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Volumn 48, Issue 1, 2008, Pages 94-118

The biochemical and functional food properties of the Bowman-Birk inhibitor

Author keywords

Angiogenesis; Bowman Birk inhibitor; Cancer; Functional foods; Soybean (Glycine max); Tryptase and or chymase inhibitor

Indexed keywords

BOWMAN BIRK INHIBITOR; PEPTIDE HYDROLASE;

EID: 39349086395     PISSN: 10408398     EISSN: 15497852     Source Type: Journal    
DOI: 10.1080/10408390601177589     Document Type: Article
Times cited : (145)

References (247)
  • 2
    • 15244338619 scopus 로고    scopus 로고
    • Collagenases in cancer
    • Ala-Aho, R., and Kahari, V. M. 2005. Collagenases in cancer. Biochimie, 87:273-286.
    • (2005) Biochimie , vol.87 , pp. 273-286
    • Ala-Aho, R.1    Kahari, V.M.2
  • 3
    • 0031771536 scopus 로고    scopus 로고
    • Effects of soy protein on renal function and proteinuria in patients with type 2 diabetes
    • Anderson, J. W., Blake, J. E., Turner, J., and Smith, B. M. 1998. Effects of soy protein on renal function and proteinuria in patients with type 2 diabetes. Am. J. Clin. Nutr. 68:1347S-1353S.
    • (1998) Am. J. Clin. Nutr , vol.68
    • Anderson, J.W.1    Blake, J.E.2    Turner, J.3    Smith, B.M.4
  • 4
    • 0031771536 scopus 로고    scopus 로고
    • Effects of soy protein on renal function and proteinuria in patients with type 2 diabetes
    • Anderson, J. W., Blake, J. E., Turner, J., and Smith, B. M. 1998. Effects of soy protein on renal function and proteinuria in patients with type 2 diabetes. Am. J. Clin. Nutr., 68(Suppl.):1347S-1353S.
    • (1998) Am. J. Clin. Nutr , vol.68 , Issue.SUPPL.
    • Anderson, J.W.1    Blake, J.E.2    Turner, J.3    Smith, B.M.4
  • 5
    • 0000918361 scopus 로고
    • Characterization of a trypsin/chymotrypsin inhibitor from Jack fruit
    • Annapuma, S. S., Ramadoss, C. S., and Prasad, D. S. 1991. Characterization of a trypsin/chymotrypsin inhibitor from Jack fruit. J. Sci. Food Agric., 54:605-618.
    • (1991) J. Sci. Food Agric , vol.54 , pp. 605-618
    • Annapuma, S.S.1    Ramadoss, C.S.2    Prasad, D.S.3
  • 6
    • 0027452304 scopus 로고
    • High performance capillary electrophoresis for the determination of trypsin and chymotrypsin inhibitors and their association with trypsin, chymotrypsin and monoclonal antibodies
    • Arentoft, A. M., Frokiaer H., Michaelsen, S., Sorensen, H., and Sorensen, S. J. 1993. High performance capillary electrophoresis for the determination of trypsin and chymotrypsin inhibitors and their association with trypsin, chymotrypsin and monoclonal antibodies. J. Chromatogr., 652:189-198.
    • (1993) J. Chromatogr , vol.652 , pp. 189-198
    • Arentoft, A.M.1    Frokiaer, H.2    Michaelsen, S.3    Sorensen, H.4    Sorensen, S.J.5
  • 9
    • 0141752847 scopus 로고    scopus 로고
    • Development of the Bowman-Birk inhibitor for oral cancer chemoprevention and analysis of Neu immunohistochemical staining intensity with Bowman-Birk inhibitor concentrate treatment
    • Armstrong, W. B., Wan, S. X., Kennedy, A. R., Taylor, T. H., and Meyskens, F. L. Jr. 2003. Development of the Bowman-Birk inhibitor for oral cancer chemoprevention and analysis of Neu immunohistochemical staining intensity with Bowman-Birk inhibitor concentrate treatment. Laryngoscope, 113:1687-1702.
    • (2003) Laryngoscope , vol.113 , pp. 1687-1702
    • Armstrong, W.B.1    Wan, S.X.2    Kennedy, A.R.3    Taylor, T.H.4    Meyskens Jr., F.L.5
  • 10
    • 0024299197 scopus 로고
    • The amino acid sequence of a cereal Bowman-Birk type trypsin inhibitor from seeds of Job's tears (Coix lachryma-jobi L.)
    • Ary, M. B., Shewry, P. R., and Richardson, M. (1988).The amino acid sequence of a cereal Bowman-Birk type trypsin inhibitor from seeds of Job's tears (Coix lachryma-jobi L.). FEBS Lett., 229:111-118.
    • (1988) FEBS Lett , vol.229 , pp. 111-118
    • Ary, M.B.1    Shewry, P.R.2    Richardson, M.3
  • 11
    • 15944405794 scopus 로고    scopus 로고
    • Effects of plant protease inhibitors, oryzacystatin I and soybean Bowman-Birk inhibitor, on the aphid Macrosiphum euphorbiae (Homoptera, Aphididae) and its parasitoid Aphelinus abdominalis (Hymenoptera, Aphelinidae)
    • Azzouz, H., Cherqui, A., Campan, E. D., Rahbe, Y., Duport, G., Jouanin, L., Kaiser, L., and Giordanengo, P. 2005. Effects of plant protease inhibitors, oryzacystatin I and soybean Bowman-Birk inhibitor, on the aphid Macrosiphum euphorbiae (Homoptera, Aphididae) and its parasitoid Aphelinus abdominalis (Hymenoptera, Aphelinidae). J. Insect Physiol., 51:75-86.
    • (2005) J. Insect Physiol , vol.51 , pp. 75-86
    • Azzouz, H.1    Cherqui, A.2    Campan, E.D.3    Rahbe, Y.4    Duport, G.5    Jouanin, L.6    Kaiser, L.7    Giordanengo, P.8
  • 12
    • 0028426861 scopus 로고
    • Nucleotide sequence homology of cDNAs encoding soybean Bowman-Birk type proteinase inhibitor and its isoinhibitors
    • Baek, J. M., Song, J. C., Choi, Y. D., and Kim, S. I. 1994. Nucleotide sequence homology of cDNAs encoding soybean Bowman-Birk type proteinase inhibitor and its isoinhibitors. Biosci. Biotechnol. Biochem. 58:843-846.
    • (1994) Biosci. Biotechnol. Biochem , vol.58 , pp. 843-846
    • Baek, J.M.1    Song, J.C.2    Choi, Y.D.3    Kim, S.I.4
  • 13
    • 0033831933 scopus 로고    scopus 로고
    • Matrix metalloproteinases, their tissue inhibitors and colorectal cancer staging
    • Baker, E. A., Bergin, F. G., and Leaper, D. J. 2000. Matrix metalloproteinases, their tissue inhibitors and colorectal cancer staging. Br. J. Surg., 87:1215-1221.
    • (2000) Br. J. Surg , vol.87 , pp. 1215-1221
    • Baker, E.A.1    Bergin, F.G.2    Leaper, D.J.3
  • 15
    • 0025720521 scopus 로고
    • In vitro reduction of peroxidation in UVC-irradiated cell cultures by concurrent exposure with Bowman-Birk protease inhibitor
    • Baturay, N. Y., and Roque, H. 1991. In vitro reduction of peroxidation in UVC-irradiated cell cultures by concurrent exposure with Bowman-Birk protease inhibitor. Teratog. Carcinog., Mutagen, 11:195-202.
    • (1991) Teratog. Carcinog., Mutagen , vol.11 , pp. 195-202
    • Baturay, N.Y.1    Roque, H.2
  • 16
    • 3242815965 scopus 로고    scopus 로고
    • In vitro inhibition of the activation of pro-metalloproteinase-1 (pro-MMP-1) and prometalloproteinase-9 (pro-MMP-9) by rice and soybean Bowman-Birk inhibitors
    • Bawadi, H. A., Antunes, T. M., Shih, F., and Losso, J. N. 2004. In vitro inhibition of the activation of pro-metalloproteinase-1 (pro-MMP-1) and prometalloproteinase-9 (pro-MMP-9) by rice and soybean Bowman-Birk inhibitors. J. Agric. Food Chem., 52:4730-4736.
    • (2004) J. Agric. Food Chem , vol.52 , pp. 4730-4736
    • Bawadi, H.A.1    Antunes, T.M.2    Shih, F.3    Losso, J.N.4
  • 17
    • 84868393289 scopus 로고    scopus 로고
    • Bernkop-Schnürch, A., Krauland, A., and Valenta, C. 1998. Development of drug delivery systems with protective effect towards Gl-proteinases. In: 2nd World Meeting on Pharmaceutics, Biopharmaceutics, Pharmaceutical Technology, pp. 989-990. APGI/APV Ed., Paris.
    • Bernkop-Schnürch, A., Krauland, A., and Valenta, C. 1998. Development of drug delivery systems with protective effect towards Gl-proteinases. In: 2nd World Meeting on Pharmaceutics, Biopharmaceutics, Pharmaceutical Technology, pp. 989-990. APGI/APV Ed., Paris.
  • 18
    • 0026039082 scopus 로고
    • A protease activity in human fibroblasts which is inhibited by the anticarcinogenic Bowman-Birk protease inhibitor
    • Billings, P. C., Habres, J. M., Liao, D. C., and Tuttle, S. W. 1991. A protease activity in human fibroblasts which is inhibited by the anticarcinogenic Bowman-Birk protease inhibitor. Cancer Res., 51:5539-5543.
    • (1991) Cancer Res , vol.51 , pp. 5539-5543
    • Billings, P.C.1    Habres, J.M.2    Liao, D.C.3    Tuttle, S.W.4
  • 19
    • 0026535123 scopus 로고
    • Distribution of the Bowman-Birk protease inhibitor in mice following oral administration
    • Billings, P. C., St. Clair, W. H., Maki, P. A., and Kennedy, A. R. 1992. Distribution of the Bowman-Birk protease inhibitor in mice following oral administration. Cancer Lett., 62:191-197.
    • (1992) Cancer Lett , vol.62 , pp. 191-197
    • Billings, P.C.1    St. Clair, W.H.2    Maki, P.A.3    Kennedy, A.R.4
  • 20
    • 0000137738 scopus 로고
    • Purification and some properties of a highly active inhibitor of trypsin and chymotrypsin from soybeans
    • Birk, Y. (1961). Purification and some properties of a highly active inhibitor of trypsin and chymotrypsin from soybeans. Biochim. Biophys.Acta, 54:378-38.
    • (1961) Biochim. Biophys.Acta , vol.54 , pp. 378-438
    • Birk, Y.1
  • 21
    • 0017246522 scopus 로고
    • Trypsin and Chymotryspin inhibitors from soybeans
    • Birk, Y. 1976. Trypsin and Chymotryspin inhibitors from soybeans. Methods Enzymol., XLV:700-707.
    • (1976) Methods Enzymol , vol.45 , pp. 700-707
    • Birk, Y.1
  • 22
    • 0022017412 scopus 로고
    • The Bowman-Birk inhibitor
    • Birk, Y. 1985. The Bowman-Birk inhibitor. Int. J. Peptide Protein Res., 25:113-131.
    • (1985) Int. J. Peptide Protein Res , vol.25 , pp. 113-131
    • Birk, Y.1
  • 23
    • 77956855897 scopus 로고
    • Proteinase Inhibitors
    • Neuberger, A. and Brocklehurst, K. Eds, Elsevier Science Publishers, New York
    • Birk, Y. 1987. Proteinase Inhibitors. In: Hydrolytic Enzymes. pp. 257-305. Neuberger, A. and Brocklehurst, K. Eds., Elsevier Science Publishers, New York.
    • (1987) Hydrolytic Enzymes , pp. 257-305
    • Birk, Y.1
  • 24
    • 0000835634 scopus 로고
    • A pure trypsin inhibitor from soya beans
    • Birk, Y., Gertler, A., and Khalef, S. 1963. A pure trypsin inhibitor from soya beans. Biochem. J., 87:281-284.
    • (1963) Biochem. J , vol.87 , pp. 281-284
    • Birk, Y.1    Gertler, A.2    Khalef, S.3
  • 25
    • 0023016287 scopus 로고
    • Photoreactive, active derivatives of trypsin and chymotrypsin inhibitors from soybeans and chickpeas
    • Birk, Y., Smirnoff, P., and Ramachandran, J. 1986. Photoreactive, active derivatives of trypsin and chymotrypsin inhibitors from soybeans and chickpeas. Adv. Exp. Med. Biol., 199:469-81.
    • (1986) Adv. Exp. Med. Biol , vol.199 , pp. 469-481
    • Birk, Y.1    Smirnoff, P.2    Ramachandran, J.3
  • 27
    • 0000498303 scopus 로고
    • Monoclonal antibody-based enzyme immunoassay of the Bowman-Birk protease inhibitor of soybean
    • Brandon, D. L., Bates, A. H., and Friedman, M. 1989. Monoclonal antibody-based enzyme immunoassay of the Bowman-Birk protease inhibitor of soybean. J. Agric. Food Chem., 37:1192-1196.
    • (1989) J. Agric. Food Chem , vol.37 , pp. 1192-1196
    • Brandon, D.L.1    Bates, A.H.2    Friedman, M.3
  • 28
    • 0025770572 scopus 로고
    • ELISA analysis of soybean trypsin inhibitors in processed foods
    • Brandon, D. L., Bates, A. H., and Friedman, M. 1991. ELISA analysis of soybean trypsin inhibitors in processed foods. Adv. Exp. Med. Biol. 289:321-337.
    • (1991) Adv. Exp. Med. Biol , vol.289 , pp. 321-337
    • Brandon, D.L.1    Bates, A.H.2    Friedman, M.3
  • 29
    • 0020324688 scopus 로고
    • Dietary protein intake and the progressive nature of kidney disease: The role of hemodynamically mediated glomerular injury in the pathogenesis of progressive glomerular sclerosis in aging, renal ablation, and intrinsic renal disease
    • Brenner, B. M., Meyer, T. W., and Hostetter, T. H. 1982. Dietary protein intake and the progressive nature of kidney disease: the role of hemodynamically mediated glomerular injury in the pathogenesis of progressive glomerular sclerosis in aging, renal ablation, and intrinsic renal disease. N. Engl. J. Med., 307:652-659.
    • (1982) N. Engl. J. Med , vol.307 , pp. 652-659
    • Brenner, B.M.1    Meyer, T.W.2    Hostetter, T.H.3
  • 30
    • 0022430999 scopus 로고
    • Wound-induced trypsin inhibitor in alfalfa leaves: Identity as a member of the Bowman-Birk inhibitor family
    • Brown, W. E., Takio, K., Titani, K., and Ryan, C. 1985. Wound-induced trypsin inhibitor in alfalfa leaves: identity as a member of the Bowman-Birk inhibitor family. Biochemistry, 24:2105-2108.
    • (1985) Biochemistry , vol.24 , pp. 2105-2108
    • Brown, W.E.1    Takio, K.2    Titani, K.3    Ryan, C.4
  • 32
    • 0024437191 scopus 로고
    • c-fos mRNA levels are reduced in the presence of antipain and Bowman-Birk inhibitor
    • Caggana, M., and Kennedy, A. R. 1989. c-fos mRNA levels are reduced in the presence of antipain and Bowman-Birk inhibitor. Carcinogenesis. 10(11):2145-2148.
    • (1989) Carcinogenesis , vol.10 , Issue.11 , pp. 2145-2148
    • Caggana, M.1    Kennedy, A.R.2
  • 33
    • 0030735597 scopus 로고    scopus 로고
    • Metabolic and hormonal controls of food intake: Highlights of the last 25 years- 1972-1997
    • Campfield, L. A. 1997. Metabolic and hormonal controls of food intake: highlights of the last 25 years- 1972-1997. Appetite, 29:135-152.
    • (1997) Appetite , vol.29 , pp. 135-152
    • Campfield, L.A.1
  • 34
    • 0036842625 scopus 로고    scopus 로고
    • Plant toxic proteins with insecticidal properties. A review on their potentialities as bioinsecticides
    • Carlini, C. R., and Grossi-de-Sa, M. F. 2002. Plant toxic proteins with insecticidal properties. A review on their potentialities as bioinsecticides. Toxicon, 40(11):1515-1539.
    • (2002) Toxicon , vol.40 , Issue.11 , pp. 1515-1539
    • Carlini, C.R.1    Grossi-de-Sa, M.F.2
  • 35
    • 30744479430 scopus 로고    scopus 로고
    • Angiogenesis in life, disease and medicine
    • Carmeliet, P. 2005. Angiogenesis in life, disease and medicine. Nature, 438:932-936.
    • (2005) Nature , vol.438 , pp. 932-936
    • Carmeliet, P.1
  • 36
    • 0034648765 scopus 로고    scopus 로고
    • Angiogenesis in cancer and other diseases
    • Carmeliet, P., and Jain, R. K. 2000. Angiogenesis in cancer and other diseases. Nature, 407:249-257.
    • (2000) Nature , vol.407 , pp. 249-257
    • Carmeliet, P.1    Jain, R.K.2
  • 37
    • 0037327370 scopus 로고    scopus 로고
    • Selection by phage display of a variant mustard trypsin inhibitor toxic against aphids
    • Ceci, L. R., Volpicella, M., Rahbé, Y., Gallerani, R., Beekwilder, J., and Jongsma, M. A. 2003. Selection by phage display of a variant mustard trypsin inhibitor toxic against aphids, Plant J., 33:557-566.
    • (2003) Plant J , vol.33 , pp. 557-566
    • Ceci, L.R.1    Volpicella, M.2    Rahbé, Y.3    Gallerani, R.4    Beekwilder, J.5    Jongsma, M.A.6
  • 38
    • 0025123666 scopus 로고
    • Effects of protease inhibitors on c-myc expression in normal and transformed C3H 10T1/2 cell lines
    • Chang, J. D., Li, J. H., Billings, P. C., and Kennedy, A. R. 1990. Effects of protease inhibitors on c-myc expression in normal and transformed C3H 10T1/2 cell lines. Mol Carcinog., 3:226-232.
    • (1990) Mol Carcinog , vol.3 , pp. 226-232
    • Chang, J.D.1    Li, J.H.2    Billings, P.C.3    Kennedy, A.R.4
  • 39
    • 0035192944 scopus 로고    scopus 로고
    • Differential inhibition and inactivation of human CYP1 enzymes by trans-resveratrol: Evidence for mechanism-based inactivation of CYP1A2
    • Chang, T. K., Chen, J., and Lee, W. B. 2001. Differential inhibition and inactivation of human CYP1 enzymes by trans-resveratrol: evidence for mechanism-based inactivation of CYP1A2. J Pharmacol. Exp. Ther., 299:874-882.
    • (2001) J Pharmacol. Exp. Ther , vol.299 , pp. 874-882
    • Chang, T.K.1    Chen, J.2    Lee, W.B.3
  • 40
    • 22844434892 scopus 로고    scopus 로고
    • Bowman-birk inhibitor abates proteasome function and suppresses the proliferation of MCF7 breast cancer cells through accumulation of MAP kinase phosphatase-1
    • Chen, Y. N., Huang, S. C., Lin-Shiau, S. Y., and Lin, J. K. 2005. Bowman-birk inhibitor abates proteasome function and suppresses the proliferation of MCF7 breast cancer cells through accumulation of MAP kinase phosphatase-1. Carcinogenesisg, 26:1296-1306.
    • (2005) Carcinogenesisg , vol.26 , pp. 1296-1306
    • Chen, Y.N.1    Huang, S.C.2    Lin-Shiau, S.Y.3    Lin, J.K.4
  • 41
    • 0026526805 scopus 로고
    • Reactive sites of an anticarcinogenic Bowman-Birk proteinase inhibitor are similar to other trypsin inhibitors
    • Chen, P., Rose, J., Love, R., Wei, C. H., and Wang, B. C. 1992. Reactive sites of an anticarcinogenic Bowman-Birk proteinase inhibitor are similar to other trypsin inhibitors. J Biol Chem., 267(3):1990-4.
    • (1992) J Biol Chem , vol.267 , Issue.3 , pp. 1990-1994
    • Chen, P.1    Rose, J.2    Love, R.3    Wei, C.H.4    Wang, B.C.5
  • 42
    • 0031965487 scopus 로고    scopus 로고
    • Gelatinase A (MMP-2) and cysteine proteinase are essential for the degradation of collagen in soft connective tissue
    • Creemers, L. B., Jansen, I. D. C., Docherty, A. J. P., Reynolds, J. J., Beersten, W., and Everts, V. 1998. Gelatinase A (MMP-2) and cysteine proteinase are essential for the degradation of collagen in soft connective tissue. Matrix Biol., 17:35-46.
    • (1998) Matrix Biol , vol.17 , pp. 35-46
    • Creemers, L.B.1    Jansen, I.D.C.2    Docherty, A.J.P.3    Reynolds, J.J.4    Beersten, W.5    Everts, V.6
  • 43
    • 0030983121 scopus 로고    scopus 로고
    • Analysis of the black-eyed pea trypsin and chymotrypsin inhibitor α- chymotrypsin complex
    • De Freitas, S. M., Mello, L. V., da Silva, C. M., Vriend, G., Neshich, G., and Ventura, M. 1997. Analysis of the black-eyed pea trypsin and chymotrypsin inhibitor α- chymotrypsin complex. FEBS Lett., 409:121-127.
    • (1997) FEBS Lett , vol.409 , pp. 121-127
    • De Freitas, S.M.1    Mello, L.V.2    da Silva, C.M.3    Vriend, G.4    Neshich, G.5    Ventura, M.6
  • 45
    • 0030592186 scopus 로고    scopus 로고
    • N-peptidyl, O-acyl hydroxamates: Comparison of the selective inhibition of serine and cysteine proteinases
    • Demuth, H. U., Schierhorn, A., Bryan, P., Hofke, R., Kirschke, H., and Bromme, D. 1996. N-peptidyl, O-acyl hydroxamates: comparison of the selective inhibition of serine and cysteine proteinases. Biochim. Biophys. Acta, 1295:179-186.
    • (1996) Biochim. Biophys. Acta , vol.1295 , pp. 179-186
    • Demuth, H.U.1    Schierhorn, A.2    Bryan, P.3    Hofke, R.4    Kirschke, H.5    Bromme, D.6
  • 46
    • 0035282656 scopus 로고    scopus 로고
    • Ajoene, a natural product with non-steroidal anti-inflammatory drug (NSAID)-like properties?
    • Dirsch, V. M., and Vollmar, A. M. 2001. Ajoene, a natural product with non-steroidal anti-inflammatory drug (NSAID)-like properties? Biochem. Pharmacol., 61:587-593.
    • (2001) Biochem. Pharmacol , vol.61 , pp. 587-593
    • Dirsch, V.M.1    Vollmar, A.M.2
  • 47
    • 0031756893 scopus 로고    scopus 로고
    • The presence of wild-type TP53 is necessary for the radioprotective effect of the Bowman-Birk proteinase inhibitor in normal fibroblasts
    • Dittmann, K. H, Gueven, N., Mayer, C., Ohneseit, P., Zell, R., Begg, A. C., and Rodemann, H. P. 1998. The presence of wild-type TP53 is necessary for the radioprotective effect of the Bowman-Birk proteinase inhibitor in normal fibroblasts. Radiat. Res., 150:648-655.
    • (1998) Radiat. Res , vol.150 , pp. 648-655
    • Dittmann, K.H.1    Gueven, N.2    Mayer, C.3    Ohneseit, P.4    Zell, R.5    Begg, A.C.6    Rodemann, H.P.7
  • 48
    • 0031756893 scopus 로고    scopus 로고
    • The presence of wild-type TP53 is necessary for the radioprotective effect of the Bowman-Birk proteinase inhibitor in normal fibroblasts
    • Dittmann, K. H., Güven, N., Mayer, C., Ohneseit, P., Zell, R., Begg, A. C., and Rodemann, H. P. 1998a. The presence of wild-type TP53 is necessary for the radioprotective effect of the Bowman-Birk proteinase inhibitor in normal fibroblasts. Radiat. Res., 150:648-655.
    • (1998) Radiat. Res , vol.150 , pp. 648-655
    • Dittmann, K.H.1    Güven, N.2    Mayer, C.3    Ohneseit, P.4    Zell, R.5    Begg, A.C.6    Rodemann, H.P.7
  • 49
    • 0033974657 scopus 로고    scopus 로고
    • The Bowman-Birk protease inhibitor enhances clonogenic cell survival of ionizing radiation-treated nucleotide excision repair-competent cells but not of xeroderma pigmentosum cells
    • Dittmann, K., Dikomey, E., Mayer, C., and Rodemann, H. P. 2000. The Bowman-Birk protease inhibitor enhances clonogenic cell survival of ionizing radiation-treated nucleotide excision repair-competent cells but not of xeroderma pigmentosum cells. Int. J. Radiat. Biol., 76:223-229.
    • (2000) Int. J. Radiat. Biol , vol.76 , pp. 223-229
    • Dittmann, K.1    Dikomey, E.2    Mayer, C.3    Rodemann, H.P.4
  • 50
    • 0034952968 scopus 로고    scopus 로고
    • Bowman-Birk proteinase inhibitor-mediated radioprotection against UV irradiation is TP53-dependent and associated with stimulation of nucleotide excision repair
    • Dittmann, K., Knaus-Dittmann, D., Mayer, C., and Rodemann, H. P. 2001. Bowman-Birk proteinase inhibitor-mediated radioprotection against UV irradiation is TP53-dependent and associated with stimulation of nucleotide excision repair. Radiat. Ernviron. Biophys., 40:163-167.
    • (2001) Radiat. Ernviron. Biophys , vol.40 , pp. 163-167
    • Dittmann, K.1    Knaus-Dittmann, D.2    Mayer, C.3    Rodemann, H.P.4
  • 51
    • 17044370493 scopus 로고    scopus 로고
    • Dittmann, K., Toulany, M., Classen, J., Heinrich, V., Milas, L., and Rodemann, H. P. 2005. Selective Radioprotection of Normal Tissues by Bowman-Birk Proteinase Inhibitor (BBI) in Mice. Strahlenther Onkol., 181(3):191-196s, 161.
    • Dittmann, K., Toulany, M., Classen, J., Heinrich, V., Milas, L., and Rodemann, H. P. 2005. Selective Radioprotection of Normal Tissues by Bowman-Birk Proteinase Inhibitor (BBI) in Mice. Strahlenther Onkol., 181(3):191-196s, 161.
  • 52
    • 39349117166 scopus 로고    scopus 로고
    • Domagalski, J. M., Kollipara, K. P., Bates, A. H., Brandon, D. L., Friedman, M., and Hymowitz, T. 1992. Nulls for the major soybean Bowman-Birk protease inhibitor in the genus Glycine. Crop. Sci. 32:1502-1505.
    • Domagalski, J. M., Kollipara, K. P., Bates, A. H., Brandon, D. L., Friedman, M., and Hymowitz, T. 1992. Nulls for the major soybean Bowman-Birk protease inhibitor in the genus Glycine. Crop. Sci. 32:1502-1505.
  • 53
    • 0031870510 scopus 로고    scopus 로고
    • Limited proteolysis of enzyme inhibitor proteins during seed dessication in Pisum
    • Domoney, C., and Welham, T. 1998. Limited proteolysis of enzyme inhibitor proteins during seed dessication in Pisum. J. Plant Physol., 52:692-695.
    • (1998) J. Plant Physol , vol.52 , pp. 692-695
    • Domoney, C.1    Welham, T.2
  • 54
    • 0000229676 scopus 로고
    • Purification and characterization of Pisum seed trypsin inhibitors
    • Domoney, C., Welham, T., and Sidebottom, C. 1993. Purification and characterization of Pisum seed trypsin inhibitors. J. Exp Bot., 44:701-709.
    • (1993) J. Exp Bot , vol.44 , pp. 701-709
    • Domoney, C.1    Welham, T.2    Sidebottom, C.3
  • 55
    • 0028893996 scopus 로고
    • Multiple isoforms of Pisum trypsin inhibitors result from modification of two primary gene products
    • Domoney, C., Welham, T., Sidebottom, C., and Firmin, J. L. 1995. Multiple isoforms of Pisum trypsin inhibitors result from modification of two primary gene products. FEBS Lett. 360:5-20.
    • (1995) FEBS Lett , vol.360 , pp. 5-20
    • Domoney, C.1    Welham, T.2    Sidebottom, C.3    Firmin, J.L.4
  • 56
    • 0035953180 scopus 로고    scopus 로고
    • Bowman-Birk protease inhibitor and its palmitic acid conjugate prevent 7,12-dimethylbenz[a] anthracene-induced transformation in cultured mouse mammary glands
    • Du, X., Beloussow, K., and Shen, W. C. 2001. Bowman-Birk protease inhibitor and its palmitic acid conjugate prevent 7,12-dimethylbenz[a] anthracene-induced transformation in cultured mouse mammary glands. Cancer Lett., 164:135-141.
    • (2001) Cancer Lett , vol.164 , pp. 135-141
    • Du, X.1    Beloussow, K.2    Shen, W.C.3
  • 58
    • 0032533729 scopus 로고    scopus 로고
    • Human matrix metalloproteinase-9: Activation by limited trypsin treatment and generation of monoclonal antibodies specific for the activated form
    • Duncan, M. E., Richardson, J. P., Murray, G. I., Melvin, W. T., and Fothergill J. E. 1998. Human matrix metalloproteinase-9: activation by limited trypsin treatment and generation of monoclonal antibodies specific for the activated form. Eur. J. Biochemg., 15:37-43.
    • (1998) Eur. J. Biochemg , vol.15 , pp. 37-43
    • Duncan, M.E.1    Richardson, J.P.2    Murray, G.I.3    Melvin, W.T.4    Fothergill, J.E.5
  • 59
    • 0028946492 scopus 로고
    • Disposition of positively charged Bowman-Birk protease inhibitor conjugates in mice: Influence of protein conjugate charge density and size on lung targeting
    • Ekrami, H., Kennedy, A. R., and Shen, W. C. 1995. Disposition of positively charged Bowman-Birk protease inhibitor conjugates in mice: influence of protein conjugate charge density and size on lung targeting. J. Pharm. Sci., 84:456-461.
    • (1995) J. Pharm. Sci , vol.84 , pp. 456-461
    • Ekrami, H.1    Kennedy, A.R.2    Shen, W.C.3
  • 60
    • 0027793865 scopus 로고
    • Cationized Bowman-Birk protease inhibitor as a targeted cancer chemopreventive agent
    • Ekrami, H., Kennedy, A. R., Witschi, H., and Shen, W. C. 1993. Cationized Bowman-Birk protease inhibitor as a targeted cancer chemopreventive agent. J. Drug Target, 1:41-49.
    • (1993) J. Drug Target , vol.1 , pp. 41-49
    • Ekrami, H.1    Kennedy, A.R.2    Witschi, H.3    Shen, W.C.4
  • 61
    • 0026485698 scopus 로고
    • Protection against metastasis of radiation induced thymic lymphosarcoma and weight loss in C57B1/6NCr1BR mice by an autoclave resistant factor present in soybeans
    • Evans, S. M., Szuhaj, B. F., Van Winkle, T., Michel, K., and Kennedy, A. R. 1992. Protection against metastasis of radiation induced thymic lymphosarcoma and weight loss in C57B1/6NCr1BR mice by an autoclave resistant factor present in soybeans. Radiat. Res., 132:259-262.
    • (1992) Radiat. Res , vol.132 , pp. 259-262
    • Evans, S.M.1    Szuhaj, B.F.2    Van Winkle, T.3    Michel, K.4    Kennedy, A.R.5
  • 62
    • 0029119829 scopus 로고
    • Amino acid sequence of a Bowman-Birk proteinase inhibitor from pea seeds
    • Ferrasson E., Quillien L., and Gueguen J. 1995. Amino acid sequence of a Bowman-Birk proteinase inhibitor from pea seeds. J. Protein Chem., 14:467-475.
    • (1995) J. Protein Chem , vol.14 , pp. 467-475
    • Ferrasson, E.1    Quillien, L.2    Gueguen, J.3
  • 63
    • 0023195312 scopus 로고
    • Chemical synthesis, molecular cloning and expression of gene coding for Bowman-Birk-type proteinase inhibitor
    • Flecker, P. 1987. Chemical synthesis, molecular cloning and expression of gene coding for Bowman-Birk-type proteinase inhibitor. FEBS Lett., 252:151-156.
    • (1987) FEBS Lett , vol.252 , pp. 151-156
    • Flecker, P.1
  • 64
    • 85013312416 scopus 로고
    • Tumor angiogenesis: Therapeutic implications
    • Folkman, J. 1971. Tumor angiogenesis: therapeutic implications. N. Engl. J. Med. 285:1182-1186.
    • (1971) N. Engl. J. Med , vol.285 , pp. 1182-1186
    • Folkman, J.1
  • 65
    • 32944463899 scopus 로고    scopus 로고
    • Angiogenesis
    • Folkman, J. 2006. Angiogenesis. Annu Rev Med. 57:1-18.
    • (2006) Annu Rev Med , vol.57 , pp. 1-18
    • Folkman, J.1
  • 66
    • 0014469352 scopus 로고
    • Soybean Inhibitors. II. Preparative electrophoretic purification of soybean proteinase inhibitors on polyacrylamide gels.Anal
    • Fratali, V., and Steiner, R. F. 1969. Soybean Inhibitors. II. Preparative electrophoretic purification of soybean proteinase inhibitors on polyacrylamide gels.Anal. Biochem., 27:285-291.
    • (1969) Biochem , vol.27 , pp. 285-291
    • Fratali, V.1    Steiner, R.F.2
  • 68
    • 0034833829 scopus 로고    scopus 로고
    • Nutritional and health benefits of soy proteins
    • Friedman, M., and Brandon, D. L. 2001. Nutritional and health benefits of soy proteins. J. Agric Food Chem., 49:1069-1086.
    • (2001) J. Agric Food Chem , vol.49 , pp. 1069-1086
    • Friedman, M.1    Brandon, D.L.2
  • 69
    • 0027586778 scopus 로고
    • Primary structures of proteinase inhibitors from Phaseolus vulgaris var. nanus (cv. Borlotto)
    • Funk, A., Weder, J. K., and Belitz, H. D. 1993. Primary structures of proteinase inhibitors from Phaseolus vulgaris var. nanus (cv. Borlotto). Z Lebensm Unters Forsch. 196(4) :343-50.
    • (1993) Z Lebensm Unters Forsch , vol.196 , Issue.4 , pp. 343-350
    • Funk, A.1    Weder, J.K.2    Belitz, H.D.3
  • 71
    • 0014709196 scopus 로고
    • Isolation and characterization of porcine proelastase
    • Getler, A., and Birk, Y. 1970. Isolation and characterization of porcine proelastase. Eur J Biochem., 12:170-176.
    • (1970) Eur J Biochem , vol.12 , pp. 170-176
    • Getler, A.1    Birk, Y.2
  • 72
    • 0036527018 scopus 로고    scopus 로고
    • Study on interaction between duodenase-protease with dual specificity and inhibitors of Bowman-Birk family
    • Gladysheva I. P., Popykina N. A., Zamolodchikova T. S., and Larionova N. I. 2002. Study on interaction between duodenase-protease with dual specificity and inhibitors of Bowman-Birk family. Prot. Peptide Lett., 9:139-144.
    • (2002) Prot. Peptide Lett , vol.9 , pp. 139-144
    • Gladysheva, I.P.1    Popykina, N.A.2    Zamolodchikova, T.S.3    Larionova, N.I.4
  • 73
    • 0034132819 scopus 로고    scopus 로고
    • Isolation and characterization of soybean Bowman-Birk inhibitor from different sources
    • Gladysheva, I. P., Balabushevich, N. G., Moroz, N. A., and Larionova, N. I. 2000. Isolation and characterization of soybean Bowman-Birk inhibitor from different sources. Biochemistry (Mosc.), 65:198-203.
    • (2000) Biochemistry (Mosc.) , vol.65 , pp. 198-203
    • Gladysheva, I.P.1    Balabushevich, N.G.2    Moroz, N.A.3    Larionova, N.I.4
  • 74
    • 0028418799 scopus 로고
    • The classical Bowman-Birk soy inhibitor is an effective inhibitor of human granulocyte alpha-chymotrypsin and cathepsin G]
    • Russian
    • Gladysheva, I. P., Larionova, N. I., Gladyshev, D. P., Tikhonova, T. V., and Kazanskaia, N. F. 1994. [The classical Bowman-Birk soy inhibitor is an effective inhibitor of human granulocyte alpha-chymotrypsin and cathepsin G]. Biokhimiia, 59(4):513-8. Russian.
    • (1994) Biokhimiia , vol.59 , Issue.4 , pp. 513-518
    • Gladysheva, I.P.1    Larionova, N.I.2    Gladyshev, D.P.3    Tikhonova, T.V.4    Kazanskaia, N.F.5
  • 77
    • 0033217716 scopus 로고    scopus 로고
    • Interaction between duodenase, a proteinase with dual specificity, and soybean inhibitors of Bowman-Birk and Kunitz type
    • Gladysheva, I. P., Zamolodchikova, T. S., Sokolova, E. A., and Larionova, N. I. 1999. Interaction between duodenase, a proteinase with dual specificity, and soybean inhibitors of Bowman-Birk and Kunitz type. Biochem. (Mosc.), 64:244-1249.
    • (1999) Biochem. (Mosc.) , vol.64 , pp. 244-1249
    • Gladysheva, I.P.1    Zamolodchikova, T.S.2    Sokolova, E.A.3    Larionova, N.I.4
  • 78
    • 0033217716 scopus 로고    scopus 로고
    • Interaction between duodenase, a proteinase with dual specificity, and soybean inhibitors of Bowman-Birk and Kunitz type
    • Gladysheva, I. P., Zamolodchikova, T. S., Sokolova, E. A., and Larionova, N. I. 1999. Interaction between duodenase, a proteinase with dual specificity, and soybean inhibitors of Bowman-Birk and Kunitz type. Biochem. (Mosc.), 64:1244-1249.
    • (1999) Biochem. (Mosc.) , vol.64 , pp. 1244-1249
    • Gladysheva, I.P.1    Zamolodchikova, T.S.2    Sokolova, E.A.3    Larionova, N.I.4
  • 79
    • 0028121297 scopus 로고
    • Purification and characterization of proteinases inhibitors from pigeon pea (Cajanus Cajan (L) Millsp) seeds
    • Godebole, S. A., Krishna, T. G., and Bhatia, C. R. 1994. Purification and characterization of proteinases inhibitors from pigeon pea (Cajanus Cajan (L) Millsp) seeds. J. Sci. Food Agric., 64:87-93.
    • (1994) J. Sci. Food Agric , vol.64 , pp. 87-93
    • Godebole, S.A.1    Krishna, T.G.2    Bhatia, C.R.3
  • 80
    • 0035076093 scopus 로고    scopus 로고
    • Role of Cadherins and matrixins in melanoma
    • Grass, C., and Herlyn, M. 2001. Role of Cadherins and matrixins in melanoma. Curr. Opin. Oncol., 13:117-123.
    • (2001) Curr. Opin. Oncol , vol.13 , pp. 117-123
    • Grass, C.1    Herlyn, M.2
  • 81
    • 14544302321 scopus 로고    scopus 로고
    • Biorational approaches for insect control by enzymatic inhibition
    • Guerrero, A., and Rosell, G. 2005. Biorational approaches for insect control by enzymatic inhibition. Curr. Med. Chem., 12(4):461-469.
    • (2005) Curr. Med. Chem , vol.12 , Issue.4 , pp. 461-469
    • Guerrero, A.1    Rosell, G.2
  • 82
    • 0026576203 scopus 로고
    • Intestinal epithelial cells contain a high molecular weight protease subject to inhibition by anticarcinogenic protease inhibitors
    • Habres, J. M., and Billings, P. C. 1992. Intestinal epithelial cells contain a high molecular weight protease subject to inhibition by anticarcinogenic protease inhibitors. Cancer Lett., 63:135-142.
    • (1992) Cancer Lett , vol.63 , pp. 135-142
    • Habres, J.M.1    Billings, P.C.2
  • 83
    • 0035085285 scopus 로고    scopus 로고
    • Anti-cariogenic properties of tea (Camellia sinensis)
    • Hamilton-Miller, J. M. 2001. Anti-cariogenic properties of tea (Camellia sinensis). J. Med. Microbiol., 50:299-302.
    • (2001) J. Med. Microbiol , vol.50 , pp. 299-302
    • Hamilton-Miller, J.M.1
  • 84
    • 0021759598 scopus 로고
    • Molecular cloning and analysis of a gene coding for the Bowman-Birk protease inhibitor in soybean
    • Hammond R. W., Foard, D. E., and Larkins, B. A. 1984. Molecular cloning and analysis of a gene coding for the Bowman-Birk protease inhibitor in soybean. J. Biol. Chem., 259(15):9883-9890.
    • (1984) J. Biol. Chem , vol.259 , Issue.15 , pp. 9883-9890
    • Hammond, R.W.1    Foard, D.E.2    Larkins, B.A.3
  • 85
    • 20344361933 scopus 로고    scopus 로고
    • Metalloproteinases and their inhibitors in tumor angiogenesis
    • Handsley M. M., and Edwards D. R. 2005. Metalloproteinases and their inhibitors in tumor angiogenesis. Int. J. Cancer 115:849-860.
    • (2005) Int. J. Cancer , vol.115 , pp. 849-860
    • Handsley, M.M.1    Edwards, D.R.2
  • 86
    • 0034044162 scopus 로고    scopus 로고
    • Addition of matrix metalloproteinase inhibition to conventional cytotoxic therapy reduces tumor implantation and prolongs survival in a murine model of human, pancreatic cancer
    • Haq, M., Shafii, A., Zervos, E. E., and Rosemurgy, A. S. 2000. Addition of matrix metalloproteinase inhibition to conventional cytotoxic therapy reduces tumor implantation and prolongs survival in a murine model of human, pancreatic cancer. Cancer Res., 15:3207-3211.
    • (2000) Cancer Res , vol.15 , pp. 3207-3211
    • Haq, M.1    Shafii, A.2    Zervos, E.E.3    Rosemurgy, A.S.4
  • 87
    • 0014633548 scopus 로고
    • Characterization of the self-association of a soybean proteinase inhibitor by membrane osmometry
    • Harry, J. B., and Steiner, R. F. 1969. Characterization of the self-association of a soybean proteinase inhibitor by membrane osmometry. Biochem., 8:5060-5064.
    • (1969) Biochem , vol.8 , pp. 5060-5064
    • Harry, J.B.1    Steiner, R.F.2
  • 88
    • 0029918951 scopus 로고    scopus 로고
    • Solution structure of bromelain inhibitor from pineapple stem: Structural similarity with Bowman-Birk trypsin/chymotrypsin inhibitor from soybeans
    • Hatano, K. I., Kojima, M., Tanokura, M., and Takahashi, K. 1996. Solution structure of bromelain inhibitor from pineapple stem: structural similarity with Bowman-Birk trypsin/chymotrypsin inhibitor from soybeans. Biochem., 35:5379-5384.
    • (1996) Biochem , vol.35 , pp. 5379-5384
    • Hatano, K.I.1    Kojima, M.2    Tanokura, M.3    Takahashi, K.4
  • 89
    • 0014217353 scopus 로고
    • Fractionation and properties of trypsin and chymotrypsin inhibitors from lima beans. Fractionation
    • Haynes, R., and Feeney, R. E. 1967. Fractionation and properties of trypsin and chymotrypsin inhibitors from lima beans. Fractionation. J. Biol. Chem., 242:5378-5385.
    • (1967) J. Biol. Chem , vol.242 , pp. 5378-5385
    • Haynes, R.1    Feeney, R.E.2
  • 90
    • 0034036315 scopus 로고    scopus 로고
    • Clinical potential of matrix metalloprotease inhibitors in cancer therapy
    • Heath, E. I., and Grochow, L. B. 2000. Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs 59:1043-105.
    • (2000) Drugs , vol.59 , pp. 1043-1105
    • Heath, E.I.1    Grochow, L.B.2
  • 91
    • 0024917815 scopus 로고
    • Protein and cDNA sequences of Bowman-Birk protease inhibitors from the cowpea (Vigna unguiculata Walp.)
    • Hilder, V. A., Barker, R. F., Samour, R. A., Gatehouse, A. M. R., Gatehouse, J. A., and Boulter, D. 1989. Protein and cDNA sequences of Bowman-Birk protease inhibitors from the cowpea (Vigna unguiculata Walp.). Plant Mol. Biol., 13:701-710.
    • (1989) Plant Mol. Biol , vol.13 , pp. 701-710
    • Hilder, V.A.1    Barker, R.F.2    Samour, R.A.3    Gatehouse, A.M.R.4    Gatehouse, J.A.5    Boulter, D.6
  • 92
    • 0029857980 scopus 로고    scopus 로고
    • Comparison of pharmacokinetic parameters of a polypeptide, the Bowman-Birk protease inhibitor (BBI), and its palmitic acid conjugate
    • Honeycutt, L., Wang, J., Ekrami, H., and Shen, W. C. 1996. Comparison of pharmacokinetic parameters of a polypeptide, the Bowman-Birk protease inhibitor (BBI), and its palmitic acid conjugate. Pharm. Res., 13(9):1373- 1377.
    • (1996) Pharm. Res , vol.13 , Issue.9 , pp. 1373-1377
    • Honeycutt, L.1    Wang, J.2    Ekrami, H.3    Shen, W.C.4
  • 93
    • 0020539549 scopus 로고
    • Ultrastractural localization of Bowman-Birk inhibitor on thin sections of Glycine max (soybean) cv. Maple Arrow by the gold method
    • Horisberger, M., and Tacchini-Voulanthen, T. M. 1983. Ultrastractural localization of Bowman-Birk inhibitor on thin sections of Glycine max (soybean) cv. Maple Arrow by the gold method. Histochem. 77:313-321.
    • (1983) Histochem , vol.77 , pp. 313-321
    • Horisberger, M.1    Tacchini-Voulanthen, T.M.2
  • 94
    • 0034938365 scopus 로고    scopus 로고
    • Elevated level of circulating matrix metalloproteinase-9 in patients with lung cancer
    • Hrabec, E., Strek, M., Nowak, D., and Hrabec, Z. 2001. Elevated level of circulating matrix metalloproteinase-9 in patients with lung cancer. Respir. Med., 95:1-4.
    • (2001) Respir. Med , vol.95 , pp. 1-4
    • Hrabec, E.1    Strek, M.2    Nowak, D.3    Hrabec, Z.4
  • 95
    • 4043161356 scopus 로고    scopus 로고
    • Inhibitory effect of topical applications of nondenatured soymilk on the formation and growth of UVB-induced skin tumors
    • Huang, M. T., Xie, J. G., Lin, C .B., Kizoulis. M., Seiberg, M., Shapiro, S., and Conney, A. H. 2004. Inhibitory effect of topical applications of nondenatured soymilk on the formation and growth of UVB-induced skin tumors. Oncol. Res., 14:387-397.
    • (2004) Oncol. Res , vol.14 , pp. 387-397
    • Huang, M.T.1    Xie, J.G.2    Lin, C.B.3    Kizoulis, M.4    Seiberg, M.5    Shapiro, S.6    Conney, A.H.7
  • 96
    • 0017753251 scopus 로고
    • Purification, partial characterization, and immunological relationships of multiple low molecular weight protease inhibitors of soybean
    • Hwang, D. L., Lin, K. T., Yang, W. K., and Foard, D. E. 1977. Purification, partial characterization, and immunological relationships of multiple low molecular weight protease inhibitors of soybean. Biochim. Biophys. Acta, 495:369-382.
    • (1977) Biochim. Biophys. Acta , vol.495 , pp. 369-382
    • Hwang, D.L.1    Lin, K.T.2    Yang, W.K.3    Foard, D.E.4
  • 97
    • 0028265212 scopus 로고
    • Potential of food modification in cancer prevention
    • Ip, C., Lisk, D. J., and Scimera, J. A. 1994. Potential of food modification in cancer prevention CancerRes., 54:1957s-1959s.
    • (1994) CancerRes , vol.54
    • Ip, C.1    Lisk, D.J.2    Scimera, J.A.3
  • 99
    • 0030607710 scopus 로고    scopus 로고
    • Proteolytic cleavage of soybean Bowman-Birk inhibitor monitored by means of high-performance capillary electrophoresis. Implications for the mechanism of proteinase inhibitors
    • Jensen, B., Unger, K. K., Uebe, J., Gey, M., Kim, Y.-M., and Flecker, P. 1996. Proteolytic cleavage of soybean Bowman-Birk inhibitor monitored by means of high-performance capillary electrophoresis. Implications for the mechanism of proteinase inhibitors. J. Biochem. Biophys. Methods, 33:171-185.
    • (1996) J. Biochem. Biophys. Methods , vol.33 , pp. 171-185
    • Jensen, B.1    Unger, K.K.2    Uebe, J.3    Gey, M.4    Kim, Y.-M.5    Flecker, P.6
  • 100
    • 0034473193 scopus 로고    scopus 로고
    • Suppression of human microvascular endothelial cell invasion and morphogenesis with synthetic matrixin inhibitors. Targeting angiogenesis with MMP inhibitors
    • Jia, M. C, Schwartz, M. A., and Sang, Q. A. 2000. Suppression of human microvascular endothelial cell invasion and morphogenesis with synthetic matrixin inhibitors. Targeting angiogenesis with MMP inhibitors. Adv. Exp. Med. Biol., 476:181-194.
    • (2000) Adv. Exp. Med. Biol , vol.476 , pp. 181-194
    • Jia, M.C.1    Schwartz, M.A.2    Sang, Q.A.3
  • 101
    • 0019594131 scopus 로고
    • Circular dichroism spectra of trypsin and chymotrypsin complexes with Bowman-Birk or chickpea trypsin inhibitor
    • Jibson, M. D., Birk, Y., and Bewley, T. A. 1981. Circular dichroism spectra of trypsin and chymotrypsin complexes with Bowman-Birk or chickpea trypsin inhibitor. Int. J. Peptide Prot. Res., 18:26-32.
    • (1981) Int. J. Peptide Prot. Res , vol.18 , pp. 26-32
    • Jibson, M.D.1    Birk, Y.2    Bewley, T.A.3
  • 102
    • 0002067383 scopus 로고
    • Isolation and sequence of cDNA encoding the soybean protease inhibitors PI IV and C-II
    • Joudrier, P. E., Foard, D. E., Floener, L. A., and Larkins, B. A. 1987. Isolation and sequence of cDNA encoding the soybean protease inhibitors PI IV and C-II. Plant Mol. Biol., 10:35-42.
    • (1987) Plant Mol. Biol , vol.10 , pp. 35-42
    • Joudrier, P.E.1    Foard, D.E.2    Floener, L.A.3    Larkins, B.A.4
  • 104
    • 0014955686 scopus 로고
    • The molecular weight of the Bowman-Birk soybean protease inhibitor
    • Kakade, M. L., Simons, N. R., and Liener, I. E. 1970. The molecular weight of the Bowman-Birk soybean protease inhibitor. Biochem. Biophys. Acta, 200:168-169.
    • (1970) Biochem. Biophys. Acta , vol.200 , pp. 168-169
    • Kakade, M.L.1    Simons, N.R.2    Liener, I.E.3
  • 105
    • 0029617837 scopus 로고
    • Purification, characterization, sequence determination, and mass spectrometric analysis of a trypsin inhibitor from seeds of the Brazilian tree Dipteryx alata (Leguminosae)
    • Kalume, D. E., Sousa, M. V., and Morhy, L. 1995. Purification, characterization, sequence determination, and mass spectrometric analysis of a trypsin inhibitor from seeds of the Brazilian tree Dipteryx alata (Leguminosae). J. Protein Chem., 14:685-693.
    • (1995) J. Protein Chem , vol.14 , pp. 685-693
    • Kalume, D.E.1    Sousa, M.V.2    Morhy, L.3
  • 106
    • 77956992367 scopus 로고
    • Trypsin and chymotrypsin inhibitors from soybeans
    • Kassell, B. 1970. Trypsin and chymotrypsin inhibitors from soybeans. Methods Enzymol., 19:853-862.
    • (1970) Methods Enzymol , vol.19 , pp. 853-862
    • Kassell, B.1
  • 109
    • 0036468843 scopus 로고    scopus 로고
    • Effects of the Bowman-Birk inhibitor on growth, invasion, and clonogenic survival of human prostate epithelial cells and prostate cancer cells
    • Kennedy A. R., and Wan X. S. 2002. Effects of the Bowman-Birk inhibitor on growth, invasion, and clonogenic survival of human prostate epithelial cells and prostate cancer cells. Prostate, 50:125-133.
    • (2002) Prostate , vol.50 , pp. 125-133
    • Kennedy, A.R.1    Wan, X.S.2
  • 110
    • 0003025605 scopus 로고
    • Anticarcinogenic activity of protease inhibitors: An Overview
    • Troll, W. and Kennedy, A.R, Eds, Plenum Press
    • Kennedy, A. R. 1993. Anticarcinogenic activity of protease inhibitors: An Overview. In: Protease Inhibitors as Chemopreventive Agents. pp. 9-64. Troll, W. and Kennedy, A.R. (Eds.), Plenum Press.
    • (1993) Protease Inhibitors as Chemopreventive Agents , pp. 9-64
    • Kennedy, A.R.1
  • 111
    • 39349089974 scopus 로고    scopus 로고
    • A reply to Liener
    • Kennedy, A. R. 1996. A reply to Liener. J. Nutr. 126:584-584. .
    • (1996) J. Nutr , vol.126 , pp. 584-584
    • Kennedy, A.R.1
  • 112
    • 0031741056 scopus 로고    scopus 로고
    • The Bowman-Birk inhibitor from soybeans as an anticarcinogenic agent
    • Kennedy, A. R. 1998. The Bowman-Birk inhibitor from soybeans as an anticarcinogenic agent. Am. J. Clin. Nutr., 68(Suppl):1406S-1412S.
    • (1998) Am. J. Clin. Nutr , vol.68 , Issue.SUPPL.
    • Kennedy, A.R.1
  • 113
    • 0004646331 scopus 로고
    • Bowman-Birk inhibitor product for use as an anticarcinogenesis agent,
    • US Patent. 5,338,547
    • Kennedy, A. R., and Szuhaj, B. 1984. Bowman-Birk inhibitor product for use as an anticarcinogenesis agent, US Patent. 5,338,547.
    • (1984)
    • Kennedy, A.R.1    Szuhaj, B.2
  • 114
    • 0346216093 scopus 로고    scopus 로고
    • Effects of spermine-conjugated Bowman-Birk inhibitor (spermine-BBI) on. carcinogenesis and cholesterol biosynthesis in mice
    • Kennedy, A. R., Kritchevsky, D., and Shen, W. C. 2003. Effects of spermine-conjugated Bowman-Birk inhibitor (spermine-BBI) on. carcinogenesis and cholesterol biosynthesis in mice. Pharm. Res., 20:1908-1910.
    • (2003) Pharm. Res , vol.20 , pp. 1908-1910
    • Kennedy, A.R.1    Kritchevsky, D.2    Shen, W.C.3
  • 115
    • 0021356170 scopus 로고
    • Protease inhibitors reduce the frequency of spontaneous chromosome abnormalities in cells from patients with, bloom syndrome
    • Kennedy, A. R., Radner, B. S., and Nagasawa, H. 1984. Protease inhibitors reduce the frequency of spontaneous chromosome abnormalities in cells from patients with, bloom syndrome. Proc. Natl. Acad. Sci. USA., 81:1827-1830.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 1827-1830
    • Kennedy, A.R.1    Radner, B.S.2    Nagasawa, H.3
  • 116
    • 2442566635 scopus 로고    scopus 로고
    • Soy saponins and the anticancer effects of soybeans and soy-based foods
    • Kerwin, S. M. 2004. Soy saponins and the anticancer effects of soybeans and soy-based foods. Curr Med Chem Anticancer Agents, 4:263-272.
    • (2004) Curr Med Chem Anticancer Agents , vol.4 , pp. 263-272
    • Kerwin, S.M.1
  • 117
    • 2542482634 scopus 로고    scopus 로고
    • Antiproliferative crude soy saponin extract modulates the expression of IkappaB alpha, protein kinase C, and cyclooxygenase-2 in human colon cancer cells
    • Kim, H. Y., Yu, R., Kim, J. S., Kim, Y. K., and Sung, M. K. 2004. Antiproliferative crude soy saponin extract modulates the expression of IkappaB alpha, protein kinase C, and cyclooxygenase-2 in human colon cancer cells. Cancer Lett., 210:1-6.
    • (2004) Cancer Lett , vol.210 , pp. 1-6
    • Kim, H.Y.1    Yu, R.2    Kim, J.S.3    Kim, Y.K.4    Sung, M.K.5
  • 118
    • 0028329989 scopus 로고
    • On a Bowman-Birk family proteinase inhibitor from Erythrina variegata, seeds
    • Kimura, M., Kouzuma, Y., Abe, K., and Yamasaki, N. 1994. On a Bowman-Birk family proteinase inhibitor from Erythrina variegata, seeds. J. Biochem., 115:369-372.
    • (1994) J. Biochem , vol.115 , pp. 369-372
    • Kimura, M.1    Kouzuma, Y.2    Abe, K.3    Yamasaki, N.4
  • 120
    • 0034607547 scopus 로고    scopus 로고
    • Crystal structure of cancer chemopreventive Bowman-Birk inhibitor in ternary complex with bovine trypsin at 2.3 Å resolution. Structural basis of Janus-faced serine protease inhibitor specificity
    • Koepke, J., Ermler, U., Warkentin, E., Wenzl, G., and Flecker, P. (2000). Crystal structure of cancer chemopreventive Bowman-Birk inhibitor in ternary complex with bovine trypsin at 2.3 Å resolution. Structural basis of Janus-faced serine protease inhibitor specificity. J. Mol. Biol., 298:477-491.
    • (2000) J. Mol. Biol , vol.298 , pp. 477-491
    • Koepke, J.1    Ermler, U.2    Warkentin, E.3    Wenzl, G.4    Flecker, P.5
  • 121
    • 0014766151 scopus 로고
    • In vitro synthesis of pancreatic enzymes:effect of soybean trypsin inhibitor
    • Konijn, A. M., Birk, Y., and Guggenheim, K. 1970. In vitro synthesis of pancreatic enzymes:effect of soybean trypsin inhibitor. Am. J. Physiol., 218:1113-1117.
    • (1970) Am. J. Physiol , vol.218 , pp. 1113-1117
    • Konijn, A.M.1    Birk, Y.2    Guggenheim, K.3
  • 122
    • 0027980308 scopus 로고
    • Phosphotyrosine inhibition and control of vascular endothelial cell proliferation by genistein
    • Koroma, B. M., and de Juan Jr., E. 1994. Phosphotyrosine inhibition and control of vascular endothelial cell proliferation by genistein. Biochem. Pharmacol, 48:809-818.
    • (1994) Biochem. Pharmacol , vol.48 , pp. 809-818
    • Koroma, B.M.1    de Juan Jr., E.2
  • 123
    • 0014959622 scopus 로고
    • Lima bean trypsin inhibitor. Limited proteolysis by trypsin and chymotrypsin
    • Krahn, J., and Stevens, F. C. 1970. Lima bean trypsin inhibitor. Limited proteolysis by trypsin and chymotrypsin. Biochem., 9:2646-2650.
    • (1970) Biochem , vol.9 , pp. 2646-2650
    • Krahn, J.1    Stevens, F.C.2
  • 128
    • 0000066265 scopus 로고
    • Inhibition of cathepsin G and human granulocyte by multiple forms of Bowman-Birk soybean inhibitor
    • Mosc
    • Larionova, N. I, Gladysheva, I. P., Tikhonova, T. V., and Kazanskaia, N. F. 1993. Inhibition of cathepsin G and human granulocyte by multiple forms of Bowman-Birk soybean inhibitor. Biochem., (Mosc), 58:1046-1052.
    • (1993) Biochem , vol.58 , pp. 1046-1052
    • Larionova, N.I.1    Gladysheva, I.P.2    Tikhonova, T.V.3    Kazanskaia, N.F.4
  • 129
    • 0032151598 scopus 로고    scopus 로고
    • Interaction of human, leukocyte elastase with, plasma fibronectin and its inhibition by soybean. Bowman-Birk protease inhibitor
    • Mosc
    • Larionova, N. I., Balabushevitch, N. G., and Zhatikov, P. A. 1998. Interaction of human, leukocyte elastase with, plasma fibronectin and its inhibition by soybean. Bowman-Birk protease inhibitor. Biochem. (Mosc) 63:1078-1082.
    • (1998) Biochem , vol.63 , pp. 1078-1082
    • Larionova, N.I.1    Balabushevitch, N.G.2    Zhatikov, P.A.3
  • 130
    • 0031041505 scopus 로고    scopus 로고
    • Human leukocyte elastase inhibition by Bowman-Birk soybean inhibitor. Discrimination of the inhibition mechanism
    • Larionova, N. I., Gladysheva, I. P., and Gladyshev, D. P. 1997. Human leukocyte elastase inhibition by Bowman-Birk soybean inhibitor. Discrimination of the inhibition mechanism. FEBS Lett., 404:245-248.
    • (1997) FEBS Lett , vol.404 , pp. 245-248
    • Larionova, N.I.1    Gladysheva, I.P.2    Gladyshev, D.P.3
  • 131
    • 0031041505 scopus 로고    scopus 로고
    • Human leukocyte elastase inhibition by Bowman-Birk soybean inhibitor. Discrimination of the inhibition mechanisms
    • Larionova, N. I., Gladysheva, I. P., and Gladyshev, D. P. 1997. Human leukocyte elastase inhibition by Bowman-Birk soybean inhibitor. Discrimination of the inhibition mechanisms. FEBS Lett., 404(2-3):245-248.
    • (1997) FEBS Lett , vol.404 , Issue.2-3 , pp. 245-248
    • Larionova, N.I.1    Gladysheva, I.P.2    Gladyshev, D.P.3
  • 132
  • 133
    • 0030256015 scopus 로고    scopus 로고
    • Synthesis and biodistribution of Bowman-Birk soybean protease inhibitor conjugate with amphiphilic polyester
    • Larionova, N. I., Gladysheva, I. P., Polekhina, O. V., Kurochkina, L. P., and Gorbatova, E. N. 1996. Synthesis and biodistribution of Bowman-Birk soybean protease inhibitor conjugate with amphiphilic polyester. Appl. Biochem. Biotechnol., 61(1-2):139-48.
    • (1996) Appl. Biochem. Biotechnol , vol.61 , Issue.1-2 , pp. 139-148
    • Larionova, N.I.1    Gladysheva, I.P.2    Polekhina, O.V.3    Kurochkina, L.P.4    Gorbatova, E.N.5
  • 134
    • 0028129673 scopus 로고
    • The Bowman-Birk inhibitor-polyester conjugate: Synthesis, inhibition of serine proteinases, and suppression of radiation transformation in vitro
    • Larionova, N. I., Topchieva, I. N., Gladysheva, I. P., and Kennedy, A. R. 1994. The Bowman-Birk inhibitor-polyester conjugate: synthesis, inhibition of serine proteinases, and suppression of radiation transformation in vitro. Cancer J., 7:158-163.
    • (1994) Cancer J , vol.7 , pp. 158-163
    • Larionova, N.I.1    Topchieva, I.N.2    Gladysheva, I.P.3    Kennedy, A.R.4
  • 135
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski, M. D., and Kato, I. 1980. Protein inhibitors of proteinases. Ann. Rev. Biochem. 49:593-626.
    • (1980) Ann. Rev. Biochem , vol.49 , pp. 593-626
    • Laskowski, M.D.1    Kato, I.2
  • 136
    • 0026646956 scopus 로고
    • Transcriptional downregulation of gap-junction proteins block junctional communication in human mammary tumor cell lines
    • Lee, S., Tomasetto, C., Paul, D., Keyomarsi, K., and Sager, R. 1992. Transcriptional downregulation of gap-junction proteins block junctional communication in human mammary tumor cell lines. J. Cell Biol., 118:1213-1221.
    • (1992) J. Cell Biol , vol.118 , pp. 1213-1221
    • Lee, S.1    Tomasetto, C.2    Paul, D.3    Keyomarsi, K.4    Sager, R.5
  • 137
    • 0033083536 scopus 로고    scopus 로고
    • The refolding, purification, and activity analysis of a rice Bowman-Birk inhibitor expressed in Escherichia coli
    • Li, N., Qu, L. J., Liu, Y., Li, Q., Gu, H., and Chen, Z. 1999. The refolding, purification, and activity analysis of a rice Bowman-Birk inhibitor expressed in Escherichia coli. Prot. Expr. Purif., 15:99-104.
    • (1999) Prot. Expr. Purif , vol.15 , pp. 99-104
    • Li, N.1    Qu, L.J.2    Liu, Y.3    Li, Q.4    Gu, H.5    Chen, Z.6
  • 138
    • 0022989201 scopus 로고
    • The effect of the long-term feeding of raw soyflour on the pancreas of the mouse and hamster
    • Liener, I. E., and Hasdai, A. 1985. The effect of the long-term feeding of raw soyflour on the pancreas of the mouse and hamster. In Adv. Exp. Med. Biol., 199:189-197.
    • (1985) In Adv. Exp. Med. Biol , vol.199 , pp. 189-197
    • Liener, I.E.1    Hasdai, A.2
  • 140
    • 0344444539 scopus 로고
    • The Con A conjugate of Bowman-Birk soybean trypsin inhibitor as an anticancerogen
    • Bog-Hansen, T. C, and van Driessche, E. Eds, Walter de Gruyter, Berlin, New York
    • Lin, J. Y., and Hu, M. N. 1986. The Con A conjugate of Bowman-Birk soybean trypsin inhibitor as an anticancerogen. In: Lectins: Biology, Biochemistry, Clinical Biochemistry., pp. 409-416 Bog-Hansen, T. C., and van Driessche, E. Eds., Walter de Gruyter, Berlin, New York.
    • (1986) Lectins: Biology, Biochemistry, Clinical Biochemistry , pp. 409-416
    • Lin, J.Y.1    Hu, M.N.2
  • 141
    • 0034489699 scopus 로고    scopus 로고
    • Protease inhibitors in oral carcinogenesis and chemoprevention
    • Lippman, S. M., and Matrisian, L. M. 2000. Protease inhibitors in oral carcinogenesis and chemoprevention. Clin. Cancer Res., 6:4599-4603.
    • (2000) Clin. Cancer Res , vol.6 , pp. 4599-4603
    • Lippman, S.M.1    Matrisian, L.M.2
  • 142
    • 0018382741 scopus 로고
    • Junctional intercellular communication and the control of growth
    • Loewenstein, W. 1979. Junctional intercellular communication and the control of growth. Biochim. Biophys. Acta., 561:1-65.
    • (1979) Biochim. Biophys. Acta , vol.561 , pp. 1-65
    • Loewenstein, W.1
  • 143
    • 3342975587 scopus 로고    scopus 로고
    • Inhibition of metalloproteinase-1 activity by the soybean Bowman-Birk inhibitor
    • Losso, J. N., Munene, C. N., and Bansode, R. R. 2004. Inhibition of metalloproteinase-1 activity by the soybean Bowman-Birk inhibitor. Biotechnol. Lett., 26:901-905.
    • (2004) Biotechnol. Lett , vol.26 , pp. 901-905
    • Losso, J.N.1    Munene, C.N.2    Bansode, R.R.3
  • 146
    • 0033039659 scopus 로고    scopus 로고
    • Purification and characterization of protease inhibitor from rice bean (Vigna umbellata T.) seeds
    • Maggo, S., Malhorta, S. P., Dhawan, K., and Singh, R. 1999. Purification and characterization of protease inhibitor from rice bean (Vigna umbellata T.) seeds. J. Plant Biochem. Biotechnol., 8:61-64.
    • (1999) J. Plant Biochem. Biotechnol , vol.8 , pp. 61-64
    • Maggo, S.1    Malhorta, S.P.2    Dhawan, K.3    Singh, R.4
  • 147
    • 0026460944 scopus 로고
    • Humoral and cellular immune functions are not compromised by the anticarcinogenic Bowman-Birk inhibitor
    • Maki, P. A., and Kennedy, A. R. 1992. Humoral and cellular immune functions are not compromised by the anticarcinogenic Bowman-Birk inhibitor. Nutr. Cancer, 18:165-173.
    • (1992) Nutr. Cancer , vol.18 , pp. 165-173
    • Maki, P.A.1    Kennedy, A.R.2
  • 149
    • 0036994808 scopus 로고    scopus 로고
    • Study of antiproteinase activity of acylated derivatives of Bowman-Birk soybean proteinase inhibitor
    • Malykh, E. V., and Larionova, N. I. 2002. Study of antiproteinase activity of acylated derivatives of Bowman-Birk soybean proteinase inhibitor. Biochem., (Mosc), 67:1383-1387.
    • (2002) Biochem., (Mosc) , vol.67 , pp. 1383-1387
    • Malykh, E.V.1    Larionova, N.I.2
  • 150
    • 0242295902 scopus 로고    scopus 로고
    • Conjugates of Bowman-Birk proteinase inhibitor with unsaturated fatty acids: Preparation, characterization and the uptake by Caco-2 cells
    • San Diego, USA
    • Malykh, E. V., Larionova, N. I., Villemson, A. L., and Shen, W.-C. 2001a. Conjugates of Bowman-Birk proteinase inhibitor with unsaturated fatty acids: preparation, characterization and the uptake by Caco-2 cells. Proceed. Int. Symp. Controll. Rel. Bioact. Mater., San Diego, USA, 28, pp. 123-124.
    • (2001) Proceed. Int. Symp. Controll. Rel. Bioact. Mater , vol.28 , pp. 123-124
    • Malykh, E.V.1    Larionova, N.I.2    Villemson, A.L.3    Shen, W.-C.4
  • 151
    • 0035297568 scopus 로고    scopus 로고
    • Acylation of Bowman-Birk soybean, proteinase inhibitor by unsaturated fatty acid derivatives
    • Malykh, E. V., Tiourina, O. P., and Larionova, N. I. 2001b. Acylation of Bowman-Birk soybean, proteinase inhibitor by unsaturated fatty acid derivatives. Biochem. (Mosc), 66:444-448.
    • (2001) Biochem. (Mosc) , vol.66 , pp. 444-448
    • Malykh, E.V.1    Tiourina, O.P.2    Larionova, N.I.3
  • 153
    • 0034945422 scopus 로고    scopus 로고
    • Synthetic peptide mimics of the Bowman-Birk inhibitor protein
    • McBride, J. D., and Leatherbarrow, R. J. 2001. Synthetic peptide mimics of the Bowman-Birk inhibitor protein. Curr. Med. Chem., 8:909-917.
    • (2001) Curr. Med. Chem , vol.8 , pp. 909-917
    • McBride, J.D.1    Leatherbarrow, R.J.2
  • 154
    • 0000591892 scopus 로고
    • Degradation of trypsin inhibitors during soybean germination
    • McGain, A. K., Chen, J. C. Wilson, K. A., and Tan-Wilson, A. L. 1989. Degradation of trypsin inhibitors during soybean germination. Phytochem., 28:1013-1017.
    • (1989) Phytochem , vol.28 , pp. 1013-1017
    • McGain, A.K.1    Chen, J.C.2    Wilson, K.A.3    Tan-Wilson, A.L.4
  • 155
    • 0028533929 scopus 로고
    • Wounding induces a series of closely related trypsin/chymotrypsin inhibitory peptides in leaves of tobacco
    • McMunnus, M. T., Laing, W. A., and Christeller, J. T. 1994. Wounding induces a series of closely related trypsin/chymotrypsin inhibitory peptides in leaves of tobacco. Phytochem., 37:921-926.
    • (1994) Phytochem , vol.37 , pp. 921-926
    • McMunnus, M.T.1    Laing, W.A.2    Christeller, J.T.3
  • 156
    • 0035236512 scopus 로고    scopus 로고
    • Development of difluoromethyl-ornithine and Bowman-Birk inhibitor as chemopreventive agents by assessment of relevant biomarker modulation: Some lessons learned
    • Meyskens, F. L. Jr. 2001. Development of difluoromethyl-ornithine and Bowman-Birk inhibitor as chemopreventive agents by assessment of relevant biomarker modulation: some lessons learned. IARC Sci. Publ., 154:49-55.
    • (2001) IARC Sci. Publ , vol.154 , pp. 49-55
    • Meyskens Jr., F.L.1
  • 157
    • 0014690003 scopus 로고
    • The irreversible self-association of a soybean proteinase inhibitor
    • Millar, D. B. S., Willick, G. E., Steiner, R. F., and Frattali, V. 1969. The irreversible self-association of a soybean proteinase inhibitor. J. Biol. Chem., 244:281-840.
    • (1969) J. Biol. Chem , vol.244 , pp. 281-840
    • Millar, D.B.S.1    Willick, G.E.2    Steiner, R.F.3    Frattali, V.4
  • 158
    • 27544510642 scopus 로고    scopus 로고
    • Attenuation of skeletal muscle atrophy via protease inhibition
    • Morris, C. A., Morris, L. D., Kennedy A. R., and Sweeney H. L. 2005. Attenuation of skeletal muscle atrophy via protease inhibition. J. Appl. Physiol., 99:1719-1727.
    • (2005) J. Appl. Physiol , vol.99 , pp. 1719-1727
    • Morris, C.A.1    Morris, L.D.2    Kennedy, A.R.3    Sweeney, H.L.4
  • 159
    • 0028016014 scopus 로고
    • A proteolytic activity in a human breast cancer cell line which is inhibited by the anticarcinogenic Bowman-Birk protease inhibitor
    • Moy, L. Y., and Billings, P. C. 1994. A proteolytic activity in a human breast cancer cell line which is inhibited by the anticarcinogenic Bowman-Birk protease inhibitor. Cancer Lett., 85:205-210.
    • (1994) Cancer Lett , vol.85 , pp. 205-210
    • Moy, L.Y.1    Billings, P.C.2
  • 160
    • 0032434350 scopus 로고    scopus 로고
    • Diet that prevents cancer: Recommendations from the American Institute for Cancer Research
    • Munoz de Chavez, M., and Chavez, A. 1998. Diet that prevents cancer: recommendations from the American Institute for Cancer Research, Int. J. Cancer., 11:S85-S99.
    • (1998) Int. J. Cancer , vol.11
    • Munoz de Chavez, M.1    Chavez, A.2
  • 162
    • 39349112991 scopus 로고    scopus 로고
    • National Institute of Dental and Craniofacial Research (NIDCR) Homepage. 2006. http://www.nidcr.nih.gov/HealthInformation/DiseasesAndConditions/ SpectrumSeries/OralCancerEnemy.htm. Accessed on online 14 August 2006.
    • National Institute of Dental and Craniofacial Research (NIDCR) Homepage. 2006. http://www.nidcr.nih.gov/HealthInformation/DiseasesAndConditions/ SpectrumSeries/OralCancerEnemy.htm. Accessed on online 14 August 2006.
  • 164
    • 0020806430 scopus 로고
    • Amino acid sequences of trypsin-chymotrypsin inhibitors (A-I, A-II, B-I, and B-II) from peanut (Arachis hypogaea): A discussion on the molecular evolution of legume Bowman-Birk type inhibitors
    • Norioka, S., and Ikenaka, T. 1983. Amino acid sequences of trypsin-chymotrypsin inhibitors (A-I, A-II, B-I, and B-II) from peanut (Arachis hypogaea): a discussion on the molecular evolution of legume Bowman-Birk type inhibitors. J Biochem (Tokyo)., 94(2):589-99.
    • (1983) J Biochem (Tokyo) , vol.94 , Issue.2 , pp. 589-599
    • Norioka, S.1    Ikenaka, T.2
  • 165
    • 0020118199 scopus 로고
    • Purification and characterization of protease inhibitors from peanuts (Arachis hypogaea)
    • Norioka, S., Omichi, K., and Ikenaka, T. J. 1982. Purification and characterization of protease inhibitors from peanuts (Arachis hypogaea). J. Biochem., 991:1427-1434.
    • (1982) J. Biochem , vol.991 , pp. 1427-1434
    • Norioka, S.1    Omichi, K.2    Ikenaka, T.J.3
  • 166
    • 39349103475 scopus 로고    scopus 로고
    • Who would have thought...? Prepared Foods
    • 07 December
    • O'Donnell, C. D. 2001. Who would have thought...? Prepared Foods, 07 December.
    • (2001)
    • O'Donnell, C.D.1
  • 167
    • 0015840847 scopus 로고
    • Study on soybean trypsin inhibitors. VIII. Disulphide bridges in soybean Bowman-Birk proteinase inhibitor
    • Odani, S., and Ikenaka, T. 1973. Study on soybean trypsin inhibitors. VIII. Disulphide bridges in soybean Bowman-Birk proteinase inhibitor. J. Biochem., 74:697-715.
    • (1973) J. Biochem , vol.74 , pp. 697-715
    • Odani, S.1    Ikenaka, T.2
  • 168
    • 0017697389 scopus 로고
    • Studies on soybean trypsin inhibitors X. Isolation and partial characterization of four soybean double-headed proteinase inhibitors
    • Odani, S., and Ikenaka, T. 1977. Studies on soybean trypsin inhibitors X. Isolation and partial characterization of four soybean double-headed proteinase inhibitors. J. Biochem., 82:1513-1522.
    • (1977) J. Biochem , vol.82 , pp. 1513-1522
    • Odani, S.1    Ikenaka, T.2
  • 169
    • 0017860655 scopus 로고    scopus 로고
    • Odani, S., and Ikenaka, T. 1978. Studies on soybean trypsin, inhibitors. IV. Change of the inhibitory activity of Bowman-Birk inhibitor upon replacements of the alpha-chymotrypsin reactive site serine residue by other amino acids. J. Biochem., (Tokyo) 84:1-9.
    • Odani, S., and Ikenaka, T. 1978. Studies on soybean trypsin, inhibitors. IV. Change of the inhibitory activity of Bowman-Birk inhibitor upon replacements of the alpha-chymotrypsin reactive site serine residue by other amino acids. J. Biochem., (Tokyo) 84:1-9.
  • 170
    • 0022801966 scopus 로고
    • Wheat germ trypsin, inhibitors. Isolation and structural characterization of a single-headed and double-headed inhibitors of the Bowman-Birk type
    • Odani, S., Koide, T., and Ono, T. 1986. Wheat germ trypsin, inhibitors. Isolation and structural characterization of a single-headed and double-headed inhibitors of the Bowman-Birk type. J. Biochem., 100:975-983.
    • (1986) J. Biochem , vol.100 , pp. 975-983
    • Odani, S.1    Koide, T.2    Ono, T.3
  • 171
    • 0343433408 scopus 로고    scopus 로고
    • Cysteine proteases and their inhibitors
    • Otto, H.-H. and Schirmeister, T. 1997. Cysteine proteases and their inhibitors. Chem. Rev., 97:133-17.
    • (1997) Chem. Rev , vol.97 , pp. 133-217
    • Otto, H.-H.1    Schirmeister, T.2
  • 172
    • 0000041312 scopus 로고
    • Initiation of the degradation of the soybean Kunitz and Bowman-Birk trypsin inhibitors by a cysteine protease
    • Papastoitsis, G., and Wilson, K. A. 1991. Initiation of the degradation of the soybean Kunitz and Bowman-Birk trypsin inhibitors by a cysteine protease. Plant Physiol., 96:1086-1092.
    • (1991) Plant Physiol , vol.96 , pp. 1086-1092
    • Papastoitsis, G.1    Wilson, K.A.2
  • 173
    • 0025735806 scopus 로고
    • Polylysine conjugates of Bowman-Birk protease inhibitor as targeted anticarcinogenic agents
    • Persiani, S., Yeung, A., Shen, W. C., and Kennedy, A. R. 1991. Polylysine conjugates of Bowman-Birk protease inhibitor as targeted anticarcinogenic agents. Carcinogenesis, 12:1149-1152.
    • (1991) Carcinogenesis , vol.12 , pp. 1149-1152
    • Persiani, S.1    Yeung, A.2    Shen, W.C.3    Kennedy, A.R.4
  • 174
    • 0032005175 scopus 로고    scopus 로고
    • Mutational analysis of disulfide bonds in the trypsin-reactive subdomain of a Bowman-Birk type inhibitor of trypsin, and chymotrypsin. Cooperative versus autonomous refolding of subdomains
    • Philipp, S., Kim, Y-M., Durr , I. Wenzl, G., Vogt, M., and Flecker, P. 1998. Mutational analysis of disulfide bonds in the trypsin-reactive subdomain of a Bowman-Birk type inhibitor of trypsin, and chymotrypsin. Cooperative versus autonomous refolding of subdomains. Eur. J. Biochem., 251:854-862.
    • (1998) Eur. J. Biochem , vol.251 , pp. 854-862
    • Philipp, S.1    Kim, Y.-M.2    Durr, I.3    Wenzl, G.4    Vogt, M.5    Flecker, P.6
  • 176
    • 0028147717 scopus 로고
    • Crystallization and preliminary X-ray diffraction studies on a trypsin/chymotrypsin double-headed inhibitor from horse gram
    • Prakash, B, Murray, M. R., Sreerama, Y. N., Sarma, P. R., and Rao, D. R. 1994. Crystallization and preliminary X-ray diffraction studies on a trypsin/chymotrypsin double-headed inhibitor from horse gram. J. Mol. Biol., 235(1):364-366.
    • (1994) J. Mol. Biol , vol.235 , Issue.1 , pp. 364-366
    • Prakash, B.1    Murray, M.R.2    Sreerama, Y.N.3    Sarma, P.R.4    Rao, D.R.5
  • 178
    • 0014303284 scopus 로고
    • General, properties of a protease inhibitor from the seeds of kidney bean
    • Pusztai, A. 1968. General, properties of a protease inhibitor from the seeds of kidney bean. Eur J Biochem., 5:252-259.
    • (1968) Eur J Biochem , vol.5 , pp. 252-259
    • Pusztai, A.1
  • 179
    • 0030965716 scopus 로고    scopus 로고
    • Trypsin inhibitor polymorphism: Multigene family expression and postradiational modification
    • Quillien, L., Ferrasson, E., Molle, D., and Gueguen, J. 1997.Trypsin inhibitor polymorphism: multigene family expression and postradiational modification. J. Prot. Chem., 16:195-203.
    • (1997) J. Prot. Chem , vol.16 , pp. 195-203
    • Quillien, L.1    Ferrasson, E.2    Molle, D.3    Gueguen, J.4
  • 180
    • 0015998033 scopus 로고
    • Biological and physiological factors in soybeans
    • Rackis, J. J. 1974. Biological and physiological factors in soybeans. J. Amer. Oil Chem. Soc., 51:161A-174A.
    • (1974) J. Amer. Oil Chem. Soc , vol.51
    • Rackis, J.J.1
  • 181
    • 0037373527 scopus 로고    scopus 로고
    • Toxicity to the pea aphid Acyrthosiphon pisum of anti-chymotrypsin isoforms and fragments of Bowman-Birk protease inhibitors from pea seeds
    • Rahbé, Y., Ferrasson, E., Rabesona, H., and Quillien, L. 2003. Toxicity to the pea aphid Acyrthosiphon pisum of anti-chymotrypsin isoforms and fragments of Bowman-Birk protease inhibitors from pea seeds, Insect Biochem. Mol. Biol., 33:299-306.
    • (2003) Insect Biochem. Mol. Biol , vol.33 , pp. 299-306
    • Rahbé, Y.1    Ferrasson, E.2    Rabesona, H.3    Quillien, L.4
  • 182
    • 0035941486 scopus 로고    scopus 로고
    • Characterization of a rice (Oryza sativa L.) Bowman-Birk proteinase inhibitor: Tightly light, regulated induction in response to cut, jasmonic acid, ethylene and protein phosphatase 2A inhibitors
    • Rakwal, R., Kumar Agrawal, G., and Jwa, N. S. (2001).Characterization of a rice (Oryza sativa L.) Bowman-Birk proteinase inhibitor: tightly light, regulated induction in response to cut, jasmonic acid, ethylene and protein phosphatase 2A inhibitors. Gene, 263:189-198.
    • (2001) Gene , vol.263 , pp. 189-198
    • Rakwal, R.1    Kumar Agrawal, G.2    Jwa, N.S.3
  • 183
    • 0033231127 scopus 로고    scopus 로고
    • Crystallization and preliminary x-ray diffraction studies of a Bowman-Birk inhibitor from Vigna unguiculata seeds
    • Rao, K. N., Hegde, S.S., Lewis, R. J., and Suresh, C. G. 1999. Crystallization and preliminary x-ray diffraction studies of a Bowman-Birk inhibitor from Vigna unguiculata seeds. Acta Crystallogr D. Biol. Crystallogr., 155:1920-1922.
    • (1999) Acta Crystallogr D. Biol. Crystallogr , vol.155 , pp. 1920-1922
    • Rao, K.N.1    Hegde, S.S.2    Lewis, R.J.3    Suresh, C.G.4
  • 184
    • 0029968525 scopus 로고    scopus 로고
    • Proteinase inhibitors induce selective stimulation of human trypsin, and chymotrypsin secretion
    • Reseland, J. E., Holm, H., Jacobsen, M. B., Jenssen, T. G., Hanssen, L. E. 1996. Proteinase inhibitors induce selective stimulation of human trypsin, and chymotrypsin secretion, J. Nutr. 126:634-642.
    • (1996) J. Nutr , vol.126 , pp. 634-642
    • Reseland, J.E.1    Holm, H.2    Jacobsen, M.B.3    Jenssen, T.G.4    Hanssen, L.E.5
  • 185
    • 0022379193 scopus 로고
    • Carcinogen-induced lesions in the rat pancreas: Effects of varying levels of essential fatty acid
    • Roebuck, B. D., Longnecker, D. S., Baumgartner, K. J., and Thron, C. D. 1985. Carcinogen-induced lesions in the rat pancreas: effects of varying levels of essential fatty acid. Cancer Res., 45:5252-5256.
    • (1985) Cancer Res , vol.45 , pp. 5252-5256
    • Roebuck, B.D.1    Longnecker, D.S.2    Baumgartner, K.J.3    Thron, C.D.4
  • 186
    • 0031796289 scopus 로고    scopus 로고
    • Biotechnology and the soybean
    • Rogers, S. G. 1998. Biotechnology and the soybean. Am. J. Clin. Nutr. 68(6 Suppl):1330S-1332S.
    • (1998) Am. J. Clin. Nutr , vol.68 , Issue.6 SUPPL.
    • Rogers, S.G.1
  • 187
    • 0000180578 scopus 로고
    • Protease inhibitors in plants: Genes for improving defenses against insects and pathogens
    • Ryan, C. A. 1990. Protease inhibitors in plants: Genes for improving defenses against insects and pathogens. Ann Rev Phytopathol., 28:425-449.
    • (1990) Ann Rev Phytopathol , vol.28 , pp. 425-449
    • Ryan, C.A.1
  • 188
    • 0035031111 scopus 로고    scopus 로고
    • Excessive Matrix Metalloproteinase activity in diabetes inhibition by tetracycline analogues with zinc reactivity
    • Ryan, M. E., Usman, A., Ramamurthy, N. S., Golub, L. M., Greenwald, R. A. 2001. Excessive Matrix Metalloproteinase activity in diabetes inhibition by tetracycline analogues with zinc reactivity. Curr. Med. Chem. 8:305-316.
    • (2001) Curr. Med. Chem , vol.8 , pp. 305-316
    • Ryan, M.E.1    Usman, A.2    Ramamurthy, N.S.3    Golub, L.M.4    Greenwald, R.A.5
  • 189
    • 77957007391 scopus 로고
    • The porcine pepsins and pepsinogens
    • Ryle, A. P. 1970.The porcine pepsins and pepsinogens. Methods Enzymol., 19:316.
    • (1970) Methods Enzymol , vol.19 , pp. 316
    • Ryle, A.P.1
  • 190
    • 0024845393 scopus 로고
    • Purification and characterization of trypsins from, the digestive tract of Locusta migratoria
    • Sakai, E., Applebaum, S. W., and Birk, Y. 1989. Purification and characterization of trypsins from, the digestive tract of Locusta migratoria. Int. J. Pept. Prot. Res, 34:498-505.
    • (1989) Int. J. Pept. Prot. Res , vol.34 , pp. 498-505
    • Sakai, E.1    Applebaum, S.W.2    Birk, Y.3
  • 191
    • 0035185809 scopus 로고    scopus 로고
    • The role of nutrition in preventing and treating breast and prostate cancer
    • Sawey, M. J. 2001. The role of nutrition in preventing and treating breast and prostate cancer. J. Nutr., 131:167S-169S.
    • (2001) J. Nutr , vol.131
    • Sawey, M.J.1
  • 192
    • 0019270387 scopus 로고
    • Structure of the elastase-cathepsin G inhibitor of the leech Hirudo medicinalis
    • Seemuller, U., Eulitz, M., Fritz, H., and Strobl, A. 1980. Structure of the elastase-cathepsin G inhibitor of the leech Hirudo medicinalis. Hoppe Seylers Z. Physiol. Chem., 361:1841-1846.
    • (1980) Hoppe Seylers Z. Physiol. Chem , vol.361 , pp. 1841-1846
    • Seemuller, U.1    Eulitz, M.2    Fritz, H.3    Strobl, A.4
  • 193
    • 0015231995 scopus 로고
    • Guanidination of the Bowman-Birk soybean inhibitor: Evidence for the tryptic hydrolysis of peptide bonds involving homoarginine
    • Seidl, D. S., and Liener, I. E. 1971. Guanidination of the Bowman-Birk soybean inhibitor: evidence for the tryptic hydrolysis of peptide bonds involving homoarginine. Biochem. Biophys. Res. Commun., 42:1101-1107.
    • (1971) Biochem. Biophys. Res. Commun , vol.42 , pp. 1101-1107
    • Seidl, D.S.1    Liener, I.E.2
  • 194
    • 0009512652 scopus 로고
    • Inactivation of trypsin inhibitors in whole and cracked soybeans with sodium metabisulfite
    • Sessa, D. J., Baker, E. C., and Friedrich, J. P. 1988. Inactivation of trypsin inhibitors in whole and cracked soybeans with sodium metabisulfite. Lebensm.-Wiss. U-Technol., 21:163-168.
    • (1988) Lebensm.-Wiss. U-Technol , vol.21 , pp. 163-168
    • Sessa, D.J.1    Baker, E.C.2    Friedrich, J.P.3
  • 195
    • 0033550195 scopus 로고    scopus 로고
    • Crystal structure of a 16 kDa double-headed Bowman-Birk trypsin inhibitor from barley seeds at 1.9 A resolution
    • Song, H. K., Kim, Y. S., Yang, J. K., Moon, J., Lee, J. Y., and Sun, S. W. 1999. Crystal structure of a 16 kDa double-headed Bowman-Birk trypsin inhibitor from barley seeds at 1.9 A resolution. J. Mol. Biol., 293:1133-1144.
    • (1999) J. Mol. Biol , vol.293 , pp. 1133-1144
    • Song, H.K.1    Kim, Y.S.2    Yang, J.K.3    Moon, J.4    Lee, J.Y.5    Sun, S.W.6
  • 196
    • 0015762456 scopus 로고
    • A human cell from, a pleural effusion derived from a breast carcinoma
    • Soule, H. D., Vazquez, J., Long, A., Albert, S., and Brennan, M. 1973. A human cell from, a pleural effusion derived from a breast carcinoma. J. Natl. Cancer Inst., 51:1409-1413.
    • (1973) J. Natl. Cancer Inst , vol.51 , pp. 1409-1413
    • Soule, H.D.1    Vazquez, J.2    Long, A.3    Albert, S.4    Brennan, M.5
  • 197
    • 0031555386 scopus 로고    scopus 로고
    • Antigenic determinants and reactive sites of a trypsin/chymotrypsin double-headed inhibitor from horse gram (Dolichos biflorus)
    • Sreerama, Y. N., and Gowda, L. R. 1997. Antigenic determinants and reactive sites of a trypsin/chymotrypsin double-headed inhibitor from horse gram (Dolichos biflorus). Biochim. Biophys. Acta, 1343:235-242.
    • (1997) Biochim. Biophys. Acta , vol.1343 , pp. 235-242
    • Sreerama, Y.N.1    Gowda, L.R.2
  • 198
    • 0025331001 scopus 로고
    • The effects of the Bowman-Birk protease inhibitor on c-myc expression and cell proliferation in the unirradiated and irradiated mouse colon
    • St Clair, W. H., Billings, P. C., and Kennedy, A. R. 1990. The effects of the Bowman-Birk protease inhibitor on c-myc expression and cell proliferation in the unirradiated and irradiated mouse colon. Cancer Lett., 52:145-152.
    • (1990) Cancer Lett , vol.52 , pp. 145-152
    • St Clair, W.H.1    Billings, P.C.2    Kennedy, A.R.3
  • 199
    • 0025938195 scopus 로고
    • Effect of the Bowman-Birk protease inhibitor on the expression of oncogenes in the irradiated rat colon
    • St. Clair, W. H., and St Clair, D. K. 1991. Effect of the Bowman-Birk protease inhibitor on the expression of oncogenes in the irradiated rat colon. Cancer Res., 51:4539-4543.
    • (1991) Cancer Res , vol.51 , pp. 4539-4543
    • St. Clair, W.H.1    St Clair, D.K.2
  • 200
    • 0001251613 scopus 로고
    • Variation in the low molecular weight. proteinase inhibitors of soybeans
    • Stahlhut, R. W., and Hymowitz, T. 1983. Variation in the low molecular weight. proteinase inhibitors of soybeans. Crop. Sci. 23:766-76.
    • (1983) Crop. Sci , vol.23 , pp. 766-776
    • Stahlhut, R.W.1    Hymowitz, T.2
  • 201
    • 0033134622 scopus 로고    scopus 로고
    • Matrix metalloproteinases in angiogenesis: A moving target, for therapeutic intervention
    • Stetler-Stevenson, W. G. 1999. Matrix metalloproteinases in angiogenesis: a moving target, for therapeutic intervention.J. Clin. Invest., 103:1237-1241.
    • (1999) J. Clin. Invest , vol.103 , pp. 1237-1241
    • Stetler-Stevenson, W.G.1
  • 202
    • 13744252369 scopus 로고    scopus 로고
    • Cancer prevention: A global, perspective
    • Stewart, B. W., and Coates, A. S. 2005. Cancer prevention: a global, perspective, J. Clin. Oncol., 23:392-403.
    • (2005) J. Clin. Oncol , vol.23 , pp. 392-403
    • Stewart, B.W.1    Coates, A.S.2
  • 203
    • 0035218742 scopus 로고    scopus 로고
    • Proteases and antiproteases
    • Stockley, R. A. 2001. Proteases and antiproteases. Novartis Found. Symp., 234:189-99.
    • (2001) Novartis Found. Symp , vol.234 , pp. 189-199
    • Stockley, R.A.1
  • 204
    • 3743076488 scopus 로고
    • Structure-function relationships in the serine proteases
    • Reich, E. Rifkin, D.B. and Shaw, E. Eds. Cold Spring Harbor Laboratory
    • Stroud, R. M., Krieger, M., Koeppe, R. E., Kossiakoff, A. A., and Chambers, J. L. 1975. Structure-function relationships in the serine proteases. In Proteases and Biological Control. pp.13-32 Reich., E. Rifkin, D.B. and Shaw, E. Eds. Cold Spring Harbor Laboratory.
    • (1975) Proteases and Biological Control , pp. 13-32
    • Stroud, R.M.1    Krieger, M.2    Koeppe, R.E.3    Kossiakoff, A.A.4    Chambers, J.L.5
  • 205
    • 0035174039 scopus 로고    scopus 로고
    • Testosterone and prostate specific antigen stimulate generation of reactive oxygen species in prostate cancer cells
    • Sun, X. Y., Donald, S. P., and Phang, J. M. 2001. Testosterone and prostate specific antigen stimulate generation of reactive oxygen species in prostate cancer cells. Carcinogenesis, 22:1775-1780.
    • (2001) Carcinogenesis , vol.22 , pp. 1775-1780
    • Sun, X.Y.1    Donald, S.P.2    Phang, J.M.3
  • 207
    • 0000421846 scopus 로고
    • Different rates of metabolism of soybean proteinase inhibitors during germination
    • Tan-Wilson, A., Rightmire, B. R., and Wilson, K. A. 1982. Different rates of metabolism of soybean proteinase inhibitors during germination. Plant Physiol., 70:493-497.
    • (1982) Plant Physiol , vol.70 , pp. 493-497
    • Tan-Wilson, A.1    Rightmire, B.R.2    Wilson, K.A.3
  • 209
    • 0018618549 scopus 로고
    • Purification and characterization of a trypsin inhibitor from rice bran
    • Tashiro, M., and Maki, Z. 1979. Purification and characterization of a trypsin inhibitor from rice bran. J. Nutr. Sci. Vitaminol (Tokyo), 25(3):255-64.
    • (1979) J. Nutr. Sci. Vitaminol (Tokyo) , vol.25 , Issue.3 , pp. 255-264
    • Tashiro, M.1    Maki, Z.2
  • 210
    • 0023389904 scopus 로고
    • The complete amino acid sequence of rice bran trypsin inhibitor
    • Tashiro, M., Hashino, K., Shiozaki, M., Ibuki, F., and Maki, Z. 1987. The complete amino acid sequence of rice bran trypsin inhibitor. J. Biochem., 102:297-306.
    • (1987) J. Biochem , vol.102 , pp. 297-306
    • Tashiro, M.1    Hashino, K.2    Shiozaki, M.3    Ibuki, F.4    Maki, Z.5
  • 211
    • 39349094064 scopus 로고    scopus 로고
    • Tikhonova T. V., Gladysheva I. P., Kazanskaia N. F., and Larionova, N. I. 1994. Hydrolysis of elastin by human leukocyte elastase and cathepsin G: Inhibition by Bowman-Birk-type soybean inhibitor. Biochem., (Mosc) 59:1295-1299.
    • Tikhonova T. V., Gladysheva I. P., Kazanskaia N. F., and Larionova, N. I. 1994. Hydrolysis of elastin by human leukocyte elastase and cathepsin G: Inhibition by Bowman-Birk-type soybean inhibitor. Biochem., (Mosc) 59:1295-1299.
  • 212
    • 0028929097 scopus 로고
    • Retardation by the soybean Bowman-Birk inhibitor of elastin hydrolysis catalyzed by leukocyte proteinases
    • Tikhonova, T. V., Gladysheva, I. P., and Larionova, N. I. 1995. Retardation by the soybean Bowman-Birk inhibitor of elastin hydrolysis catalyzed by leukocyte proteinases. FEBS Lett., 362:225-228.
    • (1995) FEBS Lett , vol.362 , pp. 225-228
    • Tikhonova, T.V.1    Gladysheva, I.P.2    Larionova, N.I.3
  • 213
    • 0034973651 scopus 로고    scopus 로고
    • Other novel agents: Rationale and current status as chemopreventive agents
    • Tolcher, A. W., Kennedy, A. R., Padley, R. J., Majeed, N., Pollak, M., and Kantoff, P. W 2001. Other novel agents: Rationale and current status as chemopreventive agents. Urology, 57(Suppl 1):86-89.
    • (2001) Urology , vol.57 , Issue.SUPPL. 1 , pp. 86-89
    • Tolcher, A.W.1    Kennedy, A.R.2    Padley, R.J.3    Majeed, N.4    Pollak, M.5    Kantoff, P.W.6
  • 214
    • 0347110493 scopus 로고
    • Prevention of cancer by vitamin B3 (nicotamide and nicotinic acid): A protease inhibitor available in pure form
    • Troll, W. and Kennedy, A.R. Eds. Plenum Press, New York
    • Troll, W. 1993. Prevention of cancer by vitamin B3 (nicotamide and nicotinic acid): A protease inhibitor available in pure form. In: Protease Inhibitors as Cancer Chemopreventive Agents, pp. 177-189. Troll, W. and Kennedy, A.R. Eds. Plenum Press, New York.
    • (1993) Protease Inhibitors as Cancer Chemopreventive Agents , pp. 177-189
    • Troll, W.1
  • 215
    • 0016409584 scopus 로고
    • Equilibria of Bowman-Birk inhibitor association, with, trypsin and α-chymotrypsin
    • Turner, R., Liener, I. E., and Lovrien, R. E. 1975. Equilibria of Bowman-Birk inhibitor association, with, trypsin and α-chymotrypsin. Biochem., 14:275-282.
    • (1975) Biochem , vol.14 , pp. 275-282
    • Turner, R.1    Liener, I.E.2    Lovrien, R.E.3
  • 216
    • 39349087784 scopus 로고    scopus 로고
    • US Pat-ent 5,217,717. 1993. Kennedy; A. R, Wynnewood, PA) and Szuhaj; B. R Fort Wayne, IN, Method of making soybean. Bowman-Birk inhibitor concentrate and use of same as a human, cancer preventative and therapy
    • US Pat-ent 5,217,717. 1993. Kennedy; A. R. (Wynnewood, PA) and Szuhaj; B. R (Fort Wayne, IN). Method of making soybean. Bowman-Birk inhibitor concentrate and use of same as a human, cancer preventative and therapy.
  • 217
    • 39349107580 scopus 로고    scopus 로고
    • US Patent. 5,338,547.(August 16, 1994, Kennedy; Ann R, Wynnewood, PA, Szuhaj; Bernard R Fort Wayne, IN, Bowman-Birk inhibitor product for use as an anticarcinogenesis agent
    • US Patent. 5,338,547.(August 16, 1994). Kennedy; Ann R. (Wynnewood, PA), Szuhaj; Bernard R (Fort Wayne, IN). Bowman-Birk inhibitor product for use as an anticarcinogenesis agent.
  • 218
    • 39349107928 scopus 로고    scopus 로고
    • US Patents 6,887, 498, May 3, 2005, Konwinski; Arthur H, Fort Wayne, IN, Szuhaj; Bernard R Fort Wayne, IN, Method of making Bowman-Birk inhibitor product
    • US Patents 6,887, 498. (May 3, 2005). Konwinski; Arthur H. (Fort Wayne, IN), Szuhaj; Bernard R (Fort Wayne, IN). Method of making Bowman-Birk inhibitor product.
  • 219
    • 0003705447 scopus 로고    scopus 로고
    • Inactivation kinetics study of the Kunitz soybean trypsin inhibitor and the Bowman-Birk Inhibitor
    • van den Hout, R., Pouw, M., Gruppen, H., and van't Riet, K. 1998. Inactivation kinetics study of the Kunitz soybean trypsin inhibitor and the Bowman-Birk Inhibitor. J. Agric. Food Chem., 46:281-285.
    • (1998) J. Agric. Food Chem , vol.46 , pp. 281-285
    • van den Hout, R.1    Pouw, M.2    Gruppen, H.3    van't Riet, K.4
  • 220
    • 39349108631 scopus 로고    scopus 로고
    • Von der Helm, K., Korant, B. D., and Cheronis, J. C. 2000. In: Proteases as targets for therapy. Von der Helm, K., Korant, B.D., and Cheronis, J.C Eds.,SpringerVerlag. Berlin, Heidelberg, New York.
    • Von der Helm, K., Korant, B. D., and Cheronis, J. C. 2000. In: Proteases as targets for therapy. Von der Helm, K., Korant, B.D., and Cheronis, J.C Eds.,SpringerVerlag. Berlin, Heidelberg, New York.
  • 221
    • 0025338904 scopus 로고
    • Inhibition of X-ray induced exencephaly by protease inhibitors
    • Von Hofe, E., Brent, R., and Kennedy, A. R. 1990. Inhibition of X-ray induced exencephaly by protease inhibitors. Radiat. Res, 123:108-111.
    • (1990) Radiat. Res , vol.123 , pp. 108-111
    • Von Hofe, E.1    Brent, R.2    Kennedy, A.R.3
  • 222
    • 0029658121 scopus 로고    scopus 로고
    • Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution. Structural, peculiarities in a folded protein, conformation
    • Voss, R. H., Ermler, U., Essen, L. O., Wenzl, G., Kim, Y. M., and Flecker, P. 1996. Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution. Structural, peculiarities in a folded protein, conformation. Eur J Biochem., 242(1):122-31.
    • (1996) Eur J Biochem , vol.242 , Issue.1 , pp. 122-131
    • Voss, R.H.1    Ermler, U.2    Essen, L.O.3    Wenzl, G.4    Kim, Y.M.5    Flecker, P.6
  • 223
    • 0033942129 scopus 로고    scopus 로고
    • Urinary excretion of Bowman-Birk inhibitor in human after soy consump tion as determined by a monoclonal antibody-based immunoassay
    • Wan, X. S., Lu, L. J. W.; Anderson, K. E., Ware, J. H.; and Kennedy, A. R. 2000. Urinary excretion of Bowman-Birk inhibitor in human after soy consump tion as determined by a monoclonal antibody-based immunoassay. Cancer Epidemiol. Biomarkers Prev., 9:741-747.
    • (2000) Cancer Epidemiol. Biomarkers Prev , vol.9 , pp. 741-747
    • Wan, X.S.1    Lu, L.J.W.2    Anderson, K.E.3    Ware, J.H.4    Kennedy, A.R.5
  • 224
    • 0036969221 scopus 로고    scopus 로고
    • Detection of Bowman-Birk inhibitor and anti-Bowman-Birk inhibitor antibodies in sera of humans and animals treated with Bowman-Birk inhibitor concentrate
    • Wan, X. S., Serota, D. G., Ware, J. H., Crowell, J. A., and Kennedy, A. R. 2002. Detection of Bowman-Birk inhibitor and anti-Bowman-Birk inhibitor antibodies in sera of humans and animals treated with Bowman-Birk inhibitor concentrate. Nutr. Cancer, 3:167-173.
    • (2002) Nutr. Cancer , vol.3 , pp. 167-173
    • Wan, X.S.1    Serota, D.G.2    Ware, J.H.3    Crowell, J.A.4    Kennedy, A.R.5
  • 225
    • 0032957934 scopus 로고    scopus 로고
    • Bowman-Birk inhibitor concentrate reduces colon inflammation in mice with dextran sulfate sodium-induced ulcerative colitis
    • Ware, J. H., Wan, X. S., Newberne, P., and Kennedy, A. R. 1999. Bowman-Birk inhibitor concentrate reduces colon inflammation in mice with dextran sulfate sodium-induced ulcerative colitis. Dig. Dis. Sci. 44:986-990.
    • (1999) Dig. Dis. Sci , vol.44 , pp. 986-990
    • Ware, J.H.1    Wan, X.S.2    Newberne, P.3    Kennedy, A.R.4
  • 226
    • 0031214119 scopus 로고    scopus 로고
    • Soybean Bowman-Birk protease inhibitor is a highly effective inhibitor of human mast cell chymase
    • Ware, J. H., Wan, X. S., Rubin, H., Schechter, N. M., and Kennedy, A. R. 1997. Soybean Bowman-Birk protease inhibitor is a highly effective inhibitor of human mast cell chymase. Arch. Biochem. Biophys., 344:133-138.
    • (1997) Arch. Biochem. Biophys , vol.344 , pp. 133-138
    • Ware, J.H.1    Wan, X.S.2    Rubin, H.3    Schechter, N.M.4    Kennedy, A.R.5
  • 227
    • 0026590679 scopus 로고
    • Inhibition of carcinogenesis by minor dietary constituents
    • Wattenberg, L. W. 1992. Inhibition of carcinogenesis by minor dietary constituents. Cancer Res., 52:2085s-2091s.
    • (1992) Cancer Res , vol.52
    • Wattenberg, L.W.1
  • 228
    • 0023034367 scopus 로고
    • Inhibition of human proteinases by grain legumes
    • Weder, J. K. 1986. Inhibition of human proteinases by grain legumes. Adv. Exp. Med. Biol., 199:239-279.
    • (1986) Adv. Exp. Med. Biol , vol.199 , pp. 239-279
    • Weder, J.K.1
  • 229
    • 0026176486 scopus 로고
    • Inhibitors of human and bovine trypsin and chymotrypsin in fenugreek (Trigonella foenum-graecum L.) seeds. Isolation and characterization
    • Weder, J. K., and Haussner, K. 1991. Inhibitors of human and bovine trypsin and chymotrypsin in fenugreek (Trigonella foenum-graecum L.) seeds. Isolation and characterization. ZLebensm Unters Forsch., 192:535-540.
    • (1991) ZLebensm Unters Forsch , vol.192 , pp. 535-540
    • Weder, J.K.1    Haussner, K.2
  • 230
    • 0026234371 scopus 로고
    • Inhibitors of human and bovine trypsin and chymotrypsin. in fenugreek (Trigoneilafoenum-graecum L.) seeds. Reaction with the human, and bovine proteinases
    • Weder, J. K., and Haussner, K. 1991. Inhibitors of human and bovine trypsin and chymotrypsin. in fenugreek (Trigoneilafoenum-graecum L.) seeds. Reaction with the human, and bovine proteinases. Z Lebensm Unters Forsch., 193:321-325.
    • (1991) Z Lebensm Unters Forsch , vol.193 , pp. 321-325
    • Weder, J.K.1    Haussner, K.2
  • 231
    • 0026218129 scopus 로고
    • Inhibitors of human and bovine trypsin and chymotrypsin in fenugreek (Trigoneilafoenum-graecum L.) seeds. Reactive sites and C-terminal sequences
    • Weder, J. K., and Haussner, K. 1991. Inhibitors of human and bovine trypsin and chymotrypsin in fenugreek (Trigoneilafoenum-graecum L.) seeds. Reactive sites and C-terminal sequences. Z Lebensm Unters Forsch., 193:242-246.
    • (1991) Z Lebensm Unters Forsch , vol.193 , pp. 242-246
    • Weder, J.K.1    Haussner, K.2
  • 232
    • 0025922173 scopus 로고
    • Identification of a protein-binding surface by differential amide hydrogen-exchange measurements. Application to Bowman-Birk serine-protease inhibitor
    • Werner, M. H., and Wemmer, D. E. 1991. Identification of a protein-binding surface by differential amide hydrogen-exchange measurements. Application to Bowman-Birk serine-protease inhibitor. Biochem., 30:3356-3364.
    • (1991) Biochem , vol.30 , pp. 3356-3364
    • Werner, M.H.1    Wemmer, D.E.2
  • 233
    • 0026694158 scopus 로고
    • Expression of Cx26, Cx32 and Cx43 gap junction proteins in normal and neoplastic human tissues
    • Wilgenbus, K. K., Kirkpatrick, C. J., Knuechel, R., Willecke, K., and Traub, O. 1992. Expression of Cx26, Cx32 and Cx43 gap junction proteins in normal and neoplastic human tissues. Int. J. Cancer, 51:522-529.
    • (1992) Int. J. Cancer , vol.51 , pp. 522-529
    • Wilgenbus, K.K.1    Kirkpatrick, C.J.2    Knuechel, R.3    Willecke, K.4    Traub, O.5
  • 234
    • 0033779258 scopus 로고    scopus 로고
    • Diet and cancer
    • Willett, W. C. 2000. Diet and cancer: Oncologist, 5(5):393-404.
    • (2000) Oncologist , vol.5 , Issue.5 , pp. 393-404
    • Willett, W.C.1
  • 235
    • 0035131928 scopus 로고    scopus 로고
    • Diet and cancer: One view at the start of the millennium
    • Willett, W. C. 2001. Diet and cancer: one view at the start of the millennium. Cancer Epidemiol. Biomarkers Prev., 10:3-8.
    • (2001) Cancer Epidemiol. Biomarkers Prev , vol.10 , pp. 3-8
    • Willett, W.C.1
  • 236
    • 0036728623 scopus 로고    scopus 로고
    • MMPs and TIMPs-a historical perspective
    • Woessner, J. E Jr. 2002. MMPs and TIMPs-a historical perspective. Mol. Biotechnol., 22:33-49.
    • (2002) Mol. Biotechnol , vol.22 , pp. 33-49
    • Woessner Jr., J.E.1
  • 237
    • 0141973232 scopus 로고
    • Homology among trypsin/ chymotrypsin inhibitors from red kidney bean, brazilian pink bean, lima bean, and soybean
    • Wu, C., and Whitaker, J. R. (1991). Homology among trypsin/ chymotrypsin inhibitors from red kidney bean, brazilian pink bean, lima bean, and soybean. J. Agric. Food Chem., 39:1583-1589.
    • (1991) J. Agric. Food Chem , vol.39 , pp. 1583-1589
    • Wu, C.1    Whitaker, J.R.2
  • 238
    • 0642303251 scopus 로고
    • Conformation of Bowman-Birk inhibitor
    • Wu, Y. V., and Sessa, D. J. (1994). Conformation of Bowman-Birk inhibitor. J. Agric. Food Chem., 42:2136-2138.
    • (1994) J. Agric. Food Chem , vol.42 , pp. 2136-2138
    • Wu, Y.V.1    Sessa, D.J.2
  • 239
    • 0022114154 scopus 로고
    • Nanomolar concentrations of Bowman-Birk soybean protease inhibitor suppress X-ray induced transformation in vitro
    • Yavelow, J., Collins, M., Birk, Y., Troll, W., and Kennedy, A. R. 1985. Nanomolar concentrations of Bowman-Birk soybean protease inhibitor suppress X-ray induced transformation in vitro. Proc. Natl. Acad. Sci. USA. 82:5395-5399.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 5395-5399
    • Yavelow, J.1    Collins, M.2    Birk, Y.3    Troll, W.4    Kennedy, A.R.5
  • 240
    • 0020631151 scopus 로고
    • Bowman-Birk soybean protease inhibitor as an anticarcinogen
    • Yavelow, J., Finlay, T. H., Kennedy, A. R., and Troll, W A. 1983. Bowman-Birk soybean protease inhibitor as an anticarcinogen. Cancer Res., 43:2454-2459.
    • (1983) Cancer Res , vol.43 , pp. 2454-2459
    • Yavelow, J.1    Finlay, T.H.2    Kennedy, A.R.3    Troll, W.A.4
  • 241
    • 0035941043 scopus 로고    scopus 로고
    • A Bowman-Birk-type trypsin-chymotrypsin inhibitor from broad beans
    • Ye, X. Y., Ng, T. B, and Rao, P. F. 2001. A Bowman-Birk-type trypsin-chymotrypsin inhibitor from broad beans. Biochem. Biophys. Res. Commun., 289:91-96.
    • (2001) Biochem. Biophys. Res. Commun , vol.289 , pp. 91-96
    • Ye, X.Y.1    Ng, T.B.2    Rao, P.F.3
  • 242
    • 0030151999 scopus 로고    scopus 로고
    • A rapid purification method for soybean Bowman-Birk protease inhibitor using hydrophobic interaction chromatography
    • Yeboah, N. A., Arahira, M., Udaka, K., and Fukuzawa, C. 1996. A rapid purification method for soybean Bowman-Birk protease inhibitor using hydrophobic interaction chromatography. Prot. Expr. Purif, 7:309-314.
    • (1996) Prot. Expr. Purif , vol.7 , pp. 309-314
    • Yeboah, N.A.1    Arahira, M.2    Udaka, K.3    Fukuzawa, C.4
  • 243
    • 0017602120 scopus 로고
    • Effect of dietary raw soybean and soybean trypsin inhibitor on trypsin and chymotrypsin activities in the pancreas and in small intestinal juice of growing swine
    • Yen, J. T., Jensen, A. H., and Simon, J. 1977. Effect of dietary raw soybean and soybean trypsin inhibitor on trypsin and chymotrypsin activities in the pancreas and in small intestinal juice of growing swine. J. Nutr., 107:156-165.
    • (1977) J. Nutr , vol.107 , pp. 156-165
    • Yen, J.T.1    Jensen, A.H.2    Simon, J.3
  • 244
    • 0036290075 scopus 로고    scopus 로고
    • Chemical synthesis and kinetic study of thesmallest naturally occurring trypsin inhibitor SFTI-I isolated from sunflower seeds and its analogues
    • Zablotna, E., Kazmierczak, K., Jaskiewicz A., Stawikowski, M., Kupryszewski, G., and Rolka, K. 2002. Chemical synthesis and kinetic study of thesmallest naturally occurring trypsin inhibitor SFTI-I isolated from sunflower seeds and its analogues. Biochem Biophys Res Commun. 292:855-859.
    • (2002) Biochem Biophys Res Commun , vol.292 , pp. 855-859
    • Zablotna, E.1    Kazmierczak, K.2    Jaskiewicz, A.3    Stawikowski, M.4    Kupryszewski, G.5    Rolka, K.6
  • 245
    • 0028877683 scopus 로고
    • Duodenase, a new serine protease of unusual specificity from bovine duodenal mucosa. Primary structure of the enzyme
    • Zamolodchikova, T. S., Vorotyntseva, T. I., Najimov, T. V., and Grishina, G. A. 1995. Duodenase, a new serine protease of unusual specificity from bovine duodenal mucosa. Primary structure of the enzyme. Eur. J. Biochem., 227:873-879.
    • (1995) Eur. J. Biochem , vol.227 , pp. 873-879
    • Zamolodchikova, T.S.1    Vorotyntseva, T.I.2    Najimov, T.V.3    Grishina, G.A.4
  • 246
    • 0035831328 scopus 로고    scopus 로고
    • X-Ray study on an artificial mung bean inhibitor complex with bovine beta-trypsin in neat cyclohexane
    • Zhu, G., Huang, Q., Zhu, Y., Li, Y., Chi, C., and Tang, Y. 2001. X-Ray study on an artificial mung bean inhibitor complex with bovine beta-trypsin in neat cyclohexane. Biochim. Biophys. Acta, 1546:98-106.
    • (2001) Biochim. Biophys. Acta , vol.1546 , pp. 98-106
    • Zhu, G.1    Huang, Q.2    Zhu, Y.3    Li, Y.4    Chi, C.5    Tang, Y.6
  • 247
    • 0029195536 scopus 로고
    • Cysteine proteinase inhibitors from soy seeds
    • Zimacheva, A. V. and Mosolov, V. V. 1995. Cysteine proteinase inhibitors from soy seeds. Biokhimiia, 60:118-123.
    • (1995) Biokhimiia , vol.60 , pp. 118-123
    • Zimacheva, A.V.1    Mosolov, V.V.2


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