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Volumn 128, Issue 2, 1996, Pages 218-227

Molecular basis for protein s hereditary deficiency: Genetic defects observed in 118 patients with type I and type IIa deficiencies

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EID: 0030205254     PISSN: 00222143     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2143(96)90015-3     Document Type: Article
Times cited : (61)

References (64)
  • 1
    • 0001627642 scopus 로고
    • Inherited antithrombin deficiency causing thrombophilia
    • Egeberg O. Inherited antithrombin deficiency causing thrombophilia. Thromb Diath Haemorrh 1965;13:516-30.
    • (1965) Thromb Diath Haemorrh , vol.13 , pp. 516-530
    • Egeberg, O.1
  • 2
    • 0027520285 scopus 로고
    • Venous thrombosis due to poor anticoagulant response to activated protein C: Leiden thrombophilia study
    • Koster T, Rosendaal FR, de Ronde H, Briët E, Vandenbroucke JP, Bettina RM. Venous thrombosis due to poor anticoagulant response to activated protein C: Leiden thrombophilia study. Lancet 1993;342:1503-7.
    • (1993) Lancet , vol.342 , pp. 1503-1507
    • Koster, T.1    Rosendaal, F.R.2    De Ronde, H.3    Briët, E.4    Vandenbroucke, J.P.5    Bettina, R.M.6
  • 3
    • 0028098210 scopus 로고
    • Resistance to activated protein C as a basis for venous thrombosis
    • Svensson PJ, Dahlbäck B. Resistance to activated protein C as a basis for venous thrombosis. N Engl J Med 1994;330: 517-22.
    • (1994) N Engl J Med , vol.330 , pp. 517-522
    • Svensson, P.J.1    Dahlbäck, B.2
  • 5
    • 0021720421 scopus 로고
    • Recurrent venous thromboembolism in patients with a partial deficiency of protein S
    • Comp PC, Esmon CT. Recurrent venous thromboembolism in patients with a partial deficiency of protein S. N Engl J Med 1984;311:1525-8.
    • (1984) N Engl J Med , vol.311 , pp. 1525-1528
    • Comp, P.C.1    Esmon, C.T.2
  • 6
    • 0021740029 scopus 로고
    • Familial protein S deficiency is associated with recurrent thrombosis
    • Schwartz H, Fischer M, Hopmeier P, Batard MA, Griffin HH. Familial protein S deficiency is associated with recurrent thrombosis. Blood 1984;64:1297-300.
    • (1984) Blood , vol.64 , pp. 1297-1300
    • Schwartz, H.1    Fischer, M.2    Hopmeier, P.3    Batard, M.A.4    Griffin, H.H.5
  • 7
    • 0028314865 scopus 로고
    • Mutation in blood coagulation F V associated with resistance to activated protein C
    • Bertina RM, Koeleman BPC, Koster T, et al. Mutation in blood coagulation F V associated with resistance to activated protein C. Nature 1994;369:64-7.
    • (1994) Nature , vol.369 , pp. 64-67
    • Bertina, R.M.1    Koeleman, B.P.C.2    Koster, T.3
  • 8
    • 0029043736 scopus 로고
    • Protein C deficiency: A database of mutations. 1995 update. on behalf of the subcommittee on plasma coagulation inhibitors of the scientific and standardization committee of the ISTH
    • Reitsma PH, Bernardi F, Doig RG, et al. Protein C deficiency: a database of mutations. 1995 update. On behalf of the subcommittee on plasma coagulation inhibitors of the scientific and standardization committee of the ISTH. Thromb Haemost 1995;73:876-89.
    • (1995) Thromb Haemost , vol.73 , pp. 876-889
    • Reitsma, P.H.1    Bernardi, F.2    Doig, R.G.3
  • 10
    • 0026029146 scopus 로고
    • A 5.3-kb deletion including exon XIII of the protein S gene occurs in two protein S-deficient families
    • Schmidel DK, Nelson RM, Broxson EH Jr, Comp PC, Marlar RA, Long GL. A 5.3-kb deletion including exon XIII of the protein S gene occurs in two protein S-deficient families. Blood 1991;77:551-9.
    • (1991) Blood , vol.77 , pp. 551-559
    • Schmidel, D.K.1    Nelson, R.M.2    Broxson Jr., E.H.3    Comp, P.C.4    Marlar, R.A.5    Long, G.L.6
  • 11
    • 23444453692 scopus 로고
    • Three novel mutations in five unrelated subjects with hereditary protein S deficiency type I
    • Reitsma PH, Ploos van Amstel HK, Bertina RM. Three novel mutations in five unrelated subjects with hereditary protein S deficiency type I. J Clin Invest 1994;93:486-92.
    • (1994) J Clin Invest , vol.93 , pp. 486-492
    • Reitsma, P.H.1    Ploos Van Amstel, H.K.2    Bertina, R.M.3
  • 12
    • 0028132684 scopus 로고
    • First frameshift mutation in the active protein S gene associated with a quantitative hereditary deficiency
    • Borgel D, Gandrille S, Gouault-Heilmann M, Aiach M. First frameshift mutation in the active protein S gene associated with a quantitative hereditary deficiency. Blood Coagul Fibrinolysis 1994;5:593-600.
    • (1994) Blood Coagul Fibrinolysis , vol.5 , pp. 593-600
    • Borgel, D.1    Gandrille, S.2    Gouault-Heilmann, M.3    Aiach, M.4
  • 13
    • 0028175686 scopus 로고
    • Homozygous protein S deficiency due to a one base pairdeletion that leads to a stop codon in exon III of the protein S gene
    • Gomez E, Ledford MR, Pegelow CH, Reitsma PH, Bertina RM. Homozygous protein S deficiency due to a one base pairdeletion that leads to a stop codon in exon III of the protein S gene. Thromb Haemost 1994;71:723-6.
    • (1994) Thromb Haemost , vol.71 , pp. 723-726
    • Gomez, E.1    Ledford, M.R.2    Pegelow, C.H.3    Reitsma, P.H.4    Bertina, R.M.5
  • 14
    • 0027953010 scopus 로고
    • Protein S Tokushima: Abnormal molecule with a substitution of Glu for Lys-155 in the second epidermal growth F-like domains of protein S
    • Hayashi T, Nishioka J, Shigekiyo T, Saito S, Suzuki K. Protein S Tokushima: abnormal molecule with a substitution of Glu for Lys-155 in the second epidermal growth F-like domains of protein S. Blood 1994;83:683-90.
    • (1994) Blood , vol.83 , pp. 683-690
    • Hayashi, T.1    Nishioka, J.2    Shigekiyo, T.3    Saito, S.4    Suzuki, K.5
  • 15
    • 0029060076 scopus 로고
    • Identification of eight point mutations in protein S deficiency type I. Analysis of 15 pedigrees
    • Gomez E, Poort SR, Bertina RM, Reitsma PH. Identification of eight point mutations in protein S deficiency type I. Analysis of 15 pedigrees. Thromb Haemost 1995;73:750-5.
    • (1995) Thromb Haemost , vol.73 , pp. 750-755
    • Gomez, E.1    Poort, S.R.2    Bertina, R.M.3    Reitsma, P.H.4
  • 16
    • 0028871033 scopus 로고
    • Identification of 15 different candidate causal point mutations and 3 polymorphisms in 19 patients with protein S deficiency using a scanning method for the analysis of the protein S active gene
    • Gandrille S, Borgel D, Eschwege-Gufflet V, et al. Identification of 15 different candidate causal point mutations and 3 polymorphisms in 19 patients with protein S deficiency using a scanning method for the analysis of the protein S active gene. Blood 1995;85:130-8.
    • (1995) Blood , vol.85 , pp. 130-138
    • Gandrille, S.1    Borgel, D.2    Eschwege-Gufflet, V.3
  • 17
    • 0029021380 scopus 로고
    • A quantitative protein S deficiency associated with a novel nonsense mutation and markedly reduced levels of mutated mRNA
    • Yamazaki T, Motohiro H, Akira K, et al. A quantitative protein S deficiency associated with a novel nonsense mutation and markedly reduced levels of mutated mRNA. Thromb Haemost 1995;74:590-5.
    • (1995) Thromb Haemost , vol.74 , pp. 590-595
    • Yamazaki, T.1    Motohiro, H.2    Akira, K.3
  • 18
    • 0029112835 scopus 로고
    • Detection and characterization of seven novel protein S (PROS) gene. Lesions: Evaluation of reverse transcript-polymerase chain reaction as a mutation screening strategy
    • Formstone C, Wacey A, Berg L, et al. Detection and characterization of seven novel protein S (PROS) gene. Lesions: evaluation of reverse transcript-polymerase chain reaction as a mutation screening strategy. Blood 1995;86: 2632-41.
    • (1995) Blood , vol.86 , pp. 2632-2641
    • Formstone, C.1    Wacey, A.2    Berg, L.3
  • 19
    • 0028818519 scopus 로고
    • Protein S deficiency type I: Identification of point mutations in 9 of 10 families
    • Mustafa S, Pabinger I, Mannhalter C. Protein S deficiency type I: identification of point mutations in 9 of 10 families. Blood 1995;86:3444-51.
    • (1995) Blood , vol.86 , pp. 3444-3451
    • Mustafa, S.1    Pabinger, I.2    Mannhalter, C.3
  • 20
    • 0029926730 scopus 로고    scopus 로고
    • Five novel mutations of the protein S active gene (PROS1) in 8 Norman families
    • Duchemin J, Borg JY, Borgel D, et al. Five novel mutations of the protein S active gene (PROS1) in 8 Norman families. Thromb Haemost 1996;75:437-44.
    • (1996) Thromb Haemost , vol.75 , pp. 437-444
    • Duchemin, J.1    Borg, J.Y.2    Borgel, D.3
  • 21
    • 0026452551 scopus 로고
    • Protein S and protein C. Biochemistry, physiology, and clinical manifestation of deficiencies
    • Esmon CT. Protein S and protein C. Biochemistry, physiology, and clinical manifestation of deficiencies. Trends Cardiovasc Med 1992;2:214-9.
    • (1992) Trends Cardiovasc Med , vol.2 , pp. 214-219
    • Esmon, C.T.1
  • 22
    • 0027404562 scopus 로고
    • Binding of protein S to F Va associated with inhibition of prothrombinase that is independent of activated protein C
    • Heeb MJ, Mesters RM, Tans G, Rosing J, Griffin JH. Binding of protein S to F Va associated with inhibition of prothrombinase that is independent of activated protein C. J Biol Chem 1993;268:2872-7.
    • (1993) J Biol Chem , vol.268 , pp. 2872-2877
    • Heeb, M.J.1    Mesters, R.M.2    Tans, G.3    Rosing, J.4    Griffin, J.H.5
  • 24
    • 0025833619 scopus 로고
    • Protein S and C4b-binding protein: Components involved in the regulation of the protein C anticoagulant system
    • Dahlbäck B. Protein S and C4b-binding protein: components involved in the regulation of the protein C anticoagulant system. Thromb Haemost 1991;66:49-61.
    • (1991) Thromb Haemost , vol.66 , pp. 49-61
    • Dahlbäck, B.1
  • 25
    • 0026654203 scopus 로고
    • Reevaluation of total, free, and bound protein S and C4b-binding protein levels in plasma anticoagulated with citrate or hirudin
    • Griffin JH, Gruber A, Fernandez JA. Reevaluation of total, free, and bound protein S and C4b-binding protein levels in plasma anticoagulated with citrate or hirudin. Blood 1992;79: 3203-11.
    • (1992) Blood , vol.79 , pp. 3203-3211
    • Griffin, J.H.1    Gruber, A.2    Fernandez, J.A.3
  • 26
    • 0023922249 scopus 로고
    • Changes in the plasma levels of vitamin K-dependent proteins C and S and of C4b-binding protein during pregnancy and oral contraception
    • Malm J, Laurell M, Dahlbäck B. Changes in the plasma levels of vitamin K-dependent proteins C and S and of C4b-binding protein during pregnancy and oral contraception. Br J Haematol 1988;68:437-43.
    • (1988) Br J Haematol , vol.68 , pp. 437-443
    • Malm, J.1    Laurell, M.2    Dahlbäck, B.3
  • 27
    • 0024003059 scopus 로고
    • Acquired deficiencies of protein S. Protein S activity during oral anticoagulation, in liver disease, and in disseminated intravascular coagulation
    • D'Angelo A, Vigano-D'Angelo S, Esmon CT, Comp PC. Acquired deficiencies of protein S. Protein S activity during oral anticoagulation, in liver disease, and in disseminated intravascular coagulation. J Clin Invest 1988;81: 1445-54.
    • (1988) J Clin Invest , vol.81 , pp. 1445-1454
    • D'Angelo, A.1    Vigano-D'Angelo, S.2    Esmon, C.T.3    Comp, P.C.4
  • 28
    • 0028783339 scopus 로고
    • Plasma levels of protein S, protein C, and F X: Effect of sex, hormonal state and age
    • Henkens C, Bom V, van der Schaaf W, et al. Plasma levels of protein S, protein C, and F X: effect of sex, hormonal state and age. Thromb Haemost 1995;74:1271-5.
    • (1995) Thromb Haemost , vol.74 , pp. 1271-1275
    • Henkens, C.1    Bom, V.2    Van Der Schaaf, W.3
  • 29
    • 0022636454 scopus 로고
    • An abnormal plasma distribution of protein S occurs in functional protein S deficiency
    • Comp PC, Doray D, Patton D, Esmon CT. An abnormal plasma distribution of protein S occurs in functional protein S deficiency. Blood 1985;67:504-8.
    • (1985) Blood , vol.67 , pp. 504-508
    • Comp, P.C.1    Doray, D.2    Patton, D.3    Esmon, C.T.4
  • 30
    • 0025217659 scopus 로고
    • Laboratory evaluation of protein S status
    • Comp PC. Laboratory evaluation of protein S status. Semin Thromb Hemost 1990;16:177-81.
    • (1990) Semin Thromb Hemost , vol.16 , pp. 177-181
    • Comp, P.C.1
  • 31
    • 0023851558 scopus 로고
    • The gene for protein S maps near the centomer of human chromosome 3
    • Watkins P, Eddy R, Fukushima Y, et al. The gene for protein S maps near the centomer of human chromosome 3. Blood 1988;71:238-41.
    • (1988) Blood , vol.71 , pp. 238-241
    • Watkins, P.1    Eddy, R.2    Fukushima, Y.3
  • 32
    • 0025182946 scopus 로고
    • Molecular analysis of the gene for vitamin K dependent protein S and its pseudogene. Cloning and partial gene organization
    • Edenbrandt CM, Lundwall A, Wydro R, Stenflo J. Molecular analysis of the gene for vitamin K dependent protein S and its pseudogene. Cloning and partial gene organization. Biochemistry 1990;29:7861-8.
    • (1990) Biochemistry , vol.29 , pp. 7861-7868
    • Edenbrandt, C.M.1    Lundwall, A.2    Wydro, R.3    Stenflo, J.4
  • 33
    • 0025003450 scopus 로고
    • Intron-exon organization of the active human protein S gene PSa and its pseudogene PSb: Duplication and silencing during primate evolution
    • Ploos van Amstel HK, Reitsma PH, van der Logt PE, Bertina RM. Intron-exon organization of the active human protein S gene PSa and its pseudogene PSb: duplication and silencing during primate evolution. Biochemistry 1990; 29:7853-61.
    • (1990) Biochemistry , vol.29 , pp. 7853-7861
    • Ploos Van Amstel, H.K.1    Reitsma, P.H.2    Van Der Logt, P.E.3    Bertina, R.M.4
  • 35
    • 0028240822 scopus 로고
    • Scanning method to establish the molecular basis of protein C deficiencies
    • Gandrille S, Goossens M, Aiach M. Scanning method to establish the molecular basis of protein C deficiencies. Hum Mutat 1994;4:20-30.
    • (1994) Hum Mutat , vol.4 , pp. 20-30
    • Gandrille, S.1    Goossens, M.2    Aiach, M.3
  • 36
    • 0029050714 scopus 로고
    • Incidence of activated protein C resistance due to the Arg 506 Gln mutation in F V in 113 unrelated symptomatic protein C deficient patients
    • Gandrille S, Greengard J, Alhenc-Gelas M, et al. Incidence of activated protein C resistance due to the Arg 506 Gln mutation in F V in 113 unrelated symptomatic protein C deficient patients. Blood 1995;86:219-24.
    • (1995) Blood , vol.86 , pp. 219-224
    • Gandrille, S.1    Greengard, J.2    Alhenc-Gelas, M.3
  • 39
    • 0025151012 scopus 로고
    • Heerlen polymorphism of protein S, an immunologic polymorphism due to dimorphism of residue 460
    • Bertina RM, Ploos van Amstel HK, van Wijngaarden A, et al. Heerlen polymorphism of protein S, an immunologic polymorphism due to dimorphism of residue 460. Blood 1990;76: 538-48.
    • (1990) Blood , vol.76 , pp. 538-548
    • Bertina, R.M.1    Ploos Van Amstel, H.K.2    Van Wijngaarden, A.3
  • 40
    • 0028850076 scopus 로고
    • The Ser 460 to Pro substitution of the protein S a (PROS1) gene is a frequent mutation associated with free protein S (type IIa) deficiency
    • Duchemin J, Gandrille S, Borgel D, et al. The Ser 460 to Pro substitution of the protein S a (PROS1) gene is a frequent mutation associated with free protein S (type IIa) deficiency. Blood 1995;86:3436-43.
    • (1995) Blood , vol.86 , pp. 3436-3443
    • Duchemin, J.1    Gandrille, S.2    Borgel, D.3
  • 41
    • 0026465569 scopus 로고
    • Hereditary deficiency of antithrombin III, protein C and protein S: Prevalence in patients with a history of venous thrombosis and criteria for ratio nal patient screening
    • Pabinger I, Brücker S, Kyrie PA, Schneider B, Korninger HC, Niessner H, et al. Hereditary deficiency of antithrombin III, protein C and protein S: prevalence in patients with a history of venous thrombosis and criteria for ratio nal patient screening. Blood Coagul Fibrinolysis 1992;3: 547-53.
    • (1992) Blood Coagul Fibrinolysis , vol.3 , pp. 547-553
    • Pabinger, I.1    Brücker, S.2    Kyrie, P.A.3    Schneider, B.4    Korninger, H.C.5    Niessner, H.6
  • 42
    • 0023476284 scopus 로고
    • Computational simulation of DNA melting and its application to denaturing gradient gel electrophoresis
    • New York: Academic Press
    • Lerman LS, Silverstein K. Computational simulation of DNA melting and its application to denaturing gradient gel electrophoresis. In: Methods in enzymology. New York: Academic Press, 1987:482-501.
    • (1987) Methods in Enzymology , pp. 482-501
    • Lerman, L.S.1    Silverstein, K.2
  • 43
    • 0025989429 scopus 로고
    • Molecular characterization of mild-to-moderate hemophilia A: Detection of the mutation in 25 of 29 patients by denaturing gradient gel electrophoresis
    • Higuchi M, Antonarakis SE, Kasch L, et al. Molecular characterization of mild-to-moderate hemophilia A: detection of the mutation in 25 of 29 patients by denaturing gradient gel electrophoresis. Proc Natl Acad Sci USA 1991;88:8307-11.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8307-8311
    • Higuchi, M.1    Antonarakis, S.E.2    Kasch, L.3
  • 44
    • 0024651105 scopus 로고
    • Mutations in the catalytic domain of human coagulation F IX: Rapid characterization by direct genomic sequencing of DNA fragments displaying an altered melting behavior
    • Attree O, Vidaud D, Vidaud M, Amselem S, Lavergne JM, Goossens M. Mutations in the catalytic domain of human coagulation F IX: rapid characterization by direct genomic sequencing of DNA fragments displaying an altered melting behavior. Genomics 1989;4:266-72.
    • (1989) Genomics , vol.4 , pp. 266-272
    • Attree, O.1    Vidaud, D.2    Vidaud, M.3    Amselem, S.4    Lavergne, J.M.5    Goossens, M.6
  • 45
    • 0027018911 scopus 로고
    • A comprehensive scanning method for rapid detection of β-globin gene mutations and polymorphisms
    • Ghanem N, Girodon E, Vidaud M, et al. A comprehensive scanning method for rapid detection of β-globin gene mutations and polymorphisms. Hum Mutat 1992;1:229-39.
    • (1992) Hum Mutat , vol.1 , pp. 229-239
    • Ghanem, N.1    Girodon, E.2    Vidaud, M.3
  • 46
    • 0027185201 scopus 로고
    • Identification of a splice-site mutation in the low density lipoprotein receptor gene by denaturing gradient gel electrophoresis
    • Top B, Van Der Zee A, Havekes LM, Van't Hooft FM, Frants RR. Identification of a splice-site mutation in the low density lipoprotein receptor gene by denaturing gradient gel electrophoresis. Hum Genet 1994;91:480-4.
    • (1994) Hum Genet , vol.91 , pp. 480-484
    • Top, B.1    Van Der Zee, A.2    Havekes, L.M.3    Van't Hooft, F.M.4    Frants, R.R.5
  • 47
    • 0026780584 scopus 로고
    • Molecular characterization of cystic fibrosis: 16 novel mutations identified by analysis of the whole cystic fibrosis conductance transmembrane regulator (CFTR) coding regions and splice site junctions
    • Fanen P, Ghanem N, Vidaud M, et al. Molecular characterization of cystic fibrosis: 16 novel mutations identified by analysis of the whole cystic fibrosis conductance transmembrane regulator (CFTR) coding regions and splice site junctions. Genomics 1992;13:770-6.
    • (1992) Genomics , vol.13 , pp. 770-776
    • Fanen, P.1    Ghanem, N.2    Vidaud, M.3
  • 48
    • 0027169164 scopus 로고
    • Detection of a molecular defect in 40 of 44 patients with haemophilia B by PCR and denaturing gradient gel electrophoresis
    • Tartary M, Vidaud D, Piao Y, et al. Detection of a molecular defect in 40 of 44 patients with haemophilia B by PCR and denaturing gradient gel electrophoresis. Br J Haematol 1993; 84:662-9.
    • (1993) Br J Haematol , vol.84 , pp. 662-669
    • Tartary, M.1    Vidaud, D.2    Piao, Y.3
  • 49
    • 0025820639 scopus 로고
    • Molecular characterization of severe hemophilia A suggests that about half the mutations are not within the coding regions and splice junctions of the F VIII gene
    • Higuchi M, Kazazian HH, Kasch L, et al. Molecular characterization of severe hemophilia A suggests that about half the mutations are not within the coding regions and splice junctions of the F VIII gene. Proc Natl Acad Sci USA 1991;88: 7405-9.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7405-7409
    • Higuchi, M.1    Kazazian, H.H.2    Kasch, L.3
  • 50
    • 0027520025 scopus 로고
    • Inversions disrupting the F VIII gene are a common cause of severe haemophilia A
    • Lakich D, Kazazian HH, Antonarakis SE, Gitschier J. Inversions disrupting the F VIII gene are a common cause of severe haemophilia A. Nat Genet 1993;5:236-41.
    • (1993) Nat Genet , vol.5 , pp. 236-241
    • Lakich, D.1    Kazazian, H.H.2    Antonarakis, S.E.3    Gitschier, J.4
  • 51
    • 0011944522 scopus 로고
    • Aberrant splicing and missense mutations cause steroid 21-hydroxylase [P-450(C21)] deficiency in humans: Possible gene conversion products
    • Higashi Y, Tanae A, Inoue H, Hiromasa T, Fujii-Kuriyama Y. Aberrant splicing and missense mutations cause steroid 21-hydroxylase [P-450(C21)] deficiency in humans: possible gene conversion products. Proc Natl Acad Sci USA 1988;85: 7486-90.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 7486-7490
    • Higashi, Y.1    Tanae, A.2    Inoue, H.3    Hiromasa, T.4    Fujii-Kuriyama, Y.5
  • 52
    • 0010336865 scopus 로고
    • Isolation and sequence of the cDNA for human protein S, a regulator of blood coagulation
    • Lundwall A, Dackowski W, Cohen E, et al. Isolation and sequence of the cDNA for human protein S, a regulator of blood coagulation. Proc Natl Acad Sci USA 1986;83:6716-20.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 6716-6720
    • Lundwall, A.1    Dackowski, W.2    Cohen, E.3
  • 53
    • 0023154513 scopus 로고
    • Cloning and characterization of human liver cDNA encoding a protein S precursor
    • Hoskins JA, Norman DK, Beckmann RJ, Long GL. Cloning and characterization of human liver cDNA encoding a protein S precursor. Proc Natl Acad Sci USA 1987;84:349-53.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 349-353
    • Hoskins, J.A.1    Norman, D.K.2    Beckmann, R.J.3    Long, G.L.4
  • 54
    • 0028323598 scopus 로고
    • Cloning and sequencing of a cDNA encoding the murine vitamin K-dependent protein S
    • Chu MD, Sun J, Bird P. Cloning and sequencing of a cDNA encoding the murine vitamin K-dependent protein S. Biochim Biophys Acta 1994;1217:325-8.
    • (1994) Biochim Biophys Acta , vol.1217 , pp. 325-328
    • Chu, M.D.1    Sun, J.2    Bird, P.3
  • 55
    • 0010662163 scopus 로고
    • Primary structure of bovine vitamin K-dependent protein S
    • Dahlbäck B, Lundwall A, Stenflo J. Primary structure of bovine vitamin K-dependent protein S. Proc Natl Acad Sci USA 1986;83:4199-203.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 4199-4203
    • Dahlbäck, B.1    Lundwall, A.2    Stenflo, J.3
  • 56
    • 0027431508 scopus 로고
    • Molecular cloning, expression and functional characterization of rabbit anticoagulant vitamin K-dependent protein S
    • He X, Dahlbäck B. Molecular cloning, expression and functional characterization of rabbit anticoagulant vitamin K-dependent protein S. Eur J Biochem 1993;217:857-65.
    • (1993) Eur J Biochem , vol.217 , pp. 857-865
    • He, X.1    Dahlbäck, B.2
  • 57
    • 0029017118 scopus 로고
    • Evaluation of the relation between protein S and C4b-binding protein isoforms in hereditary protein S deficiency demonstrating type I and type III deficiencies to be phenotypic variants of the same genetic disease
    • Zöller B, Garcia de Frutos P, Dahlbäck B. Evaluation of the relation between protein S and C4b-binding protein isoforms in hereditary protein S deficiency demonstrating type I and type III deficiencies to be phenotypic variants of the same genetic disease. Blood 1995;85:3524-31.
    • (1995) Blood , vol.85 , pp. 3524-3531
    • Zöller, B.1    Garcia De Frutos, P.2    Dahlbäck, B.3
  • 58
    • 0028103281 scopus 로고
    • Differential regulation of a and b chains of C4b-binding protein during acute-phase response resulting in stable plasma levels of free anticoagulant protein S
    • de Frutos PG, Alim RIM, Härdig Y, Zöller B, Dahlbäck B. Differential regulation of a and b chains of C4b-binding protein during acute-phase response resulting in stable plasma levels of free anticoagulant protein S. Blood 1994;84: 815-22.
    • (1994) Blood , vol.84 , pp. 815-822
    • De Frutos, P.G.1    Alim, R.I.M.2    Härdig, Y.3    Zöller, B.4    Dahlbäck, B.5
  • 60
    • 0028098080 scopus 로고
    • The influence of low protein S plasma levels in young women, on the definition of normal range
    • Gari M, Kalkon L, Urrutia T, Vallvé C, Borrell M, Fontcuberta J. The influence of low protein S plasma levels in young women, on the definition of normal range. Thromb Res 1995;73:149-52.
    • (1995) Thromb Res , vol.73 , pp. 149-152
    • Gari, M.1    Kalkon, L.2    Urrutia, T.3    Vallvé, C.4    Borrell, M.5    Fontcuberta, J.6
  • 61
    • 0028037137 scopus 로고
    • Identification of the same F V gene mutation in 47 out of 50 thrombosis-prone families with inherited resistance to activated protein C
    • Zöller B, Svensson PJ, He X, Dahlbäck B. Identification of the same F V gene mutation in 47 out of 50 thrombosis-prone families with inherited resistance to activated protein C. J Clin Invest 1994;94:2521-4.
    • (1994) J Clin Invest , vol.94 , pp. 2521-2524
    • Zöller, B.1    Svensson, P.J.2    He, X.3    Dahlbäck, B.4
  • 62
    • 0029016883 scopus 로고
    • Resistance to actived protein C as an additional genetic risk factor in hereditary deficiency of protein S
    • Zöller B, Berntsdotter A, Garcia de Frutos P, Dahlbäck B. Resistance to actived protein C as an additional genetic risk factor in hereditary deficiency of protein S. Blood 1995;85: 3518-23.
    • (1995) Blood , vol.85 , pp. 3518-3523
    • Zöller, B.1    Berntsdotter, A.2    Garcia De Frutos, P.3    Dahlbäck, B.4
  • 64
    • 0027965649 scopus 로고
    • Physiological anticoagulation. Resistance to activated protein C and venous thromboembolism
    • Dahlbäck B. Physiological anticoagulation. Resistance to activated protein C and venous thromboembolism. J Clin Invest 1994;94:923-7.
    • (1994) J Clin Invest , vol.94 , pp. 923-927
    • Dahlbäck, B.1


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