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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 KRIT1/CCM1 Functional Annotation Report

Executive summary

The identification is secure: KRIT1 is the human gene encoding Krev interaction trapped protein 1, also called cerebral cavernous malformations 1 protein (CCM1), corresponding to the supplied UniProt O00522 identity. The literature consistently describes a 736-residue, approximately 75–84-kDa protein associated with chromosome 7q21.2; no conflicting similarly named protein was encountered. Its ankyrin-repeat and FERM/band-4.1 architecture agrees with the supplied UniProt/InterPro annotation. KRIT1 is not an enzyme or transporter: its pseudo-Nudix region lacks the catalytic sequence expected of a nucleotide hydrolase. It is principally a multidomain adaptor/scaffolding protein that spatially organizes signaling and adhesion machinery in vascular endothelial cells. (zafar2019familialcerebralcavernous pages 1-2, glading2024krit1invascular pages 1-2, riolo2021moleculargeneticfeatures pages 4-5)

Its best-established primary function is to maintain a quiescent, mechanically stable endothelial barrier. Active Rap1 moves KRIT1 from microtubules to endothelial cell–cell contacts; transmembrane HEG1 anchors it there; and KRIT1 associates with CCM2 and junctional/cytoskeletal machinery. In that location, it stabilizes adherens junctions, restrains actomyosin tension and permeability, and limits inappropriate endothelial proliferation, migration, inflammatory activation, and angiogenic transcription. Loss of both functional KRIT1 alleles in lesion endothelial cells drives CCM through excessive RhoA–ROCK and MEKK3–MEK5–ERK5–KLF2/4 signaling, altered integrin and β-catenin/VEGF signaling, and disturbed redox homeostasis. (glading2024krit1invascular pages 2-3, liu2011amechanismof pages 1-2, stockton2010cerebralcavernousmalformations pages 1-3, perrelli2023krit1atraffic pages 1-3)

Table: Compact evidence map for human KRIT1/CCM1, separating established molecular functions from emerging human models and preclinical interventions. It highlights the evidence supporting KRIT1’s primary annotation as a nonenzymatic endothelial-junction scaffold.

1. Identity verification and structural basis

1.1 Required verification

1. Symbol and protein description: Human KRIT1 is explicitly synonymous with CCM1 and “Krev interaction trapped protein 1.” The name derives from its original identification as an interactor of Krev-1/Rap1A. (zafar2019familialcerebralcavernous pages 1-2, glading2024krit1invascular pages 1-1)
2. Organism: The molecular and disease literature examined concerns human KRIT1, with mechanistic validation in human endothelial cells and lesions and complementary mouse and zebrafish models. Open Targets maps it to human ENSG00000001631. (OpenTargets Search: cerebral cavernous malformation-KRIT1, liu2011amechanismof pages 1-2, stockton2010cerebralcavernousmalformations pages 1-3)
3. Domain concordance: The reported ankyrin repeats and C-terminal FERM/band-4.1 module align with the supplied InterPro annotations. Literature additionally describes an N-terminal pseudo-Nudix region and three NPxY/F interaction motifs. (glading2024krit1invascular pages 1-2, riolo2021moleculargeneticfeatures pages 4-5, su2020signallingthroughcerebral pages 2-3)
4. Ambiguity: No evidence indicated that the retrieved papers concerned a different gene or organismal orthologue masquerading as the human target.

1.2 Domain organization

KRIT1 contains an N-terminal pseudo-Nudix region, three NPxY/F motifs, ankyrin repeats, and a C-terminal FERM module divided into F1, F2, and F3 lobes. The pseudo-Nudix region is considered catalytically inactive, reinforcing a scaffolding rather than enzymatic annotation. The first NPxY motif, N192PAY, binds ICAP1α/ITGB1BP1 and can participate in intramolecular contacts; another motif binds SNX17, while the distal motif supports CCM2 association. Rap1 engages the F1/F2 surface, whereas the HEG1 cytoplasmic tail occupies a pocket at the F1/F3 interface. These partially distinct interfaces permit KRIT1 to integrate membrane anchoring, small-GTPase input, integrin regulation, and CCM-complex assembly. (glading2024krit1invascular pages 1-2, glading2024krit1invascular pages 2-3, riolo2021moleculargeneticfeatures pages 4-5)

Reported molecular masses differ modestly—approximately 75 versus 84 kDa—probably because sources use calculated versus apparent mass. They agree on the 736-residue sequence and multidomain scaffold identity. (glading2024krit1invascular pages 1-2, riolo2021moleculargeneticfeatures pages 4-5)

2. Primary molecular function

2.1 Rap1 effector and trafficking switch

KRIT1 is a genuine, selective effector of active Rap1A. Recombinant full-length KRIT1 bound the GTP-dependent Rap1A effector loop but not active H-Ras. A structure-guided KRIT1 R452E substitution reduced Rap1 affinity approximately 40-fold while preserving HEG1 and CCM2 binding. This mutant remained sequestered on microtubules, failed to accumulate at endothelial junctions, and did not support normal junction stabilization or zebrafish cardiovascular development. Thus, Rap1 does not simply activate an enzymatic KRIT1 output; it controls the scaffold’s subcellular deployment. (liu2011amechanismof pages 1-2)

The mechanistic sequence best supported by experiment is:

Rap1-GTP binding → release of microtubule-associated KRIT1 → junctional translocation → HEG1/CCM2-supported retention and complex assembly → suppression of contractile and transcriptional programs that destabilize the endothelium. (liu2011amechanismof pages 1-2, stockton2010cerebralcavernousmalformations pages 1-3)

2.2 Junctional scaffold

At endothelial cell–cell contacts, KRIT1 supports VE-cadherin/catenin-associated adherens junctions and limits radial actin stress fibers. KRIT1 depletion causes junction disassembly, loss of junctional β-catenin, increased monolayer permeability, and greater actomyosin contractility. Associations with VE-cadherin, α/β-catenin, p120-catenin, and AF-6 have been reported, although reviews caution that not all are necessarily direct interactions. (su2020signallingthroughcerebral pages 2-3, stockton2010cerebralcavernousmalformations pages 1-3)

The broader structural role is therefore best described as coupling membrane and junctional receptors to cytoskeletal and kinase-regulatory machinery, enabling endothelial cells to preserve barrier continuity under mechanical, inflammatory, and oxidative stress.

2.3 HEG1, CCM2, and ICAP1

HEG1: The single-pass membrane protein HEG1 recruits KRIT1 through its cytoplasmic tail and FERM-domain pocket. Recent flow-physiology work indicates that HEG1 and CCM proteins are dynamically redistributed at endothelial junctions under shear stress, suggesting that this complex is not merely structural but helps convert hemodynamic context into KLF2/4-dependent transcription. (abdelilahseyfried2024arenaissanceof pages 3-5, glading2024krit1invascular pages 2-3)

CCM2: An NPxY/F motif of KRIT1 binds the CCM2 phosphotyrosine-binding domain. Physical KRIT1–CCM2 association is required for normal junctional localization and barrier control. CCM2 links the junctional complex to MEKK3 regulation; consequently, KRIT1 loss can alter transcription without KRIT1 itself possessing kinase activity. (su2020signallingthroughcerebral pages 2-3, stockton2010cerebralcavernousmalformations pages 1-3)

ICAP1/β1 integrin: KRIT1 binds and stabilizes ICAP1α, a negative regulator of β1-integrin activation. By controlling ICAP1 availability, KRIT1 influences cell–matrix adhesion, migration, and angiogenesis. This is a context-sensitive regulatory relationship rather than a simple statement that KRIT1 always activates or inhibits integrins. (glading2024krit1invascular pages 2-3, riolo2021moleculargeneticfeatures pages 4-5)

3. Cellular and tissue localization

KRIT1 is widely expressed and has been detected at endothelial cell–cell contacts, in the cytosol, on microtubules, and in the nucleus. Its most firmly linked disease-relevant site of action is the cytoplasmic face of endothelial adherens junctions, especially in capillary-venous endothelium of the central nervous system. Rap1-dependent release from microtubules and HEG1-dependent membrane anchoring make localization a regulated component of function, not a passive property. (glading2024krit1invascular pages 2-3, liu2011amechanismof pages 1-2)

CCM lesions occur preferentially in low-flow brain capillary–venous beds and consist of dilated, hemorrhage-prone, endothelial-lined channels with deficient neurovascular support and blood–brain barrier integrity. The resulting phenotype explains why a ubiquitous scaffold produces a predominantly neurovascular disease: endothelial mosaic loss, specialized BBB requirements, local flow, inflammatory exposure, and additional somatic events create a selective lesion-forming context. (abdelilahseyfried2024arenaissanceof pages 1-3, fisher2024focusedultrasoundbloodbrain pages 1-4, perrelli2023krit1atraffic pages 1-3)

4. Principal signaling pathways

4.1 RhoA–ROCK and actomyosin tension

This is among the strongest experimentally established KRIT1 outputs. KRIT1 or CCM2 loss sustains RhoA and ROCK activity, increases phosphorylated myosin light chain and stress fibers, and elevates endothelial permeability. H-1152 and Y-27632 reversed the cellular permeability phenotype; fasudil reversed vascular leakage in Krit1- or Ccm2-haploinsufficient mice. Increased myosin-light-chain phosphorylation in both familial and sporadic human CCM endothelium establishes relevance beyond model systems. (stockton2010cerebralcavernousmalformations pages 1-3)

The precise biochemical link from the KRIT1–CCM2 scaffold to RhoA remains incompletely resolved. Accordingly, “KRIT1 restrains RhoA–ROCK-dependent contractility” is well established, whereas naming a single direct catalytic intermediary would overstate current evidence. (glading2024krit1invascular pages 2-3)

4.2 MEKK3–MEK5–ERK5–KLF2/4

The CCM complex normally constrains endothelial MEKK3 signaling. KRIT1/CCM-complex loss causes excessive MEKK3–MEK5–ERK5 signaling and induction of KLF2 and KLF4. Excess KLF2/4 activity is required for major CCM-like vascular phenotypes and promotes abnormal endothelial transcription, permeability, proliferative behavior, and endothelial-to-mesenchymal transition. (abdelilahseyfried2024arenaissanceof pages 1-3, abdelilahseyfried2024arenaissanceof pages 5-6, glading2024krit1invascular pages 2-3)

The 2024 flow-centered interpretation refines this pathway: HEG1, KRIT1/CCM1, CCM2, and KLF2/4 form a shear-responsive regulatory system. HEG1 relocates to junctions under stable or high shear and co-localizes with CCM1; low-flow venous-capillary environments may favor pathological pathway activation after CCM loss. However, some observations under physiological high flow differ from chronic genetic loss, so temporal context and subcellular trafficking remain active research questions. (abdelilahseyfried2024arenaissanceof pages 3-5, abdelilahseyfried2024arenaissanceof pages 5-6)

4.3 β-catenin, VEGF, PI3K–AKT, and mTOR

KRIT1 loss destabilizes adherens junctions, redistributes β-catenin, activates β-catenin-dependent transcription, and enhances VEGFA/VEGFR2 signaling. Conditional Krit1 models have consequently identified VEGFR2, ERK5, ROCK, and potentially PI3K as intervention points. (glading2024krit1invascular pages 2-3)

Human lesions can contain activating PIK3CA or AKT1 changes in addition to biallelic CCM-gene loss, supporting a refined “three-hit” model in which loss of barrier-regulatory identity combines with a proliferative/growth signal. Disease-associated PIK3CA activation engages mTORC1; rapamycin produced strong therapeutic responses in a mouse model, but this should not be interpreted as established efficacy in human KRIT1-associated CCM. (abdelilahseyfried2024arenaissanceof pages 1-3, glading2024krit1invascular pages 7-8)

4.4 Redox and inflammatory signaling

The 2023 expert synthesis argues that redox dysregulation may unify several apparently separate consequences of KRIT1 loss. KRIT1 supports redox homeostasis and cellular resistance to oxidative and inflammatory stress; loss perturbs ROS-sensitive control of adhesion, GTPases, MAPKs, and endothelial phenotype. Human CCM vessels show increased nuclear NRF2 accumulation, while experimental KRIT1 deficiency has been linked to c-Jun activation and oxidative, inflammatory, and proangiogenic responses. The broad association is strong, but the field has not yet established a single linear ROS pathway as the sole primary KRIT1 mechanism. (OpenTargets Search: cerebral cavernous malformation-KRIT1, perrelli2023krit1atraffic pages 1-3)

5. Disease mechanism and quantitative genetics

Familial CCM is autosomal dominant at the organismal level, with incomplete penetrance and variable expressivity, but lesion formation follows a largely recessive endothelial two-hit mechanism: an inherited pathogenic KRIT1 allele is followed by somatic loss of the remaining functional allele in a subset of endothelial cells. Biallelic endothelial deletion produces lesions in mice, whereas ordinary heterozygotes generally do not; increasing somatic mutation pressure through Trp53 or mismatch-repair deficiency promotes lesion development. (su2020signallingthroughcerebral pages 2-3, glading2024krit1invascular pages 7-8)

KRIT1 variants account for approximately 53–65% of genetically characterized familial CCM in reviewed series; another 2023 synthesis states that they cause more than 50% of familial cases. More than 300 KRIT1 variants had been catalogued in HGMD by 2021. A notable Southwest US founder allele is c.1363C>T, p.Gln455*. (zafar2019familialcerebralcavernous pages 1-2, riolo2021moleculargeneticfeatures pages 4-5, su2020signallingthroughcerebral pages 2-3, perrelli2023krit1atraffic pages 1-3)

Population burden estimates vary with ascertainment. The 2023 redox review cites CCM prevalence of 0.3–0.5%, with approximately 70% of cases sporadic and 30% familial. Another clinical review estimated familial CCM at 1 in 5,000–10,000, with exome-derived estimates around 1 in 3,300–3,800. These figures describe CCM disease broadly, not the prevalence of pathogenic KRIT1 variants alone. (zafar2019familialcerebralcavernous pages 1-2, perrelli2023krit1atraffic pages 1-3)

Open Targets independently ranks human KRIT1 as strongly associated with CCM, with association scores of 0.8245 for cerebral cavernous malformation, 0.8034 for familial CCM, and 0.7532 for the CCM1 disease concept. These are evidence-integration scores rather than effect sizes or clinical risks. (OpenTargets Search: cerebral cavernous malformation-KRIT1)

6. Recent developments, 2023–2024

6.1 Updated expert interpretation

Glading’s peer-reviewed review, accepted 9 July and published 19 July 2024, frames KRIT1 as a 75-kDa scaffold maintaining a quiescent, inflammation-resistant endothelial barrier, while emphasizing unresolved questions about subcellular localization and functions outside endothelium. This is a useful current consensus statement: the junctional role is established, but KRIT1’s nuclear and nonvascular functions remain less precisely defined. DOI: https://doi.org/10.1042/BSR20231675. (glading2024krit1invascular pages 1-2, glading2024krit1invascular pages 1-1)

Abdelilah-Seyfried and Jo’s June 2024 commentary integrates CCM proteins with shear-stress physiology, HEG1 trafficking, KLF2/4 regulation, and vascular-bed specificity. DOI: https://doi.org/10.1038/s44161-024-00504-1. (abdelilahseyfried2024arenaissanceof pages 1-3, abdelilahseyfried2024arenaissanceof pages 3-5)

Perrelli and colleagues’ 2023 review places KRIT1 at the intersection of endothelial adhesion, ROS, oxidative post-translational regulation, and inflammation, proposing redox control as a framework for precision therapy. DOI: https://doi.org/10.1089/ars.2021.0263. (perrelli2023krit1atraffic pages 1-3)

6.2 Human BBB and CCM assembloids

Dao et al. constructed human pluripotent-stem-cell-derived brain and vascular organoids and fused them into BBB assembloids. Patient-derived CCM assembloids reproduced cavernoma-like anatomy, barrier breakdown, and molecular/cellular features of primary human lesions, supported by functional assays, transcriptomics, spatial profiling, and tissue comparison. This is a significant real-world research implementation because it supplies a human platform for mechanistic testing and drug-permeability assessment where rodent BBB physiology is imperfect. Cell Stem Cell, published 6 June 2024; DOI: https://doi.org/10.1016/j.stem.2024.04.019. (dao2024modelingbloodbrainbarrier pages 1-3)

6.3 Focused-ultrasound BBB opening

In a postnatal endothelial-specific Krit1-knockout mouse model, MRI-guided focused ultrasound plus microbubbles halted growth in 94% of treated CCMs. At one month, treated lesions averaged a 9% reduction from pre-treatment volume, whereas untreated controls reached 670% of initial volume; repeated treatment reduced new-lesion formation by 81%, without acute hemorrhage in the reported experiments. Simulated planning suggested that some surgically inaccessible human lesions could be targeted by existing systems. However, this was a bioRxiv preprint posted 4 February 2024—not a human trial—and the biological mechanism of benefit remains incompletely established. DOI: https://doi.org/10.1101/2024.01.31.577810. (fisher2024focusedultrasoundbloodbrain pages 1-4)

7. Current applications and clinical implementation

There is no established therapy that directly replaces KRIT1 or selectively normalizes its scaffold function. Surgical resection remains the principal definitive treatment for accessible symptomatic lesions; stereotactic radiosurgery is used selectively but carries radiation-related risks. Molecular approaches—ROCK inhibition, MEKK3/ERK5/KLF2/4 modulation, VEGFR2 or PI3K–mTOR inhibition, antioxidant strategies, and focused ultrasound—remain experimental or pathway-informed rather than validated KRIT1-targeted standards of care. (fisher2024focusedultrasoundbloodbrain pages 1-4, stockton2010cerebralcavernousmalformations pages 1-3)

Current implementation is strongest in genetic diagnosis, surveillance, natural-history measurement, and trial readiness:

• NCT03652181 (CASH Trial Readiness) was a completed, prospective multicenter observational cohort with 123 actual participants. It measured two-year recurrent symptomatic hemorrhage, quantitative susceptibility mapping of lesional iron, dynamic contrast-enhanced permeability, disability, neurological status, and quality of life. Results were first posted 27 June 2024. Trial URL: https://clinicaltrials.gov/study/NCT03652181. (NCT03652181 chunk 1)
• NCT01764529, a familial CCM registry, enrolled 789 participants and collected longitudinal clinical, genetic, MRI, blood/saliva, stool, and available lesion-tissue data to identify modifiers, microbiome associations, biomarkers, lesion burden, and hemorrhage risk. Trial URL: https://clinicaltrials.gov/study/NCT01764529. (NCT01764529 chunk 1)

These cohorts are not efficacy trials, but they create the outcome measures, biospecimen resources, and risk-stratification infrastructure required for future mechanism-based interventions.

8. Evidence-weighted functional annotation

Recommended primary annotation:

KRIT1 is a nonenzymatic Rap1-regulated endothelial-junction scaffold that binds HEG1, CCM2, and ICAP1 to coordinate adherens-junction stability, cell–matrix adhesion, cytoskeletal tension, flow-responsive transcription, and redox/inflammatory homeostasis. Its endothelial loss activates RhoA–ROCK and MEKK3–MEK5–ERK5–KLF2/4 signaling, producing blood–brain barrier failure and cerebral cavernous malformations.

Evidence confidence:

• High: Human target identity; nonenzymatic scaffold classification; Rap1-specific binding; regulated microtubule-to-junction trafficking; HEG1 and CCM2 interactions; endothelial barrier role; RhoA–ROCK suppression; biallelic endothelial-loss mechanism.
• Moderate to high: MEKK3–KLF2/4 pathway placement, ICAP1–β1-integrin regulation, β-catenin/VEGF effects, and redox/inflammatory control.
• Emerging: Flow-dependent secretion or redistribution of CCM proteins, three-hit PIK3CA/AKT1 models, broader nonendothelial functions, organoid-guided precision medicine, and focused-ultrasound therapy.

The central mechanistic uncertainty is not whether KRIT1 protects endothelial junctions, but exactly how its localization, conformational state, and multiple partners prioritize RhoA, MEKK3, integrin, redox, and growth-signaling outputs across vascular beds and disease stages.

References

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2. (glading2024krit1invascular pages 1-2): Angela J. Glading. Krit1 in vascular biology and beyond. Bioscience Reports, Jul 2024. URL: https://doi.org/10.1042/bsr20231675, doi:10.1042/bsr20231675. This article has 8 citations and is from a peer-reviewed journal.

3. (riolo2021moleculargeneticfeatures pages 4-5): Giulia Riolo, Claudia Ricci, and Stefania Battistini. Molecular genetic features of cerebral cavernous malformations (ccm) patients: an overall view from genes to endothelial cells. Mar 2021. URL: https://doi.org/10.3390/cells10030704, doi:10.3390/cells10030704. This article has 48 citations.

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7. (perrelli2023krit1atraffic pages 1-3): Andrea Perrelli, Chiara Ferraris, Elisa Berni, Angela J. Glading, and Saverio Francesco Retta. Krit1: a traffic warden at the busy crossroads between redox signaling and the pathogenesis of cerebral cavernous malformation disease. Nov 2023. URL: https://doi.org/10.1089/ars.2021.0263, doi:10.1089/ars.2021.0263. This article has 19 citations and is from a domain leading peer-reviewed journal.

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9. (su2020signallingthroughcerebral pages 2-3): Valerie L. Su and David A. Calderwood. Signalling through cerebral cavernous malformation protein networks. Open Biology, Nov 2020. URL: https://doi.org/10.1098/rsob.200263, doi:10.1098/rsob.200263. This article has 42 citations and is from a peer-reviewed journal.

10. (glading2024krit1invascular pages 1-1): Angela J. Glading. Krit1 in vascular biology and beyond. Bioscience Reports, Jul 2024. URL: https://doi.org/10.1042/bsr20231675, doi:10.1042/bsr20231675. This article has 8 citations and is from a peer-reviewed journal.

11. (abdelilahseyfried2024arenaissanceof pages 1-3): Salim Abdelilah-Seyfried and Hanjoong Jo. A renaissance of cerebral cavernous malformation proteins in vascular physiology. Nature cardiovascular research, 3 7:771-773, Jun 2024. URL: https://doi.org/10.1038/s44161-024-00504-1, doi:10.1038/s44161-024-00504-1. This article has 5 citations and is from a peer-reviewed journal.

12. (abdelilahseyfried2024arenaissanceof pages 5-6): Salim Abdelilah-Seyfried and Hanjoong Jo. A renaissance of cerebral cavernous malformation proteins in vascular physiology. Nature cardiovascular research, 3 7:771-773, Jun 2024. URL: https://doi.org/10.1038/s44161-024-00504-1, doi:10.1038/s44161-024-00504-1. This article has 5 citations and is from a peer-reviewed journal.

13. (OpenTargets Search: cerebral cavernous malformation-KRIT1): Open Targets Query (cerebral cavernous malformation-KRIT1, 3 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.

14. (glading2024krit1invascular pages 7-8): Angela J. Glading. Krit1 in vascular biology and beyond. Bioscience Reports, Jul 2024. URL: https://doi.org/10.1042/bsr20231675, doi:10.1042/bsr20231675. This article has 8 citations and is from a peer-reviewed journal.

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16. (fisher2024focusedultrasoundbloodbrain pages 1-4): Delaney G. Fisher, Khadijeh A. Sharifi, Ishaan M. Shah, Catherine M. Gorick, Victoria R. Breza, Anna C. Debski, Matthew R. Hoch, Tanya Cruz, Joshua D. Samuels, Jason P. Sheehan, David Schlesinger, David Moore, John R. Lukens, G. Wilson Miller, Petr Tvrdik, and Richard J. Price. Focused ultrasound blood-brain barrier opening arrests the growth and formation of cerebral cavernous malformations. bioRxiv, Feb 2024. URL: https://doi.org/10.1101/2024.01.31.577810, doi:10.1101/2024.01.31.577810. This article has 3 citations.

17. (NCT03652181 chunk 1): CASH (Cavernous Angiomas With Symptomatic Hemorrhage) Trial Readiness. University of Chicago. 2018. ClinicalTrials.gov Identifier: NCT03652181

18. (NCT01764529 chunk 1): Modifiers of Disease Severity in Cerebral Cavernous Malformations. University of California, San Francisco. 2010. ClinicalTrials.gov Identifier: NCT01764529

Artifacts

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Citations

1. riolo2021moleculargeneticfeatures pages 4-5
2. liu2011amechanismof pages 1-2
3. abdelilahseyfried2024arenaissanceof pages 3-5
4. stockton2010cerebralcavernousmalformations pages 1-3
5. su2020signallingthroughcerebral pages 2-3
6. dao2024modelingbloodbrainbarrier pages 1-3
7. fisher2024focusedultrasoundbloodbrain pages 1-4
8. zafar2019familialcerebralcavernous pages 1-2
9. abdelilahseyfried2024arenaissanceof pages 1-3
10. abdelilahseyfried2024arenaissanceof pages 5-6
11. https://doi.org/10.1042/BSR20231675.
12. https://doi.org/10.1038/s44161-024-00504-1.
13. https://doi.org/10.1089/ars.2021.0263.
14. https://doi.org/10.1016/j.stem.2024.04.019.
15. https://doi.org/10.1101/2024.01.31.577810.
16. https://clinicaltrials.gov/study/NCT03652181.
17. https://clinicaltrials.gov/study/NCT01764529.
18. https://doi.org/10.1161/strokeaha.118.022314,
19. https://doi.org/10.1042/bsr20231675,
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21. https://doi.org/10.1091/mbc.e11-02-0157,
22. https://doi.org/10.1084/jem.20091258,
23. https://doi.org/10.1089/ars.2021.0263,
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25. https://doi.org/10.1098/rsob.200263,
26. https://doi.org/10.1016/j.stem.2024.04.019,
27. https://doi.org/10.1101/2024.01.31.577810,