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Volumn 14, Issue 6, 1996, Pages 597-608

Protease inhibitors and carcinogenesis: A review

Author keywords

[No Author keywords available]

Indexed keywords

ISOFLAVONE DERIVATIVE; PHYTIC ACID; PHYTOSTEROL; PROTEINASE INHIBITOR; SAPONIN DERIVATIVE;

EID: 0030473568     PISSN: 07357907     EISSN: None     Source Type: Journal    
DOI: 10.3109/07357909609076904     Document Type: Review
Times cited : (31)

References (114)
  • 2
    • 0028349082 scopus 로고
    • Prevention of carcinogenesis by protease inhibitors
    • Kennedy A: Prevention of carcinogenesis by protease inhibitors. Cancer Res 54:1999s-2005s, 1994.
    • (1994) Cancer Res , vol.54
    • Kennedy, A.1
  • 3
    • 0026701521 scopus 로고
    • Fruit, vegetables, and cancer prevention: A review of the epidemiological evidence
    • Block G, Patterson B, Subar A: Fruit, vegetables, and cancer prevention: A review of the epidemiological evidence. Nutr Cancer 18:1-29, 1992.
    • (1992) Nutr Cancer , vol.18 , pp. 1-29
    • Block, G.1    Patterson, B.2    Subar, A.3
  • 4
    • 0028091268 scopus 로고
    • A prospective cohort study on the relation between meat consumption and the risk of colon cancer
    • Goldbohm R, Van den Brandt P, van't Veer P, et al: A prospective cohort study on the relation between meat consumption and the risk of colon cancer. Cancer Res 54:718-723, 1994.
    • (1994) Cancer Res , vol.54 , pp. 718-723
    • Goldbohm, R.1    Van den Brandt, P.2    Van't Veer, P.3
  • 6
    • 0019469152 scopus 로고
    • Reassessment of the role of dietary fat in cancer etiology
    • Enstrom J: Reassessment of the role of dietary fat in cancer etiology. Cancer Res 41:3722-3723, 1981.
    • (1981) Cancer Res , vol.41 , pp. 3722-3723
    • Enstrom, J.1
  • 7
    • 0020456998 scopus 로고
    • Relationship of soybean paste soup intake to gastric cancer risk
    • Hirayama T: Relationship of soybean paste soup intake to gastric cancer risk. Nutr Cancer 3:223-233, 1982.
    • (1982) Nutr Cancer , vol.3 , pp. 223-233
    • Hirayama, T.1
  • 8
    • 0022017412 scopus 로고
    • The Bowman-Birk inhibitor: Trypsin- and chymotrypsin-inhibitor from soybeans
    • Birk Y: The Bowman-Birk inhibitor: Trypsin- and chymotrypsin-inhibitor from soybeans. Int J Peptide Prot Res 25:113-131, 1985.
    • (1985) Int J Peptide Prot Res , vol.25 , pp. 113-131
    • Birk, Y.1
  • 9
    • 0020727729 scopus 로고
    • Soybean isoflavones: Effect of environment and variety on composition
    • Eldridge A, Kwolek W: Soybean isoflavones: Effect of environment and variety on composition. J Agr Food Chem 31:394-396, 1983.
    • (1983) J Agr Food Chem , vol.31 , pp. 394-396
    • Eldridge, A.1    Kwolek, W.2
  • 10
    • 0025770650 scopus 로고
    • Commentary. the role of soy products in reducing risk of cancer
    • Messina M, Barnes S: Commentary. The role of soy products in reducing risk of cancer. J Natl Cancer Inst 83:541-546, 1991.
    • (1991) J Natl Cancer Inst , vol.83 , pp. 541-546
    • Messina, M.1    Barnes, S.2
  • 11
    • 0023622454 scopus 로고
    • Raw soya-bean flour increases cholecystokinin release in man
    • Calam J, Bojarski J, Springer C: Raw soya-bean flour increases cholecystokinin release in man. Br J Nutr 58:175-179, 1987.
    • (1987) Br J Nutr , vol.58 , pp. 175-179
    • Calam, J.1    Bojarski, J.2    Springer, C.3
  • 12
    • 0023076077 scopus 로고
    • Anticarcinogenic action of protease inhibitors
    • Troll W, Weisner R, Frenkel K: Anticarcinogenic action of protease inhibitors. Adv Cancer Res 49:265-283, 1987.
    • (1987) Adv Cancer Res , vol.49 , pp. 265-283
    • Troll, W.1    Weisner, R.2    Frenkel, K.3
  • 13
    • 0024986664 scopus 로고
    • Soybeans inhibit mammary tumors in models of breast cancer
    • edited by M Pariza. New York, Wiley-Liss
    • Barnes S, Grubbs C, Setchell K, Carlson J: Soybeans inhibit mammary tumors in models of breast cancer. In: Mutagens and Carcinogens in the Diet, edited by M Pariza. New York, Wiley-Liss, 1990, pp 239-253.
    • (1990) Mutagens and Carcinogens in the Diet , pp. 239-253
    • Barnes, S.1    Grubbs, C.2    Setchell, K.3    Carlson, J.4
  • 14
    • 0020631151 scopus 로고
    • Bowman-Birk soybean protease inhibitor as an anticarcinogen
    • Yavelow J, Finlay T, Kennedy A, Troll W: Bowman-Birk soybean protease inhibitor as an anticarcinogen. Cancer Res 43:2454s-2459s, 1983.
    • (1983) Cancer Res , vol.43
    • Yavelow, J.1    Finlay, T.2    Kennedy, A.3    Troll, W.4
  • 15
    • 0018403293 scopus 로고
    • The fate of the Bowman Birk trypsin inhibitor from soybeans in the digestive tract
    • Madar Z, Gertler A, Birk Y: The fate of the Bowman Birk trypsin inhibitor from soybeans in the digestive tract. Comp Biochem Physiol 62A:1057-1061, 1979.
    • (1979) Comp Biochem Physiol , vol.62 A , pp. 1057-1061
    • Madar, Z.1    Gertler, A.2    Birk, Y.3
  • 16
    • 0021235849 scopus 로고
    • Soya - A dietary source of the non-steroidal oestrogen equol in man and animals
    • Axelson M, Sjovall J, Gustafsson B, et al: Soya - A dietary source of the non-steroidal oestrogen equol in man and animals. J Endocrinol 102:49-56, 1984.
    • (1984) J Endocrinol , vol.102 , pp. 49-56
    • Axelson, M.1    Sjovall, J.2    Gustafsson, B.3
  • 17
    • 0024762368 scopus 로고
    • The use of thermospray liquid chromatography/tandem mass spectrometry for the class identification and structural verification of phytoestrogens in soy protein preparations
    • Barbuch R, Coutant J, Welsh M, et al: The use of thermospray liquid chromatography/tandem mass spectrometry for the class identification and structural verification of phytoestrogens in soy protein preparations. Biomed Environ Mass Spectrom 18:973-977, 1989.
    • (1989) Biomed Environ Mass Spectrom , vol.18 , pp. 973-977
    • Barbuch, R.1    Coutant, J.2    Welsh, M.3
  • 18
    • 0018129082 scopus 로고
    • Phytoestrogen interaction with estrogen receptors in human breast cells
    • Martin P, Horowitz K, Ryan D, McGuire W: Phytoestrogen interaction with estrogen receptors in human breast cells. Endocrinology 103:1860-1867, 1978.
    • (1978) Endocrinology , vol.103 , pp. 1860-1867
    • Martin, P.1    Horowitz, K.2    Ryan, D.3    McGuire, W.4
  • 19
    • 0018909451 scopus 로고
    • Binding of phytoestrogens and estradiol 17b by cytoplasmic receptors in the pituitary gland and the hypothalamus of the ewe
    • Mathieson R, Kills W: Binding of phytoestrogens and estradiol 17b by cytoplasmic receptors in the pituitary gland and the hypothalamus of the ewe. J Endocrinol 85:317-325, 1980.
    • (1980) J Endocrinol , vol.85 , pp. 317-325
    • Mathieson, R.1    Kills, W.2
  • 20
    • 0023664272 scopus 로고
    • Genistein, a specific inhibitor of tyrosine-specific protein kinases
    • Akiyama T, Ishida J, Nakagawa S, et al: Genistein, a specific inhibitor of tyrosine-specific protein kinases. J Biol Chem 262:5592-5595, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 5592-5595
    • Akiyama, T.1    Ishida, J.2    Nakagawa, S.3
  • 21
    • 0017986411 scopus 로고
    • Sterol content of foods of plant origin
    • Weihrauch J, Gardner J: Sterol content of foods of plant origin. J Am Diet Assoc 73:39-47, 1978.
    • (1978) J Am Diet Assoc , vol.73 , pp. 39-47
    • Weihrauch, J.1    Gardner, J.2
  • 22
    • 49049150053 scopus 로고
    • Saponins in food - A review
    • Oakenfull D: Saponins in food - A review. Food Chem 6:19-40, 1981.
    • (1981) Food Chem , vol.6 , pp. 19-40
    • Oakenfull, D.1
  • 23
    • 0018872473 scopus 로고
    • Protective effect of plant sterols against chemically induced colon tumors in rats
    • Raicht R, Cohen B, Fazzini E, et al: Protective effect of plant sterols against chemically induced colon tumors in rats. Cancer Res 40:403-405, 1980.
    • (1980) Cancer Res , vol.40 , pp. 403-405
    • Raicht, R.1    Cohen, B.2    Fazzini, E.3
  • 24
    • 0020065827 scopus 로고
    • The kinetics of the protective effect of b-sitosterol against MNU-induced colonic neoplasia
    • Deschner E, Cohen B, Raicht R: The kinetics of the protective effect of b-sitosterol against MNU-induced colonic neoplasia. J Cancer Res Clin Oncol 103:49-54, 1982.
    • (1982) J Cancer Res Clin Oncol , vol.103 , pp. 49-54
    • Deschner, E.1    Cohen, B.2    Raicht, R.3
  • 25
    • 0021967296 scopus 로고
    • Dietary suppression of colonic cancer: Fiber or phytate?
    • Graf E, Eaton J: Dietary suppression of colonic cancer: Fiber or phytate? Cancer 56:717-718, 1985.
    • (1985) Cancer , vol.56 , pp. 717-718
    • Graf, E.1    Eaton, J.2
  • 26
    • 0024405693 scopus 로고
    • Inositol and inositol hexaphosphate suppresses cell proliferation and tumor formation in CD-1 mice
    • Shamsuddin A, Ullah A, Chakravarthy A: Inositol and inositol hexaphosphate suppresses cell proliferation and tumor formation in CD-1 mice. Carcinogenesis 10:1461-1463, 1989.
    • (1989) Carcinogenesis , vol.10 , pp. 1461-1463
    • Shamsuddin, A.1    Ullah, A.2    Chakravarthy, A.3
  • 27
    • 0025021262 scopus 로고
    • Antioxidant functions of phytic acid
    • Graf E, Eaton J: Antioxidant functions of phytic acid. Free Radic Biol Med 8:61-69, 1990.
    • (1990) Free Radic Biol Med , vol.8 , pp. 61-69
    • Graf, E.1    Eaton, J.2
  • 28
    • 0021337104 scopus 로고
    • Iron-catalyzed hydroxyl formation
    • Graf J, Mahoney J, Bryant R, et al: Iron-catalyzed hydroxyl formation. J Biol Chem 259:3620-3624, 1984.
    • (1984) J Biol Chem , vol.259 , pp. 3620-3624
    • Graf, J.1    Mahoney, J.2    Bryant, R.3
  • 29
    • 0003388010 scopus 로고
    • Chemoprevention by nonnutrient components of vegetables and fruits
    • New York, Plenum Press
    • Birt D, Bresnick E: Chemoprevention by nonnutrient components of vegetables and fruits. In: Human Nutrition: A Comprehensive Treatise. New York, Plenum Press, 1990.
    • (1990) Human Nutrition: A Comprehensive Treatise
    • Birt, D.1    Bresnick, E.2
  • 30
    • 0025176844 scopus 로고
    • Inhibitory effect of apigenin, a plant flavonoid, on epidermal ornithine decarboxylase and skin tumor promotion in mice
    • Wei H, Tye L, Bresnick E, Birt D: Inhibitory effect of apigenin, a plant flavonoid, on epidermal ornithine decarboxylase and skin tumor promotion in mice. Cancer Res 50:499-502, 1990.
    • (1990) Cancer Res , vol.50 , pp. 499-502
    • Wei, H.1    Tye, L.2    Bresnick, E.3    Birt, D.4
  • 31
    • 0025116706 scopus 로고
    • Antimutagenic heat stable antioxidants
    • edited by M Pariza, J Felton, H Aeschbacher, S. Sato. New York, Wiley-Liss
    • Osawa T, Kumon H, Namiki M, Kawakishi S, Fukuda Y: Antimutagenic heat stable antioxidants. In: Mutagens and Carcinogens in the Diet, edited by M Pariza, J Felton, H Aeschbacher, S. Sato. New York, Wiley-Liss, 1990, pp 223-238.
    • (1990) Mutagens and Carcinogens in the Diet , pp. 223-238
    • Osawa, T.1    Kumon, H.2    Namiki, M.3    Kawakishi, S.4    Fukuda, Y.5
  • 32
    • 0027950688 scopus 로고
    • Chemoprevention and therapy of cancer by D-limonene
    • Crowell P, Gould M: Chemoprevention and therapy of cancer by D-limonene. Crit Rev Oncogenesis 5:1-22, 1994.
    • (1994) Crit Rev Oncogenesis , vol.5 , pp. 1-22
    • Crowell, P.1    Gould, M.2
  • 33
    • 0028343655 scopus 로고
    • Structure-activity relationships among monoterpene inhibitors of protein isoprenylation and cell proliferation
    • Crowell P, Ren Z, Lin S, Vedejs E, Gould M: Structure-activity relationships among monoterpene inhibitors of protein isoprenylation and cell proliferation. Biochem Pharm 47:1405-1415, 1994.
    • (1994) Biochem Pharm , vol.47 , pp. 1405-1415
    • Crowell, P.1    Ren, Z.2    Lin, S.3    Vedejs, E.4    Gould, M.5
  • 35
    • 0024986915 scopus 로고
    • Opportunities for nutritional scientists in cancer prevention
    • edited by M Pariza, J Felton, H Aeschbacher, S Sato. New York, Wiley-Liss
    • Boutwell R: Opportunities for nutritional scientists in cancer prevention. In: Mutagens and Carcinogens in the Diet, edited by M Pariza, J Felton, H Aeschbacher, S Sato. New York, Wiley-Liss, 1990, pp 269-284.
    • (1990) Mutagens and Carcinogens in the Diet , pp. 269-284
    • Boutwell, R.1
  • 36
    • 0021884389 scopus 로고
    • Requirement of essential fatty acid for mammary tumorigenesis
    • Ip C, Carter C, Ip M: Requirement of essential fatty acid for mammary tumorigenesis. Cancer Res 45:1997-2001, 1985.
    • (1985) Cancer Res , vol.45 , pp. 1997-2001
    • Ip, C.1    Carter, C.2    Ip, M.3
  • 37
    • 0025025176 scopus 로고
    • Conjugated dienoic derivatives of linoleic acid Mechanism of anticarcinogenic effect
    • edited by M Pariza, J Felton, H Aeschbacher, S Sato. New York, Wiley-Liss
    • Pariza M, Ha Y: Conjugated dienoic derivatives of linoleic acid Mechanism of anticarcinogenic effect. In: Mutagens and Carcinogens in the Diet, edited by M Pariza, J Felton, H Aeschbacher, S Sato. New York, Wiley-Liss, 1990, pp 217-222.
    • (1990) Mutagens and Carcinogens in the Diet , pp. 217-222
    • Pariza, M.1    Ha, Y.2
  • 38
    • 0025863657 scopus 로고
    • Internalization of the Bowman-Birk protease inhibitor by intestinal epithelial cells
    • Billings P, Brandon D, Habres J: Internalization of the Bowman-Birk protease inhibitor by intestinal epithelial cells. Eur J Cancer 27:903-908, 1991.
    • (1991) Eur J Cancer , vol.27 , pp. 903-908
    • Billings, P.1    Brandon, D.2    Habres, J.3
  • 39
    • 0023129875 scopus 로고
    • Fluorescent visualization of binding and internalization of the anticarcinogenic Bowman-Birk type protease inhibitors in transformed fibroblasts
    • Yavelow J, Scott C, Mayer T: Fluorescent visualization of binding and internalization of the anticarcinogenic Bowman-Birk type protease inhibitors in transformed fibroblasts. Cancer Res 47:1602-1607, 1987.
    • (1987) Cancer Res , vol.47 , pp. 1602-1607
    • Yavelow, J.1    Scott, C.2    Mayer, T.3
  • 40
    • 0023801170 scopus 로고
    • Protection against cancer through nutritionally-induced increase of endogenous proteinase inhibitors - An hypothesis
    • Schelp F, Pongpaew P: Protection against cancer through nutritionally-induced increase of endogenous proteinase inhibitors - An hypothesis. Int J Epidemiol 17:287-292, 1988.
    • (1988) Int J Epidemiol , vol.17 , pp. 287-292
    • Schelp, F.1    Pongpaew, P.2
  • 41
    • 0023197904 scopus 로고
    • Inhibition of radiation-induced transformation of C3H/10T1/2 cells by chymotrypsin inhibitor 1 from potatoes
    • Billings P, St. Clair W, Ryan C, Kennedy A: Inhibition of radiation-induced transformation of C3H/10T1/2 cells by chymotrypsin inhibitor 1 from potatoes. Carcinogenesis 8:809-812, 1987.
    • (1987) Carcinogenesis , vol.8 , pp. 809-812
    • Billings, P.1    St Clair, W.2    Ryan, C.3    Kennedy, A.4
  • 42
    • 0019955551 scopus 로고
    • Inhibition of human and dog serine pancreatic proteinases by naturally occurring high-molecular-weight inhibitors from plant or animal origin
    • Gertler A, Poraz I, Cohen N, Gottesfeld F: Inhibition of human and dog serine pancreatic proteinases by naturally occurring high-molecular-weight inhibitors from plant or animal origin. Biochem Med 27:143-153, 1982.
    • (1982) Biochem Med , vol.27 , pp. 143-153
    • Gertler, A.1    Poraz, I.2    Cohen, N.3    Gottesfeld, F.4
  • 43
    • 12644267570 scopus 로고
    • Immunological comparisons of chymotrypsin inhibitor 1 among several genera of the Solanaceae
    • Gurusiddaiah S, Kuo T, Ryan C: Immunological comparisons of chymotrypsin inhibitor 1 among several genera of the Solanaceae. Plant Phys 50:627-631, 1972.
    • (1972) Plant Phys , vol.50 , pp. 627-631
    • Gurusiddaiah, S.1    Kuo, T.2    Ryan, C.3
  • 44
    • 0020096073 scopus 로고
    • Proteinase inhibitors 1 and II from leaves of wounded tomato plants: Purification and properties
    • Plunkett G, Senear D, Zuroske G, Ryan C: Proteinase inhibitors 1 and II from leaves of wounded tomato plants: Purification and properties. Arch Biochem Biophys 213:463-472, 1982.
    • (1982) Arch Biochem Biophys , vol.213 , pp. 463-472
    • Plunkett, G.1    Senear, D.2    Zuroske, G.3    Ryan, C.4
  • 45
    • 0021435428 scopus 로고
    • Isolation and characterization of proteinase inhibitor 1 from etiolated tobacco leaves
    • Kuo T, Pearce G, Ryan C: Isolation and characterization of proteinase inhibitor 1 from etiolated tobacco leaves. Arch Biochem Biophys 230:504-510, 1984.
    • (1984) Arch Biochem Biophys , vol.230 , pp. 504-510
    • Kuo, T.1    Pearce, G.2    Ryan, C.3
  • 47
    • 0021187339 scopus 로고
    • Bioassay of plasma cholecystokinin in rats: Effects of food, trypsin inhibitor, and alcohol
    • Liddle R, Goldfine I, Williams J: Bioassay of plasma cholecystokinin in rats: Effects of food, trypsin inhibitor, and alcohol. Gastroenterology 87:542-549, 1984.
    • (1984) Gastroenterology , vol.87 , pp. 542-549
    • Liddle, R.1    Goldfine, I.2    Williams, J.3
  • 48
    • 0017252226 scopus 로고
    • Enzymic activities in the pancreas, digestive tract, and feces of rats fed raw or heated soy flour
    • Nitsan Z, Liener I: Enzymic activities in the pancreas, digestive tract, and feces of rats fed raw or heated soy flour. J Nutr 106:300-305, 1976.
    • (1976) J Nutr , vol.106 , pp. 300-305
    • Nitsan, Z.1    Liener, I.2
  • 49
    • 12644277658 scopus 로고
    • The potential of cholecystokinin as a cocarcinogen in the hamster-nitrosamine model
    • edited by M Friedman. New York, Plenum Press
    • Howatson A: The potential of cholecystokinin as a cocarcinogen in the hamster-nitrosamine model. In: Nutritional and Toxicological Significance of Enzyme Inhibitors in Foods, edited by M Friedman. New York, Plenum Press, 1986, pp 109-121.
    • (1986) Nutritional and Toxicological Significance of Enzyme Inhibitors in Foods , pp. 109-121
    • Howatson, A.1
  • 50
    • 0023004242 scopus 로고
    • Enhancement of pancreatic carcinogenesis by raw soy protein isolate. Quantitative rat model and nutritional considerations
    • edited by M Friedman. New York, Plenum Press
    • Roebuck B: Enhancement of pancreatic carcinogenesis by raw soy protein isolate. Quantitative rat model and nutritional considerations. In: Nutritional and Toxicological Significance of Enzyme Inhibitors in Foods, edited by M Friedman. New York, Plenum Press, 1986, pp 91-108.
    • (1986) Nutritional and Toxicological Significance of Enzyme Inhibitors in Foods , pp. 91-108
    • Roebuck, B.1
  • 51
    • 0014954362 scopus 로고
    • Tumorigenesis in mouse skin: Inhibition by synthetic inhibitors of proteases
    • Troll W, Klassen A, Janoff A: Tumorigenesis in mouse skin: Inhibition by synthetic inhibitors of proteases. Science 169:1211-1213, 1970.
    • (1970) Science , vol.169 , pp. 1211-1213
    • Troll, W.1    Klassen, A.2    Janoff, A.3
  • 52
    • 0017592706 scopus 로고
    • Elastases from human and canine granulocytes. H. Interaction with protease inhibitors of animal, plant, and microbial origin
    • Schiessler H, Ohlsson K, Olsson I, Arnhold M, Birk Y, Fritz H: Elastases from human and canine granulocytes. H. Interaction with protease inhibitors of animal, plant, and microbial origin. Hoppe-Seyler Z Physiol Chem 358:53-58, 1977.
    • (1977) Hoppe-Seyler Z Physiol Chem , vol.358 , pp. 53-58
    • Schiessler, H.1    Ohlsson, K.2    Olsson, I.3    Arnhold, M.4    Birk, Y.5    Fritz, H.6
  • 53
    • 0020568167 scopus 로고
    • Survey of plant inhibitors of polymorphonuclear leukocyte elastase, pancreatic elastase, cathepsin G, cathepsin B, hageman factor fragments, and other serine proteinases
    • Hojima Y, Pisano J, Cochrane C: Survey of plant inhibitors of polymorphonuclear leukocyte elastase, pancreatic elastase, cathepsin G, cathepsin B, hageman factor fragments, and other serine proteinases. Biochem Pharm 32:985-990, 1983.
    • (1983) Biochem Pharm , vol.32 , pp. 985-990
    • Hojima, Y.1    Pisano, J.2    Cochrane, C.3
  • 54
    • 0015384429 scopus 로고
    • Inhibition of tumorigenesis in mouse skin by leupeptin, a protease inhibitor from Actinomycetes
    • Hozumi M, Ogawa M, Sugimura T, Takeuchi T, Umezawa H: Inhibition of tumorigenesis in mouse skin by leupeptin, a protease inhibitor from Actinomycetes. Cancer Res 32:1725-1728, 1972.
    • (1972) Cancer Res , vol.32 , pp. 1725-1728
    • Hozumi, M.1    Ogawa, M.2    Sugimura, T.3    Takeuchi, T.4    Umezawa, H.5
  • 55
    • 0020434125 scopus 로고
    • Inhibition of mouse skin tumor promotion by several inhibitors of arachidonic acid metabolism
    • Fischer S, Mills G, Slaga T: Inhibition of mouse skin tumor promotion by several inhibitors of arachidonic acid metabolism. Carcinogenesis 3:1243-1245, 1982.
    • (1982) Carcinogenesis , vol.3 , pp. 1243-1245
    • Fischer, S.1    Mills, G.2    Slaga, T.3
  • 56
    • 0020571874 scopus 로고
    • Inhibition of 7-bromomethylbenz[a]anthracene-promoted mouse skin tumor formation by retinoic acid and dexamethasone
    • Verma A, Garcia C, Ashendel C, Boutwell R: Inhibition of 7-bromomethylbenz[a]anthracene-promoted mouse skin tumor formation by retinoic acid and dexamethasone. Cancer Res 43: 3045-3049, 1983.
    • (1983) Cancer Res , vol.43 , pp. 3045-3049
    • Verma, A.1    Garcia, C.2    Ashendel, C.3    Boutwell, R.4
  • 57
    • 0021931082 scopus 로고
    • Cutaneous changes during prolonged application of 12-0-tetradecanoylphorbol-13-acetate on mouse skin and residual effects after cessation of treatment
    • Aldaz C, Conti C, Gimenez I, Slaga T, Klein-Szanto A: Cutaneous changes during prolonged application of 12-0-tetradecanoylphorbol-13-acetate on mouse skin and residual effects after cessation of treatment. Cancer Res 45:2753-2759, 1985.
    • (1985) Cancer Res , vol.45 , pp. 2753-2759
    • Aldaz, C.1    Conti, C.2    Gimenez, I.3    Slaga, T.4    Klein-Szanto, A.5
  • 58
    • 84907037793 scopus 로고
    • Prevention of cancer by agents that suppress oxygen radical formation
    • Troll W: Prevention of cancer by agents that suppress oxygen radical formation. Free Rad Res Commun 12-13:751-757, 1991.
    • (1991) Free Rad Res Commun , vol.12-13 , pp. 751-757
    • Troll, W.1
  • 59
    • 0018773536 scopus 로고
    • Protease inhibitors antagonize the activation of polymorphonuclear leukocyte oxygen consumption
    • Goldstein B, Witz G, Amoruso M, Troll W: Protease inhibitors antagonize the activation of polymorphonuclear leukocyte oxygen consumption. Biochem Biophys Res Commun 88:854-860, 1979.
    • (1979) Biochem Biophys Res Commun , vol.88 , pp. 854-860
    • Goldstein, B.1    Witz, G.2    Amoruso, M.3    Troll, W.4
  • 60
    • 0026478007 scopus 로고
    • Clinical trials with anticoagulant and antiplatelet therapies
    • Zacharski L, Meehan K, Algarra S, Calvo F: Clinical trials with anticoagulant and antiplatelet therapies. Cancer Metast Rev 11:421-431, 1992.
    • (1992) Cancer Metast Rev , vol.11 , pp. 421-431
    • Zacharski, L.1    Meehan, K.2    Algarra, S.3    Calvo, F.4
  • 61
    • 0014941657 scopus 로고
    • Proteolytic enzymes initiating cell division and escape from contact inhibition of growth
    • Burger M: Proteolytic enzymes initiating cell division and escape from contact inhibition of growth. Nature 227:170-171, 1970.
    • (1970) Nature , vol.227 , pp. 170-171
    • Burger, M.1
  • 62
    • 12444327777 scopus 로고
    • Effects of added proteases on concanavalin A-specific agglutinability and proliferation of quiescent fibroblasts
    • edited by E Reich, D Rifkin, E Shaw. Cold Spring Harbor, New York, Cold Spring Harbor Laboratory
    • Cunningham D, Ho T: Effects of added proteases on concanavalin A-specific agglutinability and proliferation of quiescent fibroblasts. In: Proteases and Biological Control, edited by E Reich, D Rifkin, E Shaw. Cold Spring Harbor, New York, Cold Spring Harbor Laboratory, 1975, pp 795-806.
    • (1975) Proteases and Biological Control , pp. 795-806
    • Cunningham, D.1    Ho, T.2
  • 63
    • 0015450038 scopus 로고
    • Selective inhibition of growth of transformed cells by protease inhibitors
    • Schnebli H, Burger M: Selective inhibition of growth of transformed cells by protease inhibitors. Proc Natl Acad Sci USA 69:3825-3827, 1972.
    • (1972) Proc Natl Acad Sci USA , vol.69 , pp. 3825-3827
    • Schnebli, H.1    Burger, M.2
  • 64
    • 0029129523 scopus 로고
    • Nuclear scaffold protease: In situ nuclear localization and effects of a protease inhibitor on growth and morphology of ras-transformed hepatocytes
    • Clawson G, Ren L, Isom H: Nuclear scaffold protease: In situ nuclear localization and effects of a protease inhibitor on growth and morphology of ras-transformed hepatocytes. Hepatology 22:1230-1235, 1995.
    • (1995) Hepatology , vol.22 , pp. 1230-1235
    • Clawson, G.1    Ren, L.2    Isom, H.3
  • 65
    • 0018745785 scopus 로고
    • Inhibition of chemical transformation in C3H/10T1/2 cells by protease inhibitors
    • Kuroki T, Drevon C: Inhibition of chemical transformation in C3H/10T1/2 cells by protease inhibitors. Cancer Res 39:2755-2761, 1979.
    • (1979) Cancer Res , vol.39 , pp. 2755-2761
    • Kuroki, T.1    Drevon, C.2
  • 66
    • 0018141118 scopus 로고
    • Protease inhibitors suppress radiation induced malignant transformation in vitro
    • Kennedy A, Little J: Protease inhibitors suppress radiation induced malignant transformation in vitro. Nature 276:825-826, 1978.
    • (1978) Nature , vol.276 , pp. 825-826
    • Kennedy, A.1    Little, J.2
  • 67
    • 0019430798 scopus 로고
    • Effects of protease inhibitors on radiation transformation in vitro
    • Kennedy A, Little J: Effects of protease inhibitors on radiation transformation in vitro. Cancer Res 41:2103-2108, 1981.
    • (1981) Cancer Res , vol.41 , pp. 2103-2108
    • Kennedy, A.1    Little, J.2
  • 68
    • 0023202378 scopus 로고
    • Inhibition of H-ras oncogene transformation of NIH3T3 cells by protease inhibitors
    • Garte S, Currie D, Troll W: Inhibition of H-ras oncogene transformation of NIH3T3 cells by protease inhibitors. Cancer Res 47:3159-3162, 1989.
    • (1989) Cancer Res , vol.47 , pp. 3159-3162
    • Garte, S.1    Currie, D.2    Troll, W.3
  • 69
    • 0027633279 scopus 로고
    • An inhibitor of nuclear scaffold protease blocks chemical transformation of fibroblasts
    • Clawson G, Norbeck L, Wise J, Patierno S: An inhibitor of nuclear scaffold protease blocks chemical transformation of fibroblasts. Cell Growth Diff 4:589-594, 1993.
    • (1993) Cell Growth Diff , vol.4 , pp. 589-594
    • Clawson, G.1    Norbeck, L.2    Wise, J.3    Patierno, S.4
  • 70
    • 0021028627 scopus 로고
    • The inhibition of the mitogenic stimulation of B lymphocytes by a serine protease inhibitor: Commitment to proliferation correlates with an enhanced expression of a cell-associated arginine-specific serine enzyme
    • Ku G, Quigley J, Sultzer B: The inhibition of the mitogenic stimulation of B lymphocytes by a serine protease inhibitor: Commitment to proliferation correlates with an enhanced expression of a cell-associated arginine-specific serine enzyme. J Immunol 131:2494-2499, 1983.
    • (1983) J Immunol , vol.131 , pp. 2494-2499
    • Ku, G.1    Quigley, J.2    Sultzer, B.3
  • 72
    • 0023664344 scopus 로고
    • Platelet-activating factor stimulation of rabbit platelets is blocked by serine protease inhibitor (chymotryptic protease inhibitor)
    • Sugatani J, Miwa M, Hanahan D: Platelet-activating factor stimulation of rabbit platelets is blocked by serine protease inhibitor (chymotryptic protease inhibitor). J Biol Chem 262:5740-5747, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 5740-5747
    • Sugatani, J.1    Miwa, M.2    Hanahan, D.3
  • 73
    • 2642593603 scopus 로고
    • Detection and partial characterization of a chymostatin-sensitive endopeptidase in transformed fibroblasts
    • O'Donnell-Tormey J, Quigley J: Detection and partial characterization of a chymostatin-sensitive endopeptidase in transformed fibroblasts. Proc Natl Acad Sci USA 80:344-348, 1983.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 344-348
    • O'Donnell-Tormey, J.1    Quigley, J.2
  • 74
    • 0023839659 scopus 로고
    • Stimulation of high-affinity GTPase by trypsin and trypsin-like proteinases in membranes of human platelets
    • Jakobs K, Aktories K: Stimulation of high-affinity GTPase by trypsin and trypsin-like proteinases in membranes of human platelets. Biochem J 249:639-643, 1988.
    • (1988) Biochem J , vol.249 , pp. 639-643
    • Jakobs, K.1    Aktories, K.2
  • 75
    • 0025639942 scopus 로고
    • Inhibitors of chymotrypsin-like activities selectively block the mitotic pathway in rat hepatoma cells
    • Ponzio G, Contreres J, Debant A, Auberger P, Farahifar D, Rossi B: Inhibitors of chymotrypsin-like activities selectively block the mitotic pathway in rat hepatoma cells. Growth Factors 4:37-44, 1990.
    • (1990) Growth Factors , vol.4 , pp. 37-44
    • Ponzio, G.1    Contreres, J.2    Debant, A.3    Auberger, P.4    Farahifar, D.5    Rossi, B.6
  • 76
    • 0026948778 scopus 로고
    • Ca2+-regulated serine protease associated with the nuclear scaffold
    • Clawson G, Noroeck L, Hatem C, et al: Ca2+-regulated serine protease associated with the nuclear scaffold Cell Growth Diff 3:827-838, 1992.
    • (1992) Cell Growth Diff , vol.3 , pp. 827-838
    • Clawson, G.1    Noroeck, L.2    Hatem, C.3
  • 77
    • 0025123666 scopus 로고
    • Effects of protease inhibitors on c-myc expression in normal and transformed C3H10T1/2 cells
    • Chang J, Li J, Billings P, Kennedy A: Effects of protease inhibitors on c-myc expression in normal and transformed C3H10T1/2 cells. Mol Carcinogen 3:226-232, 1990.
    • (1990) Mol Carcinogen , vol.3 , pp. 226-232
    • Chang, J.1    Li, J.2    Billings, P.3    Kennedy, A.4
  • 78
    • 0024437191 scopus 로고
    • C-fos mRNA levels are reduced in the presence of antipain and the Bowman-Birk inhibitor
    • Caggana M, Kennedy A: C-fos mRNA levels are reduced in the presence of antipain and the Bowman-Birk inhibitor. Carcinogenesis 10:2145-2148, 1989.
    • (1989) Carcinogenesis , vol.10 , pp. 2145-2148
    • Caggana, M.1    Kennedy, A.2
  • 79
    • 0026425644 scopus 로고
    • Antipain-induced suppression of oncogene expression in H-ras-transformed NIH3T3 cells
    • Cox L, Motz J, Troll W, Garte S: Antipain-induced suppression of oncogene expression in H-ras-transformed NIH3T3 cells. Cancer Res 51:4810-4814, 1991.
    • (1991) Cancer Res , vol.51 , pp. 4810-4814
    • Cox, L.1    Motz, J.2    Troll, W.3    Garte, S.4
  • 80
    • 0017617933 scopus 로고
    • Protease activation of GI nuclei isolated from Chinese hamster fibroblasts
    • Brown R, Clark R, Chiu J, Stubblefield E: Protease activation of GI nuclei isolated from Chinese hamster fibroblasts. Exp Cell Res 104:207-213, 1977.
    • (1977) Exp Cell Res , vol.104 , pp. 207-213
    • Brown, R.1    Clark, R.2    Chiu, J.3    Stubblefield, E.4
  • 81
    • 0021201613 scopus 로고
    • The selective advantage of cancer cells: A consequence of genome mobilization in the course of the induction of DNA repair processes? (Model studies on yeast)
    • Wintersberger U: The selective advantage of cancer cells: A consequence of genome mobilization in the course of the induction of DNA repair processes? (Model studies on yeast). Adv Enzyme Reg 22:311-322, 1984.
    • (1984) Adv Enzyme Reg , vol.22 , pp. 311-322
    • Wintersberger, U.1
  • 82
    • 0027090115 scopus 로고
    • Mammalian genes induced by radiation: Activation of genes associated with growth control
    • Fornace A: Mammalian genes induced by radiation: Activation of genes associated with growth control. Annu Rev Genet 26:507-526, 1992.
    • (1992) Annu Rev Genet , vol.26 , pp. 507-526
    • Fornace, A.1
  • 83
    • 0028569767 scopus 로고
    • Interaction of the p53-regulated protein Gadd45 with proliferating cell nuclear antigen
    • Smith M, Chen I, Zhan Q, et al: Interaction of the p53-regulated protein Gadd45 with proliferating cell nuclear antigen. Science 266:1376-1380, 1994.
    • (1994) Science , vol.266 , pp. 1376-1380
    • Smith, M.1    Chen, I.2    Zhan, Q.3
  • 84
    • 0026801062 scopus 로고
    • Altered cell cycle arrest and gene amplification potential accompany loss of wild-type p53
    • Livingstone L, White A, Sprouse J, Livanos E, Jacks T, Tlsty T: Altered cell cycle arrest and gene amplification potential accompany loss of wild-type p53. Cell 70:923-935, 1992.
    • (1992) Cell , vol.70 , pp. 923-935
    • Livingstone, L.1    White, A.2    Sprouse, J.3    Livanos, E.4    Jacks, T.5    Tlsty, T.6
  • 85
    • 0020316054 scopus 로고
    • The SOS regulatory system of Escherichia coli
    • Little J, Mount D: The SOS regulatory system of Escherichia coli. Cell 29:11-22, 1982.
    • (1982) Cell , vol.29 , pp. 11-22
    • Little, J.1    Mount, D.2
  • 86
    • 0026515714 scopus 로고
    • Transmission of chromosomal instability after plutonium α-particle irradiation
    • Kadhim M, Macdonald D, Goodhead D, Lorimore S, Marsden S, Wright E: Transmission of chromosomal instability after plutonium α-particle irradiation. Nature 355:738-740, 1992.
    • (1992) Nature , vol.355 , pp. 738-740
    • Kadhim, M.1    Macdonald, D.2    Goodhead, D.3    Lorimore, S.4    Marsden, S.5    Wright, E.6
  • 87
    • 0026514035 scopus 로고
    • Gamma-irradiated DNA activates histone H1-specific proteinase of rat liver nuclei
    • Gaziev A, Kutsy M: Gamma-irradiated DNA activates histone H1-specific proteinase of rat liver nuclei. Int J Radiat Biol 61:169-174, 1992.
    • (1992) Int J Radiat Biol , vol.61 , pp. 169-174
    • Gaziev, A.1    Kutsy, M.2
  • 88
    • 0028909134 scopus 로고
    • DNA structure-dependent requirements for yeast RAD genes in gene conversion
    • Sugawara N, Ivanov K, Fishman-Lobell J, Ray B, Wu X, Haber J: DNA structure-dependent requirements for yeast RAD genes in gene conversion. Nature 373:84-86, 1995.
    • (1995) Nature , vol.373 , pp. 84-86
    • Sugawara, N.1    Ivanov, K.2    Fishman-Lobell, J.3    Ray, B.4    Wu, X.5    Haber, J.6
  • 89
    • 0023916560 scopus 로고
    • Potential intracellular target proteins of the anticarcinogenic Bowman-Birk protease inhibitor identified by affinity chromatography
    • Billings P, St. Clair W, Owen A, Kennedy A: Potential intracellular target proteins of the anticarcinogenic Bowman-Birk protease inhibitor identified by affinity chromatography. Cancer Res 48:1798-1802, 1988.
    • (1988) Cancer Res , vol.48 , pp. 1798-1802
    • Billings, P.1    St Clair, W.2    Owen, A.3    Kennedy, A.4
  • 90
    • 0028206262 scopus 로고
    • The serpin superfamily of proteinase inhibitors: Structure, function, and regulation
    • Potempa J, Korzus E, Travis J: The serpin superfamily of proteinase inhibitors: Structure, function, and regulation. J Biol Chem 269:15957-15960, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 15957-15960
    • Potempa, J.1    Korzus, E.2    Travis, J.3
  • 92
    • 0025130625 scopus 로고
    • Endocytosis and degradation of α1-antitrypsin-protease complexes is mediated by the serpin-enzyme complex (SEC) receptor
    • Perlmutter D, Joslin G, Nelson P, Schasteen C, Adams S, Fallon R: Endocytosis and degradation of α1-antitrypsin-protease complexes is mediated by the serpin-enzyme complex (SEC) receptor. J Biol Chem 265:16713-16716, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 16713-16716
    • Perlmutter, D.1    Joslin, G.2    Nelson, P.3    Schasteen, C.4    Adams, S.5    Fallon, R.6
  • 93
    • 0025336126 scopus 로고
    • Identification of a serpin-enzyme complex receptor on human hepatoma cells and human monocytes
    • Perlmutter D, Glover G, Rivetna M, Schasteen C, Fallon R: Identification of a serpin-enzyme complex receptor on human hepatoma cells and human monocytes. Proc Natl Acad Sci USA 87:3753-3757, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3753-3757
    • Perlmutter, D.1    Glover, G.2    Rivetna, M.3    Schasteen, C.4    Fallon, R.5
  • 94
    • 0028208912 scopus 로고
    • Maspin, a serpin with tumor-suppressing activity in human mammary epithelial cells
    • Zou Z, Anisowicz A, Hendrix M, et al: Maspin, a serpin with tumor-suppressing activity in human mammary epithelial cells. Science 263:526-529, 1994.
    • (1994) Science , vol.263 , pp. 526-529
    • Zou, Z.1    Anisowicz, A.2    Hendrix, M.3
  • 95
    • 0026509220 scopus 로고
    • A growth-regulated protease activity that is inhibited by the anticarcinogenic Bowman-Birk protease inhibitor
    • Billings P, Habres J: A growth-regulated protease activity that is inhibited by the anticarcinogenic Bowman-Birk protease inhibitor. Proc Natl Acad Sci USA 89:3120-3124, 1991.
    • (1991) Proc Natl Acad Sci USA , vol.89 , pp. 3120-3124
    • Billings, P.1    Habres, J.2
  • 96
    • 0025016824 scopus 로고
    • Identification of a proteolytic activity which responds to anticarcinogenic protease inhibitors in C3H/10T1/2 cells
    • Carew J, Kennedy A: Identification of a proteolytic activity which responds to anticarcinogenic protease inhibitors in C3H/10T1/2 cells. Cancer Lett 49:153-163, 1990.
    • (1990) Cancer Lett , vol.49 , pp. 153-163
    • Carew, J.1    Kennedy, A.2
  • 97
    • 0023094112 scopus 로고
    • Proteases occurring in the cell membrane: A possible cell receptor for the Bowman-Birk type of protease inhibitors
    • Yavelow J, Caggana M, Beck K: Proteases occurring in the cell membrane: A possible cell receptor for the Bowman-Birk type of protease inhibitors. Cancer Res 47:1598-1601, 1987.
    • (1987) Cancer Res , vol.47 , pp. 1598-1601
    • Yavelow, J.1    Caggana, M.2    Beck, K.3
  • 98
    • 0029143239 scopus 로고
    • Nuclear multicatalytic proteinase a subunit RRC3: Differential size, tyrosine phosphorylation, and susceptibility to antisense oligonucleotide treatment
    • Benedict C, Ren L, Clawson G: Nuclear multicatalytic proteinase a subunit RRC3: Differential size, tyrosine phosphorylation, and susceptibility to antisense oligonucleotide treatment. Biochemistry 34:9587-9598, 1995.
    • (1995) Biochemistry , vol.34 , pp. 9587-9598
    • Benedict, C.1    Ren, L.2    Clawson, G.3
  • 99
    • 0018754795 scopus 로고
    • Acute phase reactant proteins in cancer
    • Cooper E, Stone J: Acute phase reactant proteins in cancer. Adv Cancer Res 30:1-44, 1979.
    • (1979) Adv Cancer Res , vol.30 , pp. 1-44
    • Cooper, E.1    Stone, J.2
  • 100
    • 0020374142 scopus 로고
    • 1-antichymotrypsin by an immunohistochemical technique
    • 1-antichymotrypsin by an immunohistochemical technique. Gann 73:742-747, 1982.
    • (1982) Gann , vol.73 , pp. 742-747
    • Takada, S.1    Tsuda, M.2    Mitomi, T.3
  • 104
    • 0020539549 scopus 로고
    • Ultrastructural localization of Bowman-Birk inhibitor on thin sections of glycine max (soybean) cv. Maple Arrow by the gold method
    • Horisberger M, Tacchini-Vonlanthen M: Ultrastructural localization of Bowman-Birk inhibitor on thin sections of glycine max (soybean) cv. Maple Arrow by the gold method. Histochemistry 77:313-321, 1983.
    • (1983) Histochemistry , vol.77 , pp. 313-321
    • Horisberger, M.1    Tacchini-Vonlanthen, M.2
  • 105
    • 0025115736 scopus 로고
    • Abnormally high expression of proteasomes in human leukemic cells
    • Kumatori A, Tanaka K, Inamura N, et al: Abnormally high expression of proteasomes in human leukemic cells. Proc Natl Acad Sci USA 87:7071-7075, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 7071-7075
    • Kumatori, A.1    Tanaka, K.2    Inamura, N.3
  • 106
    • 0026315682 scopus 로고
    • Changes in expressions of proteasome and ubiquitin genes in human renal cancer cells
    • Kanayama H, Tanaka K, Aki M, et al: Changes in expressions of proteasome and ubiquitin genes in human renal cancer cells. Cancer Res 51:6677-6685, 1991.
    • (1991) Cancer Res , vol.51 , pp. 6677-6685
    • Kanayama, H.1    Tanaka, K.2    Aki, M.3
  • 107
    • 0024467228 scopus 로고
    • Proteolytic activity associated with the nuclear scaffold: The effect of self-digestion on lamins
    • Tokes Z, Clawson G: Proteolytic activity associated with the nuclear scaffold: The effect of self-digestion on lamins. J Biol Chem 264:15059-15065, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 15059-15065
    • Tokes, Z.1    Clawson, G.2
  • 108
    • 0028967267 scopus 로고
    • Role of a ubiquilin-conjugating enzyme in degradation of S- and M-phase cyclins
    • Seufert W, Futcher B, Jentsch S: Role of a ubiquilin-conjugating enzyme in degradation of S- and M-phase cyclins. Nature 373:78-81, 1995.
    • (1995) Nature , vol.373 , pp. 78-81
    • Seufert, W.1    Futcher, B.2    Jentsch, S.3
  • 109
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-Jun degradation in vivo is mediated by the δ domain
    • Treier M, Staszewski L, Bohmann D: Ubiquitin-dependent c-Jun degradation in vivo is mediated by the δ domain. Cell 78:787-798, 1994.
    • (1994) Cell , vol.78 , pp. 787-798
    • Treier, M.1    Staszewski, L.2    Bohmann, D.3
  • 110
    • 0026025416 scopus 로고
    • Degradation of nuclear oncoproteins by the ubiquilin system in vitro
    • Ciechanover A, DiGiuseppe J, Bercovich B, et al: Degradation of nuclear oncoproteins by the ubiquilin system in vitro. Proc Natl Acad Sci USA 88:139-143, 1991.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 139-143
    • Ciechanover, A.1    DiGiuseppe, J.2    Bercovich, B.3
  • 111
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • Rogers S, Well R, Rechsteiner M: Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis. Science 234:364-369, 1986.
    • (1986) Science , vol.234 , pp. 364-369
    • Rogers, S.1    Well, R.2    Rechsteiner, M.3
  • 112
    • 0019197784 scopus 로고
    • Association of a protease with polytene chromosomes of Drosophila melanogaster
    • Cavagnaro J, Pierce D, Lucchesi J, Chae C: Association of a protease with polytene chromosomes of Drosophila melanogaster. J Cell Biol 87:415-419, 1980.
    • (1980) J Cell Biol , vol.87 , pp. 415-419
    • Cavagnaro, J.1    Pierce, D.2    Lucchesi, J.3    Chae, C.4
  • 113
    • 0017162255 scopus 로고
    • Chromatin-bound protease: [3H]Diisopropyl fluorophosphate labeling patterns of chromatin
    • Carter D, Efiro P, Chae C: Chromatin-bound protease: [3H]Diisopropyl fluorophosphate labeling patterns of chromatin. Biochemistry 15:2603-2607, 1976.
    • (1976) Biochemistry , vol.15 , pp. 2603-2607
    • Carter, D.1    Efiro, P.2    Chae, C.3
  • 114
    • 0028287944 scopus 로고
    • Granule serine proteases are normal nuclear constituents of natural killer cells
    • Trapani J, Smyth M, Apostolidis V, Dawson M, Browne K: Granule serine proteases are normal nuclear constituents of natural killer cells. J Biol Chem 269:18359-18365, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 18359-18365
    • Trapani, J.1    Smyth, M.2    Apostolidis, V.3    Dawson, M.4    Browne, K.5


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