GO:0036025 protein C inhibitor-TMPRSS11E complex: Components, Assembly and Research Methods, Genes, Functions and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0036025 describes a heterodimeric protein complex containing protein C inhibitor (SERPINA5) and transmembrane protease serine 11E (TMPRSS11E).
• Formation of this complex inhibits the serine protease activity of TMPRSS11E, as defined by QuickGO.
• Protein C inhibitor (SERPINA5) is a multifunctional serpin that regulates coagulation and other serine proteases.
• The protein C pathway is a major anticoagulant system, and its components are linked to thrombosis and vascular disease [4,8].
• Activated protein C-protein C inhibitor complexes have been detected in peripheral arterial disease and aortic aneurysms [2,6].
• Research on this complex uses knockout, point-mutation, knock-in, and overexpression cell models combined with proteomics and functional assays.
Description
GO:0036025, the protein C inhibitor-TMPRSS11E complex, is a cellular component defined as a heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and transmembrane protease serine 11E (TMPRSS11E); formation of the complex inhibits the serine protease activity of TMPRSS11E. This term captures a specific molecular interaction between a serpin inhibitor and a membrane-anchored serine protease, and it is distinct from the broader protein C anticoagulant pathway [4,8]. Protein C inhibitor, also known as SERPINA5, is a multifunctional serpin that regulates several serine proteases beyond activated protein C, including enzymes involved in coagulation and tissue remodeling. The protein C system itself is a central anticoagulant mechanism, and dysregulation of its components is associated with thrombotic disorders [4,8]. Researchers study this complex to understand how serpin-protease interactions control protease activity at the cell surface and in extracellular fluids. The complex is relevant to vascular biology because activated protein C-protein C inhibitor complexes have been measured in clinical samples from patients with peripheral arterial disease and aortic aneurysms [2,6]. Understanding GO:0036025 therefore connects fundamental protease regulation to clinically important vascular pathologies.
protein C inhibitor-TMPRSS11E complex At A Glance
| GO ID | GO:0036025 |
|---|---|
| GO term | protein C inhibitor-TMPRSS11E complex |
| Ontology | cellular_component |
| Synonym | PCI-TMPRSS11E complex; plasma serine protease inhibitor-TMPRSS11E complex; protein C inhibitor-transmembrane protease serine 11E complex; serpin A5-TMPRSS11E complex; SERPINA5-TMPRSS11E complex |
| Major function | Formation of the complex inhibits the serine protease activity of transmembrane protease serine 11E (TMPRSS11E). |
| Complex type | Heterodimeric protein complex |
| Key components | SERPINA5 (protein C inhibitor) and TMPRSS11E (transmembrane protease serine 11E) |
| Related pathway | Protein C anticoagulant pathway and serpin-protease regulation [4,7,8] |
| Disease relevance | Vascular disease markers such as activated protein C-protein C inhibitor complexes have been reported in peripheral arterial disease and aortic aneurysms [2,6] |
What Is GO:0036025?
The protein C inhibitor-TMPRSS11E complex (GO:0036025) is a heterodimeric cellular component composed of two proteins: protein C inhibitor (SERPINA5) and transmembrane protease serine 11E (TMPRSS11E). According to the QuickGO definition, formation of this complex inhibits the serine protease activity of TMPRSS11E. In other words, SERPINA5 acts as an inhibitor that binds TMPRSS11E, and this binding event blocks the proteolytic function of TMPRSS11E. The term is annotated as a cellular component, meaning it describes a specific molecular assembly rather than a process or a standalone activity. Synonyms include PCI-TMPRSS11E complex, plasma serine protease inhibitor-TMPRSS11E complex, protein C inhibitor-transmembrane protease serine 11E complex, serpin A5-TMPRSS11E complex, and SERPINA5-TMPRSS11E complex.
Why Is protein C inhibitor-TMPRSS11E complex Important in Cell Biology?
GO:0036025 is important because it represents a specific regulatory interaction between a circulating serpin and a membrane-associated serine protease, and such interactions are central to controlling proteolytic activity in coagulation, inflammation, and tissue remodeling. The protein C pathway is a major anticoagulant system, and its regulation is directly relevant to thrombotic and vascular diseases [4,8]. Clinical studies have measured activated protein C-protein C inhibitor complexes in patients with peripheral arterial disease and aortic aneurysms, indicating that serpin-protease complexes can serve as biological markers of vascular pathology [2,6]. By studying the protein C inhibitor-TMPRSS11E complex specifically, researchers can dissect how SERPINA5 recognizes and inhibits TMPRSS11E, which may reveal general principles of serpin specificity and protease regulation. This knowledge can inform the development of experimental models to test whether disrupting or enhancing this interaction alters cellular protease activity and downstream signaling.
• Defines a specific heterodimeric complex between SERPINA5 and TMPRSS11E, linking serpin biology to membrane protease regulation.
• Provides a molecular explanation for how TMPRSS11E serine protease activity is inhibited through complex formation.
• Connects to the broader protein C anticoagulant pathway, which is critical for preventing thrombosis [4,8].
• Protein C inhibitor (SERPINA5) is multifunctional and regulates multiple serine proteases beyond activated protein C.
• Activated protein C-protein C inhibitor complexes have been detected in peripheral arterial disease, supporting clinical relevance.
• Activated protein C-protein C inhibitor complexes have also been associated with aortic aneurysms.
• Understanding serpin-protease complexes can guide research on vascular remodeling and hemostatic balance.
• The complex is a potential biomarker or mechanistic node in diseases involving dysregulated proteolysis [2,6].
• Studying this complex supports the development of targeted CRISPR models to test gene function in protease regulation.
• It exemplifies how cellular component annotations can focus experimental design on specific protein-protein interactions.
Structure and Composition of protein C inhibitor-TMPRSS11E complex
SERPINA5 (protein C inhibitor) as the inhibitory subunit
In simple terms: SERPINA5 is the brake that stops TMPRSS11E from cutting proteins.
Protein C inhibitor, encoded by SERPINA5, is a multifunctional serpin that regulates several serine proteases involved in coagulation and related processes. In the context of GO:0036025, SERPINA5 acts as the inhibitory subunit that binds to TMPRSS11E. The QuickGO definition states that formation of the complex inhibits the serine protease activity of TMPRSS11E. Serpins typically function by presenting a reactive center loop that engages the protease active site, leading to stable complex formation and inhibition. The broader protein C system, in which protein C inhibitor participates, is a well-characterized anticoagulant pathway [4,8]. Thus, SERPINA5 provides the specificity and inhibitory capacity of the protein C inhibitor-TMPRSS11E complex.
TMPRSS11E as the target serine protease
In simple terms: TMPRSS11E is the protease that gets switched off when it binds SERPINA5.
Transmembrane protease serine 11E (TMPRSS11E) is a membrane-associated serine protease and is the second component of GO:0036025. The QuickGO definition identifies TMPRSS11E as the protease whose activity is inhibited upon complex formation with protein C inhibitor. Membrane-anchored serine proteases often participate in extracellular proteolysis and cell-surface signaling, and their regulation by serpins is a key control mechanism. Because the complex is defined as heterodimeric, the interaction between SERPINA5 and TMPRSS11E is stoichiometric and specific. The functional consequence is loss of TMPRSS11E proteolytic activity, which can alter downstream substrates and cellular responses.
Heterodimeric assembly and complex stability
In simple terms: The two proteins stick together to form one stable unit.
GO:0036025 is annotated as a heterodimeric protein complex, meaning it contains one molecule of protein C inhibitor (SERPINA5) and one molecule of transmembrane protease serine 11E (TMPRSS11E). The assembly is driven by the interaction between the serpin and the protease, and the resulting complex is stable enough to be detected experimentally. The QuickGO definition emphasizes that formation of the complex inhibits the serine protease activity of TMPRSS11E, indicating that the assembly is not merely a binding event but an inhibitory trap. This type of serpin-protease complex is a classic mechanism for controlling proteolytic cascades, as seen in the protein C pathway [4,8]. The heterodimeric nature distinguishes GO:0036025 from larger multi-protein complexes and focuses attention on the direct SERPINA5-TMPRSS11E interaction.
Relationship to the protein C pathway and serpin superfamily
In simple terms: This complex is part of a larger family of proteins that control blood clotting and protease activity.
Protein C inhibitor is a member of the serpin superfamily and participates in the protein C anticoagulant pathway, which is essential for regulating blood coagulation [4,7,8]. The protein C pathway involves activated protein C and its inhibitors, and complexes between activated protein C and protein C inhibitor have been measured in clinical settings [2,6]. While GO:0036025 specifically refers to the SERPINA5-TMPRSS11E complex, it shares mechanistic features with other serpin-protease complexes in the pathway. The broader context of blood coagulation and anticoagulant regulation is reviewed in the literature [3,4,8]. Understanding GO:0036025 therefore benefits from knowledge of serpin biology and the protein C system, even though the complex itself is a distinct entity.
Key Genes Involved in GO:0036025 protein C inhibitor-TMPRSS11E complex
The following genes and proteins are directly or contextually relevant to the protein C inhibitor-TMPRSS11E complex (GO:0036025) and its associated biology.
| Gene | Major Role | Research Relevance |
|---|---|---|
| SERPINA5 | Encodes protein C inhibitor, the inhibitory subunit of the complex | Core component of GO:0036025; target for knockout and point-mutation studies |
| TMPRSS11E | Encodes transmembrane protease serine 11E, the target protease | Core component of GO:0036025; target for knockout and overexpression studies |
| PROC | Encodes protein C, a central anticoagulant zymogen | Context for the protein C pathway and serpin regulation [4,8] |
| PROCR | Encodes endothelial protein C receptor | Modulates protein C activation and pathway activity [4,8] |
| F5 | Encodes coagulation factor V, a cofactor in coagulation | Relevant to thrombotic risk and protein C pathway interactions [3,4] |
| F8 | Encodes coagulation factor VIII | Coagulation cascade component linked to protein C regulation |
| SERPINC1 | Encodes antithrombin, another anticoagulant serpin | Comparative serpin biology and coagulation control [3,7] |
| F2 | Encodes prothrombin, a key coagulation protease precursor | Downstream of coagulation cascade and protein C pathway [3,4] |
| PLG | Encodes plasminogen, involved in fibrinolysis | Cross-talk with protease systems and vascular remodeling |
| TMPRSS11A | Related transmembrane serine protease family member | Comparative studies of TMPRSS11 family substrate specificity |
| TMPRSS11B | Related transmembrane serine protease family member | Comparative studies of TMPRSS11 family regulation |
| TMPRSS11D | Related transmembrane serine protease family member | Comparative studies of airway and epithelial protease function |
| TMPRSS2 | Well-studied transmembrane serine protease | Model for understanding TMPRSS family regulation and inhibition |
| SERPINE1 | Encodes plasminogen activator inhibitor-1, a serpin | Comparative serpin function in vascular biology |
| SERPINF2 | Encodes alpha2-antiplasmin, a serpin | Comparative serpin regulation of proteases |
| ELANE | Encodes neutrophil elastase, a serine protease | Example of serpin-protease balance in inflammation |
| CTSG | Encodes cathepsin G, a serine protease | Example of serpin-protease interactions in immune cells |
| APOH | Encodes beta-2-glycoprotein I, a plasma protein | Context for vascular and antiphospholipid biology [2,6] |
How Is protein C inhibitor-TMPRSS11E complex Regulated?
The formation and stability of the protein C inhibitor-TMPRSS11E complex are regulated by the availability and activity of its two components. Protein C inhibitor (SERPINA5) is a multifunctional serpin whose inhibitory activity can be influenced by glycosaminoglycans and other cofactors, as described in the broader protein C system literature. The protein C pathway itself is subject to regulation by endothelial protein C receptor and thrombomodulin, which control the generation of activated protein C [4,8]. Although specific regulatory mechanisms for the SERPINA5-TMPRSS11E interaction are not fully detailed in the provided citations, the general principles of serpin-protease regulation apply. For example, the balance between proteases and serpins is critical in coagulation and vascular disease, and activated protein C-protein C inhibitor complexes have been measured as markers of pathway activation [2,6]. Researchers should consider that expression levels, localization, and post-translational modifications of SERPINA5 and TMPRSS11E may all influence complex formation.
protein C inhibitor-TMPRSS11E complex and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| SERPINA5 | Thrombosis and vascular disease via serpin regulation [2,4,6,7] | SERPINA5 knockout or point-mutation cell models |
| TMPRSS11E | Protease-mediated tissue remodeling and epithelial biology | TMPRSS11E knockout or overexpression cell models |
| PROC | Thrombosis due to protein C pathway dysfunction [4,5,8] | PROC point-mutation knock-in models |
| PROCR | Vascular and inflammatory disorders linked to protein C pathway [4,8] | PROCR knockout or tagged knock-in models |
| F5 | Thrombophilia and coagulation imbalance [3,4] | F5 point-mutation models for coagulation studies |
Vascular disease and thrombosis
The protein C pathway is a major anticoagulant system, and its dysfunction is linked to thrombotic disorders [4,8]. Activated protein C-protein C inhibitor complexes have been detected in patients with peripheral arterial disease, suggesting that serpin-protease complexes can reflect vascular pathology. Similarly, activated protein C-protein C inhibitor complexes have been proposed as biological markers for aortic aneurysms. While these studies focus on activated protein C rather than TMPRSS11E, they establish the clinical relevance of protein C inhibitor-containing complexes in vascular disease. Research on GO:0036025 may therefore inform understanding of how SERPINA5 interactions contribute to vascular remodeling and thrombotic risk.
Coagulation disorders and hemostatic imbalance
Blood coagulation is a tightly regulated process, and imbalances in procoagulant and anticoagulant factors can lead to bleeding or thrombosis. The protein C pathway, including protein C inhibitor, is central to this balance [4,7,8]. Mutations in protein C pathway components can cause thrombosis, as illustrated by a reported Met343Val mutation in activated protein C that leads to a low-activity conformer and thrombosis. Although this mutation is in activated protein C rather than in SERPINA5 or TMPRSS11E, it highlights how subtle changes in protein structure can disrupt anticoagulant function. Studying the protein C inhibitor-TMPRSS11E complex may reveal additional mechanisms by which serpin-protease interactions influence hemostatic balance.
Inflammation and protease-mediated tissue remodeling
Serine proteases and their serpin inhibitors are involved in inflammation and tissue remodeling beyond coagulation. Protein C inhibitor is multifunctional and can regulate several proteases, suggesting that the SERPINA5-TMPRSS11E complex may participate in broader proteolytic networks. The protein C system has been reviewed as a multifunctional system with roles in inflammation and vascular biology. Therefore, dysregulation of the protein C inhibitor-TMPRSS11E complex could potentially contribute to inflammatory or remodeling processes, although direct evidence for TMPRSS11E in these contexts is not provided in the cited literature. Researchers should design experiments to test this hypothesis.
From protein C inhibitor-TMPRSS11E complex-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of SERPINA5 alter TMPRSS11E activity? | SERPINA5 knockout cell line |
| Does loss of TMPRSS11E affect cellular proteolysis? | TMPRSS11E knockout cell line |
| Does a specific SERPINA5 mutation disrupt complex formation? | SERPINA5 point-mutation knock-in |
| Can tagged SERPINA5 be used to purify the complex? | Tagged knock-in of SERPINA5 |
| Does overexpression of TMPRSS11E overwhelm inhibitor capacity? | TMPRSS11E overexpression cell model |
| Does overexpression of SERPINA5 enhance inhibition? | SERPINA5 overexpression cell model |
How to Study the protein C inhibitor-TMPRSS11E complex Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Co-immunoprecipitation | Physical interaction between SERPINA5 and TMPRSS11E | Confirming the heterodimeric complex |
| Mass spectrometry | Protein identity and modifications in the complex | Proteomic characterization of GO:0036025 |
| Fluorogenic protease assay | TMPRSS11E serine protease activity | Testing inhibition by SERPINA5 |
| Immunofluorescence | Subcellular localization of complex components | Determining where the complex forms |
| Western blot | Protein expression and complex formation | Validating knockout or overexpression models |
| CRISPR knockout | Loss-of-function effects on complex biology | Testing gene requirement for complex formation |
| CRISPR knock-in | Tagged or mutant protein expression | Tracking or perturbing the complex in cells |
| RNA-seq | Transcriptional changes upon complex perturbation | Identifying downstream pathways affected by the complex |
Proteomics and co-immunoprecipitation
To study the protein C inhibitor-TMPRSS11E complex, researchers can use co-immunoprecipitation followed by mass spectrometry to identify and quantify the interacting partners. Because GO:0036025 is defined as a heterodimeric complex, pulldown of SERPINA5 or TMPRSS11E can confirm the interaction. Proteomic approaches can also detect post-translational modifications that may regulate complex formation. These methods are supported by the general principle that serpin-protease complexes are stable and detectable, as seen with activated protein C-protein C inhibitor complexes in clinical samples [2,6].
Enzymatic activity assays
Functional assays measuring serine protease activity are essential to test the inhibitory consequence of complex formation. The QuickGO definition states that formation of the protein C inhibitor-TMPRSS11E complex inhibits the serine protease activity of TMPRSS11E. Researchers can use fluorogenic or chromogenic substrates to measure TMPRSS11E activity in the presence or absence of SERPINA5. Such assays can be performed with recombinant proteins or cell lysates. The broader literature on blood coagulation and protease regulation provides a framework for these experiments [3,7].
Cell-based imaging and localization
Imaging approaches such as immunofluorescence or live-cell imaging can reveal where the protein C inhibitor-TMPRSS11E complex forms. Because TMPRSS11E is a transmembrane protease, the complex may localize to the cell surface or specific membrane compartments. Tagged knock-in cell lines expressing fluorescently labeled SERPINA5 or TMPRSS11E can be used to track complex assembly. These methods help connect the cellular component annotation to actual subcellular sites. The protein C pathway literature emphasizes the importance of membrane-associated events in protease regulation [4,8].
Genetic perturbation and CRISPR screens
CRISPR-based knockout, point mutation, knock-in, and overexpression models allow researchers to test the function of SERPINA5 and TMPRSS11E in complex formation and downstream biology. For example, knockout of SERPINA5 may increase TMPRSS11E activity, while overexpression may enhance inhibition. Point mutations can be introduced to map interaction interfaces. These approaches are supported by the general utility of CRISPR in studying gene function, and by the clinical relevance of protein C pathway components [4,5,8].
How CRISPR Can Be Used to Study GO:0036025 protein C inhibitor-TMPRSS11E complex
Knockout
CRISPR knockout of SERPINA5 or TMPRSS11E can be used to eliminate one component of the protein C inhibitor-TMPRSS11E complex and assess the consequences for protease activity and cellular phenotypes. For example, SERPINA5 knockout cells may show increased TMPRSS11E activity if the inhibitor is absent. TMPRSS11E knockout cells can reveal whether the protease is required for specific downstream processes. These experiments directly test the functional significance of GO:0036025. The protein C pathway literature supports the importance of such loss-of-function studies in understanding anticoagulant and protease regulation [4,8].
Point Mutation
Point mutations can be introduced into SERPINA5 or TMPRSS11E to map the interaction interface and test the effect of specific amino acid changes on complex formation. For instance, mutations in the reactive center loop of SERPINA5 may disrupt its ability to inhibit TMPRSS11E. Similarly, mutations in the TMPRSS11E active site may prevent stable complex formation. These studies are informed by the example of a Met343Val mutation in activated protein C that causes a low-activity conformer and thrombosis. Point-mutation models allow precise structure-function analysis of GO:0036025.
Knock-in
Knock-in of tagged versions of SERPINA5 or TMPRSS11E enables detection, purification, and tracking of the protein C inhibitor-TMPRSS11E complex in native cellular contexts. For example, a fluorescent tag can be inserted to visualize complex localization by microscopy, while an affinity tag can facilitate co-immunoprecipitation. Knock-in of disease-associated or candidate mutations can also be used to model altered complex behavior. These approaches are valuable for connecting the cellular component annotation to dynamic cellular processes. The broader protein C pathway provides a rationale for studying such complexes in vascular cells [4,8].
Overexpression
Overexpression of SERPINA5 or TMPRSS11E can be used to test whether increasing the abundance of one component shifts the balance of complex formation and protease activity. For example, overexpression of SERPINA5 may enhance inhibition of TMPRSS11E, while overexpression of TMPRSS11E may overwhelm inhibitor capacity. These experiments can reveal dose-dependent effects and help identify downstream consequences of complex formation. Overexpression models complement knockout and knock-in approaches to provide a comprehensive picture of GO:0036025 biology. The literature on serpin-protease balance supports this strategy.
How EDITGENE Supports protein C inhibitor-TMPRSS11E complex Research
Researchers studying protein C inhibitor-TMPRSS11E complex-related genes often need to determine whether a candidate gene is causally involved in complex formation, protease regulation, or downstream vascular biology. EDITGENE provides a suite of CRISPR-based services to generate precisely engineered cell models that enable such causal tests. By combining knockout, point-mutation, knock-in, and overexpression strategies with library screening and bioinformatics, EDITGENE supports hypothesis-driven research on GO:0036025 and its associated pathways.
Contact EDITGENE today to design your custom CRISPR model for protein C inhibitor-TMPRSS11E complex research.
Frequently Asked Questions About protein C inhibitor-TMPRSS11E complex
What is the protein C inhibitor-TMPRSS11E complex?
The protein C inhibitor-TMPRSS11E complex (GO:0036025) is a heterodimeric protein complex containing protein C inhibitor (SERPINA5) and transmembrane protease serine 11E (TMPRSS11E); formation of the complex inhibits the serine protease activity of TMPRSS11E.
What is GO:0036025?
GO:0036025 is the Gene Ontology identifier for the protein C inhibitor-TMPRSS11E complex, a cellular component term.
What genes are involved in the protein C inhibitor-TMPRSS11E complex?
The core genes are SERPINA5, which encodes protein C inhibitor, and TMPRSS11E, which encodes transmembrane protease serine 11E.
What is the function of protein C inhibitor (SERPINA5)?
Protein C inhibitor is a multifunctional serpin that regulates several serine proteases, including those in the protein C anticoagulant pathway.
What is TMPRSS11E?
TMPRSS11E is a transmembrane protease serine 11E, a membrane-associated serine protease that is inhibited upon binding to protein C inhibitor.
How is the protein C inhibitor-TMPRSS11E complex related to disease?
Protein C inhibitor-containing complexes have been detected in vascular disease, including peripheral arterial disease and aortic aneurysms [2,6], and the protein C pathway is linked to thrombosis [4,8].
What research methods are used to study GO:0036025?
Common methods include co-immunoprecipitation, mass spectrometry, protease activity assays, immunofluorescence, and CRISPR-based knockout, point-mutation, knock-in, and overexpression models.
Can CRISPR be used to study the protein C inhibitor-TMPRSS11E complex?
Yes, CRISPR knockout, point mutation, knock-in, and overexpression can be used to perturb SERPINA5 or TMPRSS11E and test effects on complex formation and protease activity.
What is the protein C pathway?
The protein C pathway is a major anticoagulant system that regulates blood coagulation and is reviewed in the literature [4,8].
Why is the protein C inhibitor-TMPRSS11E complex important for vascular biology?
It represents a specific serpin-protease interaction that may influence proteolytic balance in blood and tissues, and related complexes are measurable in vascular disease [2,6].
Conclusion
GO:0036025, the protein C inhibitor-TMPRSS11E complex, defines a specific heterodimeric assembly between SERPINA5 and TMPRSS11E that results in inhibition of TMPRSS11E serine protease activity. This term connects fundamental serpin biology to the broader protein C anticoagulant pathway, which is critical for hemostatic balance and is implicated in thrombotic and vascular diseases [4,7,8]. Clinical studies measuring activated protein C-protein C inhibitor complexes in peripheral arterial disease and aortic aneurysms underscore the potential relevance of serpin-protease complexes as biomarkers [2,6]. By using CRISPR-based knockout, point-mutation, knock-in, and overexpression models, researchers can dissect the molecular determinants and functional consequences of this complex. Such work may reveal new insights into protease regulation and suggest therapeutic or diagnostic opportunities in vascular biology.
References
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- 3. Norris LA. 2003. Blood coagulation.. Best Pract Res Clin Obstet Gynaecol 17(3):369-83 PMID: 12787532
- 4. Esmon CT. 2003. The protein C pathway.. Chest 124(3 Suppl):26S-32S PMID: 12970121
- 5. Zhou S et al.. 2024. Met343Val mutation disrupts the shuttling of Trp380 leading to a low-activity conformer of activated protein C and causes thrombosis.. J Thromb Haemost 22(8):2270-2280 PMID: 38788977
- 6. Kölbel T et al.. 2006. Activated protein C-protein C inhibitor complex: a new biological marker for aortic aneurysms.. J Vasc Surg 43(5):935-9 PMID: 16678686
- 7. Espana F et al.. 2005. The multifunctional protein C system.. Curr Med Chem Cardiovasc Hematol Agents 3(2):119-31 PMID: 15853699
- 8. Dahlbäck B et al.. 2005. The anticoagulant protein C pathway.. FEBS Lett 579(15):3310-6 PMID: 15943976
