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Hereditary antithrombin deficiency(AT3D; THPH7)

MedGen UID:
75781
Concept ID:
C0272375
Disease or Syndrome
Synonyms: Antithrombin deficiency; Antithrombin III deficiency; Reduced antithrombin III activity; Thrombophilia due to antithrombin III deficiency
SNOMED CT: Antithrombin deficiency (36351005); Antithrombin 3 deficiency (36351005); AT (antithrombin) deficiency (36351005); Antithrombin III deficiency (36351005)
Modes of inheritance:
Autosomal dominant inheritance
MedGen UID:
141047
Concept ID:
C0443147
Intellectual Product
Source: Orphanet
A mode of inheritance that is observed for traits related to a gene encoded on one of the autosomes (i.e., the human chromosomes 1-22) in which a trait manifests in heterozygotes. In the context of medical genetics, an autosomal dominant disorder is caused when a single copy of the mutant allele is present. Males and females are affected equally, and can both transmit the disorder with a risk of 50% for each child of inheriting the mutant allele.
 
Gene (location): SERPINC1 (1q25.1)
 
HPO: HP:0001976
Monarch Initiative: MONDO:0013144
OMIM®: 613118
Orphanet: ORPHA82

Definition

Deficiency of antithrombin III is a major risk factor for venous thromboembolic disease. Two categories of AT-III deficiency have been defined on the basis of AT-III antigen levels in the plasma of affected individuals. The majority of AT-III deficiency families belong in the type I (classic) deficiency group and have a quantitatively abnormal phenotype in which antigen and heparin cofactor levels are both reduced to about 50% of normal. The second category of AT-III deficiency has been termed type II (functional) deficiency. Affected individuals from these kindreds produce dysfunctional AT-III molecules; they have reduced heparin cofactor activity levels (about 50% of normal) but levels of AT-III antigen are often normal or nearly normal (summary by Bock and Prochownik, 1987). The 2 categories of antithrombmin III deficiency have been classified further. Type I (low functional and immunologic antithrombin) has been subdivided into subtype Ia (reduced levels of normal antithrombin), and type Ib (reduced levels of antithrombin and the presence of low levels of a variant). Type II (low functional but normal immunologic antithrombin) has been subdivided into subtype IIa (functional abnormalities affecting both the reactive site and the heparin-binding site of AT3); subtype IIb (functional abnormalities limited to the reactive site); and subtype IIc (functional abnormalities limited to the heparin-binding site) (summary by Lane et al., 1992). [from OMIM]

Additional description

From MedlinePlus Genetics
Hereditary antithrombin deficiency is a disorder of blood clotting. People with this condition are at higher than average risk for developing abnormal blood clots, particularly a type of clot that occurs in the deep veins of the legs. This type of clot is called a deep vein thrombosis (DVT). Affected individuals also have an increased risk of developing a pulmonary embolism (PE), which is a clot that travels through the bloodstream and lodges in the lungs. In hereditary antithrombin deficiency, abnormal blood clots usually form only in veins, although they may rarely occur in arteries.

About half of people with hereditary antithrombin deficiency will develop at least one abnormal blood clot during their lifetime. These clots usually develop after adolescence.

Other factors can increase the risk of abnormal blood clots in people with hereditary antithrombin deficiency. These factors include increasing age, surgery, or immobility. The combination of hereditary antithrombin deficiency and other inherited disorders of blood clotting can also influence risk. Women with hereditary antithrombin deficiency are at increased risk of developing an abnormal blood clot during pregnancy or soon after delivery. They also may have an increased risk for pregnancy loss (miscarriage) or stillbirth.  https://medlineplus.gov/genetics/condition/hereditary-antithrombin-deficiency

Clinical features

From HPO
Pulmonary embolism
MedGen UID:
11027
Concept ID:
C0034065
Pathologic Function
An embolus (that is, an abnormal particle circulating in the blood) located in the pulmonary artery and thereby blocking blood circulation to the lung. Usually the embolus is a blood clot that has developed in an extremity (for instance, a deep venous thrombosis), detached, and traveled through the circulation before becoming trapped in the pulmonary artery.
Arterial occlusion
MedGen UID:
78117
Concept ID:
C0264995
Pathologic Function
Blockage of blood flow through an artery.
Deep venous thrombosis
MedGen UID:
57448
Concept ID:
C0149871
Disease or Syndrome
Formation of a blot clot in a deep vein. The clot often blocks blood flow, causing swelling and pain. The deep veins of the leg are most often affected.
Cerebral venous thrombosis
MedGen UID:
57743
Concept ID:
C0151945
Disease or Syndrome
Formation of a blood clot (thrombus) inside a cerebral vein, causing the obstruction of blood flow.
Hereditary antithrombin deficiency
MedGen UID:
75781
Concept ID:
C0272375
Disease or Syndrome
Deficiency of antithrombin III is a major risk factor for venous thromboembolic disease. Two categories of AT-III deficiency have been defined on the basis of AT-III antigen levels in the plasma of affected individuals. The majority of AT-III deficiency families belong in the type I (classic) deficiency group and have a quantitatively abnormal phenotype in which antigen and heparin cofactor levels are both reduced to about 50% of normal. The second category of AT-III deficiency has been termed type II (functional) deficiency. Affected individuals from these kindreds produce dysfunctional AT-III molecules; they have reduced heparin cofactor activity levels (about 50% of normal) but levels of AT-III antigen are often normal or nearly normal (summary by Bock and Prochownik, 1987). The 2 categories of antithrombmin III deficiency have been classified further. Type I (low functional and immunologic antithrombin) has been subdivided into subtype Ia (reduced levels of normal antithrombin), and type Ib (reduced levels of antithrombin and the presence of low levels of a variant). Type II (low functional but normal immunologic antithrombin) has been subdivided into subtype IIa (functional abnormalities affecting both the reactive site and the heparin-binding site of AT3); subtype IIb (functional abnormalities limited to the reactive site); and subtype IIc (functional abnormalities limited to the heparin-binding site) (summary by Lane et al., 1992).
Recurrent thrombophlebitis
MedGen UID:
763064
Concept ID:
C3550150
Finding
Repeated episodes of inflammation of a vein associated with venous thrombosis (blood clot formation within the vein).
Decreased level of heparin co-factor II
MedGen UID:
909798
Concept ID:
C4280717
Finding
An abnormality of coagulation related to a decreased concentration of heparin co-factor II

Conditions with this feature

Hereditary antithrombin deficiency
MedGen UID:
75781
Concept ID:
C0272375
Disease or Syndrome
Deficiency of antithrombin III is a major risk factor for venous thromboembolic disease. Two categories of AT-III deficiency have been defined on the basis of AT-III antigen levels in the plasma of affected individuals. The majority of AT-III deficiency families belong in the type I (classic) deficiency group and have a quantitatively abnormal phenotype in which antigen and heparin cofactor levels are both reduced to about 50% of normal. The second category of AT-III deficiency has been termed type II (functional) deficiency. Affected individuals from these kindreds produce dysfunctional AT-III molecules; they have reduced heparin cofactor activity levels (about 50% of normal) but levels of AT-III antigen are often normal or nearly normal (summary by Bock and Prochownik, 1987). The 2 categories of antithrombmin III deficiency have been classified further. Type I (low functional and immunologic antithrombin) has been subdivided into subtype Ia (reduced levels of normal antithrombin), and type Ib (reduced levels of antithrombin and the presence of low levels of a variant). Type II (low functional but normal immunologic antithrombin) has been subdivided into subtype IIa (functional abnormalities affecting both the reactive site and the heparin-binding site of AT3); subtype IIb (functional abnormalities limited to the reactive site); and subtype IIc (functional abnormalities limited to the heparin-binding site) (summary by Lane et al., 1992).
PMM2-congenital disorder of glycosylation
MedGen UID:
138111
Concept ID:
C0349653
Disease or Syndrome
PMM2-CDG, the most common of a group of disorders of abnormal glycosylation of N-linked oligosaccharides, is divided into three clinical stages: infantile multisystem, late-infantile and childhood ataxia–intellectual disability, and adult stable disability. The clinical manifestations and course are highly variable, ranging from infants who die in the first year of life to mildly affected adults. Clinical findings tend to be similar in sibs. In the infantile multisystem presentation, infants show axial hypotonia, hyporeflexia, esotropia, and developmental delay. Feeding problems, vomiting, faltering growth, and developmental delay are frequently seen. Subcutaneous fat may be excessive over the buttocks and suprapubic region. Two distinct clinical courses are observed: (1) a nonfatal neurologic course with faltering growth, strabismus, developmental delay, cerebellar hypoplasia, and hepatopathy in infancy followed by neuropathy and retinitis pigmentosa in the first or second decade; and (2) a more severe neurologic-multivisceral course with approximately 20% mortality in the first year of life. The late-infantile and childhood ataxia–intellectual disability stage, which begins between ages three and ten years, is characterized by hypotonia, ataxia, severely delayed language and motor development, inability to walk, and IQ of 40 to 70; other findings include seizures, stroke-like episodes or transient unilateral loss of function, coagulopathy, retinitis pigmentosa, joint contractures, and skeletal deformities. In the adult stable disability stage, intellectual ability is stable; peripheral neuropathy is variable, progressive retinitis pigmentosa and myopia are seen, thoracic and spinal deformities with osteoporosis worsen, and premature aging is observed; females may lack secondary sexual development and males may exhibit decreased testicular volume. Hypogonadotropic hypogonadism and coagulopathy may occur. The risk for deep venous thrombosis is increased.
Congenital disorder of glycosylation type 1E
MedGen UID:
324784
Concept ID:
C1837396
Disease or Syndrome
Congenital disorders of glycosylation (CDGs) are metabolic deficiencies in glycoprotein biosynthesis that usually cause severe mental and psychomotor retardation. Different forms of CDGs can be recognized by altered isoelectric focusing (IEF) patterns of serum transferrin. For a general discussion of CDGs, see CDG Ia (212065) and CDG Ib (602579).
MPI-congenital disorder of glycosylation
MedGen UID:
400692
Concept ID:
C1865145
Disease or Syndrome
Congenital disorders of glycosylation (CDGs) are a genetically heterogeneous group of autosomal recessive disorders caused by enzymatic defects in the synthesis and processing of asparagine (N)-linked glycans or oligosaccharides on glycoproteins. Type I CDGs comprise defects in the assembly of the dolichol lipid-linked oligosaccharide (LLO) chain and its transfer to the nascent protein. These disorders can be identified by a characteristic abnormal isoelectric focusing profile of plasma transferrin (Leroy, 2006). For a discussion of the classification of CDGs, see CDG1A (212065). CDG Ib is clinically distinct from most other CDGs by the lack of significant central nervous system involvement. The predominant symptoms are chronic diarrhea with failure to thrive and protein-losing enteropathy with coagulopathy. Some patients develop hepatic fibrosis. CDG Ib is also different from other CDGs in that it can be treated effectively with oral mannose supplementation, but can be fatal if untreated (Marquardt and Denecke, 2003). Thus, CDG Ib should be considered in the differential diagnosis of patients with unexplained hypoglycemia, chronic diarrhea, liver disease, or coagulopathy in order to allow early diagnosis and effective therapy (Vuillaumier-Barrot et al., 2002) Freeze and Aebi (1999) reviewed CDG Ib and CDG Ic (603147). Marques-da-Silva et al. (2017) systematically reviewed the literature concerning liver involvement in CDG.
PGM1-congenital disorder of glycosylation
MedGen UID:
414536
Concept ID:
C2752015
Disease or Syndrome
Congenital disorder of glycosylation type It (CDG1T) is an autosomal recessive disorder characterized by a wide range of clinical manifestations and severity. The most common features include cleft lip and bifid uvula, apparent at birth, followed by hepatopathy, intermittent hypoglycemia, short stature, and exercise intolerance, often accompanied by increased serum creatine kinase. Less common features include rhabdomyolysis, dilated cardiomyopathy, and hypogonadotropic hypogonadism (summary by Tegtmeyer et al., 2014). For a discussion of the classification of CDGs, see CDG1A (212065).
ALG6-congenital disorder of glycosylation 1C
MedGen UID:
443952
Concept ID:
C2930997
Disease or Syndrome
Congenital disorders of glycosylation, previously called carbohydrate-deficient glycoprotein syndromes (CDGSs), are caused by defects in mannose addition during N-linked oligosaccharide assembly. CDGs can be divided into 2 types, depending on whether they impair lipid-linked oligosaccharide (LLO) assembly and transfer (CDG I), or affect trimming of the protein-bound oligosaccharide or the addition of sugars to it (CDG II) (Orlean, 2000). CDG Ic is characterized by psychomotor retardation with delayed walking and speech, hypotonia, seizures, and sometimes protein-losing enteropathy. It is the second largest subtype of CDG (summary by Sun et al., 2005). For a discussion of the classification of CDGs, see CDG1A (212065). Freeze and Aebi (1999) reviewed CDG Ib (602579) and CDG Ic.
ALG12-congenital disorder of glycosylation
MedGen UID:
443954
Concept ID:
C2931001
Disease or Syndrome
Congenital disorders of glycosylation (CDG), previously called carbohydrate-deficient glycoprotein syndromes (CDGSs), are a group of hereditary multisystem disorders first recognized by Jaeken et al. (1980). The characteristic biochemical abnormality of CDGs is the hypoglycosylation of glycoproteins, which is routinely determined by isoelectric focusing (IEF) of serum transferrin. Type I CDG comprises those disorders in which there is a defect in the assembly of lipid-linked oligosaccharides or their transfer onto nascent glycoproteins, whereas type II CDG comprises defects of trimming, elongation, and processing of protein-bound glycans. CDG1G is a multisystem disorder characterized by impaired psychomotor development, dysmorphic features, failure to thrive, male genital hypoplasia, coagulation abnormalities, and immune deficiency. More variable features include skeletal dysplasia, cardiac anomalies, ocular abnormalities, and sensorineural hearing loss. Some patients die in the early neonatal or infantile period, whereas others are mildly affected and live to adulthood (summary by Tahata et al., 2019). For a general discussion of CDGs, see CDG1A (212065).
ALG8 congenital disorder of glycosylation
MedGen UID:
419692
Concept ID:
C2931002
Disease or Syndrome
CDGs, previously called carbohydrate-deficient glycoprotein syndromes, grew from hereditary multisystem disorders first recognized by Jaeken et al. (1980). The characteristic biochemical abnormality of CDGs is the hypoglycosylation of glycoproteins, which is routinely determined by isoelectric focusing of serum transferrin. Type I CDG comprises those disorders in which there is a defect in the assembly of lipid-linked oligosaccharides or their transfer onto nascent glycoproteins, whereas type II CDG comprises defects of trimming, elongation, and processing of protein-bound glycans. For a general discussion of CDGs, see CDG1A (212065). CDG1H is a severe form of CDG. The majority of patients have brain involvement, liver pathology, gastrointestinal symptoms, dysmorphism (including brachydactyly), eye involvement (especially cataract), and skin symptoms. Most patients die within the first year of life (summary by Marques-da-Silva et al., 2017).
DPAGT1-congenital disorder of glycosylation
MedGen UID:
419694
Concept ID:
C2931004
Disease or Syndrome
Like all CDGs, which are caused by a shortage of precursor monosaccharide phosphate or deficiencies in the glycosyltransferases required for lipid-linked oligosaccharide precursor (LLO) synthesis, CDG Ij is caused by a defect in the formation of DPAGT1, the first dolichyl-linked intermediate of the protein N-glycosylation pathway. For a general discussion of CDGs, see CDG1A (212065).
ALG9 congenital disorder of glycosylation
MedGen UID:
443955
Concept ID:
C2931006
Disease or Syndrome
Congenital disorders of glycosylation (CDGs) that represent defects of dolichol-linked oligosaccharide assembly are classified as CDG type I. For a general description and a discussion of the classification of CDGs, see CDG1A (212065).
MGAT2-congenital disorder of glycosylation
MedGen UID:
443956
Concept ID:
C2931008
Disease or Syndrome
Congenital disorders of glycosylation (CDGs) are a genetically heterogeneous group of autosomal recessive disorders caused by enzymatic defects in the synthesis and processing of asparagine (N)-linked glycans or oligosaccharides on glycoproteins. These glycoconjugates play critical roles in metabolism, cell recognition and adhesion, cell migration, protease resistance, host defense, and antigenicity, among others. CDGs are divided into 2 main groups: type I CDGs (see, e.g., CDG1A, 212065) comprise defects in the assembly of the dolichol lipid-linked oligosaccharide (LLO) chain and its transfer to the nascent protein, whereas type II CDGs refer to defects in the trimming and processing of the protein-bound glycans either late in the endoplasmic reticulum or the Golgi compartments. The biochemical changes of CDGs are most readily observed in serum transferrin (TF; 190000), and the diagnosis is usually made by isoelectric focusing of this glycoprotein (reviews by Marquardt and Denecke, 2003; Grunewald et al., 2002). Genetic Heterogeneity of Congenital Disorder of Glycosylation Type II Multiple forms of CDG type II have been identified; see CDG2B (606056) through CDG2Z (620201), and CDG2AA (620454) to CDG2BB (620546).
SRD5A3-congenital disorder of glycosylation
MedGen UID:
1392124
Concept ID:
C4317224
Disease or Syndrome
SRD5A3-congenital disorder of glycosylation (SRD5A3-CDG, formerly known as congenital disorder of glycosylation type Iq) is an inherited condition that causes neurological and vision problems and other signs and symptoms. The pattern and severity of this condition's features vary widely among affected individuals.\n\nIndividuals with SRD5A3-CDG typically develop signs and symptoms of the condition during infancy or early childhood. Most individuals with SRD5A3-CDG have intellectual disability, vision problems, unusual facial features,low muscle tone (hypotonia), and problems with coordination and balance (ataxia). \n\nVision problems in SRD5A3-CDG often include involuntary side-side movements of the eyes (nystagmus), a gap or hole in one of the structures of the eye (coloboma), underdevelopment of the nerves that carry signals between the eyes and the brain(optic nerve hypoplasia), or vision loss early in life (early-onset severe retinal dystrophy). Over time, affected individuals may develop clouding of the lenses of the eyes (cataracts) or increased pressure in the eyes (glaucoma).\n\nOther features of SRD5A3-CDG can include skin rash, unusually small red blood cells (microcytic anemia),and liver problems.
Congenital disorder of glycosylation, type IIw
MedGen UID:
1794196
Concept ID:
C5561986
Disease or Syndrome
Congenital disorder of glycosylation type IIw (CDG2W) is an autosomal dominant metabolic disorder characterized by liver dysfunction, coagulation deficiencies, and profound abnormalities in N-glycosylation of serum specific proteins. All reported patients carry the same mutation (602671.0017) (summary by Ng et al., 2021). For an overview of congenital disorders of glycosylation, see CDG1A (212065) and CDG2A (212066).
Congenital disorder of glycosylation, type IIaa
MedGen UID:
1841287
Concept ID:
C5830651
Disease or Syndrome
Congenital disorder of glycosylation type IIaa (CDG2AA) is an autosomal recessive disorder characterized by infantile mortality due to liver disease, skeletal abnormalities, and protein glycosylation defects (Linders et al., 2021). For an overview of congenital disorders of glycosylation, see CDG1A (212065) and CDG2A (212066).

Professional guidelines

PubMed

James AH, Bates SM, Bauer KA, Branch W, Mann K, Paidas M, Silverman N, Konkle BA
Thromb Res 2017 Sep;157:41-45. Epub 2017 May 24 doi: 10.1016/j.thromres.2017.05.017. PMID: 28689083
Bauer KA, Nguyen-Cao TM, Spears JB
Ann Pharmacother 2016 Sep;50(9):758-67. Epub 2016 Jun 8 doi: 10.1177/1060028016651276. PMID: 27281301
Rodgers GM
Thromb Haemost 2009 May;101(5):806-12. PMID: 19404531

Recent clinical studies

Etiology

James AH, Bates SM, Bauer KA, Branch W, Mann K, Paidas M, Silverman N, Konkle BA
Thromb Res 2017 Sep;157:41-45. Epub 2017 May 24 doi: 10.1016/j.thromres.2017.05.017. PMID: 28689083
Bauer KA, Nguyen-Cao TM, Spears JB
Ann Pharmacother 2016 Sep;50(9):758-67. Epub 2016 Jun 8 doi: 10.1177/1060028016651276. PMID: 27281301
Paidas MJ, Forsyth C, Quéré I, Rodger M, Frieling JT, Tait RC; Recombinant Human Antithrombin Study Group
Blood Coagul Fibrinolysis 2014 Jul;25(5):444-50. doi: 10.1097/MBC.0000000000000076. PMID: 24686101
Rogenhofer N, Bohlmann MK, Beuter-Winkler P, Würfel W, Rank A, Thaler CJ, Toth B
Ann Hematol 2014 Mar;93(3):385-92. Epub 2013 Sep 3 doi: 10.1007/s00277-013-1892-0. PMID: 23999648
Pabinger I, Grafenhofer H
Wien Klin Wochenschr 2003 Aug 14;115(13-14):482-4. doi: 10.1007/BF03041032. PMID: 13677267

Diagnosis

Ashraf VV, Salam KA, Kizhedath R, Puthussery K
Neurol India 2023 Sep-Oct;71(5):984-986. doi: 10.4103/0028-3886.388110. PMID: 37929439
Bauer KA, Nguyen-Cao TM, Spears JB
Ann Pharmacother 2016 Sep;50(9):758-67. Epub 2016 Jun 8 doi: 10.1177/1060028016651276. PMID: 27281301
Khor B, Van Cott EM
Am J Hematol 2010 Dec;85(12):947-50. doi: 10.1002/ajh.21893. PMID: 21108326
Pabinger I, Grafenhofer H
Semin Thromb Hemost 2003 Dec;29(6):633-8. doi: 10.1055/s-2004-815630. PMID: 14719179
Pabinger I, Grafenhofer H
Wien Klin Wochenschr 2003 Aug 14;115(13-14):482-4. doi: 10.1007/BF03041032. PMID: 13677267

Therapy

Tang LV, Tao Y, Feng Y, Ma J, Lin W, Zhang Y, Zhang Y, Wu T, Cai Y, Lu H, Wei J, Corral J, Hu Y
Sci Transl Med 2022 Nov 30;14(673):eabq3202. doi: 10.1126/scitranslmed.abq3202. PMID: 36449603
Bauer KA, Nguyen-Cao TM, Spears JB
Ann Pharmacother 2016 Sep;50(9):758-67. Epub 2016 Jun 8 doi: 10.1177/1060028016651276. PMID: 27281301
Rogenhofer N, Bohlmann MK, Beuter-Winkler P, Würfel W, Rank A, Thaler CJ, Toth B
Ann Hematol 2014 Mar;93(3):385-92. Epub 2013 Sep 3 doi: 10.1007/s00277-013-1892-0. PMID: 23999648
Rodgers GM
Thromb Haemost 2009 May;101(5):806-12. PMID: 19404531
Pabinger I, Grafenhofer H
Wien Klin Wochenschr 2003 Aug 14;115(13-14):482-4. doi: 10.1007/BF03041032. PMID: 13677267

Prognosis

Čápová Irena, Salaj Peter, Hrachovinová Ingrid
Ceska Gynekol 2021;86(3):175-182. doi: 10.48095/cccg2021175. PMID: 34167310
Orlando C, de la Morena-Barrio B, Pareyn I, Vanhoorelbeke K, Martínez-Martínez I, Vicente V, Corral J, Jochmans K, de la Morena-Barrio ME
Thromb Haemost 2021 Feb;121(2):182-191. Epub 2020 Sep 13 doi: 10.1055/s-0040-1716531. PMID: 32920809
Pabinger I, Thaler J
Blood 2019 Dec 26;134(26):2346-2353. doi: 10.1182/blood.2019002927. PMID: 31697819
Croles FN, Mulder R, Mulder AB, Lukens MV, Meijer K
Thromb Res 2018 Aug;168:47-52. Epub 2018 Jun 2 doi: 10.1016/j.thromres.2018.06.004. PMID: 29902631
Luxembourg B, Delev D, Geisen C, Spannagl M, Krause M, Miesbach W, Heller C, Bergmann F, Schmeink U, Grossmann R, Lindhoff-Last E, Seifried E, Oldenburg J, Pavlova A
Thromb Haemost 2011 Apr;105(4):635-46. Epub 2011 Jan 25 doi: 10.1160/TH10-08-0538. PMID: 21264449

Clinical prediction guides

Tang LV, Tao Y, Feng Y, Ma J, Lin W, Zhang Y, Zhang Y, Wu T, Cai Y, Lu H, Wei J, Corral J, Hu Y
Sci Transl Med 2022 Nov 30;14(673):eabq3202. doi: 10.1126/scitranslmed.abq3202. PMID: 36449603
Čápová Irena, Salaj Peter, Hrachovinová Ingrid
Ceska Gynekol 2021;86(3):175-182. doi: 10.48095/cccg2021175. PMID: 34167310
Orlando C, de la Morena-Barrio B, Pareyn I, Vanhoorelbeke K, Martínez-Martínez I, Vicente V, Corral J, Jochmans K, de la Morena-Barrio ME
Thromb Haemost 2021 Feb;121(2):182-191. Epub 2020 Sep 13 doi: 10.1055/s-0040-1716531. PMID: 32920809
Kjaergaard AD, Larsen OH, Hvas AM, Nissen PH
Thromb Res 2019 Mar;175:68-75. Epub 2019 Jan 31 doi: 10.1016/j.thromres.2019.01.022. PMID: 30721820
Luxembourg B, Delev D, Geisen C, Spannagl M, Krause M, Miesbach W, Heller C, Bergmann F, Schmeink U, Grossmann R, Lindhoff-Last E, Seifried E, Oldenburg J, Pavlova A
Thromb Haemost 2011 Apr;105(4):635-46. Epub 2011 Jan 25 doi: 10.1160/TH10-08-0538. PMID: 21264449

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