Affinage

F13A1

Coagulation factor XIII A chain · UniProt P00488

Round 2 corrected
Length
732 aa
Mass
83.3 kDa
Annotated
2026-04-28
76 papers in source corpus 15 papers cited in narrative 13 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

F13A1 encodes the catalytic A-subunit of coagulation factor XIII, a transglutaminase zymogen that circulates as an A₂ homodimer and is activated by thrombin cleavage of an N-terminal activation peptide followed by calcium-dependent conformational opening of a Cys-His-Asp catalytic triad structurally analogous to cysteine proteases (PMID:4811064, PMID:7913750, PMID:7920263). Activated FXIIIa catalyzes γ-glutamyl-ε-lysyl isopeptide crosslinking of fibrin, with α-chain crosslinking specifically required for red blood cell retention during clot contraction, while selective pharmacological inhibition of FXIIIa reduces thrombus formation without prolonging bleeding time (PMID:26324704, PMID:31578814). In megakaryocytes and platelets, F13A1 is transcriptionally regulated by RUNX1 and functions as a downstream effector supporting integrin αIIbβ3 activation and myosin light chain phosphorylation during clot contraction (PMID:39995753). Beyond hemostasis, intracellular F13A1 in macrophages interacts with PKM2 in a calcium-dependent manner, promoting PKM2 dimerization and nuclear translocation to drive IL-1β expression via the HIF1α axis during pro-inflammatory activation (PMID:41417477).

Mechanistic history

Synthesis pass · year-by-year structured walk · 10 steps
  1. 1974 High

    Establishing that factor XIII is a thrombin-activated zymogen resolved how transglutaminase activity is regulated in coagulation, identifying the activation peptide as the gating element.

    Evidence Amino acid sequencing of tryptic peptides and isolation of activation peptide from purified factor XIII

    PMID:4811064

    Open questions at the time
    • Mechanism by which activation peptide removal triggers catalytic competence was unknown
    • Calcium requirement not yet defined
  2. 1986 High

    Complete primary structure determination revealed F13A1 as a 731-residue transglutaminase sharing the Tyr-Gly-Gln-Cys-Trp active-site motif with tissue transglutaminase, placing it firmly in the transglutaminase family and identifying a second thrombin inactivation site at Lys-513.

    Evidence cDNA cloning from human placenta, automated amino acid sequencing, cyanogen bromide peptide analysis by two independent laboratories

    PMID:2877456 PMID:2877457 PMID:3026437

    Open questions at the time
    • Three-dimensional structure and spatial arrangement of active-site residues unknown
    • Functional significance of inactivation cleavage at Lys-513 not tested
  3. 1988 High

    Mapping the gene structure showed that functionally distinct domains (activation peptide, catalytic cysteine, calcium-binding region) reside on separate exons, providing a framework for understanding disease-causing mutations and evolutionary modularity.

    Evidence Genomic library screening, restriction mapping, Southern blotting, and DNA sequencing of the >160 kb F13A1 locus

    PMID:2901091

    Open questions at the time
    • Promoter and transcriptional regulatory elements not characterized
    • Intronic regulatory sequences not explored
  4. 1994 High

    Crystal structures of the zymogen resolved how the activation peptide from one subunit crosses the dimer interface to occlude the partner's catalytic cavity, explaining why thrombin cleavage and calcium are both required for activation, and revealed a Cys-His-Asp catalytic triad convergently similar to cysteine proteases.

    Evidence X-ray crystallography at 2.8 Å resolution of recombinant human factor XIII zymogen with structural comparison to cysteine proteinases

    PMID:7913750 PMID:7920263

    Open questions at the time
    • No structure of the fully activated enzyme or enzyme–substrate complex
    • Conformational pathway from zymogen to active form not visualized
  5. 1998 High

    Higher-resolution refinement identified non-proline cis peptide bonds near the active site and dimer interface, pinpointing structural features critical for catalysis and A₂ dimer stability, while parallel studies showed lineage-restricted expression in CD14⁺-derived dendritic cells, broadening F13A1 function beyond coagulation.

    Evidence X-ray crystallography at 2.1 Å resolution; RT-PCR-based lineage analysis of DC subpopulations from CD34⁺ progenitors

    PMID:9469423 PMID:9515726

    Open questions at the time
    • Functional role of cis peptide bonds not tested by mutagenesis
    • Function of F13A1 in dendritic cells not determined
  6. 2011 Medium

    Identification of Sp1-dependent transcriptional regulation through intron 1 provided the first mechanistic explanation for how non-coding mutations cause mild FXIII deficiency.

    Evidence Luciferase reporter assays in U937 cells, EMSA, and Sp1 co-transfection rescue for an Int1+12C>A patient mutation

    PMID:21512576

    Open questions at the time
    • No chromatin-level or in vivo confirmation of Sp1 regulation
    • Other intronic regulatory elements not surveyed
    • Single patient mutation studied
  7. 2013 Medium

    Demonstrating that M2 (CD68⁺/CD163⁺) macrophages are the principal cellular source of FXIII-A in inflamed tissue linked the transglutaminase to tissue remodeling beyond plasma clot formation.

    Evidence Real-time PCR, ELISA, immunohistochemistry, and co-immunofluorescence in human nasal polyp tissue

    PMID:23541322

    Open questions at the time
    • No knockdown or knockout to prove functional contribution in tissue remodeling
    • Mechanism of FXIII-A action in tissue not defined
  8. 2015 High

    Dissecting FXIIIa substrate specificity showed that fibrin α-chain crosslinking — not γ-chain crosslinking or other substrates — is the specific mechanism retaining red blood cells in contracting clots, redefining the functional hierarchy among FXIIIa crosslinking activities.

    Evidence Real-time clot contraction microscopy, selective FXIIIa inhibition, flow cytometry, and clots from mice lacking individual FXIIIa substrates

    PMID:26324704

    Open questions at the time
    • Structural basis for α-chain crosslinking's unique role in RBC retention unknown
    • Whether α-chain crosslinking specificity is relevant in arterial versus venous thrombi not addressed
  9. 2019 High

    Pharmacological proof-of-concept with the selective inhibitor ZED3197 demonstrated that FXIIIa transglutaminase activity can be targeted to reduce venous thrombosis without increasing bleeding, separating antithrombotic efficacy from hemostatic risk.

    Evidence Biochemical transamidation/isopeptidase assays, whole-blood thromboelastometry, rabbit venous stasis model

    PMID:31578814

    Open questions at the time
    • No data in arterial thrombosis models
    • Long-term safety and wound healing impact not assessed
    • Mechanism explaining preserved hemostasis despite FXIIIa inhibition not fully elucidated
  10. 2025 High

    Two studies expanded F13A1's mechanistic scope: RUNX1 was identified as a direct transcriptional regulator of F13A1 in megakaryocytes linking it to integrin activation and clot contraction, while in macrophages F13A1 was shown to directly interact with PKM2 to drive pro-inflammatory reprogramming via the PKM2/HIF1α/IL-1β axis.

    Evidence Promoter reporters, siRNA knockdown of RUNX1/F13A1, clot contraction and PAC1/MLC phosphorylation assays in HEL cells and primary megakaryocytes; Co-IP of F13A1–PKM2, DASA-58 pharmacological rescue, in vivo silencing in murine MASH models

    PMID:39995753 PMID:41417477

    Open questions at the time
    • RUNX1-F13A1 axis not validated in vivo with RUNX1-deficient platelets
    • F13A1–PKM2 interaction awaits structural characterization
    • Whether F13A1 transglutaminase activity or a scaffolding role drives PKM2 dimerization is unresolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • No structure of fully activated FXIIIa in complex with fibrin or PKM2 substrates exists, and the intracellular activation mechanism of F13A1 in platelets and macrophages (in the absence of thrombin) remains undefined.
  • No activated FXIIIa–substrate co-crystal structure
  • Thrombin-independent intracellular activation mechanism unknown
  • Relative contribution of enzymatic versus scaffolding functions in immune cells not delineated

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0016740 transferase activity 5 GO:0140096 catalytic activity, acting on a protein 5 GO:0098772 molecular function regulator activity 1
Localization
GO:0005576 extracellular region 3 GO:0005829 cytosol 2 GO:0005634 nucleus 1
Pathway
R-HSA-109582 Hemostasis 6 R-HSA-168256 Immune System 3
Partners
PKM2RUNX1SP1

Evidence

Reading pass · 13 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1974 Factor XIII A-subunit is activated by thrombin cleavage, releasing an activation peptide from the amino terminus. Amino acid sequence analysis of tryptic peptides and activation peptide isolation Biochemistry High 4811064
1986 The A subunit of human factor XIII (F13A1) is a 731-amino acid protein containing a catalytic triad active site with the sequence Tyr-Gly-Gln-Cys-Trp, identical to that of tissue transglutaminase; thrombin cleaves it at two sites — activation at the N-terminus and inactivation after Lys-513. cDNA cloning from human placenta library, amino acid sequencing by automated sequenator, cyanogen bromide peptide analysis Biochemistry High 2877456 2877457 3026437
1988 The F13A1 gene spans >160 kb and contains 15 exons separated by 14 introns; functionally distinct regions (activation peptide, active-site cysteine, calcium-binding regions, thrombin inactivation site) are each encoded by separate exons, suggesting domain-level structural organization. Genomic library screening, restriction mapping, Southern blotting, DNA sequencing Proceedings of the National Academy of Sciences of the United States of America High 2901091
1994 The three-dimensional crystal structure of human factor XIII zymogen at 2.8-Å resolution reveals that each A-subunit chain folds into four sequential domains; a catalytic triad (Cys-His-Asp) reminiscent of cysteine proteases is located in the core domain; the amino-terminal activation peptide of each subunit crosses the dimer interface and partially occludes the catalytic cavity of the second subunit, preventing substrate access in the zymogen. Thrombin cleavage and calcium binding are proposed to open the active site. X-ray crystallography of recombinant human factor XIII at 2.8-Å resolution Proceedings of the National Academy of Sciences of the United States of America High 7913750
1994 Factor XIII uses a cysteine proteinase-like catalytic triad (Cys-His-Asp) to catalyze transglutaminase crosslinking reactions; structural comparison shows active site architecture is shared with cysteine proteinases despite different overall fold, suggesting convergent or divergent evolution. X-ray crystallography, structural comparison of active site residues Protein science : a publication of the Protein Society High 7920263
1998 The refined 2.1-Å crystal structure of human cellular factor XIII zymogen identifies two non-proline cis peptide bonds: one between Arg310 and Tyr311 near the active site cysteine (Cys314), and one between Gln425 and Phe426 at the dimerization interface, suggesting these structural elements are important for catalytic function and dimer stability. X-ray crystallography refined to R-factor 18.3% at 2.1-Å resolution FEBS letters High 9515726
2011 An intronic mutation in intron 1 of F13A1 (Int1+12C>A) causes mild FXIII deficiency by reducing protein binding at an Sp1 site; Sp1 was shown to regulate F13A1 transcription via the first 951 bp of intron 1, and co-transfection with Sp1 restored expression, establishing intron 1 as a regulatory element. Luciferase reporter assays in U937 cells, electrophoretic mobility shift assay (EMSA), Sp1 co-transfection, direct sequencing Journal of human genetics Medium 21512576
2015 FXIIIa-dependent retention of red blood cells in contracting clots is mediated specifically by fibrin α-chain crosslinking; FXIIIa does not directly crosslink RBCs to fibrin. RBC retention was lost when α-chain crosslinking sites were absent but not when γ-chain crosslinking sites were absent, and was independent of FXIIIa substrates α2-antiplasmin, thrombin-activatable fibrinolysis inhibitor, or fibronectin. Real-time microscopy of clot contraction, fibrin band-shift assays, flow cytometry, clots from mice deficient in specific FXIIIa substrates, FXIIIa inhibition at concentrations selectively blocking α- vs γ-chain crosslinking Blood High 26324704
2019 ZED3197, a peptidomimetic inhibitor, potently and selectively inhibits FXIIIa transglutaminase activity (transamidation and isopeptidase assays) with selectivity over other human transglutaminases; it inhibits fibrin crosslinking in whole blood thromboelastometry and reduces clot weight in a rabbit venous stasis model without prolonging bleeding time, demonstrating that FXIIIa inhibition can dissociate antithrombotic effect from bleeding risk. Transamidation and isopeptidase biochemical assays, rotational thromboelastometry in whole human blood, rabbit venous stasis/reperfusion in vivo model Journal of thrombosis and haemostasis : JTH High 31578814
2025 RUNX1 transcription factor directly regulates F13A1 transcription in megakaryocytes and platelets; RUNX1 overexpression increased and siRNA knockdown decreased F13A1 promoter activity and protein. F13A1 knockdown impaired clot contraction, reduced FXIII-A surface expression, decreased myosin light chain phosphorylation, and reduced αIIbβ3 activation (PAC1 binding), establishing F13A1 as a downstream effector of RUNX1 in platelet clot contraction. Promoter luciferase assays in HEL cells, siRNA knockdown of RUNX1 and F13A1, clot contraction assays, flow cytometry (surface FXIII-A, PAC1), myosin light chain phosphorylation assays, human CD34+-derived megakaryocytes Research and practice in thrombosis and haemostasis High 39995753
2025 F13A1 in macrophages directly interacts with pyruvate kinase M2 (PKM2), promoting PKM2 dimerization in a calcium-dependent manner; dimerized PKM2 translocates to the nucleus and upregulates IL-1β via the PKM2/HIF1A axis, driving macrophage pro-inflammatory activation and the Warburg effect in MASH. F13A1 expression in macrophages is induced by lipid-stressed hepatocytes through a sphingosine-1-phosphate (S1P)-dependent mechanism. Co-immunoprecipitation (F13A1-PKM2 interaction), siRNA silencing of F13A1 in vivo and in vitro, nuclear translocation assays, IL-1β expression assays, PKM2 activator (DASA-58) pharmacological rescue, single-nucleus transcriptomic datasets, murine MASH models Advanced science (Weinheim, Baden-Wurttemberg, Germany) Medium 41417477
1998 Factor XIIIa is expressed in CD14+-derived dendritic cells but not in CD1a+-derived dendritic cells, establishing lineage-specific expression of F13A1 within the dendritic cell compartment differentiated from CD34+ progenitors. Semiquantitative RT-PCR and phenotypic analysis of two DC subpopulations generated in vitro from CD34+ progenitors Journal of immunology (Baltimore, Md. : 1950) Medium 9469423
2013 FXIII-A is overexpressed in nasal polyps and is produced predominantly by CD68+/CD163+ M2 macrophages; FXIII-A levels correlate with M2 macrophage markers, implicating macrophage-derived FXIII-A in excessive fibrin crosslinking and tissue remodeling in chronic rhinosinusitis with nasal polyps. Real-time PCR, ELISA, immunohistochemistry, immunofluorescence co-staining with macrophage markers in human sinonasal tissue The Journal of allergy and clinical immunology Medium 23541322

Source papers

Stage 0 corpus · 76 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2002 Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America 1479 12477932
1999 Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nature genetics 1381 10391209
2011 Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Briefings in bioinformatics 656 21873635
2003 Characterization of the proteins released from activated platelets leads to localization of novel platelet proteins in human atherosclerotic lesions. Blood 616 14630798
2004 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome research 438 15489334
2003 The dynamics of thrombin formation. Arteriosclerosis, thrombosis, and vascular biology 387 12524220
2005 Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. Journal of proteome research 350 16335952
2009 Antiphospholipid antibodies and risk of myocardial infarction and ischaemic stroke in young women in the RATIO study: a case-control study. The Lancet. Neurology 315 19783216
1998 The cytokine profile expressed by human dendritic cells is dependent on cell subtype and mode of activation. Journal of immunology (Baltimore, Md. : 1950) 314 9469423
2004 Meta-analysis of genetic studies in ischemic stroke: thirty-two genes involving approximately 18,000 cases and 58,000 controls. Archives of neurology 313 15534175
1994 Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII. Proceedings of the National Academy of Sciences of the United States of America 303 7913750
2011 A directed protein interaction network for investigating intracellular signal transduction. Science signaling 258 21900206
1974 Amino acid sequence studies on factor XIII and the peptide released during its activation by thrombin. Biochemistry 223 4811064
2014 Extracellular matrix signatures of human primary metastatic colon cancers and their metastases to liver. BMC cancer 203 25037231
2015 Cul3-KLHL20 Ubiquitin Ligase Governs the Turnover of ULK1 and VPS34 Complexes to Control Autophagy Termination. Molecular cell 186 26687681
1986 Amino acid sequence of the a subunit of human factor XIII. Biochemistry 186 3026437
2017 Characterization of the Extracellular Matrix of Normal and Diseased Tissues Using Proteomics. Journal of proteome research 185 28675934
2009 Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip. American journal of human genetics 164 19913121
1988 Characterization of the gene for the a subunit of human factor XIII (plasma transglutaminase), a blood coagulation factor. Proceedings of the National Academy of Sciences of the United States of America 161 2901091
1986 Primary structure of blood coagulation factor XIIIa (fibrinoligase, transglutaminase) from human placenta. Proceedings of the National Academy of Sciences of the United States of America 159 2877456
2007 Association of gene variants with incident myocardial infarction in the Cardiovascular Health Study. Arteriosclerosis, thrombosis, and vascular biology 142 17975119
2015 Factor XIIIa-dependent retention of red blood cells in clots is mediated by fibrin α-chain crosslinking. Blood 137 26324704
1986 Characterization of cDNA coding for human factor XIIIa. Proceedings of the National Academy of Sciences of the United States of America 135 2877457
1998 Two non-proline cis peptide bonds may be important for factor XIII function. FEBS letters 128 9515726
2010 Genome-wide association with MRI atrophy measures as a quantitative trait locus for Alzheimer's disease. Molecular psychiatry 127 21116278
1994 Transglutaminase factor XIII uses proteinase-like catalytic triad to crosslink macromolecules. Protein science : a publication of the Protein Society 126 7920263
2013 Ischemic stroke is associated with the ABO locus: the EuroCLOT study. Annals of neurology 125 23381943
1998 Factor XIII Val 34 Leu: a novel association with primary intracerebral hemorrhage. Stroke 115 9550516
2013 Increased expression of factor XIII-A in patients with chronic rhinosinusitis with nasal polyps. The Journal of allergy and clinical immunology 112 23541322
2006 Multiple thrombophilic gene mutations rather than specific gene mutations are risk factors for recurrent miscarriage. American journal of reproductive immunology (New York, N.Y. : 1989) 109 16635210
1988 Localization of the coagulation factor XIII A subunit gene (F13A) to chromosome bands 6p24----p25. Cytogenetics and cell genetics 92 2903011
1987 Suggestion of linkage of a major locus for nonsyndromic orofacial cleft with F13A and tentative assignment to chromosome 6. Clinical genetics 87 2888553
1988 Extensive DNA polymorphism at the factor XIIIa (F13A) locus and linkage to HLA. American journal of human genetics 47 2897163
2016 Coagulation Factor XIIIA (F13A1): Novel Perspectives in Treatment and Pharmacogenetics. Current pharmaceutical design 36 26654441
1991 Tight linkage of the gene for spinocerebellar ataxia to D6S89 on the short arm of chromosome 6 in a kindred for which close linkage to both HLA and F13A1 is excluded. American journal of human genetics 35 1928103
1985 A structural locus for coagulation factor XIIIA (F13A) is located distal to the HLA region on chromosome 6p in man. American journal of human genetics 32 2858156
2019 Novel inhibitor ZED3197 as potential drug candidate in anticoagulation targeting coagulation FXIIIa (F13a). Journal of thrombosis and haemostasis : JTH 28 31578814
1995 Genetic mapping of F13A to BTA23 by sperm typing: difference in recombination rate between bulls in the DYA-PRL interval. Genomics 26 7665157
1984 The gene for coagulation factor XIII a subunit (F13A) is distal to HLA on chromosome 6. Human genetics 25 6149187
2020 Transglutaminases and Obesity in Humans: Association of F13A1 to Adipocyte Hypertrophy and Adipose Tissue Immune Response. International journal of molecular sciences 24 33167412
2021 Platelet Phenotype Analysis of COVID-19 Patients Reveals Progressive Changes in the Activation of Integrin αIIbβ3, F13A1, the SARS-CoV-2 Target EIF4A1 and Annexin A5. Frontiers in cardiovascular medicine 20 34859078
2014 Eight novel F13A1 gene missense mutations in patients with mild FXIII deficiency: in silico analysis suggests changes in FXIII-A subunit structure/function. Annals of hematology 20 24889649
1994 Swiss population data on three tetrameric short tandem repeat loci--VWA, HUMTHO1, and F13A1--derived using multiplex PCR and laser fluorescence detection. International journal of legal medicine 20 7999643
2021 Alterations of the Platelet Proteome in Lung Cancer: Accelerated F13A1 and ER Processing as New Actors in Hypercoagulability. Cancers 19 34066760
2020 F13A1 transglutaminase expression in human adipose tissue increases in acquired excess weight and associates with inflammatory status of adipocytes. International journal of obesity (2005) 18 33221826
2017 Comparison of F13A1 gene mutations in 73 patients treated with recombinant FXIII-A2. Haemophilia : the official journal of the World Federation of Hemophilia 17 28520207
2018 F13A1 Gene Variant (V34L) and Residual Circulating FXIIIA Levels Predict Short- and Long-Term Mortality in Acute Myocardial Infarction after Coronary Angioplasty. International journal of molecular sciences 16 30223472
2015 Xueshuan Xinmaining Tablet Treats Blood Stasis through Regulating the Expression of F13a1, Car1, and Tbxa2r. Evidence-based complementary and alternative medicine : eCAM 16 25821496
2012 Androgen levels and metabolic parameters are associated with a genetic variant of F13A1 in women with polycystic ovary syndrome. Gene 16 22565190
1985 Linkage between the loci for mitochondrial malic enzyme (ME2) and coagulation factor XIIIA subunit (F13A). Human genetics 13 2860058
2019 Phenotype and genotype of FXIII deficiency in two unrelated probands: identification of a novel F13A1 large deletion mediated by complex rearrangement. Orphanet journal of rare diseases 11 31340840
2018 Activation peptide of the coagulation factor XIII (AP-F13A1) as a new biomarker for the screening of colorectal cancer. Clinical proteomics 11 29657559
2011 Homozygous intronic mutation leading to inefficient transcription combined with a novel frameshift mutation in F13A1 gene causes FXIII deficiency. Journal of human genetics 10 21512576
1994 Genetic studies on the Senegal population. II. Polymorphisms of the plasma proteins F13A, F13B, ORM1, AHSG, C6, C7, and APOC2. Human biology 10 8001915
2018 Polymorphisms of F2, PROC, PROZ, and F13A1 Genes are Associated With Recurrent Spontaneous Abortion in Chinese Han Women. Clinical and applied thrombosis/hemostasis : official journal of the International Academy of Clinical and Applied Thrombosis/Hemostasis 9 29363996
2013 Severe congenital factor XIII deficiency caused by novel W187X and G273V mutations in the F13A gene; diagnosis and classification according to the ISTH/SSC guidelines. Haemophilia : the official journal of the World Federation of Hemophilia 9 24286209
2016 Characterization of a novel large deletion caused by double-stranded breaks in 6-bp microhomologous sequences of intron 11 and 12 of the F13A1 gene. Human genome variation 8 27081562
1988 Analysis for linkage between F13A and three chromosome 6 marker loci: evidence for 6pter:F13A:HLA:GLO1:cen gene order. Human genetics 7 2900213
2024 Single-cell dissection reveals immunosuppressive F13A1+ macrophage as a hallmark for multiple primary lung cancers. Clinical and translational medicine 6 39601163
2020 Factor XIII deficiency in two Spanish families with a novel variant in gene F13A1 detected by next-generation sequencing; symptoms and clinical management. Journal of thrombosis and thrombolysis 5 32060721
2015 Novel and recurrent mutations in the F13A1 gene in unrelated Korean patients with congenital factor XIII deficiency. Blood coagulation & fibrinolysis : an international journal in haemostasis and thrombosis 5 25004025
2013 A common F13A1 intron 1 variant IVS1+12(A) is associated with mild FXIII deficiency in Caucasian population. Annals of hematology 5 23508224
1990 Formal and population genetics of F13A and FUCA1 polymorphisms in northern Portugal. Human heredity 5 2312127
2019 Identification of novel pathogenic F13A1 mutation and novel NBEAL2 gene missense mutation in a pedigree with hereditary congenital factor XIII deficiency. Gene 4 30935919
2017 Coagulation F13A1 V34L, fibrinogen and homocysteine versus conventional risk factors in the pathogenesis of MI in young persons. Acta cardiologica 3 28978253
2022 Genetic Spectrum in F13A1 Detected by Next-Generation Sequencing Among North Indian Patients with FXIII Deficiency. Indian journal of hematology & blood transfusion : an official journal of Indian Society of Hematology and Blood Transfusion 2 37006978
2000 Diversity of two short tandem repeat loci (CD4 and F13A1) in three Brazilian ethnic groups. Human biology 2 11236860
2025 Transcription factor RUNX1 regulates coagulation factor XIII-A (F13A1): decreased platelet-megakaryocyte F13A1 expression and clot contraction in RUNX1 haplodeficiency. Research and practice in thrombosis and haemostasis 1 39995753
2025 Plasma extracellular vesicle proteomics identifies FN1/F13A1-TGF-β pathway as the major signaling pathway associated with persistent atrial fibrillation. Journal of pharmaceutical and biomedical analysis 1 41177109
2025 F13A1-Mediated Macrophage Activation Promotes MASH Progression via the PKM2/HIF1A Pathway. Advanced science (Weinheim, Baden-Wurttemberg, Germany) 1 41417477
2000 Allelic affinities between the F13A common gene products inferred by the analysis of an (AAAG)n STR polymorphism within the 5' untranslated region. Human heredity 1 10686499
1990 RFLP in human F13A gene. Nucleic acids research 1 1969626
2025 Congenital factor XIII deficiency caused by F13A1 gene mutations presenting with intracranial hemorrhage: a case report. Frontiers in pediatrics 0 41488895
2024 Transcription Factor RUNX1 Regulates Coagulation Factor XIII-A ( F13A1 ): Decreased Platelet-Megakaryocyte F13A1 Expression and Clot Contraction in RUNX1 Haplodeficiency. medRxiv : the preprint server for health sciences 0 39763522
2022 A novel F13A1 gene mutation (Arg208Pro) in a Chinese patient with factor XIII deficiency. Blood coagulation & fibrinolysis : an international journal in haemostasis and thrombosis 0 35981255
1998 [Genetic polymorphisms of FABP2 and F13A1 loci in Han population]. Zhonghua yi xue yi chuan xue za zhi = Zhonghua yixue yichuanxue zazhi = Chinese journal of medical genetics 0 9456361