B Reviews, Minireviews and Book Chapters (1-71)

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B Reviews, Minireviews and Book Chapters (1-71)

B Reviews, Minireviews and Book Chapters (1-71)

1. Flohé L. [Glutathione peroxidase: enzymology and biological aspects]. Klin Wochenschr. 1971 Jun 15;49(12):669-83.

2. Flohé L. Catechol-O-methyltransferase. Int Pharmacopsychiatry. 1974;9(1):52- 60.

3. Flohé L, Günzler WA. Glutathione-dependent enzymatic oxidoreduction reactions. In: Arias IM, Jakoby WB, editors. Glutathione: Metabolism and Function. New York: Raven Press; 1976. p. 17-34.

4. Flohé L, Günzler WA, Ladenstein R. Glutathione peroxidase. In: Arias IM, Jakoby WB, editors. Glutathione: Metabolism and Function. New York: Raven Press; 1976. p. 115-38.

5. Flohé L, Friderichs E. [Old problems and new aspects in research on analgesia (author's transl)]. Arzneimittelforschung. 1978;28(1a):99-106.

6. Flohé L, Loschen G. Der therapeutische Wirkungsmechanismus von exogen zugeführter Superoxid-Dismutase: Befunde und Ausblicke. Europ J Rheumatol Inflamm. 1978;4:183-200.

7. Flohé L, Loschen G. [Mechanism of the therapeutic effect of exogenous superoxide dismutase: findings and prospects]. Eur J Rheumatol Inflamm. 1981;4(2):183-200.

8. Flohé L. Glutathione peroxidase brought into focus. In: Pryor WA, editor. Free Radicals in Biology. New York: Academic Press; 1982. p. 223-54.

9. Flohé L. Fibrinolytische Enzyme durch Genetic Engineering. Umschau. 1984;84:542-3.

10. Flohé L, Günzler WA. Assays of glutathione peroxidase. Methods Enzymol. 1984;105:114-21.

11. Flohé L, Ötting F. Superoxide dismutase assays. Methods Enzymol. 1984;105:93-104.

12. Flohé L. The glutathione peroxidase reaction: molecular basis of the antioxidant function of selenium in mammals. In: Shaltiel S, Chock PB, editors. Current Topics in Cellular Regulation: Academic Press, Inc; 1985. p. 473-8.

13. Flohé L. Single-chain urokinase-type plasminogen activators: New hopes for clot-specific lysis. Eur Heart J. 1985;6:905-8. 14. Flohé L, Beckmann R, Giertz H, Loschen G. Oxygen-centered free radicals as mediators of inflammation. In: Sies H, editor. Oxidative Stress. London, Orlando: Academic Press; 1985. p. 403-35.

15. Flohé L, Giertz H, Beckmann R. Free radical scavengers as antiinflammatory drugs? In: I. L. Bonta MABaMJP, editor. Handbook of Inflammation. Amsterdam: Elsevier Science Publishers; 1985. p. 255-81.

16. Günzler WA, Flohé L. Glutathione peroxidase. In: Greenwald RA, editor. Handbook of Methods for Oxygen Radical Research: CRC Press, Inc.; 1985. p. 285- 90.

17. Flohé L. Recombinant human pro-urokinase (non-glycosylated). Drugs of the Future. 1986;11:851-2.

18. Ladenstein R, Epp. O, Günzler WA, Flohé L. Glutathione peroxidase on approval. In: Bannister JV, Michelson AM, editors. Life Chemistry Reports. Harwood, Chur/London/Paris/New York1986. p. 37-55.

19. Beckmann R, Flohé L, Wilsmann KM. 10 Jahre therapeutische Erfahrungen mit Superoxid-Dismutase. Medizin. 1987;Suppl. 1:1-16.

20. Flohé L, Giertz H. Endotoxins, arachidonic acid, and superoxide formation. Rev Infect Dis. 1987 Sep-Oct;9 Suppl 5:S553-61.

21. Flohé L, Straßburger W, Günzler WA. Selen in der enzymatischen Katalyse. Chemie in unserer Zeit. 1987; 21:44-9.

22. Flohé L. Superoxide dismutase for therapeutic use: clinical experience, dead ends and hopes. Mol Cell Biochem. 1988 Dec;84(2):123-31.

23. Flohé L. Glutathione peroxidase. Basic Life Sci. 1988;49:663-8.

24. Flohé L. Determination of glutathione peroxidase. In: Miquel J, Quintanilha AT, Weber H, editors. CRC Handbook of Free radicals and Antioxidants in Biomedicine. Boca Raton/Florida: CRC Press, Inc; 1988. p. 281-6.

25. Flohé L, Becker R, Brigelius R, Lengfelder E, Ötting F. Convenient assays for superoxide dismutase. In: Miquel J, Quintanilha AT, Weber H, editors. CRC Handbook of Free radicals and Antioxidants in Biomedicine. Boca Raton/Florida: CRC Press, Inc; 1988. p. 287-93.

26. Flohé L. The selenoprotein glutathione peroxidase. In: D. Dolphin RP, and O. Avramovic, editor. Glutathione: Chemical, Biochemical, and Medical Aspects - Part A: John Wiley & Sons, Inc.; 1989. p. 643-731. 27. Flohé L, Günzler WA. Enzymes in therapy. In: Gerhartz(W, editor. Enzymes in Industry Production and Applications. Weinheim: VCH; 1990. p. 178-84.

28. Flohé L. Das Hobby des Chefs: die Glutathion Peroxidasen. Wissenschaftlicher Ergebnisbericht 1994. Braunschweig: GBF; 1995. p. 31- 52.

29. Ursini F, Maiorino M, Brigelius-Flohé R, Aumann KD, Roveri A, Schomburg D, et al. Diversity of glutathione peroxidases. Methods Enzymol. 1995;252:38-53.

30. Brigelius-Flohé R, Flohé L. Ascorbic acid, cell proliferation, and cell differentiation in culture. Subcell Biochem. 1996;25:83-107.

31. Flohé L. [Selenium in peroxide metabolism]. Med Klin (Munich). 1997 Sep 15;92 Suppl 3:5-7.

32. Flohé L. Selenium in peroxide metabolism. Med Klin. 1997;92:5-7.

33. Flohé L, Brigelius-Flohé R, Saliou C, Traber MG, Packer L. Redox regulation of NF-kappa B activation. Free Radic Biol Med. 1997;22(6):1115-26.

34. Flohé L, Wingender E, Brigelius-Flohé R. Regulation of Glutathione Peroxidases. In: Forman HJ, Cadenas E, editors. Oxidative Stress and Signal Transduction: Chapman & Hall; 1997. p. 415-40.

35. Flohé L, Wingender E, Brigelius-Flohé R. Regulation of Glutathione Peroxidases. In: Cadenas HJFaE, editor. Oxidative Stress and Signal Transduction. New York: Chapman & Hall; 1997. p. 415-40.

36. Flohé L. The Achilles' heel of trypanosomatids: trypanothione-mediated hydroperoxide metabolism. Biofactors. 1998;8(1-2):87-91.

37. Flohé L, Aumann K-D, Steinert P. Role of Selenium in the Enzymatic Reduction of Hydroperoxides. Phosphorus Sulphur and Silicon. 1998;136, 137 & 138:25-42.

38. Flohé L, Hecht HJ, Steinert P. Glutathione and trypanothione in parasitic hydroperoxide metabolism. Free Radic Biol Med. 1999 Nov;27(9-10):966-84.

39. Maiorino M, Flohé L, Roveri A, Steinert P, Wissing JB, Ursini F. Selenium and Reproduction. BioFactors. 1999;10:251-6.

40. Guerrero SA, Montemartini M, Spallek R, Hecht HJ, Steinert P, Flohé L, et al. Cloning and expression of tryparedoxin I from Crithidia fasciculata. Biofactors. 2000;11(1-2):67-9.

41. Flohé L, Andreesen JR, Brigelius-Flohé R, Maiorino M, Ursini F. Selenium, the element of the moon, in life on earth. IUBMB Life. 2000 May;49(5):411-20. 42. Günzler WA, Flohé L. Urinary-type Plasminogen Activator (uPA). In: Bachmann F, editor. Fibrinolytics and Antifibrinolytics Handbook of Experimental Pharmacology. Heidelberg: Springer Verlag; 2000. p. 91-110.

43. Köhrle J, Brigelius-Flohé R, Böck A, Gärtner R, Meyer O, Flohé L. Selenium in biology: facts and medical perspectives. Biol Chem. 2000 Sep-Oct;381(9-10):849-64.

44. Brigelius-Flohé R, Maiorino M, Ursini F, Flohé L. Selenium - an Antioxidant? In: Cadenas E, Packer L, editors. Handbook of Antioxidants. 2nd ed. New York Edition: Marcel Dekker, Inc.; 2001. p. 633-65.

45. Flohé L, Brigelius-Flohé R. Selenoproteins of the glutathione system. In: Hatfield DL, editor. Selenium Its Molecular Biology and Role in Human Health. Boston/Dordrecht/London: Kluwer Academic Publishers; 2001. p. 157-78.

46. Flohé L, Brigelius-Flohé R, Maiorino M, Roveri A, J. W, Ursini F. Selenium and male reproduction. In: Hatfield D, editor. Selenium Its Molecular Biology and Role in Human Health. 1st ed. Heidelberg, New York: Springer; 2001. p. 273-81.

47. Roveri A, Ursini F, Flohé L, Maiorino M. PHGPx and spermatogenesis. Biofactors. 2001;14(1-4):213-22.

48. Birringer M, Pilawa S, Flohé L. Trends in selenium biochemistry. Nat Prod Rep. 2002 Dec;19(6):693-718.

49. Flohé L, Foresta C, Garolla A, M. M, Roveri A, Ursini F. Metamorphosis of the selenoprotein PHGPx during spermatogenesis. Ann NY Acad Sci. 2002;973):287-8.

50. Flohé L, Foresta C, Garolla A, Maiorino M, Roveri A, Ursini F. Metamorphosis of the selenoprotein PHGPx during spermatogenesis. Ann N Y Acad Sci. 2002 Nov;973:287-8.

51. Flohé L, Steinert P, Hecht HJ, Hofmann B. Tryparedoxin and tryparedoxin peroxidase. Methods Enzymol. 2002;347:244-58.

52. Hofmann B, Hecht HJ, Flohé L. Peroxiredoxins. Biol Chem. 2002 Mar- Apr;383(3-4):347-64.

53. Roveri A, Flohé L, Maiorino M, Ursini F. Phospholipid-hydroperoxide glutathione peroxidase in sperm. Methods Enzymol. 2002;347:208-12.

54. Budde H, Flohé L. Enzymes of the thiol-dependent hydroperoxide metabolism in pathogens as potential drug targets. Biofactors. 2003;17(1-4):83-92.

55. Flohé L. Sulfur and Selenium Catalysis as paradigms for Redox Regulations. In: Forman J, Torres M, Fukuto J, editors. Signal Transduction by Reactive Oxygen and Nitrogen Species. Dordrecht: Kluwer; 2003. p. 15-32. 56. Flohé L. Selenium, selenoproteins and vision. Dev Ophthalmol. 2005;38:89- 102.

57. Flohé L, Brigelius-Flohé R. Selenoproteins of the glutathione system. In: Hatfield D, Berry MS, Gladyshev VN, editors. Selenium Its Molecular Biology and Role in Human Health. 2nd ed. Heidelberg, New York: Springer; 2006. p. 161-72.

58. Maiorino M, Roveri A, Ursini F, Brigelius-Flohé R, Flohé L. Selenium and male reproduction.oproteins of the glutathione system. In: Hatfield D, Berry MS, Gladyshev VN, editors. Selenium Its Molecular Biology and Role in Human Health. 2nd ed. Heidelberg, New York: Springer; 2006. p. 323-31.

59. Böck A, Flohé L, Köhrle J. Selenoproteins - biochemistry and clinical relevance. Biol Chem. 2007 Oct;388(10):985-6.

60. Flohé L. Selenium in mammalian spermiogenesis. Biol Chem. 2007 Oct;388(10):987-95.

61. Flohé L, Harris JR. Introduction. History of the peroxiredoxins and topical perspectives. Subcell Biochem. 2007;44:1-25.

62. Trujillo M, Ferrer-Sueta G, Thomson L, Flohé L, Radi R. Kinetics of peroxiredoxins and their role in the decomposition of peroxynitrite. Subcell Biochem. 2007;44:83-113.

63. Flohé L, Ursini F. Peroxidase: a term of many meanings. Antioxid Redox Signal. 2008 Sep;10(9):1485-90.

64. Irigoin F, Cibils L, Comini MA, Wilkinson SR, Flohé L, Radi R. Insights into the redox biology of Trypanosoma cruzi: Trypanothione metabolism and oxidant detoxification. Free Radic Biol Med. 2008 Sep 15;45(6):733-42.

65. Flohe L. The labour pains of biochemical selenology: the history of selenoprotein biosynthesis. Biochim Biophys Acta. 2009 Nov;1790(11):1389-403.

66. Toppo S, Flohé L, Ursini F, Vanin S, Maiorino M. Catalytic mechanisms and specificities of glutathione peroxidases: variations of a basic scheme. Biochim Biophys Acta. 2009 Nov;1790(11):1486-500.

67. Flohé L. In search of trypanocidal drugs. In: Selzer PM, editor. Antiparasitic and Antibacterial Drug Discovery. Weinheim: Wiley-VCH Verlag GmbH& Co. KGaA; 2009. p. 221-6.

68. Flohe L. Changing paradigms in thiology from antioxidant defense toward redox regulation. Methods Enzymol. 2010;473:1-39. 69. Brigelius-Flohé R, Flohé L. Basic principles and emerging concepts in the redox control of transcription factors. Antioxid Redox Signal. 2011 Oct 15;15(8):2335- 81.

70. Flohé L, Toppo S, Cozza G, Ursini F. A comparison of thiol peroxidase mechanisms. Antioxid Redox Signal. 2011 Aug 1;15(3):763-80.

71. Flohé L. The trypanothione system and the opportunities it offers to create drugs for the neglected kinetoplast diseases. Biotechnol Adv. 2012 Jan- Feb;30(1):294-301

72. Flohé L. The trypanothione system and its implications in the therapy of trypanosomatid diseases. Int J Med Microbiol. 2012 Oct;302(4-5):216-20.

73. Flohé, L. Brigelius-Flohé, R. Selenopüroteins of the Glutathione Peroxidase Family. In Hatfield, D. L., Berry, M. J., Gladyshev, V. N. Selenium. Its Molecular Biology and Role in Human Health. 3rd Edition. Springer, New York 2012, pp. 167- 180.

74. Flohé, L. Glutathione Peroxidases. In Liu, J., Luo, G. Selenoproteins and Mimics. Springer, Heidelberg 2012, pp. 1-25.

75. Flohé L. The fairytale of the GSSG/GSH redox potential. Biochim Biophys Acta. 2013 May;1830(5):3139-42..

76. Comini, M. A., Flohé, L. Trypanothione-Based Redox Metabolism of Trypanosomatids. In Jäger, T, Koch, O., Flohé, L. Trypanosomatid Diseases. Molecular Routes to Drug Discovery. Wiley-Blackwell, Weinheim 2013, pp.167-199.

77. Koch, O., Jäger, T., Flohé, L., Selzer, P. M. Inhibition of trypanothione Synthetase as a Therapeutic Concept. In Jäger, T, Koch, O., Flohé, L. Trypanosomatid Diseases. Molecular Routes to Drug Discovery. Wiley-Blackwell, Weinheim 2013, pp.429-443.

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