Department of Medicine

References

1. van Boven HH, Olds RJ, Thein SL, Reitsma PH, Lane DA, Briet E, Vandenbroucke JP, Rosendaal FR. Hereditary antithrombin deficiency: heterogeneity of the molecular basis and mortality in Dutch families. Blood 1994; 84: 4209-4213.

2. Csurgay E, Ireland H, Thompson E, Conard J, Mannucci PM, Andrews V, Worsley A, Sas G, Lane DA. Novel mutations in seven families with type I antithrombin deficiency. Thrombosis and Haemostasis 1995; 73: 935.

3. Daly M, Perry DJ, Bruce DB, Harper PL, Tait RC, Walker ID, Mayne EE, Daly HM, Brown K, Carrell RW. Type I antithrombin deficiency: 5 novel mutations associated with thrombosis. Blood Coagulation and Fibrinolysis 1996.

4. Daly ME, Perry DJ, Harper PL, Carrell RW. The molecular basis of quantitative antithrombin deficiency in 8 unrelated families. British Journal of Haematology 1992; 80: 15.

5. Daly M, Perry DJ, Harper PL, Daly HM, Roques AWW, Carrell RW. Insertions/deletions in the antithrombin gene: 3 mutations associated with non-expression. Thrombosis and Haemostasis 1992; 67: 521-525.

6. Chowdhury V, Olds RJ, Lane DA, Conard J, Pabinger I, Ryan K, Bauer K, Bhavani M, Abildgaard U, Finazzi G, Castaman G, Mannucci PM, Thein SL. Identification of nine novel mutations in type I antithrombin deficiency by heteroduplex screening. British Journal of Haematology 1993; 84: 656-661. 

7. Millar DS, Wacey AI, Ribando J, Melissari E, Laursen B, Woods P, Kakkar VV, Cooper DN. Three novel missense mutations in the antithrombin III (AT3) gene causing recurrent venous thrombosis. Human Genetics 1995; 94: 509-512.

8. Olds RJ, Lane DA, Ireland H, Leone G, De Stefano V, Wiesel ML, Cazenave JP, Thein SL. Novel point mutations leading to type I antithrombin deficiency and thrombosis. British Journal of Haematology 1991; 78: 408-413.

9. Perry DJ. Ectopic transcript analysis in human antithrombin deficiency. Blood Coagulation and Fibrinolysis 1995; 6: 531-536.

10. Olds RJ, Lane DA, Beresford CH, Abildgaard U, Hughes PM, Thein SL. A recurrent deletion in the antithrombin gene, AT106-108(-6bp), identified by DNA heteroduplex detection. Genomics 1993; 16: 298-299.

11. Millar DS, Lopez A, White D, Abraham G, Laursen B, Holding S, Reverter JC, Reynand J, Martinowitz U, Hayes JPLA, Kakkar VV, Cooper DN. Screening for mutations in the antithrombin III (AT3) gene causing recurrent venous thrombosis by single strand conformation polymorphism analysis. Human Mutation 1993; 2: 324-326.

12. Olds RJ, Lane DA, Finazzi G, Barbui T, Thein SL. A frameshift mutation leading to type 1 antithrombin deficiency and thrombosis. Blood 1990; 76: 2182-2186.

13. Emmerich J, Vidaud D, Alhenc-Gelas M, Chadeuf G, Gouault-Heilmann M, Aillaud MF, Aiach M. Three novel mutations of antithrombin inducing high molecular mass compounds. Arteriosclerosis and Thrombosis 1994; 14: 1958-1965.

14. Gandrille S, Vidaud D, Emmerich J, Clauser E, Sie P, Fiessinger JN, Alhenc-Gelas M, Priollet P, Aiach M. Molecular basis for hereditary antithrombin III quantitative deficiencies: a stop codon in exon IIIa and a frameshift in exon V1. British Journal of Haematology 1991; 78: 414-420.

15. Olds RJ, Lane DA, Ireland H, Finazzi G, Barbui T, Abildgaard U, Girolami A, Thein SL. A common point mutation producing type Ia antithrombin III deficiency: AT129 CGA to TGA (Arg to Stop). Thrombosis Research 1991; 64: 621-625.

16. Tomonori A, Iwahana H, Yoshimoto K, Shigekiyo T, Saito S, Itakura M. Two new nonsense mutations in type Ia antithrombin III deficiency at Leu140 and Arg197. Thrombosis and Haemostasis 1992; 68: 455-459.

17. Jochmans K, Lissens W, Yin T, Michiels JJ, van der Luit L, Peerlinc- K, Vervoot R, De Wale M, Liebaers I. Molecular basis for type I antithrombin deficiency: identification of two novel mutations and evidence for a de novo splice mutation. Blood 1994; 84: 3742-3748.

18. Perry DJ, Daly ME, Colvin BT, Brown K, Carrell RW. Two antithrombin mutations in a compound heterozygote: Met20Thr and Tyr166Cys. American Journal of Hematology 1995; 50: 215-216.

19. Berg LP, Grundy CB, Thomas F, Millar DS, Green PJ, Slomski R, Reiss J, Kakkar VV, Cooper DN. De novo splice site mutation in the antithrombin III (AT3) gene causing recurrent venous thrombosis: demonstration of exon skipping by ectopic transcript analysis. Genomics 1992; 13: 1359-1361.

20. Perry DJ, Marshall C, Borg JY, Tait RC, Daly ME, Walker ID, Carrell RW. Two new antithrombin variants, Asn 187 Lys, indicate a functional role for asparagine 187. Blood Coagulation and Fibrinolysis 1995; 6: 51-54.

21. Michiels JJ, van der Luit L, van Vliet H, Jochmans K, Lissens W. Nonsense mutation in Arg 197 stop in a Dutch family with type I hereditary antithrombin deficiency causing thrombophilia. Thrombosis Research 1995; 78: 251-254.

22. Vidaud D, Emmerich J, Sirieix ME, Sie P, Alhenc-Gelas M, Aiach M. Molecular basis for antithrombin III type I deficiency: 3 novel mutations located in exon IV. Blood 1991; 78: 2305-2309.

23. Grundy CB, Thomas F, Millar DS, Krawczak M, Melissari E, Lindo V, Moffat E, Kakkar VV, Cooper DN. Recurrent deletion in the human antithrombin III gene. Blood 1991; 78: 1027-1032.

24. Grundy CB, Holding S, Millar DS, Kakkar VV, Cooper DN. A novel missense mutation in the antithrombin III gene (Ser 349 to Pro) causing recurrent venous thrombosis. Human Genetics 1992; 88: 707-708.

25. Emmerich J, Chadeuf G, Alhenc-Gelas M, Gouault-Heilmann M, Toulon P, Fiessinger JN, Aiach M. Molecular basis of antithrombin type I deficiency: the first large in-frame deletion and two novel mutations in exon 6. Thrombosis and Haemostasis 1994; 72: 534-539.

26. White D, Abraham G, Carter C, Kakkar VV, Cooper DN. A novel missense mutation in the antithrombin III gene (Ala 387 to Val) causing recurrent venous thrombosis. Human Genetics 1993; 90: 472-473.

27. Jochmans K, Lissens W, Vervoot R, Peeters S, De Wale M, Liebaers I. Antithrombin-Gly 424 Arg: a novel point mutation responsible for type I antithrombin deficiency and neonatal thrombosis. Blood 1994; 83: 146-151.

28. Olds RJ, Lane DA, Chowdury V, De Stefano V, Leone G, Thein SL. Complete nucleotide sequence of the antithrombin gene. Evidence for homologous recombination causing thrombophilia. Biochemistry 1993; 32: 4216-4224.

29. Olds RJ, Lane DA, Chowdury V, Sas G, Pabinger I, Auberger K, Thein SL. (ATT) trinucleotide repeats in the antithrombin gene and their use in determining the origin of repeated mutations. Human Mutation 1994; 4: 31-41.

30. Fernandez-Rachubinski RA, Rachubinski RA, Blajchman MA. Partial deletion of antithrombin III allele in a kindred with a type I deficiency. Blood 1992; 80: 1476-1485.

31. Olds RJ, Lane DA, Chowdury V, Samson D, DeStafano V, Leone G, Wiesel ML, Cazenave JP, Conard J, Thein SL. Major rearrangements within the antithrombin gene locus: an unusual cause for antithrombin deficiency. British Journal of Haematology 1992; 40.

32. Winter JH, Bennett B, Watt JL, Brown T, San Roman C, Schinzel A, King J, Cooke PJL. Confirmation of linkage between antithrombin III and Duffy blood group and assignment of AT3 to 1q22-25. Annals of Human Genetics 1982; 26: 29-34.

33. Prochownik EV, Antonarakis S, Bauer KA, Rosenberg RD, Fearon ER, Orkin SH. Molecular heterogeneity of inherited antithrombin III deficiency. New England Journal of Medicine 1983; 308: 1549-1552.

34. Bock SC, Prochownik EV. Molecular genetic survey of 16 kindreds with hereditary antithrombin III deficiency. Blood 1987; 70: 1273-1278.

35. Bruce D, Perry DJ, Borg J-Y, Carrell RW, Wardell MR. Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen VI (187 Asn to Asp). Journal of Clinical Investigation 1994; 94: 2265-2274.

36. Devraj-Kizu- R, Chui DHK, Prochownik EV, Carter CJ, Ofosu FA, Blajchman MA. Antithrombin III Hamilton: a gene with a point mutation (guanine to adenine) in codon 382 causing impaired serine protease reactivity. Blood 1988; 72: 1518-1523.

37. Austin RC, Rachubinski RA, Ofosu FA, Blajchman MA. Antithrombin-III-Hamilton, Ala 382 to Thr: an antithrombin -III variant that acts as a substrate but not an inhibitor of a-thrombin and Factor Xa. Blood 1991; 77: 2185-2189. 
 

38. Perry DJ, Carrell RW. CpG dinucleotides are "hotspots" for mutation in the antithrombin III gene. Twelve variants identified using the polymerase chain reaction. Molecular Biology in Medicine 1989; 6: 239-243.

39. Ireland H, Lane DA, Thompson E, Walker ID, Blench I, Morris HR, Freyssinet JM, Grunebaun L, Olds R, Thein SL. Antithrombin Glasgow II: alanine to threonine mutation in the serpin P12 position, resulting in a substrate reaction with thrombin. British Journal of Haematology 1991; 79: 70-74.

40. Caso R, Lane DA, Thompson EA, Olds RJ, Thein SL, Panico M, Blench I, Morris H, Freyssinet JM, Aiach M, Rodeghiero F, Finazzi G. Antithrombin Vicenza, Ala 384 to Pro (GCA to CCA) mutation transforming the inhibitor into a substrate. British Journal of Haematology 1991; 77: 87-92.

41. Mohlo-Sabatier P, Aiach M, Gaillard I, Fiessinger JN, Fischer AM, Chadeuf G, Clauser E. Molecular characterization of antithrombin III (AT III) variants using polymerase chain reaction. Identification of the ATIII Charleville as an Ala384 Pro mutation. Journal of Clinical Investigation 1989; 84: 1236-1241.

42. Perry DJ, Harper PL, Fairham S, Daly M, Carrell RW. Antithrombin Cambridge, 384 Ala to Pro: A new variant identified using the polymerase chain reaction. Federation of European Biochemical Societies Letters 1989; 254: 174-176.

43. Penwarchuk WJ, Fernandez-Rachubinski F, Rachubinski RA, Blajchman MA. Antithrombin III Sudbury, an Ala 384 to Pro mutation with abnormal thrombin binding activity and thrombotic diathesis. Thrombosis Research. 1990; 59: 793-798.

44. Perry DJ, Daly M, Harper PL, Tait RC, Price J, Walker ID, Carrell RW. Antithrombin Cambridge II, 384 Ala to Ser. Further evidence of the role of the reactive centre loop in the inhibitory function of the serpin. Federation of European Biochemical Societies Letters 1991; 285: 248-250.

45. Blajchman MA, Fernandez-Rachubinsky F, Sheffield WP, Austin RC, Schulman S. Antithrombin III Stockholm: a codon 392 (Gly to Asp) mutation with normal heparin binding and impaired serine protease reactivity. Blood 1992; 79: 1428-1434.

46. Erdjument H, Lane DA, Ireland H, Panico M, DiMarzo V, Blench I, Morris HR. Formation of a covalent disulfide-linked antithrombin complex by an antithrombin variant, antithrombin Northwick Park. Journal of Biological Chemistry 1987; 262: 13381-13384.

47. Erdjument H, Lane DA, Panico M, diMarzo V, Morris HR. Single amino acid substitutions in the reactive site of antithrombin leading to thrombosis. Congenital substitution of arginine 393 to cysteine in antithrombin Northwick Park and to histidine in antithrombin Glasgow. Journal of Biological Chemistry 1988; 263: 5589-5593.

48. Erdjument H, Lane DA, Ireland H, DiMarzo V, Panico M, Morris HR, Tripodi A, Mannucci PM. Antithrombin Milano, single amino acid substitution at the reactive site, Arg 393 to Cys. Thombosis and Haemostasis 1988; 60: 471-475.

49. Ireland H, Lane DA, Thompson E, Olds R, Thein SL, Hach-Wunderle V, Scharrer I. Antithrombin Frankfurt I: arginine to cysteine substitution at the reactive site and formation of a variant antithrombin-albumin covalent complex. Thrombosis and Haemostasis 1991; 65: 913.

50. van Boven HH, Reitsma PH, Rosendaal FR, Bayston TA, Chowdhury V, Bauer K, Scharrer I, Conard J, Lane DA. Factor V Leiden (FV R506Q) in families with inherited antithrombin deficiency. Thromb Haemost 1996; 75: 417-421.

51. Lane DA, Erdjument H, Flynn A, DiMarzo V, Panico M, Morris H, Greaves M, Dolan G, Preston FE. Antithrombin Sheffield: amino acid substitution at the reactive site (Arg 393 to His) causing thrombosis. British Journal of Haematology 1989; 71: 91-96.

52. Erdjument H, Lane DA, Panico M, DiMarzo V, Morris HR, Bauer K, Rosenberg RD. Antithrombin Chicago, amino acid substitution of arginine 393 to histidine. Thrombosis Research 1989; 54: 613-619.

53. Lane DA, Erdjument H, Thompson E, Panico M, DiMarzo V, Morris HR, Leone G, De Stefano V, Thein SL. A novel amino acid substitution in the reactive site of a congenital variant antithrombin. Antithrombin Pescara, Arg 393 to Pro, caused by CGT to CCT mutation. Journal of Biological Chemistry 1989; 264: 10200-10204.

54. Owen MC, George PM, Lane DA, Boswell DR. P1 variant antithrombins Glasgow (393 Arg to His) and Pescara (393 Arg to Pro) have increased heparin affinity and are resistant to catalytic cleavage by elastase. Implications for the heparin activation mechanism. Federation of European Biochemical Societies Letters 1991; 280: 216-220.

55. Stephens AW, Thalley BS, Hirs CHW. Antithrombin Denver, a reactive site variant. Journal of Biological Chemistry 1987; 262: 1044-1048.

56. Olds RJ, Lane D, Caso R, Tripodi A, Mannucci PM, Thein SL. Antithrombin III Milano 2: a single base substitution in the thrombin binding domain detected with PCR and direct genomic sequencing. Nucleic Acids Research 1989; 17: 10511.

57. Brennan SO, Borg JY, George PM, Soria C, Soria J, Caen J, Carrell RW. New carbohydrate site in mutant antithrombin (7Ile-Asn) with decreased heparin affinity. Federation of European Biochemical Societies Letters 1988; 237: 118-122.

58. Borg JY, Brennan SO, Carrell RW, George P, Perry DJ, Shaw J. Antithrombin Rouen IV 24 Arg to Cys. The amino terminal contribution to heparin binding. Federation of European Biochemical Societies Letters 1990; 266: 163-166.

59. Chang JY, Tran TH. Antithrombin Basel. Identification of a Pro-Leu substitution in a hereditary abnormal antithrombin with impaired heparin cofactor activity. Journal of Biological Chemistry 1986; 261: 1174-1176.

60. Daly M, Bruce D, Perry DJ, Price J, Harper PL, O'Meara A, Carrell RW. Antithrombin Dublin (-3 Val to Glu): an N-terminal variant which has an aberrant signal peptide cleavage site. Federation of European Biochemical Societies Letters 1990; 273: 87-90.

61. Chowdhury V, Mille B, Olds RJ, Lane DA, Watton J, Barrowcliffe TW, Pabinger I, Woodcock BE, Thein SL. Antithrombins Southport (99 Leu to Val) and Vienna (118 Gln to Pro): two novel antithrombin variants with abnormal heparin binding. British Journal of Haematology 1995; 89: 602-609.

62. Koide T, Odani S, Takahashi K, Ono T, Sakuragawa N. Antithrombin III Toyama; replacement of Arginine 47 by Cysteine in hereditary abnormal antithrombin III that lacks heparin-binding ability. Proceedings of the National Academy of Science USA 1984; 81: 289-293.

63. Duchange N, Chasse JF, Cohen GN, Zakin MM. Identification of a mutation leading to cysteine replacement in a silent deficiency. Nucleic Acids Research 1986; 14: 2408.

64. Brunel F, Duchange N, Fischer AM, Cohen GN, Zakin MM. Antithrombin III Alger: a new case of Arg 47 - Cys mutation. American Journal of Haematology 1987; 25: 223-224.

65. Olds RJ, Lane DA, Caso R, Girolami A, Thein SL. Antithrombin III Padua II: a single base substitution in exon 2 detected using PCR and direct genomic sequencing. Nucleic Acids Research 1990; 18: 1926.

66. Owen MC, Shaw GJ, Grau E, Fontcuberta J, Carrell RW, Boswell DR. Molecular characterisation of antithrombin Barcelona 2: 47 arginine to cysteine. Thrombosis Research 1989; 55: 451-457.

67. Fernandez-Rachubinski F, Rachubinski R, Blajchman MA. Genetic characterisation of kindreds with antithrombin III (AT-III) deficiency using selected amplification of the gene. Blood 1990; 76: 506a.

68. Ueyama H, Murakami T, Nishiguchi S, Maeda S, Hashimoto Y, Okajima K, Shimada K, Araki S. Antithrombin Kumamoto. Identification of a point mutation and genotype analysis of the family. Thrombosis and Haemostasis 1990; 63: 231-234.

69. Borg JY, Owen MC, Soria C, Soria J, Caen J, Carrell RW. Arginine 47 is a prime heparin binding site in antithrombin. A new variant Rouen II, 47 Arg to Ser. Journal of Clinical Investigation 1988; 81: 1292-1296.

70. Owen MC, Borg JY, Soria C, Soria J, Caen J, Carrell RW. Heparin binding defect in new antithrombin III variant: Rouen, 47 Arg to His. Blood 1987; 69: 1275-1279.

71. Caso R, Lane DA, Thompson E, Zangouras D, Panico M, Morris H, Olds RJ, Thein SL, Girolami A. Antithrombin Padua I: impaired heparin binding caused by an Arg 47 to His (CGT to CAT) substitution. Thrombosis Research 1990; 58: 185-190.

72. Wolf M, Boyer-Neumann C, Mohlo-Sabatier P, Neumann C, Meyer D, Larrieu MJ. Familial variant of antithrombin III (AT III Bligny, 47 Arg to His) associated with protein C deficiency. Thrombosis and Haemostasis 1990; 63: 215-219.

73. Olds RJ, Lane DA, Boisclair M, Sas G, Bock SC, Thein SL. Antithrombin Budapest 3: an antithrombin variant with reduced heparin affinity resulting from the substitution L99F. Federation of European Societies Letters 1992; 300: 241-246.

74. Okajima K, Abe H, Maeda S, Motomura M, Tsujihata M, Nagataki S, Okabe H, Takatsuki K. Antithrombin III Nagasaki (Ser116-Pro): a heterozygous variant with defective heparin binding associated with thrombosis. Blood 1993; 81: 1300-1305.

75. Gandrille S, Aiach M, Lane DA, Vidaud D, Mohlo-Sabatier P, Caso R, de Moerloose P, Fiessinger JN, Clauser E. Important role of Arg 129 in heparin binding site of antithrombin III: identification of novel mutation Arg 129 to Gln. Journal of Biological Chemistry 1990; 265: 18997-19001.

76. Olds RJ, Thein SL, Ireland H, Lane DA, Boisclair M, Conard J, Horellou MH. Identification of 402 phenylalanine as a functionally important residue in antithrombin. Thrombosis and Haemostasis 1991; 65: 670.

77. Lane DA, Olds RJ, Conard J, Boisclair M, Bock SC, Hultin M, Abildgaard U, Ireland H, Thompson E, Sas G, Horellou MH, Tamponi G, Thein SL. Pleiotropic effects of antithrombin strand 1C substitution mutations. Journal of Clinical Investigation 1992; 90: 2422-2433.

78. Emmerich J, Chadeuf G, Coetzee MJ, Alhenc-Gelas M, Friessinger J-N, Aiach M. A phenylalanine 402 to leucine mutation is responsible for a stable inactive conformation of antithrombin. Thrombosis Research 1994; 76: 307-315.

79. Bock SC, Silberman JA, Wikoff W, Abildgaard U, Hultin MB. Identification of a threonine for alanine substitution at residue 404 of antithrombin III Oslo suggests integrity of the 404-407 region is important for maintaining normal inhibitor levels. Thrombosis and Haemostasis 1989; 62: 494.

80. Nakagawa M, Tanaka S, Tsuji H, Takada O, Ono T. Congenital antithrombin deficiency (ATIII Kyoto): identification of a point mutation altering arginine-406 to methionine behind the reactive site. Thrombosis Research 1991; 64: 101-108.

81. Bock SC, Marrinan JA, Radziejewska E. Antithrombin III Utah: proline 407 to leucine mutation in a highly conserved region near the inhibitor reactive site. Biochemistry 1988; 27: 6171-6178.

82. Olds RJ, Lane DA, Caso R, Panico M, Morris HR, Sas G, Dawes J, Thein SL. Antithrombin III Budapest: a single amino acid substitution (429Pro to Leu) in a region highly conserved in the serpin super family. Blood 1992; 79: 1206-1212.

83. Bock SC, Levitan DJ. Characterisation of an unusual length polymorphism 5' to the antithrombin III gene. Nucleic Acids Research 1983; 11: 8569-8582.

84. Bock SC, Radziejewska E. A Nhe 1 RFLP in the human antithrombin III gene (1q23-25) (AT3). Nucleic Acids Research 1991; 19: 2519.

85. Daly ME, Perry DJ. Dde I polymorphism in intron 5 in the antithrombin III gene. Nucleic Acid Research 1990; 18: 5583.

86. Wu S, Seino S, Bell GI. Human antithrombin III (AT3) gene length polymorphism revealed by the polymerase chain reaction. Nucleic Acids Research 1989; 17: 6433.

87. Whisstock J, Skinner R, Lesk AM. An atlas of serpin conformations. TIBS 1998; 63-67

88. Desai UR, Petitou M, Bjork I, Olson ST. Mechanism of heparin activation of antithrombin. Journal of Biological Chemistry 1998; 273: 7478-7487.

89. Huntington JA, Gettins PGW. Conformational conversion of antithrombin to a fully activated substrate of factor Xa without need for heparin. Biochemistry 1998; 37: 3272-3277.

90. Jin L, Abrahams JP, Skinner R, Petitou M, Pike RN, Carrell RW. The anticoagulant activation of antithrombin by heparin. Proceedings of the National Academy of Sciences USA 1997; 94: 14683-14688.

91. Lane DA, Ireland H, Olds RJ, Thein SL, Perry DJ, Aiach M. Antithrombin III: a database of mutations.Thrombosis and Haemostasis 1991; 66: 657-661.

92. Lane DA, Olds RJ, Boisclair M, Chowdhury V, Thein SL, Cooper DN, Blajchman M, Perry D, Emmerich J, Aiach M. Antithrombin III mutation database: first update. For the Thrombin and its Inhibitors Subcommittee of the Scientific and Standardization Committee of the International Society on Thrombosis and Haemostasis. Thrombosis and Haemostasis 1993; 70: 361-369.

93. Lane DA, Bayston T, Olds RJ, Fitches AC, Cooper DN, Millar DS, Jochmans K, Perry DJ, Okajima K, Thein SL, Emmerich, J. Antithrombin mutation database: 2nd (1997) update. Thrombosis and Haemostasis 1997; 77: 197-211.

94. Antonarakis SE, Nomenclature working group. Recommendations for a nomenclature system for human gene mutations. Human Mutation 1998; 11: 1-3.

95. Olds et al, Unpublished

96. Emmerich et al, Unpublished

97. Jochmans et al, Unpublished

98. Perry et al, Unpublished

99. Blajchman et al Unpublished

100. Okajima et al, Unpublished

101. Aiach et al, Unpublished

102. Daly et al, Unpublished

103. Keeling et al Unpublished

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