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Volumn 24, Issue 2, 1998, Pages 149-164

Ribonuclease inhibitor protein of human erythrocytes: Characterization, loss of activity in response to oxidative stress, and association with Heinz bodies

Author keywords

Aging; Heinz bodies; Oxidative stress; Red blood cell; Ribonuclease inhibitor; RNASIN

Indexed keywords

RIBONUCLEASE;

EID: 0032104746     PISSN: 10799796     EISSN: None     Source Type: Journal    
DOI: 10.1006/bcmd.1998.0182     Document Type: Article
Times cited : (30)

References (59)
  • 1
    • 0017673101 scopus 로고
    • Ribonuclease inhibitor from human placenta
    • 1. Blackburn P, Wilson G, Moore S: Ribonuclease inhibitor from human placenta. J Biol Chem 252: 5904-5910, 1977.
    • (1977) J Biol Chem , vol.252 , pp. 5904-5910
    • Blackburn, P.1    Wilson, G.2    Moore, S.3
  • 3
    • 0023796670 scopus 로고
    • Amino acid sequence of the ribonuclease inhibitor from porcine liver reveals the presence of leucine-rich repeats
    • 3. Hofsteenge J, Kieffer B, Matthies R, Hemmings B, Stone SR: Amino acid sequence of the ribonuclease inhibitor from porcine liver reveals the presence of leucine-rich repeats. Biochemistry 27:8537-8544, 1988.
    • (1988) Biochemistry , vol.27 , pp. 8537-8544
    • Hofsteenge, J.1    Kieffer, B.2    Matthies, R.3    Hemmings, B.4    Stone, S.R.5
  • 4
    • 0020120837 scopus 로고
    • Ribonuclease inhibitors from the livers of five mammalian species
    • 4. Burton LE, Fucci NP: Ribonuclease inhibitors from the livers of five mammalian species. Int J Peptide Protein Res 19:372-379, 1982.
    • (1982) Int J Peptide Protein Res , vol.19 , pp. 372-379
    • Burton, L.E.1    Fucci, N.P.2
  • 5
    • 0023944006 scopus 로고
    • Ribonuclease-RNAase inhibitor complex from rat testis. Purification of the RNAase inhibitor
    • 5. Fominaya J, Garcia-Segura J, Galvilanes J: Ribonuclease-RNAase inhibitor complex from rat testis. Purification of the RNAase inhibitor. Biochim Biophys Acta 954:216-223, 1988.
    • (1988) Biochim Biophys Acta , vol.954 , pp. 216-223
    • Fominaya, J.1    Garcia-Segura, J.2    Galvilanes, J.3
  • 6
    • 0027350918 scopus 로고
    • Structure and action of mammalian ribonuclease (angiogenin) inhibitor
    • 6. Lee FS, Vallee BL. Structure and action of mammalian ribonuclease (angiogenin) inhibitor. Progr Nucleic Acid Res Mol Biol 44:1-30, 1993.
    • (1993) Progr Nucleic Acid Res Mol Biol , vol.44 , pp. 1-30
    • Lee, F.S.1    Vallee, B.L.2
  • 7
    • 0002130286 scopus 로고    scopus 로고
    • Ribonuclease inhibitor
    • D'Alessio G, Riordan JF, eds. New York: Academic Press
    • 7. Hofsteenge J: Ribonuclease inhibitor. In: D'Alessio G, Riordan JF, eds. Ribonucleases: Structures and Functions. New York: Academic Press, pp. 621-658, 1997.
    • (1997) Ribonucleases: Structures and Functions , pp. 621-658
    • Hofsteenge, J.1
  • 8
    • 0024293566 scopus 로고
    • The primary structure of human ribonuclease/angiogenin inhibitor (RAI) discloses a novel highly diversified protein superfamily with a common repetitive module
    • 8. Schneider R, Schneider-Scherzer E, Thurnher M, Auer B, Schweiger M: The primary structure of human ribonuclease/angiogenin inhibitor (RAI) discloses a novel highly diversified protein superfamily with a common repetitive module. EMBO J 7:4151-4156, 1988.
    • (1988) EMBO J , vol.7 , pp. 4151-4156
    • Schneider, R.1    Schneider-Scherzer, E.2    Thurnher, M.3    Auer, B.4    Schweiger, M.5
  • 9
    • 0028080261 scopus 로고
    • The leucine-rich repeat: A versatile binding motif
    • 9. Kobe B, Deisenhofer J: The leucine-rich repeat: a versatile binding motif. Trends Biochem Sci 19:415-421, 1994.
    • (1994) Trends Biochem Sci , vol.19 , pp. 415-421
    • Kobe, B.1    Deisenhofer, J.2
  • 10
    • 0027718173 scopus 로고
    • Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats
    • 10. Kobe B, Deisenhofer J: Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats. Nature 366:751-756, 1993.
    • (1993) Nature , vol.366 , pp. 751-756
    • Kobe, B.1    Deisenhofer, J.2
  • 11
    • 0028911034 scopus 로고
    • A structural basis of the interactions between leucine-rich repeats and protein ligands
    • 11. Kobe B, Deisenhofer J: A structural basis of the interactions between leucine-rich repeats and protein ligands. Nature 374:183-186, 1995.
    • (1995) Nature , vol.374 , pp. 183-186
    • Kobe, B.1    Deisenhofer, J.2
  • 12
    • 0030596012 scopus 로고    scopus 로고
    • Mechanism of ribonuclease inhibition by ribonuclease inhibitor protein based on the crystal structure of its complex with ribonuclease a
    • 12. Kobe B, Deisenhofer J: Mechanism of ribonuclease inhibition by ribonuclease inhibitor protein based on the crystal structure of its complex with ribonuclease A. J Mol Biol 264:1028-1043, 1996.
    • (1996) J Mol Biol , vol.264 , pp. 1028-1043
    • Kobe, B.1    Deisenhofer, J.2
  • 13
    • 0026316880 scopus 로고
    • Studies on the interaction of ribonuclease inhibitor with pancreatic ribonuclease involving differential labeling of cysteinyl residues
    • 13. Hofsteenge J, Servis C, Stone SR: Studies on the interaction of ribonuclease inhibitor with pancreatic ribonuclease involving differential labeling of cysteinyl residues. J Biol Chem 266:24198-24204, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 24198-24204
    • Hofsteenge, J.1    Servis, C.2    Stone, S.R.3
  • 14
    • 0026470181 scopus 로고
    • Inactivation of ribonuclease inhibitor by thiol-disulfide exchange
    • 14. Fominaya JM, Hofsteenge J: Inactivation of ribonuclease inhibitor by thiol-disulfide exchange. J Biol Chem 267:24655-24661, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 24655-24661
    • Fominaya, J.M.1    Hofsteenge, J.2
  • 15
    • 0015087751 scopus 로고
    • Degradation of RNA in rat reticulocytes. II. Relationship between RNase and its corresponding inhibitor in rat reticulocyte
    • 15. Goto S, Mizuno D: Degradation of RNA in rat reticulocytes. II. Relationship between RNase and its corresponding inhibitor in rat reticulocyte. Arch Biochem Biophys, 145:71-77, 1971.
    • (1971) Arch Biochem Biophys , vol.145 , pp. 71-77
    • Goto, S.1    Mizuno, D.2
  • 16
    • 37049241349 scopus 로고
    • Hemin: An inhibitor of erythroid cell ribonuclease
    • 16. Burka ER: Hemin: an inhibitor of erythroid cell ribonuclease. Science 162:1287, 1968.
    • (1968) Science , vol.162 , pp. 1287
    • Burka, E.R.1
  • 17
    • 0029023978 scopus 로고
    • Ribonuclease inhibitors in human blood: Comparative studies on the inhibitors detected in erythrocytes, platelets, mononuclear leukocytes and granulocytes
    • 17. Nadano D, Yasuda T, Takeshita T, Kishi K: Ribonuclease inhibitors in human blood: comparative studies on the inhibitors detected in erythrocytes, platelets, mononuclear leukocytes and granulocytes. Int J Biochem Cell Biol 27:971-979, 1995.
    • (1995) Int J Biochem Cell Biol , vol.27 , pp. 971-979
    • Nadano, D.1    Yasuda, T.2    Takeshita, T.3    Kishi, K.4
  • 18
    • 0010599893 scopus 로고
    • Boca Raton: CRC Press
    • 18. Rapaport SM: The Reticulocyte, Boca Raton: CRC Press Vol. 27, pp. 46-47, 1986.
    • (1986) The Reticulocyte , vol.27 , pp. 46-47
    • Rapaport, S.M.1
  • 19
    • 77956940788 scopus 로고
    • Pancreatic Ribonuclease
    • 19. Blackburn P, Moore S: Pancreatic Ribonuclease. Enzymes 15:317-433, 1982.
    • (1982) Enzymes , vol.15 , pp. 317-433
    • Blackburn, P.1    Moore, S.2
  • 20
    • 0026515433 scopus 로고
    • cDNA cloning and sequence of rat ribonuclease inhibitor, and tissue distribution of the mRNA
    • 20. Kawanomoto M, Motojima K, Sasaki M, Hattori H, Goto S: cDNA cloning and sequence of rat ribonuclease inhibitor, and tissue distribution of the mRNA. Biochim Biophys Acta 1129:335-338, 1992.
    • (1992) Biochim Biophys Acta , vol.1129 , pp. 335-338
    • Kawanomoto, M.1    Motojima, K.2    Sasaki, M.3    Hattori, H.4    Goto, S.5
  • 21
    • 0000238273 scopus 로고
    • Human placental ribonuclease inhibitor abolishes both angiogenic and ribonucleolytic activities of angiogenin
    • 21. Shapiro R, Vallee BL: Human placental ribonuclease inhibitor abolishes both angiogenic and ribonucleolytic activities of angiogenin. Proc Natl Acad Sci USA 84:2238-2241, 1987.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 2238-2241
    • Shapiro, R.1    Vallee, B.L.2
  • 22
    • 0010566074 scopus 로고
    • Studies on the properties and distribution of ribonuclease inhibitor in the rat
    • 22. Roth JS: Studies on the properties and distribution of ribonuclease inhibitor in the rat. Biochim Biophys Acta 21:34-43, 1956.
    • (1956) Biochim Biophys Acta , vol.21 , pp. 34-43
    • Roth, J.S.1
  • 24
    • 0017185162 scopus 로고
    • The removal of leukocytes and platelets from whole blood
    • 24. Beutler E, West C, Blume K-G: The removal of leukocytes and platelets from whole blood. J Lab Clin Med 88:328-333, 1976.
    • (1976) J Lab Clin Med , vol.88 , pp. 328-333
    • Beutler, E.1    West, C.2    Blume, K.G.3
  • 25
    • 0017124296 scopus 로고
    • Purification and properties of alkaline ribonuclease from human serum
    • 25. Akagi K, Murai K, Hirao N, Yamanaka M: Purification and properties of alkaline ribonuclease from human serum. Biochim Biophys Acta 442:368-378, 1976.
    • (1976) Biochim Biophys Acta , vol.442 , pp. 368-378
    • Akagi, K.1    Murai, K.2    Hirao, N.3    Yamanaka, M.4
  • 26
    • 0019519419 scopus 로고
    • Ribonucleases of human serum, urine, cerebrospinal fluid, and leukocytes. Activity staining following electrophoresis in sodium dodecylsulfate-polyacrylamide gels
    • 26. Blank A, Dekker CA: Ribonucleases of human serum, urine, cerebrospinal fluid, and leukocytes. Activity staining following electrophoresis in sodium dodecylsulfate-polyacrylamide gels. Biochemistry 20:2261-2267, 1981.
    • (1981) Biochemistry , vol.20 , pp. 2261-2267
    • Blank, A.1    Dekker, C.A.2
  • 27
    • 0001151615 scopus 로고
    • The purification and properties of ribonucleic acid from wheat germ
    • 27. Glitz DG, Dekker CA: The purification and properties of ribonucleic acid from wheat germ. Biochemistry 2:1185-1192, 1963.
    • (1963) Biochemistry , vol.2 , pp. 1185-1192
    • Glitz, D.G.1    Dekker, C.A.2
  • 29
    • 0028145749 scopus 로고
    • Rheologic and pathophysiologic significance of red cell passage through narrow pores
    • 29. Nakamura T, Hasegawa S, Shio H, Uyesaka N: Rheologic and pathophysiologic significance of red cell passage through narrow pores. Blood Cells 20:151-165, 1994.
    • (1994) Blood Cells , vol.20 , pp. 151-165
    • Nakamura, T.1    Hasegawa, S.2    Shio, H.3    Uyesaka, N.4
  • 30
    • 0010533117 scopus 로고
    • The mechanism of glutathione destruction and protection in drug-sensitive and non-sensitive erythrocytes
    • 30. Beutler E, Robson M, Buttenwieser E: The mechanism of glutathione destruction and protection in drug-sensitive and non-sensitive erythrocytes. J Clin Invest 36:617-628, 1957.
    • (1957) J Clin Invest , vol.36 , pp. 617-628
    • Beutler, E.1    Robson, M.2    Buttenwieser, E.3
  • 31
    • 73649194769 scopus 로고
    • Improved method for the determination of blood glutathione
    • 31. Beutler E, Duron O, Kelly BM: Improved method for the determination of blood glutathione. J Lab Clin Med 61:882-890, 1963.
    • (1963) J Lab Clin Med , vol.61 , pp. 882-890
    • Beutler, E.1    Duron, O.2    Kelly, B.M.3
  • 32
    • 0025006582 scopus 로고
    • Protein chemical and kinetic characterization of recombi-nant porcine ribonuclease inhibitor expressed in Saccharomyces cerevesiae
    • 32. Vicentini A, Kieffer B, Matthies R, et al: Protein chemical and kinetic characterization of recombi-nant porcine ribonuclease inhibitor expressed in Saccharomyces cerevesiae. Biochemistry 29:8827-8834, 1990.
    • (1990) Biochemistry , vol.29 , pp. 8827-8834
    • Vicentini, A.1    Kieffer, B.2    Matthies, R.3
  • 34
    • 0025118967 scopus 로고
    • Molecular and cellular aspects of thiol-disulfide exchange
    • 34. Gilbert HF: Molecular and cellular aspects of thiol-disulfide exchange. Adv Enzymol 63:69-172, 1990.
    • (1990) Adv Enzymol , vol.63 , pp. 69-172
    • Gilbert, H.F.1
  • 35
    • 0015053529 scopus 로고
    • General aspects of erythrocyte physiology and biology
    • 35. Beutler E: General aspects of erythrocyte physiology and biology. Exp Eye Res 11:261-263, 1971.
    • (1971) Exp Eye Res , vol.11 , pp. 261-263
    • Beutler, E.1
  • 36
    • 0001439977 scopus 로고
    • Oxidative hemolysis and precipitation of hemoglobin. II. Role of thiols in oxidant drug action
    • 36. Allen DW, Jandl JH: Oxidative hemolysis and precipitation of hemoglobin. II. Role of thiols in oxidant drug action. J Clin Invest 40:454-475, 1961.
    • (1961) J Clin Invest , vol.40 , pp. 454-475
    • Allen, D.W.1    Jandl, J.H.2
  • 37
    • 0010602569 scopus 로고
    • Oxidative hemolysis and precipitation of hemoglobin. I. Heinz body anemia as an acceleration of red cell aging
    • 37. Jandl JH, Engle LK, Allen DW: Oxidative hemolysis and precipitation of hemoglobin. I. Heinz body anemia as an acceleration of red cell aging. J Clin Invest 39:1818-1836, 1960.
    • (1960) J Clin Invest , vol.39 , pp. 1818-1836
    • Jandl, J.H.1    Engle, L.K.2    Allen, D.W.3
  • 38
    • 0029768918 scopus 로고    scopus 로고
    • Oxidation of sulfhydryl groups of ribonuclease inhibitor in epithelial cells is sufficient for its intracellular degradation
    • 38. Blazquez M, Fominaya JM, Hofsteenge J: Oxidation of sulfhydryl groups of ribonuclease inhibitor in epithelial cells is sufficient for its intracellular degradation. J Biol Chem 271:18638-16842, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 18638-116842
    • Blazquez, M.1    Fominaya, J.M.2    Hofsteenge, J.3
  • 39
    • 0024845155 scopus 로고
    • Multiple splice forms of ribonuclease inhibitor mRNA differ in the 5′-untranslated region
    • 39. Crawford D, Hagerty K, Beutler B: Multiple splice forms of ribonuclease inhibitor mRNA differ in the 5′-untranslated region. Gene 85:525-531, 1989.
    • (1989) Gene , vol.85 , pp. 525-531
    • Crawford, D.1    Hagerty, K.2    Beutler, B.3
  • 40
    • 0014952989 scopus 로고
    • A suggested control function for the animal tissue ribonuclease-ribonuclease inhibitor system, based on studies of isolated cells and by phytohemagglutinin-transformed lymphocytes
    • 40. Kraft N, Shortman K: A suggested control function for the animal tissue ribonuclease-ribonuclease inhibitor system, based on studies of isolated cells and by phytohemagglutinin-transformed lymphocytes. Biochim Biophys Acta 217:164-175, 1970.
    • (1970) Biochim Biophys Acta , vol.217 , pp. 164-175
    • Kraft, N.1    Shortman, K.2
  • 41
    • 4244105397 scopus 로고
    • The levels of ribonucleases and ribonuclease inhibitor during the regeneration of rat liver
    • 41. Shortman K: The levels of ribonucleases and ribonuclease inhibitor during the regeneration of rat liver. Biochim Biophys Acta 61:50-55, 1962.
    • (1962) Biochim Biophys Acta , vol.61 , pp. 50-55
    • Shortman, K.1
  • 42
    • 0014743840 scopus 로고
    • The phylogeny of the ribonuclease-ribonuclease inhibitor system: Its distribution in tissues and its response during leukaemogenesis and aging
    • 42. Kraft N, Shortman K: The phylogeny of the ribonuclease-ribonuclease inhibitor system: its distribution in tissues and its response during leukaemogenesis and aging. Aust J Biol Sci 23:175-184, 1970.
    • (1970) Aust J Biol Sci , vol.23 , pp. 175-184
    • Kraft, N.1    Shortman, K.2
  • 44
    • 0002498741 scopus 로고
    • Scaling-up of animal cell cultures
    • Freshney RI, ed. Oxford: IRL Press
    • 44. Griffiths JB: Scaling-up of animal cell cultures. In: Freshney RI, ed. Animal Cell Culture: A Practical Approach. Oxford: IRL Press, pp. 33-69, 1986.
    • (1986) Animal Cell Culture: A Practical Approach , pp. 33-69
    • Griffiths, J.B.1
  • 45
    • 0015055578 scopus 로고
    • Glucose-6 phosphate dehydrogenase deficiency: Mechanisms of drug-induced hemolysis
    • 45. Hochstein P: Glucose-6 phosphate dehydrogenase deficiency: mechanisms of drug-induced hemolysis. Exp Eye Res 11:389-395, 1971.
    • (1971) Exp Eye Res , vol.11 , pp. 389-395
    • Hochstein, P.1
  • 46
    • 0015054737 scopus 로고
    • Introduction to discussion of regulation of erythrocyte glycolysis
    • 46. Valentine WN: Introduction to discussion of regulation of erythrocyte glycolysis. Expl Eye Res 11:273-279, 1971.
    • (1971) Expl Eye Res , vol.11 , pp. 273-279
    • Valentine, W.N.1
  • 47
    • 0027463316 scopus 로고
    • Mechanism of red blood cell aging: Relationship of cell density and cell age
    • 47. Piomelli S, Seaman C: Mechanism of red blood cell aging: relationship of cell density and cell age. Am J Hematol 42:46-52, 1993.
    • (1993) Am J Hematol , vol.42 , pp. 46-52
    • Piomelli, S.1    Seaman, C.2
  • 48
    • 0018746182 scopus 로고
    • An extrinsic membrane polypeptide associated with high molecular weight protein aggregates in human cataract
    • 48. Spector A, Garner MH, Garner WH, Roy D, Farnsworth P, Shyne S: An extrinsic membrane polypeptide associated with high molecular weight protein aggregates in human cataract. Science 204:1323-1326, 1979.
    • (1979) Science , vol.204 , pp. 1323-1326
    • Spector, A.1    Garner, M.H.2    Garner, W.H.3    Roy, D.4    Farnsworth, P.5    Shyne, S.6
  • 49
    • 0010567476 scopus 로고
    • Electron microscopic observations of the splenic red pulp with special reference to the pitting function
    • 49. Koyama S, Aoki S, Deguchi K: Electron microscopic observations of the splenic red pulp with special reference to the pitting function. Mie Medical J 14:143-188, 1964.
    • (1964) Mie Medical J , vol.14 , pp. 143-188
    • Koyama, S.1    Aoki, S.2    Deguchi, K.3
  • 50
    • 0015055541 scopus 로고
    • Metabolism of red cell glutathione
    • 50. Srivastava SK: Metabolism of red cell glutathione. Exp Eye Res 11:294-305, 1971.
    • (1971) Exp Eye Res , vol.11 , pp. 294-305
    • Srivastava, S.K.1
  • 51
    • 0015055253 scopus 로고
    • Metabolism of glutathione in the lens
    • 51. Reddy VN: Metabolism of glutathione in the lens. Exp Eye Res 11:310-328, 1971.
    • (1971) Exp Eye Res , vol.11 , pp. 310-328
    • Reddy, V.N.1
  • 52
    • 0015053178 scopus 로고
    • Mechanisms of hemoglobin precipitation into heinz bodies: Possible relevance to cataract formation
    • 52. Jacob H: Mechanisms of hemoglobin precipitation into Heinz bodies: possible relevance to cataract formation. Exp Eye Res 11:356-364, 1971.
    • (1971) Exp Eye Res , vol.11 , pp. 356-364
    • Jacob, H.1
  • 54
    • 0015399076 scopus 로고
    • Further studies on the purification and properties of a ribonuclease inhibitor from lens cortex
    • 54. Ortwerth BJ, Byrnes RJ: Further studies on the purification and properties of a ribonuclease inhibitor from lens cortex. Exp Eye Res 14:114-122, 1972.
    • (1972) Exp Eye Res , vol.14 , pp. 114-122
    • Ortwerth, B.J.1    Byrnes, R.J.2
  • 55
    • 0015429033 scopus 로고
    • Radiation-induced changes in the activities of alkaline ribonuclease and ribonuclease inhibitor in rat thymus supernatant fraction
    • 55. Patil MS, Saroja S, Sreenivasan A: Radiation-induced changes in the activities of alkaline ribonuclease and ribonuclease inhibitor in rat thymus supernatant fraction. Strahlentherapie 144:602-606, 1972.
    • (1972) Strahlentherapie , vol.144 , pp. 602-606
    • Patil, M.S.1    Saroja, S.2    Sreenivasan, A.3
  • 56
    • 0014572067 scopus 로고
    • The effect of x-irradiation on the balance between the alkaline ribonuclease and the ribonuclease inhibitor of mammalian tissues
    • 56. Kraft N, Shortman K, Jamieson D: The effect of x-irradiation on the balance between the alkaline ribonuclease and the ribonuclease inhibitor of mammalian tissues. Radiation Res 39:655-668, 1969.
    • (1969) Radiation Res , vol.39 , pp. 655-668
    • Kraft, N.1    Shortman, K.2    Jamieson, D.3
  • 57
    • 0028136499 scopus 로고
    • Whole blood, plasma and red blood cell glutathione and cysteine in patients with kidney disease and during hemodialysis
    • 57. Jacobson SH, Moldeus P: Whole blood, plasma and red blood cell glutathione and cysteine in patients with kidney disease and during hemodialysis. Clinical Nephrol 42:189-192, 1994.
    • (1994) Clinical Nephrol , vol.42 , pp. 189-192
    • Jacobson, S.H.1    Moldeus, P.2
  • 58
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 58. Bradford M: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254, 1976.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 59
    • 0025218070 scopus 로고
    • Modular mutagenesis of human placental ribonuclease inhibitor, a protein with leucine-rich repeats
    • 59. Lee FS, Vallee BL. Modular mutagenesis of human placental ribonuclease inhibitor, a protein with leucine-rich repeats. Proc Natl Acad Sci USA 87: 1879-1883, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 1879-1883
    • Lee, F.S.1    Vallee, B.L.2


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