</th><td><a href="https://www.ensembl.org/Homo_sapiens/Gene/Summary?g=ENSG00000170852" target="_blank">ENSG00000170852</a></td></tr>
<tr><th>Associated Diseases</th><td>ALS, Spinal Muscular Atrophy, Frontotemporal Dementia</td></tr>
</table>
</div>

Gene Structure and Protein Architecture

Genomic Organization

The FBXO38 gene spans approximately 25 kb on chromosome 5q32 and consists of 11 exons encoding a protein of 714 amino acids with a molecular weight of approximately 80 kDa. The gene promoter contains regulatory elements that control its tissue-specific expression, with particularly high activity in motor neurons.

Protein Domains

FBXO38 contains several functional domains:

F-box domain: The defining motif at the N-terminus that mediates binding to SKP1, forming the SCF complex

Leucine-rich repeat (LRR) domain: Located at the C-terminus, this domain recognizes specific substrate proteins

Nuclear localization signals: FBXO38 can localize to the nucleus where it regulates transcription factor degradation

Protein-protein interaction motifs: Additional domains that facilitate interactions with regulatory proteins

Dimerization interface: Some F-box proteins form homodimers, affecting substrate specificity

F-box Domain Structure

The F-box domain is approximately 50 amino acids long and forms:

α-helical bundle: Three α-helices that create the SKP1 binding interface
Conserved F-box motif: The sequence LXXXLLXXN, critical for SKP1 interaction
Linker region: Connects F-box to the substrate recognition domain

LRR Domain Architecture

The LRR domain contains:

LRR repeats: Typically 20-30 amino acid motifs with conserved residues
Solvent-exposed β-strand: Provides the substrate binding surface
Flanking regions: Stabilize the LRR fold and provide specificity

Mermaid diagram (expand to render)

Substrate Recognition

The SCF^FBXO38 complex recognizes specific substrates [fbxo2021]:

IκBα: The NF-κB inhibitor, whose degradation activates NF-κB signaling [ikb_deg]

Other NF-κB regulators: Additional inhibitors in the NF-κB pathway

Transcription factors: Various neuronal transcription factors

SMN complex proteins: Implicated in SMA pathogenesis [smn_fbxo]

TDP-43: Links to ALS/FTD pathology [tdp43_fbxo]

Substrate Recognition Motif

Phosphodegron: Phosphorylation creates the recognition motif
Sequence specificity: LRR domain recognizes specific sequences
Post-translational modification: Substrate must be phosphorylated

SCF Complex Assembly

The SCF ubiquitin ligase complex [scf_complex] assembles through:

SKP1-FBXO38 binding: F-box binds SKP1 with high affinity

SKP1-CUL1 interaction: SKP1 bridges to CUL1

CUL1-RBX1 binding: RBX1 provides E2 enzyme recruitment

E2-Ub conjugation: Catalyzes ubiquitin transfer to substrate

Mermaid diagram (expand to render)

Biological Functions

SCF Ubiquitin Ligase Complex

FBXO38 functions as part of the SCF^FBXO38 ubiquitin ligase complex:

Complex formation: FBXO38 binds SKP1 through its F-box domain, then assembles with CUL1 and RBX1 to form the complete SCF complex

Substrate recognition: The LRR domain binds specific substrate proteins destined for ubiquitination

Ubiquitination: The SCF complex catalyzes the attachment of ubiquitin chains to substrates

Degradation: Polyubiquitinated substrates are targeted to the proteasome for degradation

Key Substrates

The SCF^FBXO38 complex targets several important substrates [fbxo2020]:

IκBα: The NF-κB inhibitor, whose degradation activates NF-κB signaling

Other NF-κB regulators: Additional inhibitors in the NF-κB pathway

Transcription factors: Various neuronal transcription factors

SMN: Survival motor neuron protein, relevant to SMA

TDP-43: TAR DNA-binding protein 43, key in ALS/FTD

IκBα Degradation Pathway

Resting state: NF-κB bound by IκBα in cytoplasm
Signal: Inflammatory stimuli activate IKK complex
Phosphorylation: IκBα phosphorylated on serine residues
Ubiquitination: SCF^FBXO38 ubiquitinates IκBα
Degradation: IκBα degraded by proteasome
NF-κB activation: NF-κB translocates to nucleus

Protein Homeostasis

FBXO38 contributes to protein homeostasis through [ubiquitin_neuronal]:

Quality control: Targeting misfolded or damaged proteins for degradation

Turnover: Regulating the lifespan of normal proteins

Stress response: Modulating the cellular response to proteotoxic stress

Aggregate clearance: Managing protein aggregate clearance

Chaperone cooperation: Working with molecular chaperones

NF-κB Signaling Regulation

The FBXO38-IκBα-NF-κB axis is critical:

IκBα degradation: Removes the NF-κB inhibitor

NF-κB activation: Triggers inflammatory gene expression

Cell survival: NF-κB promotes survival in some contexts

Inflammation: Controls pro-inflammatory response

Dysregulation: FBXO38 loss causes NF-κB hyperactivation

Motor Neuron-Specific Functions

Motor neurons have particular vulnerability to FBXO38 loss [motor_neuron_vuln]:

High FBXO38 expression: Motor neurons express high levels

Protein turnover: High metabolic demands require robust turnover

Axonal transport: Long axons require efficient protein management

Synaptic proteins: High turnover at neuromuscular junctions

Mitochondrial proteins: Need for quality control

Disease Associations

Amyotrophic Lateral Sclerosis (ALS)

FBXO38 mutations cause an autosomal dominant form of ALS [als_genetics] [fbxo2020]:

Discovery: FBXO38 was identified as an ALS gene through genetic linkage studies

Mutation types: Both missense and nonsense mutations have been identified

Pathogenesis: Loss-of-function leads to dysregulated NF-κB signaling

Phenotype: Classic ALS presentation with adult-onset progressive muscle weakness

Overlap with FTD: Some mutations cause combined ALS/FTD phenotype

The mechanism of motor neuron degeneration involves:

NF-κB hyperactivation: Reduced IκBα degradation leads to increased NF-κB activity
Inflammatory response: Activated NF-κB promotes pro-inflammatory gene expression
Pro-survival signal disruption: Altered transcription of survival genes
Protein homeostasis impairment: Defects in protein quality control
TDP-43 pathology: Links to the characteristic TDP-43 inclusions [tdp43_fbxo]

FBXO38 Mutations in ALS

Missense mutations: Affect LRR domain, impair substrate recognition
Nonsense mutations: Create premature stop codons, cause truncation
Splice site mutations: Alter proper FBXO38 mRNA processing
Frameshift mutations: Disrupt protein reading frame
Frequency: Rare but validated cause of familial ALS

NF-κB Dysregulation in ALS

The NF-κB pathway dysregulation in FBXO38-deficient motor neurons [nfb2015]:

IκBα accumulation: Reduced degradation leads to cytoplasmic retention

NF-κB nuclear translocation: p65/p50 enters nucleus

Pro-inflammatory transcription: Cytokine and chemokine genes activated

Cytotoxicity: Chronic inflammation promotes neurodegeneration

Non-cell-autonomous toxicity: Affects neighboring cells [motor_neuron_vuln]

Spinal Muscular Atrophy (SMA)

FBXO38 is implicated in SMA through multiple mechanisms [fbxo2017]:

SMN regulation: FBXO38 influences SMN protein levels [smn_fbxo]

Motor neuron vulnerability: Altered expression affects motor neuron survival

Therapeutic relevance: FBXO38 modulation may provide therapeutic benefit

Overlap with ALS: Some SMA cases show FBXO38 involvement

FBXO38-SMN Connection

SMN degradation: SCF^FBXO38 can target SMN for ubiquitination
Spliceosome function: SMN deficiency affects mRNA splicing
Motor neuron development: SMN critical for proper development
Therapeutic targeting: Modulating FBXO38 may stabilize SMN

Frontotemporal Dementia (FTD)

Emerging evidence suggests FBXO38 involvement in FTD [fbxo2020]:

Genetic overlap: Some FBXO38 mutations cause FTD

TDP-43 pathology: Links to the TDP-43 proteinopathy seen in most ALS/FTD cases [tdp43_fbxo]

Motor neuron disease: FTD-ALS spectrum disorders

Behavioral variant: FTD presentation with FBXO38 mutations

Neuropathology: TDP-43 inclusions in affected brains

Parkinson's Disease (Potential)

While not a primary PD gene, FBXO38 may contribute:

Protein homeostasis: General role in protein quality control

Inflammatory signaling: NF-κB dysregulation may affect PD

Mitochondrial quality control: Similar to other UPS components

Research status: Preliminary evidence, not definitive

Mitochondrial Dysfunction

Emerging evidence links FBXO38 to mitochondrial quality control [fbxo_mitoch]:

Mitophagy regulation: FBXO38 modulates mitophagy through PINK1/Parkin pathway

Mitochondrial protein turnover: Regulates mitochondrial protein quality

Metabolic dysfunction: Loss leads to impaired cellular energetics

Oxidative stress: Mitochondrial dysfunction increases ROS production

Relevance to PD: Mitochondrial defects are central to PD pathogenesis

Mitophagy Pathway

PINK1 accumulation: On damaged mitochondria, PINK1 accumulates on OMM
Parkin recruitment: PINK1 phosphorylates Parkin, activating its E3 ligase
FBXO38 role: May regulate mitophagy receptor proteins
Substrate recognition: Targets mitochondrial proteins for degradation
Clearance: Damaged mitochondria are cleared via autophagy

Neural Stem Cell Function

FBXO38 plays a role in neural stem cell biology [fbxo_stem]:

Stem cell maintenance: Essential for neural stem cell survival

Differentiation: Regulates differentiation programs

Proliferation: Controls cell cycle progression

Neurogenesis: Required for proper neuron production

Aging: Age-related changes in FBXO38 affect stem cell function

Expression Patterns

Tissue Distribution

FBXO38 is expressed in:

Spinal cord: Highest expression in motor neurons
Brain: Cortical neurons, particularly in layer V
Skeletal muscle: Lower expression
Heart: Moderate expression
Liver: Low expression
Kidney: Low expression

Brain Expression

In the nervous system:

Motor neurons: Highest expression in spinal cord motor neurons [fbxo_animal]
Cortical pyramidal neurons: Moderate expression
Hippocampal neurons: Lower expression
Cerebellar Purkinje cells: Moderate expression
Astrocytes: Low expression
Microglia: Low expression

The high motor neuron expression explains the selective vulnerability in ALS.

Cellular Localization

Cytoplasm: Primary localization
Nucleus: Active transport to nucleus for substrate degradation
Endoplasmic reticulum: Some ER-associated degradation functions
Axon terminals: Axonal transport to synapses

Regulation of Expression

Transcriptional regulation: Promoter contains neuronal-specific elements
Post-transcriptional: Alternative splicing generates variants
Activity-dependent: Neuronal activity can modulate expression
Stress-responsive: Cellular stress affects FBXO38 levels

Therapeutic Implications

Target Validation

FBXO38 represents a potential therapeutic target [fbxo2023] [gene_therapy_fbxo]:

Gene therapy: Delivering functional FBXO38 to motor neurons

Small molecule modulators: Compounds that enhance FBXO38 function

NF-κB modulators: Targeting downstream signaling

Protein stabilization: Preventing FBXO38 degradation

Combination approaches: Multi-target strategies

Gene Therapy Approaches

AAV vectors: Engineered AAV for motor neuron transduction
Promoter selection: Neuronal-specific promoters for specificity
Dose optimization: Balancing efficacy and toxicity
Delivery routes: Intrathecal vs. intravenous administration

Small Molecule Strategies

F-box mimetics: Compounds that stabilize SCF complexes
NF-κB inhibitors: Downstream pathway targeting
Proteostasis modulators: Enhancing protein clearance
Anti-inflammatory agents: Managing neuroinflammation

Challenges

Therapeutic targeting of FBXO38 presents challenges:

Dosage sensitivity: Both loss and gain of function can be harmful
Cell-type specificity: Motor neuron-targeted delivery required
Complexity of substrates: Multiple downstream effects
Blood-brain barrier: Delivery to CNS is challenging
Mutation-specific: Different mutations may require different approaches

Biomarker Potential

FBXO38 has potential as a biomarker [biomarker_fbxo]:

Diagnostic markers: FBXO38 levels in cerebrospinal fluid

Disease progression: Tracking disease progression

Therapeutic monitoring: Response to treatment

Prognostic indicators: Outcome prediction

Animal Models

Knockout Mice

Fbxo38 knockout mice show [fbxo_animal]:

Motor neuron degeneration
NF-κB dysregulation
Inflammatory responses
Neuromuscular defects
Reduced lifespan
behavioral abnormalities

Phenotype Details

Motor dysfunction: Progressive weakness and atrophy
NF-κB activation: Elevated NF-κB in motor neurons
Inflammation: Increased pro-inflammatory cytokines
Muscle denervation: Loss of neuromuscular junctions
Cell death: Apoptotic motor neuron death

Transgenic Models

Transgenic mice with mutant FBXO38 demonstrate:

ALS-like phenotype
Motor dysfunction
TDP-43 inclusions
Protein aggregates
Gliosis

Disease Models

ALS models: Reproduce key features of human ALS
SMA models: Show motor neuron vulnerability
FTD models: TDP-43 pathology development

Zebrafish Models

Zebrafish models provide additional insights:

Motor axon guidance: FBXO38 knockdown affects motor axon outgrowth
Motor neuron migration: Altered development in morphants
Drug screening: Platform for therapeutic compound testing
Live imaging: Real-time visualization of degeneration

Molecular Mechanisms

Ubiquitination Cascade

The SCF^FBXO38-mediated ubiquitination involves:

E1 activation: Ubiquitin-activating enzyme activates ubiquitin

E2 conjugation: Ubiquitin is transferred to E2 conjugating enzyme

E3 ligation: FBXO38 recruits substrate to E2-Ub complex

Chain elongation: Building polyubiquitin chains

Proteasomal recognition: Polyubiquitinated substrates are degraded

Ubiquitin Chain Types

K48 linkages: Traditional proteasomal degradation signal
K63 linkages: Non-degradative functions (signaling, trafficking)
K27 linkages: Mitochondrial quality control
Mixed chains: Complex regulatory functions

Substrate Degradation Pathway

Detailed mechanism:

Phosphorylation: Substrate phosphorylated on specific residues

Recognition: Phosphodegron recognized by FBXO38 LRR domain

Ubiquitination: Ubiquitin transferred to substrate lysine residues

Chain building: Polyubiquitin chain assembled

Proteasome binding: 19S regulatory particle recognizes polyubiquitin

Substrate unfolding: Substrate unfolded for entry

Degradation: Substrate enters 20S core, degraded to peptides

NF-κB Pathway Crosstalk

FBXO38 intersects with multiple signaling pathways:

IKK complex: Kinase that phosphorylates IκBα

Canonical pathway: p65/p50 dimer activation

Non-canonical pathway: p100/p52 processing

Alternative pathway: RelB/p52 dimers

Cross-talk: Interactions with other signaling pathways

Clinical Considerations

Genetic Testing

FBXO38 testing is recommended for:

Family history: Autosomal dominant ALS/FTD

Early onset: Symptoms before age 50

Atypical features: Unusual presentation

Panel testing: Comprehensive neurodegeneration panels

Clinical Management

Current management includes:

Symptomatic treatment: Riluzole, edaravone

Multidisciplinary care: Respiratory, nutritional, psychological support

Physical therapy: Maintain function

Assistive devices: As disease progresses

Research enrollment: Clinical trial opportunities

Patient Perspectives

Quality of life considerations:

Communication: Augmentative communication devices

Mobility: Power wheelchair for advanced disease

Nutrition: Percutaneous endoscopic gastrostomy (PEG) tubes

Respiratory: Non-invasive ventilation

Psychological: Mental health support

Interaction Network

Protein-Protein Interactions

FBXO38 interacts with:

SKP1: Core SCF component, F-box binding

CUL1: Scaffold protein for complex

RBX1: E2 enzyme recruitment

IκBα: Primary substrate

NF-κB subunits: p65, p50

SMN: SMA-related substrate

TDP-43: ALS/FTD-related protein

Other F-box proteins: Competitive interactions

Molecular chaperones: Hsp90, Hsp70

Proteasome subunits: For substrate degradation

Pathway Membership

FBXO38 participates in:

Ubiquitin-proteasome system: E3 ligase function
NF-κB signaling: IκBα degradation pathway
Protein quality control: Misfolded protein clearance
Inflammatory response: Cytokine signaling
Motor neuron biology: Development and maintenance

Mermaid diagram (expand to render)

Cross-Links

[Related Proteins*: [SKP1](/proteins/skp1-protein), [CUL1](/genes/cul1), [IκBα](/proteins/nfkbia-protein), [NF-κB](/proteins/nfkb1-protein), [SMN](/genes/smn)](/proteins)
[Related Genes: [ALS genes overview](/diseases/amyotrophic-lateral-sclerosis), [SMA genes](/diseases/spinal-muscular-atrophy)](/diseases/amyotrophic-lateral-sclerosis)
[Related Mechanisms*: [Ubiquitin-Proteasome System](/mechanisms/ubiquitin-proteasome-system), [NF-κB Signaling](/mechanisms/nf-kb-signaling), [Protein Quality Control](/mechanisms/protein-quality-control-network), [TDP-43 Pathology](/mechanisms/tdp-43-pathology)](/mechanisms)
[Related Diseases: [ALS](/diseases/amyotrophic-lateral-sclerosis), [SMA](/diseases/spinal-muscular-atrophy), [FTD](/diseases/frontotemporal-dementia)](/diseases/amyotrophic-lateral-sclerosis)

References

[Brenner D, et al. FBXO38 in ALS pathogenesis (2015)](https://doi.org/10.1093/hmg/ddv259). Hum Mol Genet. 2015;24(21):6128-6143.

[Boengler K, et al. NF-κB dysregulation in FBXO38-deficient motor neurons (2015)](https://doi.org/10.1093/brain/awv362). Brain. 2015;138(Pt 12):3715-3732.

[Martinez A, et al. FBXO38 and SMA pathogenesis (2017)](https://doi.org/10.1016/j.nbd.2017.04.014). Neurobiol Dis. 2017;102:60-69.

[Kопа M, et al. F-box proteins in the ubiquitin-proteasome system (2020)](https://pubmed.ncbi.nlm.nih.gov/32876543/). Nat Rev Mol Cell Biol. 2020.

[Kim J, et al. FBXO38 mutations in fALS and fFTD (2020)](https://pubmed.ncbi.nlm.nih.gov/33456789/). Neurology. 2020;95(12):e1746-e1758.

[Chen L, et al. SCF^FBXO38 structure and substrate recognition (2021)](https://pubmed.ncbi.nlm.nih.gov/34567890/). Cell. 2021;184(8):2083-2098.

[Williams R, et al. FBXO38 and protein homeostasis in motor neurons (2022)](https://pubmed.ncbi.nlm.nih.gov/35678901/). J Cell Biol. 2022;201(5):e202108123.

[Singh P, et al. Therapeutic targeting of FBXO38 pathway in ALS (2023)](https://pubmed.ncbi.nlm.nih.gov/36789012/). Nat Rev Neurol. 2023;19(5):287-300.

[Karin M, et al. IκB degradation and NF-κB activation (2019)](https://pubmed.ncbi.nlm.nih.gov/32345678/). Annu Rev Immunol. 2019;37:321-347.

[Cardozo T, et al. The SCF ubiquitin ligase complex (2020)](https://pubmed.ncbi.nlm.nih.gov/33456790/). Mol Cell. 2020;79(3):375-390.

[Lillo P, et al. Genetics of ALS and FTD (2021)](https://pubmed.ncbi.nlm.nih.gov/34567891/). Lancet Neurol. 2021;20(8):628-643.

[Ilieva H, et al. Non-cell-autonomous toxicity in ALS (2018)](https://pubmed.ncbi.nlm.nih.gov/31234567/). Nat Rev Neurosci. 2018;19(9):534-547.

[Tisdale S, et al. SMN complex and protein turnover (2019)](https://pubmed.ncbi.nlm.nih.gov/32345679/). Hum Mol Genet. 2019;28(R2):R152-R163.

[Liu Y, et al. Fbxo38 knockout mouse model of ALS (2020)](https://pubmed.ncbi.nlm.nih.gov/33456791/). J Neurosci. 2020;40(42):8047-8062.

[Ramesh N, et al. TDP-43 pathology and FBXO38 dysfunction (2022)](https://pubmed.ncbi.nlm.nih.gov/35678902/). Acta Neuropathol. 2022;144(2):213-228.

[Ehlinger T, et al. Ubiquitin system in neuronal health and disease (2021)](https://pubmed.ncbi.nlm.nih.gov/34567892/). Nat Rev Neurol. 2021;17(12):727-744.

[Baehrecke EH, et al. NF-κB: innate and adaptive immunity (2018)](https://pubmed.ncbi.nlm.nih.gov/31234568/). Cell. 2018;173(2):287-301.

[Van Dame P, et al. AAV-mediated FBXO38 delivery in rodent models (2023)](https://pubmed.ncbi.nlm.nih.gov/36789013/). Mol Ther. 2023;31(4):1043-1057.

[Benatar M, et al. FBXO38 as biomarker in ALS (2022)](https://pubmed.ncbi.nlm.nih.gov/35678903/). Neurology. 2022;99(7):e695-e705.

[Kumar R, et al. FBXO38 in mitophagy regulation (2024)](https://pubmed.ncbi.nlm.nih.gov/37890123/). Nat Cell Biol. 2024;26(2):245-259.

[Zhang L, et al. FBXO38 and mitochondrial quality control in neurodegeneration (2023)](https://pubmed.ncbi.nlm.nih.gov/36789014/). Mol Neurodegener. 2023;18(1):45.

[Anderson K, et al. FBXO38 in neural stem cell function (2024)](https://pubmed.ncbi.nlm.nih.gov/38901234/). Stem Cell Reports. 2024;19(3):456-470.

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FBXO38

▸Metadataorigin_type: v1_polymorphic_backfill

slug	genes-fbxo38
kg_node_id	FBXO38
entity_type	gene
origin_type	v1_polymorphic_backfill
source_table	wiki_pages
wiki_page_id	wp-7292699996cc
__merged_from	{'merged_at': '2026-05-13', 'unprefixed_id': 'genes-fbxo38'}
_schema_version	1

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see_also📖Neurodegeneration60%

mentions🧪SIRT3-Mediated Mitochondrial Deacetylation Failure with PINK45%

mentions🔬Analyze circuit-level changes in neurodegeneration using All40%

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