Cryptic Exon Silencing Restoration
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From Analysis:
RNA binding protein dysregulation across ALS FTD and AD
RNA binding protein dysregulation across ALS FTD and AD
Hypotheses from Same Analysis (6)
These hypotheses emerged from the same multi-agent debate that produced this hypothesis.
Description
Mechanistic Overview
Cryptic Exon Silencing Restoration starts from the claim that modulating TARDBP within the disease context of neurodegeneration can redirect a disease-relevant process. The original description reads: "Molecular Mechanism and Rationale The TAR DNA-binding protein 43 (TDP-43), encoded by the TARDBP gene, serves as a critical RNA-binding protein (RBP) that orchestrates complex post-transcriptional regulatory networks essential for neuronal homeostasis. Under physiological conditions, TDP-43 functions as a master regulator of cryptic exon silencing through its preferential binding to UG-rich and GU-rich sequences located within introns and 3' untranslated regions of target transcripts....
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Curated Mechanism Pathway
Curated pathway diagram from expert analysis
flowchart TD
subgraph Normal["✅ Normal TDP-43 Function"]
N1["TDP-43 in Nucleus
(43 kDa, RNA-binding)"] --> N2["Binds UG-rich Intronic
Sequences"]
N2 --> N3["Suppresses Cryptic
Exon Inclusion"]
N3 --> N4["Normal STMN2 mRNA"]
N3 --> N5["Normal UNC13A mRNA"]
N4 --> N6["Stathmin-2 Protein
-> Axonal Stability"]
N5 --> N7["UNC13A Protein
-> Synaptic Transmission"]
end
subgraph Disease["❌ TDP-43 Proteinopathy"]
D1["TDP-43 Nuclear Depletion
(seen in 97% ALS, 45% FTLD)"] --> D2["Cytoplasmic
Aggregation"]
D1 --> D3["Loss of Splicing
Regulation"]
D3 --> D4["Cryptic Exon Inclusion
in STMN2 (Exon 2a/2b)"]
D3 --> D5["Cryptic Exon Inclusion
in UNC13A (Intron 20/21)"]
D4 --> D6["Premature Stop Codon
-> NMD Activation"]
D5 --> D7["Premature Stop Codon
-> NMD Activation"]
D6 --> D8["STMN2 Loss
(>90% reduction)"]
D7 --> D9["UNC13A Loss
(>80% reduction)"]
D8 --> D10["Axonal Degeneration"]
D9 --> D11["Synaptic Failure"]
D10 --> D12["Motor Neuron Death"]
D11 --> D12
end
subgraph Genetic["🧬 Genetic Modifiers"]
G1["UNC13A rs12973192
(GWAS risk SNP)"] --> G2["Creates Stronger
Cryptic Splice Site"]
G2 --> D5
G3["STMN2 Variants
(under investigation)"] -.-> D4
end
subgraph Therapy["💊 Therapeutic Approaches"]
T1["Antisense Oligonucleotides
(ASO targeting cryptic exon)"]
T2["Small Molecule Splicing
Modulators (risdiplam-like)"]
T3["AAV Gene Therapy
(STMN2 replacement)"]
T4["TDP-43 Nuclear
Retention Strategies"]
end
T1 -.->|"block cryptic
splice site"| D4
T1 -.->|"block cryptic
splice site"| D5
T2 -.->|"modulate
splicing"| D3
T3 -.->|"restore
protein"| D8
T4 -.->|"prevent
depletion"| D1
style N1 fill:#4fc3f7,color:#000
style N6 fill:#81c784,color:#000
style N7 fill:#81c784,color:#000
style D1 fill:#ef5350,color:#fff
style D2 fill:#ff8a65,color:#000
style D12 fill:#ef5350,color:#fff
style G1 fill:#ce93d8,color:#000
style T1 fill:#81c784,color:#000
style T2 fill:#81c784,color:#000
style T3 fill:#81c784,color:#000
style T4 fill:#81c784,color:#000
3D Protein Structure
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Dimension Scores
Legacy Card View — expandable citation cards
✓ Supporting Evidence 15
Amyotrophic lateral sclerosis (ALS) is a rapidly progressing neurodegenerative disease that is characterized by motor neuron loss and that leads to paralysis and death 2-5 years after disease onset. Nearly all patients with ALS have aggregates of the RNA-binding protein TDP-43 in their brains and spinal cords, and rare mutations in the gene encoding TDP-43 can cause ALS. There are no effective TDP-43-directed therapies for ALS or related TDP-43 proteinopathies, such as frontotemporal dementia. Antisense oligonucleotides (ASOs) and RNA-interference approaches are emerging as attractive therapeutic strategies in neurological diseases. Indeed, treatment of a rat model of inherited ALS (caused by a mutation in Sod1) with ASOs against Sod1 has been shown to substantially slow disease progression. However, as SOD1 mutations account for only around 2-5% of ALS cases, additional therapeutic strategies are needed. Silencing TDP-43 itself is probably not appropriate, given its critical cellular
Amyotrophic lateral sclerosis (ALS) is an adult-onset motor neuron disease with a mean survival time of three years. The 97% of the cases have TDP-43 nuclear depletion and cytoplasmic aggregation in motor neurons. TDP-43 prevents non-conserved cryptic exon splicing in certain genes, maintaining transcript stability, including ATG4B, which is crucial for autophagosome maturation and Microtubule-associated proteins 1A/1B light chain 3B (LC3B) homeostasis. In ALS mice (G93A), Atg4b depletion worsens survival rates and autophagy function. For the first time, we observed an elevation of LC3ylation in the CNS of both ALS patients and atg4b-/- mouse spinal cords. Furthermore, LC3ylation modulates the distribution of ATG3 across membrane compartments. Antisense oligonucleotides (ASOs) targeting cryptic exon restore ATG4B mRNA in TARDBP knockdown cells. We further developed multi-target ASOs targeting TDP-43 binding sequences for a broader effect. Importantly, our ASO based in peptide-PMO conju
Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease characterized by the selective death of motor neurons, which causes muscle atrophy. Genetic forms of ALS are recorded only in 10% of cases. However, over the past decade, studies in genetics have substantially contributed to our understanding of the molecular mechanisms underlying ALS. The identification of key mutations such as SOD1, C9orf72, FUS, and TARDBP has led to the development of targeted therapy that is gradually being introduced into clinical trials, opening up a broad range of opportunities for correcting these mutations. In this review, we aimed to present an extensive overview of the currently known mechanisms of motor neuron degeneration associated with mutations in these genes and also the gene therapy methods for inhibiting the expression of their mutant proteins. Among these, antisense oligonucleotides, RNA interference (siRNA and miRNA), and gene-editing (CRISPR/Cas9) methods are of particular interes
Selective Silencing of TDP-43 P. G376D Mutation Reverses Key Amyotrophic Lateral Sclerosis-Related Cellular De… MEDIUM▼
Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease for which there is currently no cure. Dominant mutations in the TARDBP gene are causative of ALS. In particular, the p. G376D substitution in TDP-43 causes familial ALS and it is associated with TDP-43 mislocalization in the cytosol, increased presence of cytoplasmic aggregates, and lysosomal and mitochondrial dysfunction. We previously designed a small interfering RNA (siRNA) that specifically targets and silences the mutant allele and we demonstrated that, in patient-derived fibroblasts, it can reduce TDP-43 aggregation, decrease oxidative stress, and improve cell viability. Here, we investigated the ability of this siRNA to revert some ALS-associated pathological phenotypes in motor neurons derived from induced pluripotent stem cells (iPSCs), as motor neurons are the primary cells affected in ALS. siRNA treatment reduced TDP-43 mislocalization, enhanced lysosomal function and cell viability, and decreased oxidative s
Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disorder characterized by progressive loss of upper and lower motor neurons. Despite marked genetic and pathological heterogeneity, a unifying pathogenic framework remains lacking. We propose that axonal transport impairment represents an early and convergent but genotype-modulated upstream vulnerability in ALS, contributing to distal synaptic failure, bioenergetic stress, protein aggregation, neuroinflammation, and neuronal death. Across many ALS models, including SOD1, TARDBP (TDP-43), FUS, and C9orf72, transport deficits are frequently detectable in presymptomatic stages, often preceding overt motor neuron loss or clinical manifestation, although temporal ordering varies by molecular subtype. Human data from induced pluripotent stem cell-derived motor neurons and neuroimaging in mutation carriers further support early transport dysfunction in both familial and sporadic ALS. We synthesize genetic, cellular, and systems-
TDP-43 pathology is a hallmark of fatal neurodegenerative disorders, including amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), and limbic-predominant age-related TDP-43-encephalopathy (LATE). In affected patients, cytoplasmic TDP-43 aggregates are accompanied by disruption of its normal nuclear localization and function. Because TDP-43 is an RNA binding protein that controls transcript processing, including repression of cryptic exon splicing, its loss leads to dysregulation of gene expression. Despite its central significance in disease, the connection between TDP-43 aggregation and dysfunction remains poorly understood, and models to study the underlying mechanisms are limited. Here, we characterize a robust and quantitative cell-based reporter that captures both aggregation and the resulting loss of function. Using this human biosensor cell line, we show that aggregation initiated by prion-like seeding drives progressive depletion of nuclear TDP-43 and induces si
Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disorder characterized by progressive motor neuron degeneration and cytoplasmic mislocalization of TDP-43. While metabolic dysfunction is increasingly recognized in ALS, the mechanistic link between impaired energy metabolism and TDP-43 pathology remains unknown. Here, we show that cytoplasmic TDP-43 directly disrupts glycolysis by targeting hexokinase 1 (HK1), the first rate-limiting enzyme of the pathway. In cells expressing a TDP-43 variant lacking its nuclear localization signal and in patient-derived iPSC motor neurons, TDP-43 accumulation in the cytoplasm reduces glycolytic capacity, indicating a neuron-intrinsic metabolic defect. Across cellular models including patient-derived neurons, TDP-43 mutant mice, and postmortem spinal cord tissue from ALS patients, we observe consistent decreases in HK1 protein level, mitochondrial association, and enzymatic activity, despite unchanged transcript levels. Mechanistically,
Cytoplasmic TDP-43 pathology is a pathological sign of ALS/ALS-FTD and a converging disease event across different genotypes, phenotypes and CNS areas. To understand this process and target it therapeutically, we need to define which cell types are affected and which cell-type specific effects make them particularly vulnerable. We coupled flow-cytometry nuclear sorting and sequencing with single-nucleus multi-omic ATAC-seq and RNA-seq and spatial transcriptomics to define the transcriptional cell type of affected neurons in the post-mortem ALS/ALS-FTD motor cortex (30 ALS, 20 ALS-FTD & 32 control samples). Here, we show that mainly excitatory cortical neurons are affected by TDP-43 pathology and define the cell types that are affected the most: intratelencephalic L2-L3-LINC00507-FREM3, L3-L5-RORB-LNX2, L3-L5-RORB-ADGRL4 & L6-THEMIS-LINC00343 neurons and extratelencephalic L5-FEZF2-NTNG1 neurons. Transcriptional aberrations by TDP-43 pathology, like cryptic exon inclusion, are cell-type
Demonstrates TDP-43-dependent cryptic splicing mechanism by identifying a neurotoxic cryptic peptide arising f…▼
Identifies cryptic exon-derived peptides as potential diagnostic markers for ALS, supporting the hypothesis's …▼
Demonstrates antisense oligonucleotide targeting of splicing axis, aligning with the hypothesis's therapeutic …▼
✗ Opposing Evidence 7
PURPOSE OF REVIEW: Amyotrophic lateral sclerosis (ALS) has a strong genetic basis, but the genetic landscape of ALS appears to be complex. The purpose of this article is to review recent developments in the genetics of ALS. RECENT FINDINGS: Large-scale genetic studies have uncovered more than 40 genes contributing to ALS susceptibility. Both rare variants with variable effect size and more common variants with small effect size have been identified. The most common ALS genes are C9orf72 , SOD1 , TARDBP and FUS . Some of the causative genes of ALS are shared with frontotemporal dementia, confirming the molecular link between both diseases. Access to diagnostic gene testing for ALS has to improve, as effective gene silencing therapies for some genetic subtypes of ALS are emerging, but there is no consensus about which genes to test for. SUMMARY: Our knowledge about the genetic basis of ALS has improved and the first effective gene silencing therapies for specific genetic subtypes of ALS
Variants of UNC13A, a critical gene for synapse function, increase the risk of amyotrophic lateral sclerosis and frontotemporal dementia1-3, two related neurodegenerative diseases defined by mislocalization of the RNA-binding protein TDP-434,5. Here we show that TDP-43 depletion induces robust inclusion of a cryptic exon in UNC13A, resulting in nonsense-mediated decay and loss of UNC13A protein. Two common intronic UNC13A polymorphisms strongly associated with amyotrophic lateral sclerosis and frontotemporal dementia risk overlap with TDP-43 binding sites. These polymorphisms potentiate cryptic exon inclusion, both in cultured cells and in brains and spinal cords from patients with these conditions. Our findings, which demonstrate a genetic link between loss of nuclear TDP-43 function and disease, reveal the mechanism by which UNC13A variants exacerbate the effects of decreased TDP-43 function. They further provide a promising therapeutic target for TDP-43 proteinopathies.
BACKGROUND: Genetic studies are challenging in many complex diseases, particularly those with limited diagnostic certainty, low prevalence or of old age. The result is that genes may be reported as disease-causing with varying levels of evidence, and in some cases, the data may be so limited as to be indistinguishable from chance findings. When there are large numbers of such genes, an objective method for ranking the evidence is useful. Using the neurodegenerative and complex disease amyotrophic lateral sclerosis (ALS) as a model, and the disease-specific database ALSoD, the objective is to develop a method using publicly available data to generate a credibility score for putative disease-causing genes. METHODS: Genes with at least one publication suggesting involvement in adult onset familial ALS were collated following an exhaustive literature search. SQL was used to generate a score by extracting information from the publications and combined with a pathogenicity analysis using bio
The cytoplasmic accumulation of TDP-43 aggregates remains a persistent pathological hallmark of neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), and limbic-predominant age-related TDP-43 encephalopathy (LATE). The cell's natural clearance mechanisms, the Ubiquitin-Proteasome System (UPS) and the autophagy-lysosome pathway (ALP), are hypothesized to fail, at least in part, due to the sequestration of key components of these pathways by pathological TDP-43 species, thereby impairing autophagosome-lysosome fusion and lysosomal competence. Classical autophagic activators (e.g., rapamycin) can initiate upstream steps in the pathway but cannot address downstream flux bottlenecks, limiting their ability to restore effective TDP-43 clearance. This review revisits classical strategies and discusses newer approaches to modulate TDP-43 clearance, including transcription factor EB (TFEB) activators, proteolysis-targeting chimeras (PROTACs),
Amyotrophic lateral sclerosis is a complex neurodegenerative disease affecting motor neurons, characterized by the involvement of various factors, including oxidative stress, inflammatory processes, glutamate excitotoxicity, mitochondrial dysfunction, protein aggregation, axonal transport abnormalities, and apoptosis. The complexity of amyotrophic lateral sclerosis arises from its multifactorial aetiology involving diverse genetic, protein, metabolic, and cellular alterations. Mutations of different genes, such as SOD1, C9ORF72, TARDBP, and FUS, have been identified as critical contributors to disease pathophysiology through their facilitation of aberrant protein misfolding and aggregation. All these factors disrupt glutamate homeostasis, leading to calcium-mediated neurotoxicity. Under oxidative stress, motor neurons exhibit a diminished capacity to regulate calcium influx, along with impaired functioning of the mitochondria and endoplasmic reticulum, further compromising cellular int
Amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) are progressive neurodegenerative diseases characterized by the nuclear clearance and cytoplasmic aggregation of transactive response DNA/RNA-binding protein of 43 kDa (TDP43). Alternative splicing of TARDBP, the gene encoding TDP43, leads to a surprising diversity of RNA and protein isoforms with unique functions and potential implications for disease pathogenesis. Here, we review the production, properties, and functional consequences of alternative splicing in the development of ALS and FTD, focusing primarily on TDP43 due to its integral connection with the pathogenesis of sporadic as well as familial forms of these diseases. We synthesize current evidence on the biology of alternative TARDBP splicing, highlight key questions regarding its role in TDP43 proteinopathies such as ALS and FTD, and touch on the larger phenomenon of alternative splicing and its relationship to disease.
Failed to rescue disease phenotypes in TDP-43 model mice, challenging the effectiveness of targeted interventi…▼
🧬 Theorist Proposes novel mechanisms and generates creative hypotheses ▼
Novel Therapeutic Hypotheses for RNA Binding Protein Dysregulation in Neurodegeneration
1. Stress Granule Phase Separation Modulators
Target: G3BP1/2, TIA1, TIAR Mechanism: Pharmacological modulation of liquid-liquid phase separation dynamics to prevent pathological stress granule persistence and restore RNA homeostasis. Description: Small molecules that enhance stress granule dissolution kinetics could prevent the chronic sequestration of RNA-binding proteins and maintain cytoplasmic RNA processing. This approach targets the biophysical properties of ribonucleoprotein conden🔍 Skeptic Identifies weaknesses, alternative explanations, and methodological concerns ▼
Critical Evaluation of RNA Binding Protein Therapeutic Hypotheses
1. Stress Granule Phase Separation Modulators
Specific Weaknesses:
- Temporal specificity problem: No evidence provided for when to intervene - early stress granules may be protective while persistent ones are pathological
- Target selectivity: G3BP1/2 knockout is embryonic lethal (PMID: 28424515), suggesting these proteins have essential functions that blanket inhibition would disrupt
- Dosage sensitivity: Phase separation is exquisitely sensitive to protein concentration; small perturbations could cause
🎯 Domain Expert Assesses practical feasibility, druggability, and clinical translation ▼
Druggability Assessment of RNA Binding Protein Therapeutic Hypotheses
1. Stress Granule Phase Separation Modulators (Confidence: 0.55)
Druggability Assessment: MODERATE
Target proteins: G3BP1/2, TIA1, TIAR are challenging targets due to:- Lack of deep binding pockets (intrinsically disordered regions dominate)
- Phase separation driven by weak multivalent interactions
- Essential cellular functions make selective modulation difficult
- Existing tool compounds:
- ISRIB (integrated stress response inhibitor, targets eIF2B) - modulates upstream str
⚖ Synthesizer Integrates perspectives and produces final ranked assessments ▼
Price History
| Event | Price | Change | Source | Time | |
|---|---|---|---|---|---|
| 📄 | New Evidence | $0.487 | ▲ 1.5% | evidence_batch_update | 2026-04-13 02:18 |
| 📄 | New Evidence | $0.480 | ▲ 3.8% | evidence_batch_update | 2026-04-13 02:18 |
| ⚖ | Recalibrated | $0.462 | ▼ 0.9% | 2026-04-12 05:13 | |
| ⚖ | Recalibrated | $0.467 | ▼ 1.2% | 2026-04-10 15:58 | |
| ⚖ | Recalibrated | $0.472 | ▲ 1.4% | 2026-04-10 15:53 | |
| ⚖ | Recalibrated | $0.466 | ▼ 1.9% | 2026-04-08 18:39 | |
| ⚖ | Recalibrated | $0.475 | ▼ 0.4% | 2026-04-06 04:04 | |
| ⚖ | Recalibrated | $0.477 | ▼ 0.7% | 2026-04-04 16:38 | |
| ⚖ | Recalibrated | $0.480 | ▼ 1.5% | 2026-04-04 16:02 | |
| 📄 | New Evidence | $0.487 | ▲ 1.9% | evidence_batch_update | 2026-04-04 09:08 |
| ⚖ | Recalibrated | $0.478 | ▼ 37.0% | 2026-04-03 23:46 | |
| 📄 | New Evidence | $0.759 | ▲ 0.6% | evidence_batch_update | 2026-04-03 01:06 |
| ⚖ | Recalibrated | $0.754 | ▲ 7.7% | market_dynamics | 2026-04-03 01:06 |
| 📄 | New Evidence | $0.700 | ▲ 2.2% | evidence_batch_update | 2026-04-03 01:06 |
| ⚖ | Recalibrated | $0.685 | ▲ 36.7% | market_dynamics | 2026-04-03 01:06 |
Clinical Trials (13) Relevance: 57%
Active
Completed
Total Enrolled
Highest Phase
📚 Cited Papers (48)
📓 Linked Notebooks (2)
Wiki Pages
KG Entities (35)
Dependency Graph (1 upstream, 5 downstream)
Linked Experiments (10)
Related Hypotheses
Estimated Development
🧪 Falsifiable Predictions (4)
Knowledge Subgraph (75 edges)
associated with (4)
catalyzes (1)
co associated with (16)
co discussed (32)
▸ Show 27 more
disrupted in (1)
dysregulated in (1)
implicated in (7)
▸ Show 2 more
mediates (1)
mutation causes (1)
participates in (4)
Mechanism Pathway for TARDBP
Molecular pathway showing key causal relationships underlying this hypothesis
graph TD
SETX["SETX"] -->|co discussed| TARDBP["TARDBP"]
TARDBP_1["TARDBP"] -->|co discussed| HNRNPA2B1["HNRNPA2B1"]
TARDBP_2["TARDBP"] -->|co discussed| NPM1["NPM1"]
TARDBP_3["TARDBP"] -->|co discussed| SYNCRIP["SYNCRIP"]
APOE4["APOE4"] -->|co discussed| TARDBP_4["TARDBP"]
TARDBP_5["TARDBP"] -->|co discussed| TREM2["TREM2"]
NPM1_6["NPM1"] -->|co discussed| TARDBP_7["TARDBP"]
TARDBP_8["TARDBP"] -->|co discussed| SETX_9["SETX"]
HNRNPA2B1_10["HNRNPA2B1"] -->|co discussed| TARDBP_11["TARDBP"]
SYNCRIP_12["SYNCRIP"] -->|co discussed| TARDBP_13["TARDBP"]
G3BP1["G3BP1"] -->|co associated with| TARDBP_14["TARDBP"]
HNRNPA2B1_15["HNRNPA2B1"] -->|co associated with| TARDBP_16["TARDBP"]
NPM1_17["NPM1"] -->|co associated with| TARDBP_18["TARDBP"]
SETX_19["SETX"] -->|co associated with| TARDBP_20["TARDBP"]
SYNCRIP_21["SYNCRIP"] -->|co associated with| TARDBP_22["TARDBP"]
style SETX fill:#ce93d8,stroke:#333,color:#000
style TARDBP fill:#ce93d8,stroke:#333,color:#000
style TARDBP_1 fill:#ce93d8,stroke:#333,color:#000
style HNRNPA2B1 fill:#ce93d8,stroke:#333,color:#000
style TARDBP_2 fill:#ce93d8,stroke:#333,color:#000
style NPM1 fill:#ce93d8,stroke:#333,color:#000
style TARDBP_3 fill:#ce93d8,stroke:#333,color:#000
style SYNCRIP fill:#ce93d8,stroke:#333,color:#000
style APOE4 fill:#ce93d8,stroke:#333,color:#000
style TARDBP_4 fill:#ce93d8,stroke:#333,color:#000
style TARDBP_5 fill:#ce93d8,stroke:#333,color:#000
style TREM2 fill:#ce93d8,stroke:#333,color:#000
style NPM1_6 fill:#ce93d8,stroke:#333,color:#000
style TARDBP_7 fill:#ce93d8,stroke:#333,color:#000
style TARDBP_8 fill:#ce93d8,stroke:#333,color:#000
style SETX_9 fill:#ce93d8,stroke:#333,color:#000
style HNRNPA2B1_10 fill:#ce93d8,stroke:#333,color:#000
style TARDBP_11 fill:#ce93d8,stroke:#333,color:#000
style SYNCRIP_12 fill:#ce93d8,stroke:#333,color:#000
style TARDBP_13 fill:#ce93d8,stroke:#333,color:#000
style G3BP1 fill:#ce93d8,stroke:#333,color:#000
style TARDBP_14 fill:#ce93d8,stroke:#333,color:#000
style HNRNPA2B1_15 fill:#ce93d8,stroke:#333,color:#000
style TARDBP_16 fill:#ce93d8,stroke:#333,color:#000
style NPM1_17 fill:#ce93d8,stroke:#333,color:#000
style TARDBP_18 fill:#ce93d8,stroke:#333,color:#000
style SETX_19 fill:#ce93d8,stroke:#333,color:#000
style TARDBP_20 fill:#ce93d8,stroke:#333,color:#000
style SYNCRIP_21 fill:#ce93d8,stroke:#333,color:#000
style TARDBP_22 fill:#ce93d8,stroke:#333,color:#000
3D Protein Structure
🧬 TARDBP — PDB 4BS2 Click to expand 3D viewer
Source Analysis
RNA binding protein dysregulation across ALS FTD and AD
neurodegeneration | 2026-04-01 | completed
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