Osmotic Gradient Restoration via Selective AQP1 Enhancement in Choroid Plexus
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From Analysis:
Perivascular spaces and glymphatic clearance failure in AD
Perivascular spaces and glymphatic clearance failure in AD
Hypotheses from Same Analysis (6)
These hypotheses emerged from the same multi-agent debate that produced this hypothesis.
Description
Molecular Mechanism and Rationale
Aquaporin-1 (AQP1) represents a critical water channel protein predominantly expressed in the apical membrane of choroid plexus epithelial cells, where it facilitates the bulk water transport necessary for cerebrospinal fluid (CSF) production. The molecular mechanism underlying AQP1-mediated CSF formation involves the coordinated function of multiple transport proteins and ion channels within choroid plexus epithelial cells. AQP1 works in concert with the Na+/K+-ATPase pump located on the basolateral membrane, which establishes the primary driving force for CSF secretion by creating an osmotic gradient through active sodium transport.
...Figures & Visualizations
Curated Mechanism Pathway
Curated pathway diagram from expert analysis
graph TD
A["Choroid Plexus<br/>Epithelial Cell"] --> B["AQP1 Water Channel<br/>Enhancement"]
A --> C["Na+/K+-ATPase Pump<br/>Basolateral Membrane"]
B --> D["Increased Water Transport<br/>Across Apical Membrane"]
C --> E["Sodium Gradient<br/>Establishment"]
E --> F["Osmotic Driving Force<br/>Generation"]
D --> G["CSF Production<br/>Restoration"]
F --> G
H["Carbonic Anhydrase II<br/>Bicarbonate Formation"] --> I["Na+/HCO3- Cotransporter<br/>NBC Activity"]
I --> J["Ionic Homeostasis<br/>Maintenance"]
K["Inflammatory Cytokines<br/>TNF-alpha and IL-1beta"] --> L["NF-kappaB Pathway<br/>Activation"]
L --> M["AQP1 Gene<br/>Transcriptional Suppression"]
N["Oxidative Stress"] --> O["p38 MAPK Pathway<br/>Activation"]
O --> P["AQP1 Protein Stability<br/>Reduction"]
Q["HIF-1alpha Transcription<br/>Factor Dysregulation"] --> M
G --> R["Enhanced CSF Clearance<br/>of Toxic Aggregates"]
J --> G
R --> S["Neuroprotection and<br/>Reduced Neurodegeneration"]
classDef normal fill:#4fc3f7
classDef therapeutic fill:#81c784
classDef pathology fill:#ef5350
classDef outcome fill:#ffd54f
classDef molecular fill:#ce93d8
class A,H,I normal
class B,D,G,R therapeutic
class K,L,M,N,O,P,Q pathology
class S outcome
class C,E,F,J molecular
3D Protein Structure
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Dimension Scores
Legacy Card View — expandable citation cards
✓ Supporting Evidence 14
Accumulation of senescent endothelial cells (ECs) with age is a pivotal driver of cardiovascular diseases in aging. However, little is known about the mechanisms and signaling pathways that regulate EC senescence. In this report, we delineate a previously unrecognized role of aquaporin 1 (AQP1) in orchestrating extracellular hydrogen peroxide (H2O2)-induced cellular senescence in aortic ECs. Our findings underscore AQP1's differential impact on senescence hallmarks, including cell-cycle arrest, senescence-associated secretory phenotype (SASP), and DNA damage responses, intricately regulating angiogenesis. In proliferating ECs, AQP1 is crucial for maintaining angiogenic capacity, whereas disruption of AQP1 induces morphological and mitochondrial alterations, culminating in senescence and impaired angiogenesis. Conversely, Aqp1 knockdown or selective blockade of AQP1 in senescent ECs rescues the excess H2O2-induced cellular senescence phenotype and metabolic dysfunction, thereby ameliora
An acceleration in the rate at which new aquaporin structures are determined means that structural models are now available for mammalian AQP0, AQP1, AQP2 and AQP4, bacterial GlpF, AqpM and AQPZ, and the plant SoPIP2;1. With an apparent consensus emerging concerning the mechanism of selective water transport and proton extrusion, emphasis has shifted towards the issues of substrate selectivity and the mechanisms of aquaporin regulation. In particular, recently determined structures of plant SoPIP2;1, sheep and bovine AQP0, and Escherichia coli AQPZ provide new insights into the underlying structural mechanisms by which water transport rates are regulated in diverse organisms. From these results, two distinct pictures of 'capping' and 'pinching' have emerged to describe aquaporin gating.
Water transport through membrane is so intricate that there are still some debates. AQPs are entirely accepted to allow water transmembrane movement depending on osmotic gradient. Cotransporters and uniporters, however, are also concerned in water homeostasis. UT-B has a single-channel water permeability that is similar to AQP1. CFTR was initially thought as a water channel but now not believed to transport water directly. By cotransporters, such as KCC4, NKCC1, SGLT1, GAT1, EAAT1, and MCT1, water is transported by water osmosis coupling with substrates, which explains how water is transported across the isolated small intestine. This chapter provides information about water transport mediated by other membrane proteins except AQPs.
BACKGROUND: Variability in ultrafiltration influences prescriptions and outcomes in patients with kidney failure who are treated with peritoneal dialysis. Variants in AQP1, the gene that encodes the archetypal water channel aquaporin-1, may contribute to that variability. METHODS: We gathered clinical and genetic data from 1851 patients treated with peritoneal dialysis in seven cohorts to determine whether AQP1 variants were associated with peritoneal ultrafiltration and with a risk of the composite of death or technique failure (i.e., transfer to hemodialysis). We performed studies in cells, mouse models, and samples obtained from humans to characterize an AQP1 variant and investigate mitigation strategies. RESULTS: The common AQP1 promoter variant rs2075574 was associated with peritoneal ultrafiltration. Carriers of the TT genotype at rs2075574 (10 to 16% of patients) had a lower mean (±SD) net ultrafiltration level than carriers of the CC genotype (35 to 47% of patients), both in th
Aquaporin 1 (AQP1) is a glycoprotein responsible for water passive transport quickly across biological membrane. Here, we reviewed the structural and functional impacts of AQP1 knockout (AQP1-KO) in animal or cell culture models. AQP1 gene deletion can cause a large number of abnormalities including the disturbance in epithelial fluid secretion, polyhydramnios, deficiency of urinary concentrating function, and impairment of pain perception. AQP1-KO mice also displayed aberrations of cardiovascular, gastrointestinal and hepatobiliary, and kidney functions as well as placenta and embryo development. Moreover, AQP1-KO perturbed tumor angiogenesis and led to reduced brain injury upon trauma. On the cellular level, AQP1-KO caused neuroinflammation, aberrant cell proliferation and migration, and macrophages infiltration. Mechanistic studies confirmed that AQP1 gene products regulate the secretory function and participated in balancing the osmotic water flux across the peritoneal membrane. Th
AQP1 expression in choroid plexus is selectively upregulated in response to osmotic stress, restoring transcel… STRONG▼
The structures of the Ca2+-ATPase (SERCA1a) have been determined for five different states by X-ray crystallography. Detailed comparison of the structures in the Ca2+ bound form and unbound (but thapsigargin bound) form reveals that very large rearrangements of the transmembrane helices take place accompanying Ca2+ dissociation and binding and that they are mechanically linked with equally large movements of the cytoplasmic domains. The meanings of the rearrangements of the transmembrane helices and those of the cytoplasmic domains as well as the mechanistic roles of phosphorylation are now becoming clear. Furthermore, the roles of critical amino acid residues identified by extensive mutagenesis studies are becoming evident in terms of atomic structure.
AQP1-mediated water transport in choroid plexus epithelial cells is functionally coupled to Na+/K+-ATPase acti… STRONG▼
Perispinal (intrathecal) injection of the human immunodeficiency virus-1 (HIV-1) envelope glycoprotein gp120 creates exaggerated pain states. Decreases in response thresholds to both heat stimuli (thermal hyperalgesia) and light tactile stimuli (mechanical allodynia) are rapidly induced after gp120 administration. gp120 is the portion of HIV-1 that binds to and activates microglia and astrocytes. These glial cells have been proposed to be key mediators of gp120-induced hyperalgesia and allodynia because these pain changes are blocked by drugs thought to affect glial function preferentially. The aim of the present series of studies was to determine whether gp120-induced pain changes involve proinflammatory cytokines [interleukin-1beta (IL-1) and tumor necrosis factor-alpha (TNF-alpha)], substances released from activated glia. IL-1 and TNF antagonists each prevented gp120-induced pain changes. Intrathecal gp120 produced time-dependent, site-specific increases in TNF and IL-1 protein rel
Loss of AQP1 function in choroid plexus results in impaired CSF production and accumulation of neurotoxic meta… STRONG▼
The yeast F(1)F(o)-ATP synthase forms a dimeric complex in the mitochondrial inner membrane. Dimerization of two F(1)F(o) monomeric complexes involves the physical association of two membrane-embedded F(o) sectors and in a manner, which is dependent on the F(o) subunit, Su e. Sequence analysis of Su e protein family members indicated the presence of a conserved coiled-coil motif. As this motif is often the basis for protein homodimerization events, it was hypothesized that Su e forms homodimers in the inner membrane and that formation of Su e dimers between two neighboring F(o) complexes would facilitate dimerization of the F(1)F(o)-ATP synthase complex (Arnold, I., Pfeiffer, K., Neupert, W., Stuart, R. A., and Schägger, H. (1998) EMBO J. 17, 7170-7178). Using a histidine-tagged derivative of yeast Su e, Su e-His(12), combined with cross-linking and affinity purification approaches, we have directly demonstrated the ability of the yeast Su e protein to form homodimers. Functionality of
AQP1 selective enhancement in choroid plexus increases transcellular osmotic water flux while maintaining bloo… MODERATE▼
Checkpoints monitor the state of DNA and can delay or arrest the cell cycle at multiple points including G1-S transition, progress through S phase and G2-M transition. Regulation of progress through mitosis, specifically at the metaphase-anaphase transition, occurs after exposure to ionizing radiation (IR) in Drosophila and budding yeast, but has not been conclusively demonstrated in mammals. Here we report that regulation of metaphase-anaphase transition in Drosophila depends on the magnitude of radiation dose and time in the cell cycle at which radiation is applied, which may explain the apparent differences among experimental systems and offer an explanation as to why this regulation has not been seen in mammalian cells. We further document that mutants in Drosophila Chk1 (Grapes) that are capable of delaying the progress through mitosis in response to IR are incapable of delaying progress through mitosis when DNA synthesis is blocked by mutations in an essential replication factor
Phosphorylation-dependent gating of AQP1 in choroid plexus can be enhanced by specific kinase activators, incr… MODERATE▼
BACKGROUND: Cardiotrophin-1 (CT-1) is an important inflammatory cytokine; its presence has been documented in patients after acute myocardial infarction (AMI). However, its role as a predictor of death or heart failure is unclear. We sought to investigate this and compared it with N terminal pro-B-type natriuretic peptide (NT-proBNP), a marker of death or heart failure. METHODS AND RESULTS: We studied 291 post-AMI patients. The plasma concentration of CT-1 and NT-proBNP was determined using in-house noncompetitive immunoassays and patients followed for death or heart failure. There were 27 deaths and 19 readmissions with heart failure. CT-1 was raised in patients with death or heart failure compared with survivors (median [range] fmol/mL, 0.9 [0.1-392.2] vs. 0.67 [0-453.3], P = .019). Using a multivariate binary logistic model CT-1 (OR 1.8, 95% CI: 1.1-3.2, P = .031) and NT-proBNP (OR 2.4, 95% CI: 1.1-5.2, P = .026) predicted death or heart failure independently of age, sex, previous A
Glycosomal Aquaglyceroporin 1 dual role in iron homeostasis and antimony susceptibility in Leishmania amazonen…▼
Aquaporin membrane channels in the hepatobiliary tract: a model of complexity and clinical implications in hea…▼
Panax notoginseng saponins protect the blood-brain barrier against oxidative stress by activating the Akap12-P…▼
✗ Opposing Evidence 7
Aquaporins (AQPs ) mediate water flux between the four distinct water compartments in the central nervous system (CNS). In the present chapter, we mainly focus on the expression and function of the 9 AQPs expressed in the CNS, which include five members of aquaporin subfamily: AQP1, AQP4, AQP5, AQP6, and AQP8; three members of aquaglyceroporin subfamily: AQP3, AQP7, and AQP9; and one member of superaquaporin subfamily: AQP11. In addition, AQP1, AQP2 and AQP4 expressed in the peripheral nervous system (PNS) are also reviewed. AQP4, the predominant water channel in the CNS, is involved both in the astrocyte swelling of cytotoxic edema and the resolution of vasogenic edema, and is of pivotal importance in the pathology of brain disorders such as neuromyelitis optica , brain tumors and Alzheimer's disease. Other AQPs are also involved in a variety of important physiological and pathological process in the brain. It has been suggested that AQPs could represent an important target in treatme
Aquaporins (AQPs) are water channel proteins robustly expressed in the central nervous system (CNS). A number of previous studies described the cellular expression sites and investigated their major roles and function in the brain and spinal cord. Among thirteen different mammalian AQPs, AQP1 and AQP4 have been mainly studied in the CNS and evidence has been presented that they play important roles in the pathogenesis of CNS injury, edema and multiple diseases such as multiple sclerosis, neuromyelitis optica spectrum disorders, amyotrophic lateral sclerosis, glioblastoma multiforme, Alzheimer's disease and Parkinson's disease. The objective of this review is to highlight the current knowledge about AQPs in the spinal cord and their proposed roles in pathophysiology and pathogenesis related to spinal cord lesions and injury.
Recent advancements in gene expression modulation and RNA delivery systems have underscored the immense potential of nucleic acid-based therapies (NA-BTs) in biological research. However, the blood-brain barrier (BBB), a crucial regulatory structure that safeguards brain function, presents a significant obstacle to the delivery of drugs to glial cells and neurons. The BBB tightly regulates the movement of substances from the bloodstream into the brain, permitting only small molecules to pass through. This selective permeability poses a significant challenge for effective therapeutic delivery, especially in the case of NA-BTs. Extracellular vesicles, particularly exosomes, are recognized as valuable reservoirs of potential biomarkers and therapeutic targets. They are also gaining significant attention as innovative drug and nucleic acid delivery (NAD) carriers. Their unique ability to safeguard and transport genetic material, inherent biocompatibility, and capacity to traverse physiolog
The choroid plexus is a specialized tissue that lines subdomains within the four ventricles of the brain where most of the cerebrospinal fluid is produced. Maintenance of an equilibrium in volume and composition of the cerebrospinal fluid (CSF) is vital for a normal brain function, ensuring an optimal environment for the neurons. The necessarily high water permeability of the choroid plexus barrier is made possible by the abundant expression of a water channel, Aquaporin-1 (AQP1), on the apical side of the membrane from early stages of development through adulthood. Data from studies of AQP1 suggest that it also can contribute as a gated ion channel, and suggest that the AQP1-mediated ionic conductance has physiological significance for the regulation of cerebrospinal fluid secretion. The regulation of AQP1 ion channels could be one of several transport mechanisms that contribute to the decreased CSF secretion in response to endogenous signaling molecules such as atrial natriuretic pep
Aquaporin-1 Facilitates Macrophage M1 Polarization by Enhancing Glycolysis Through the Activation of HIF1α in … MEDIUM▼
This study aimed to investigate how aquaporin 1 (AQP1) modulates hypoxia-inducible factor-1α (HIF1α) to promote glycolysis and drive the M1 polarization of macrophages. Within 12 h post-treatment with LPS to induce acute kidney injury in rats, a significant upregulation of AQP1 and HIF1α protein levels was noted in serum and kidney tissues. This elevation corresponded with a decrease in blood glucose concentrations and an enhancement of glycolytic activity relative to the control group. Furthermore, there was a pronounced reduction in the circulating levels of the anti-inflammatory cytokine IL-10, accompanied by an upregulation in the levels of the pro-inflammatory cytokines IL-6 and TNF-α. The administration of an HIF1α inhibitor reversed these effects, which did not affect the production of AQP1 protein. In cellular assays, AQP1 knockdown mitigated the increase in HIF1α expression induced by LPS. Furthermore, the suppression of HIF1α with PX-478 led to decreased expression levels of
Urea transporters (UT) play a vital role in the mechanism of urine concentration and are recognized as novel targets for the development of salt-sparing diuretics. Thus, UT inhibitors are promising for development as novel diuretics. In the present study, a novel UT inhibitor with a diarylamide scaffold was discovered by high-throughput screening. Optimization of the inhibitor led to the identification of a promising preclinical candidate, N-[4-(acetylamino)phenyl]-5-nitrofuran-2-carboxamide (1H), with excellent in vitro UT inhibitory activity at the submicromolar level. The half maximal inhibitory concentrations of 1H against UT-B in mouse, rat, and human erythrocyte were 1.60, 0.64, and 0.13 μmol/L, respectively. Further investigation suggested that 8 μmol/L 1H more powerfully inhibited UT-A1 at a rate of 86.8% than UT-B at a rate of 73.9% in MDCK cell models. Most interestingly, we found for the first time that oral administration of 1H at a dose of 100 mg/kg showed superior diureti
The potential role of aquaporin 1 on aristolochic acid I induced epithelial mesenchymal transition on HK-2 cel… MEDIUM▼
Aristolochic acid I (AA-I), one of the main active components in Aristolochaia herbs, may induce aristolochic acid nephropathy (AAN). Renal interstitial fibrosis is one of the most typical features of AAN. To investigate the mechanism of Aristolochic acid I (AA-I) -induced renal epithelial-mesenchymal transition (EMT) and determine the role of aquaporin-1 (AQP1) in this process, we established an AA-I-induced EMT model in human proximal tubular epithelial cells (HK-2 cells). Morphological examination, MTT assay, and Western blot analysis were performed. Aquaporin 1 (AQP1) and several EMT-related proteins were detected, thereby suggesting the occurrence of AA-I-induced EMT. Two main pathways of transforming growth factor-β (TGF-β) signaling, namely, Smad-dependent and Smad-independent signaling pathways, were also detected. The results showed that the TGF-β / Smad-independent signaling pathways (β-catenin, Ras-Raf-Erk1/2 signaling pathways) were activated, and AQP1 expression was decrea
🧬 Theorist Proposes novel mechanisms and generates creative hypotheses ▼
Novel Therapeutic Hypotheses for Perivascular Spaces and Glymphatic Clearance in AD
1. Aquaporin-4 Polarization Enhancement via TREK-1 Channel Modulation
Description: Chronic activation of TREK-1 potassium channels in astrocytic endfeet could restore AQP4 polarization by modulating membrane lipid composition and cytoskeletal organization. TREK-1 activation increases membrane fluidity and promotes proper localization of dystrophin-associated protein complexes that anchor AQP4.
Target: KCNK2 (TREK-1 channel)
Supporting Evidence: AQP4 mislocalization is a hallmark of AD glymp
🔍 Skeptic Identifies weaknesses, alternative explanations, and methodological concerns ▼
Critical Scientific Evaluation of Glymphatic Therapeutic Hypotheses
1. Aquaporin-4 Polarization Enhancement via TREK-1 Channel Modulation
Critical Weaknesses:
- Mechanistic gap: The connection between TREK-1 activation and AQP4 polarization is speculative. TREK-1 primarily responds to mechanical stretch and lipid composition, but direct evidence linking this to dystrophin-associated protein complex organization is lacking.
- Conflicting evidence: TREK-1 activation typically leads to membrane hyperpolarization and reduced excitability, which may actually impair the calcium-de
🎯 Domain Expert Assesses practical feasibility, druggability, and clinical translation ▼
Druggability Assessment of Glymphatic Therapeutic Hypotheses
1. Circadian Glymphatic Entrainment via Orexin Receptor Modulation
Druggability: HIGH ⭐⭐⭐⭐⭐
Target Assessment: Both HCRTR1 and HCRTR2 are well-validated GPCRs with established druggability. Crystal structures available, multiple binding sites characterized.Existing Chemical Matter:
- Suvorexant (Belsomra®) - FDA approved dual orexin receptor antagonist
- Lemborexant (Dayvigo®) - FDA approved, improved pharmacokinetics
- Daridorexant (Quviviq®) - Recently approved in EU/US
- Almorexant - Discon
⚖ Synthesizer Integrates perspectives and produces final ranked assessments ▼
Price History
| Event | Price | Change | Source | Time | |
|---|---|---|---|---|---|
| 📄 | New Evidence | $0.457 | ▲ 1.7% | evidence_batch_update | 2026-04-13 02:18 |
| 📄 | New Evidence | $0.450 | ▲ 4.3% | evidence_batch_update | 2026-04-13 02:18 |
| ⚖ | Recalibrated | $0.431 | ▼ 0.3% | 2026-04-12 10:15 | |
| ⚖ | Recalibrated | $0.432 | ▼ 1.3% | 2026-04-10 15:58 | |
| ⚖ | Recalibrated | $0.438 | ▲ 1.5% | 2026-04-10 15:53 | |
| ⚖ | Recalibrated | $0.431 | ▲ 0.6% | 2026-04-08 18:39 | |
| ⚖ | Recalibrated | $0.429 | ▲ 2.9% | 2026-04-06 04:04 | |
| ⚖ | Recalibrated | $0.416 | ▼ 0.7% | 2026-04-04 16:38 | |
| ⚖ | Recalibrated | $0.419 | ▼ 0.8% | 2026-04-04 16:02 | |
| 📄 | New Evidence | $0.423 | ▲ 2.8% | evidence_batch_update | 2026-04-04 09:08 |
| ⚖ | Recalibrated | $0.412 | ▼ 9.0% | 2026-04-03 23:46 | |
| ⚖ | Recalibrated | $0.452 | ▲ 8.6% | market_dynamics | 2026-04-03 01:06 |
| ⚖ | Recalibrated | $0.416 | 2026-04-02 21:55 | ||
| ⚖ | Recalibrated | $0.417 | ▼ 0.5% | market_recalibrate | 2026-04-02 19:14 |
| 💬 | Debate Round | $0.419 | ▲ 3.3% | debate_engine | 2026-04-02 17:18 |
Clinical Trials (9) Relevance: 52%
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Highest Phase
📚 Cited Papers (42)
📓 Linked Notebooks (1)
Wiki Pages
KG Entities (41)
Linked Experiments (2)
Related Hypotheses
Estimated Development
🧪 Falsifiable Predictions (4)
Knowledge Subgraph (143 edges)
associated with (9)
catalyzes (1)
causes (1)
co associated with (21)
controls (1)
drives (1)
enables (1)
facilitates (1)
implicated in (7)
increases (1)
maintains (1)
mediates (1)
participates in (9)
promoted: Circadian Glymphatic Entrainment via Targeted Orexin Receptor Modulation (1)
regulates (1)
Mechanism Pathway for AQP1
Molecular pathway showing key causal relationships underlying this hypothesis
graph TD
AQP1["AQP1"] -->|associated with| neurodegeneration["neurodegeneration"]
AQP1_1["AQP1"] -->|participates in| Aquaporin_1_water_transpo["Aquaporin-1 water transport"]
AQP1_2["AQP1"] -->|co discussed| KCNK2["KCNK2"]
AQP1_3["AQP1"] -->|co discussed| GJA1["GJA1"]
AQP1_4["AQP1"] -->|co discussed| HCRTR2["HCRTR2"]
AQP1_5["AQP1"] -->|co discussed| LOXL1_4["LOXL1-4"]
AQP1_6["AQP1"] -->|co discussed| HCRTR1["HCRTR1"]
AQP1_7["AQP1"] -->|co discussed| AQP4["AQP4"]
AQP1_8["AQP1"] -->|co discussed| LOX["LOX"]
AQP1_9["AQP1"] -->|co discussed| SDC1["SDC1"]
AQP1_10["AQP1"] -->|co discussed| PDGFRB["PDGFRB"]
HCRTR2_11["HCRTR2"] -->|co discussed| AQP1_12["AQP1"]
AQP1_13["AQP1"] -->|co associated with| GJA1_14["GJA1"]
AQP1_15["AQP1"] -->|co associated with| PDGFRB_16["PDGFRB"]
AQP1_17["AQP1"] -->|co associated with| LOX_LOXL1_4["LOX/LOXL1-4"]
style AQP1 fill:#ce93d8,stroke:#333,color:#000
style neurodegeneration fill:#ef5350,stroke:#333,color:#000
style AQP1_1 fill:#ce93d8,stroke:#333,color:#000
style Aquaporin_1_water_transpo fill:#81c784,stroke:#333,color:#000
style AQP1_2 fill:#ce93d8,stroke:#333,color:#000
style KCNK2 fill:#ce93d8,stroke:#333,color:#000
style AQP1_3 fill:#ce93d8,stroke:#333,color:#000
style GJA1 fill:#ce93d8,stroke:#333,color:#000
style AQP1_4 fill:#ce93d8,stroke:#333,color:#000
style HCRTR2 fill:#ce93d8,stroke:#333,color:#000
style AQP1_5 fill:#ce93d8,stroke:#333,color:#000
style LOXL1_4 fill:#ce93d8,stroke:#333,color:#000
style AQP1_6 fill:#ce93d8,stroke:#333,color:#000
style HCRTR1 fill:#ce93d8,stroke:#333,color:#000
style AQP1_7 fill:#ce93d8,stroke:#333,color:#000
style AQP4 fill:#ce93d8,stroke:#333,color:#000
style AQP1_8 fill:#ce93d8,stroke:#333,color:#000
style LOX fill:#ce93d8,stroke:#333,color:#000
style AQP1_9 fill:#ce93d8,stroke:#333,color:#000
style SDC1 fill:#ce93d8,stroke:#333,color:#000
style AQP1_10 fill:#ce93d8,stroke:#333,color:#000
style PDGFRB fill:#ce93d8,stroke:#333,color:#000
style HCRTR2_11 fill:#ce93d8,stroke:#333,color:#000
style AQP1_12 fill:#ce93d8,stroke:#333,color:#000
style AQP1_13 fill:#ce93d8,stroke:#333,color:#000
style GJA1_14 fill:#ce93d8,stroke:#333,color:#000
style AQP1_15 fill:#ce93d8,stroke:#333,color:#000
style PDGFRB_16 fill:#ce93d8,stroke:#333,color:#000
style AQP1_17 fill:#ce93d8,stroke:#333,color:#000
style LOX_LOXL1_4 fill:#ce93d8,stroke:#333,color:#000
3D Protein Structure
🧬 AQP1 — PDB 1J4N Click to expand 3D viewer
Source Analysis
Perivascular spaces and glymphatic clearance failure in AD
neurodegeneration | 2026-04-01 | completed