메뉴 건너뛰기




Volumn 44, Issue 6, 2006, Pages 622-631

A fibrinolytic enzyme from the medicinal mushroom Cordyceps militaris

Author keywords

Cordyceps militaris; Fibrinolysis; Fibrinolytic enzyme; Serine protease; Subtilisin; Thrombus

Indexed keywords

BASIDIOMYCOTA; CORDYCEPS; CORDYCEPS MILITARIS; METARHIZIUM ANISOPLIAE;

EID: 33846995165     PISSN: 12258873     EISSN: 12258873     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (80)

References (55)
  • 1
    • 0033912136 scopus 로고    scopus 로고
    • Cordycepin: Selective growth inhibitor derived from liquid culture of Cordyceps militaris against Clostridium spp
    • Ahn, Y.J, S.J. Park, S.G. Lee, S.C. Shin, and D.H. Choi. 2004. Cordycepin: Selective growth inhibitor derived from liquid culture of Cordyceps militaris against Clostridium spp. J. Agric. Food Chem. 48, 2744-2748.
    • (2004) J. Agric. Food Chem , vol.48 , pp. 2744-2748
    • Ahn, Y.J.1    Park, S.J.2    Lee, S.G.3    Shin, S.C.4    Choi, D.H.5
  • 2
    • 33947169675 scopus 로고    scopus 로고
    • Alicja, S. 1998. Towards an integrated management of Dendrolimus pini L. Proceedings: Population dynamics, impacts, and integrated management of forest defoliation insects. USDA forest service general technical report NE 247, 129-142.
    • Alicja, S. 1998. Towards an integrated management of Dendrolimus pini L. Proceedings: Population dynamics, impacts, and integrated management of forest defoliation insects. USDA forest service general technical report NE 247, 129-142.
  • 3
    • 50449151040 scopus 로고
    • The fibrin plate method for estimating of fibrinolytic activity
    • Astrup, T. and S. Mullertz. 1952. The fibrin plate method for estimating of fibrinolytic activity. Arch. Biochem. Biophys. 40, 346-351.
    • (1952) Arch. Biochem. Biophys , vol.40 , pp. 346-351
    • Astrup, T.1    Mullertz, S.2
  • 4
    • 0348049996 scopus 로고    scopus 로고
    • Reconstructing the diversification of subtilisins in the pathogenic fungus Metarhizium anisopliae
    • Bagga, S., G. Hu, S.E. Screen, and R.J. St. Leger. 2004. Reconstructing the diversification of subtilisins in the pathogenic fungus Metarhizium anisopliae. Gene 324, 159-169.
    • (2004) Gene , vol.324 , pp. 159-169
    • Bagga, S.1    Hu, G.2    Screen, S.E.3    St. Leger, R.J.4
  • 5
    • 0000083031 scopus 로고
    • Isolation and partial characterization of a chymotrypsinlike endoprotease from cockroach intestinal system
    • Baumann, E. 1990. Isolation and partial characterization of a chymotrypsinlike endoprotease from cockroach intestinal system. Insect Biochem. 20, 761-768.
    • (1990) Insect Biochem , vol.20 , pp. 761-768
    • Baumann, E.1
  • 6
    • 27944497471 scopus 로고    scopus 로고
    • Isolation and biochemical characterization of a fibrinolytic proteinase from Bothrops leucurus (white-tailed jararaca) snake venom
    • Bello, C.A., A.L.N. Hermogenes, A. Magalhaes, S.S. Veiga, L.H. Gremski, M. Richardson, and E.F. Sanchez. 2006. Isolation and biochemical characterization of a fibrinolytic proteinase from Bothrops leucurus (white-tailed jararaca) snake venom. Biochimie 88, 189-200.
    • (2006) Biochimie , vol.88 , pp. 189-200
    • Bello, C.A.1    Hermogenes, A.L.N.2    Magalhaes, A.3    Veiga, S.S.4    Gremski, L.H.5    Richardson, M.6    Sanchez, E.F.7
  • 7
    • 0033864203 scopus 로고    scopus 로고
    • Potent fibrinolytic enzyme from a mutant of Bacillus subtilis IMR-NK1
    • Chang, C.T., M.H. Fan, F.C. Kuo, and H.Y. Sung. 2000. Potent fibrinolytic enzyme from a mutant of Bacillus subtilis IMR-NK1. J. Agric. Food Chem. 48, 3210-3216.
    • (2000) J. Agric. Food Chem , vol.48 , pp. 3210-3216
    • Chang, C.T.1    Fan, M.H.2    Kuo, F.C.3    Sung, H.Y.4
  • 9
    • 0002391495 scopus 로고    scopus 로고
    • Mushroom research and development-equality and mutual benefit
    • D.J. Royse, Editor, The Pennsylvania State University, USA
    • Chang, S.T. 1996. Mushroom research and development-equality and mutual benefit. In: D.J. Royse, Editor, Mushroom Biology and Mushroom Products, p 1-10, The Pennsylvania State University, USA.
    • (1996) Mushroom Biology and Mushroom Products , pp. 1-10
    • Chang, S.T.1
  • 10
    • 0042069504 scopus 로고    scopus 로고
    • Fibrinolytic and antithrombotic protease from Ganoderma lucidum
    • Choi, H.S. and Y.S. Sa. 2000. Fibrinolytic and antithrombotic protease from Ganoderma lucidum. Mycologia 92, 545-552.
    • (2000) Mycologia , vol.92 , pp. 545-552
    • Choi, H.S.1    Sa, Y.S.2
  • 11
    • 33644480000 scopus 로고    scopus 로고
    • Screening of mushroom having fibrinolytic activity
    • Choi, N.S., S.Y. Seo, and S.H. Kim. 1999. Screening of mushroom having fibrinolytic activity. Korean J. Food Sci. Technol. 31, 553-557.
    • (1999) Korean J. Food Sci. Technol , vol.31 , pp. 553-557
    • Choi, N.S.1    Seo, S.Y.2    Kim, S.H.3
  • 12
    • 0029906384 scopus 로고    scopus 로고
    • New insights into the mechanisms of fungal pathogenesis in insects
    • Clarkson, J.M. and A.K. Charnley. 1996. New insights into the mechanisms of fungal pathogenesis in insects. Trends Microbiol. 4, 197-203.
    • (1996) Trends Microbiol , vol.4 , pp. 197-203
    • Clarkson, J.M.1    Charnley, A.K.2
  • 13
    • 0018893682 scopus 로고
    • On the regulation and control of fibrinolysis
    • Collen, D. 1980. On the regulation and control of fibrinolysis. Thromb. Haemost. 43, 77-89.
    • (1980) Thromb. Haemost , vol.43 , pp. 77-89
    • Collen, D.1
  • 14
    • 0026331304 scopus 로고
    • Basic and clinical aspects of fibriolysis and thrombosis
    • Collen, D. and H.R. Lijnen. 1991. Basic and clinical aspects of fibriolysis and thrombosis. Blood 78, 3114-3124.
    • (1991) Blood , vol.78 , pp. 3114-3124
    • Collen, D.1    Lijnen, H.R.2
  • 15
    • 0001615432 scopus 로고
    • Cordycepin, a metabolic product from cultures of Cordyceps militaris (Linn.) Link
    • Cunningham, K.G., S.A. Hutchinson, W. Manson, and F.S. Spring. 1950. Cordycepin, a metabolic product from cultures of Cordyceps militaris (Linn.) Link. Nature 166, 949.
    • (1950) Nature , vol.166 , pp. 949
    • Cunningham, K.G.1    Hutchinson, S.A.2    Manson, W.3    Spring, F.S.4
  • 16
    • 0028986636 scopus 로고
    • Biochemical- characterization of basilase. A fibrinolytic protease from Crotalus basiliscus basiliscus
    • Datta, G., A. Dong, J. Witt, and A.T. Tu. 1995. Biochemical- characterization of basilase. A fibrinolytic protease from Crotalus basiliscus basiliscus. Arch. Biochem. Biophys. 317, 365-373.
    • (1995) Arch. Biochem. Biophys , vol.317 , pp. 365-373
    • Datta, G.1    Dong, A.2    Witt, J.3    Tu, A.T.4
  • 17
    • 0029411216 scopus 로고
    • Purification and characterization of intracellular proteinases in Pleurotus ostreatus fruiting bodies
    • Dohmae, N., K. Hayashi, K. Miki, Y. Tsumuraya, and Y. Hashimoto. 1995. Purification and characterization of intracellular proteinases in Pleurotus ostreatus fruiting bodies. Biosci. Biotechnol. Biochem. 59, 2074-2080.
    • (1995) Biosci. Biotechnol. Biochem , vol.59 , pp. 2074-2080
    • Dohmae, N.1    Hayashi, K.2    Miki, K.3    Tsumuraya, Y.4    Hashimoto, Y.5
  • 19
    • 0033016160 scopus 로고    scopus 로고
    • Digestive proteolytic activity in larvae of tomato moth, Lacanobia oleracea; effects of plant protease inhibitors in vitro and in vivo
    • Gatehouse, A.M.R., E. Norton, G.M. Davison, S.M. Babbé, C.A. Newell, and J.A. Gatehouse. 1999. Digestive proteolytic activity in larvae of tomato moth, Lacanobia oleracea; effects of plant protease inhibitors in vitro and in vivo. J. Insect Phys. 45, 545-558.
    • (1999) J. Insect Phys , vol.45 , pp. 545-558
    • Gatehouse, A.M.R.1    Norton, E.2    Davison, G.M.3    Babbé, S.M.4    Newell, C.A.5    Gatehouse, J.A.6
  • 20
    • 0033027428 scopus 로고    scopus 로고
    • Purification and characterization of a serine protease with fibrinolytic activity from Tenodera sinensis (praying mantis)
    • Hahn, B.S., S.Y. Cho, S.J. Wu, I.M. Chang, K.H. Baek, Y.C. Kim, and Y.S. Kim. 1999. Purification and characterization of a serine protease with fibrinolytic activity from Tenodera sinensis (praying mantis). Biochim. Biophys. Acta 1430, 376-386.
    • (1999) Biochim. Biophys. Acta , vol.1430 , pp. 376-386
    • Hahn, B.S.1    Cho, S.Y.2    Wu, S.J.3    Chang, I.M.4    Baek, K.H.5    Kim, Y.C.6    Kim, Y.S.7
  • 21
    • 0035957664 scopus 로고    scopus 로고
    • Purification and characterization of a plasmin-like protease from Tenodera sinensis (Chinese mantis)
    • Hahn, B.S., S.Y. Cho, M.Y. Ahn, and Y.S. Kim. 2001. Purification and characterization of a plasmin-like protease from Tenodera sinensis (Chinese mantis). Insect Biochem. Mol. Biol. 31, 573-581.
    • (2001) Insect Biochem. Mol. Biol , vol.31 , pp. 573-581
    • Hahn, B.S.1    Cho, S.Y.2    Ahn, M.Y.3    Kim, Y.S.4
  • 23
    • 0035024732 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a fibrinolytic enzyme from Bacillus subtilis BK-17
    • Jeong, Y.K., J.U. Park, H. Baek, S.H. Park, and I.S. Kong. 2001. Purification and biochemical characterization of a fibrinolytic enzyme from Bacillus subtilis BK-17. World J. Microbiol. Biotechnol. 17, 89-92.
    • (2001) World J. Microbiol. Biotechnol , vol.17 , pp. 89-92
    • Jeong, Y.K.1    Park, J.U.2    Baek, H.3    Park, S.H.4    Kong, I.S.5
  • 24
    • 4644229549 scopus 로고    scopus 로고
    • Cloning and developmental expression of a family metalloprotease cDNA from oyster mushroom Pleurotus ostreatus
    • Joh, J.H., B.G. Kim, W.S. Kong, Y.B. Yoo, N.K. Kim, H.R. Park, B.G. Cho, and C.S. Lee. 2004. Cloning and developmental expression of a family metalloprotease cDNA from oyster mushroom Pleurotus ostreatus. FEBS Microbiol. Lett. 239, 57-62.
    • (2004) FEBS Microbiol. Lett , vol.239 , pp. 57-62
    • Joh, J.H.1    Kim, B.G.2    Kong, W.S.3    Yoo, Y.B.4    Kim, N.K.5    Park, H.R.6    Cho, B.G.7    Lee, C.S.8
  • 25
    • 0029138570 scopus 로고
    • Protease activities in the larval midgut of Heliothis virescens: Evidence for trypsin and chymotrypsin-like enzymes
    • Johnston, K.A., M.J. Lee, C. Brough, V.A. Hilder, A.M.R. Gatehouse, and J.A. Gatehouse. 1995. Protease activities in the larval midgut of Heliothis virescens: evidence for trypsin and chymotrypsin-like enzymes. Insect Biochem. Mol. Biol. 25, 375-383.
    • (1995) Insect Biochem. Mol. Biol , vol.25 , pp. 375-383
    • Johnston, K.A.1    Lee, M.J.2    Brough, C.3    Hilder, V.A.4    Gatehouse, A.M.R.5    Gatehouse, J.A.6
  • 26
    • 0043022776 scopus 로고    scopus 로고
    • The screening of fibrinolytic activities of extracts from mushroom in Mt. Chiak
    • Kim, J., H. Lee, K. Yoo, Y. Kim, S. Seok, and Y. Kim. 1998. The screening of fibrinolytic activities of extracts from mushroom in Mt. Chiak. Korean J. Mycol. 26, 589-593.
    • (1998) Korean J. Mycol , vol.26 , pp. 589-593
    • Kim, J.1    Lee, H.2    Yoo, K.3    Kim, Y.4    Seok, S.5    Kim, Y.6
  • 27
    • 0035259942 scopus 로고    scopus 로고
    • Characterization of a metalloenzyme from a wild mushroom Tricholoma saponaceum
    • Kim, J.H. and Y.S. Kim. 2001. Characterization of a metalloenzyme from a wild mushroom Tricholoma saponaceum. Biosci. Biotechnol. Biochem. 65, 356-362.
    • (2001) Biosci. Biotechnol. Biochem , vol.65 , pp. 356-362
    • Kim, J.H.1    Kim, Y.S.2
  • 28
    • 0032190365 scopus 로고    scopus 로고
    • Fibrin zymography: A direct analysis of fibrinolytic proteases on gels
    • Kim, S.H., N.S. Choi, and W.Y. Lee. 1998. Fibrin zymography: a direct analysis of fibrinolytic proteases on gels. Anal. Biochem. 263, 115-116.
    • (1998) Anal. Biochem , vol.263 , pp. 115-116
    • Kim, S.H.1    Choi, N.S.2    Lee, W.Y.3
  • 29
    • 0011448806 scopus 로고
    • Yu-Pung Co. Ltd, Seoul, Korea
    • Kim, S.S. and Y.P. Kim. 1995. Korean mushrooms, Yu-Pung Co. Ltd., Seoul, Korea, 321
    • (1995) Korean mushrooms , pp. 321
    • Kim, S.S.1    Kim, Y.P.2
  • 30
    • 0029960565 scopus 로고    scopus 로고
    • Purification and characterization of a fibrinolytic enzyme produced from Bacillus sp. Strain CK 11-4 screened from Chungkook-Jang
    • Kim, W., K. Choi, and Y. Kim. 1996. Purification and characterization of a fibrinolytic enzyme produced from Bacillus sp. Strain CK 11-4 screened from Chungkook-Jang. Appl. Environ. Microbiol. 62, 2482-2488.
    • (1996) Appl. Environ. Microbiol , vol.62 , pp. 2482-2488
    • Kim, W.1    Choi, K.2    Kim, Y.3
  • 31
    • 0342844374 scopus 로고    scopus 로고
    • Biochemical characterization of a thrombin-like enzyme and a fibrinolytic serine protease from snake (Agkistrodon saxatilis) venom
    • Koh, Y.S., K.H. Chung, and D.S. Kim. 2001. Biochemical characterization of a thrombin-like enzyme and a fibrinolytic serine protease from snake (Agkistrodon saxatilis) venom. Toxicon 39, 555-560.
    • (2001) Toxicon , vol.39 , pp. 555-560
    • Koh, Y.S.1    Chung, K.H.2    Kim, D.S.3
  • 32
    • 0032792920 scopus 로고    scopus 로고
    • Isolation and characterization of two chymotrypsins from the midgut of Locusta migratoria
    • Lam, W., G.M. Coast, and R.C. Rayne. 1999. Isolation and characterization of two chymotrypsins from the midgut of Locusta migratoria. Insect Biochem. Mol. Biol. 29, 653-660.
    • (1999) Insect Biochem. Mol. Biol , vol.29 , pp. 653-660
    • Lam, W.1    Coast, G.M.2    Rayne, R.C.3
  • 33
    • 0014944179 scopus 로고
    • A factor preventing the major head protein of bacteriophage T4 from random aggregation
    • Laemmli, U.K., F. Beguin, and G. Gujer-Kellenberger. 1970. A factor preventing the major head protein of bacteriophage T4 from random aggregation. J. Mol. Biol. 47, 69-74.
    • (1970) J. Mol. Biol , vol.47 , pp. 69-74
    • Laemmli, U.K.1    Beguin, F.2    Gujer-Kellenberger, G.3
  • 35
    • 0029152568 scopus 로고
    • Endoproteases from the midgut of larval Spodoptera littoralis include a chymotrypsin-like enzyme with an extended binding site
    • Lee, M.J. and J.H. Anstee. 1995. Endoproteases from the midgut of larval Spodoptera littoralis include a chymotrypsin-like enzyme with an extended binding site. Insect Biochem. Mol. Biol. 25, 49-61.
    • (1995) Insect Biochem. Mol. Biol , vol.25 , pp. 49-61
    • Lee, M.J.1    Anstee, J.H.2
  • 38
    • 0034129048 scopus 로고    scopus 로고
    • Purification and characterization of a fibrinolytic enzyme and identification of fibrinogen clotting enzyme in a marine green alga
    • Matsubara, K., K. Hori, Y. Matsubara, and K. Miyazawa. 2000. Purification and characterization of a fibrinolytic enzyme and identification of fibrinogen clotting enzyme in a marine green alga, Codium divaricatum. Comp. Biochem. Physiol. B. 125, 137-143.
    • (2000) Codium divaricatum. Comp. Biochem. Physiol. B , vol.125 , pp. 137-143
    • Matsubara, K.1    Hori, K.2    Matsubara, Y.3    Miyazawa, K.4
  • 39
    • 0035957677 scopus 로고    scopus 로고
    • Identification of six chymotrypsin cDNAs from larval midguts of Helicoverpa zea and Agrotis ipsilon feeding on the soybean (Kunitz) trypsin inhibitor
    • Mazumdar-Leighton, S. and R.M. Broadway. 2001. Identification of six chymotrypsin cDNAs from larval midguts of Helicoverpa zea and Agrotis ipsilon feeding on the soybean (Kunitz) trypsin inhibitor. Insect Biochem. Mol. Biol. 31, 633-644.
    • (2001) Insect Biochem. Mol. Biol , vol.31 , pp. 633-644
    • Mazumdar-Leighton, S.1    Broadway, R.M.2
  • 41
    • 28644435115 scopus 로고    scopus 로고
    • Pharmacological actions of Cordyceps, a prized folk medicine
    • Ng, T.B. and H.X. Wang. 2005. Pharmacological actions of Cordyceps, a prized folk medicine. J. Pharm. Pharmacol. 57, 1509-1519.
    • (2005) J. Pharm. Pharmacol , vol.57 , pp. 1509-1519
    • Ng, T.B.1    Wang, H.X.2
  • 42
    • 0021241015 scopus 로고
    • Isolation and biochemical characterization of hemorrhagic toxin from the venom of Crotalus atrox
    • Nikai, T., N. Mori, M. Kishida, H. Sugihara, and A. Tu. 1984. Isolation and biochemical characterization of hemorrhagic toxin from the venom of Crotalus atrox. Arch. Biochem. Biophys. 231, 309-319.
    • (1984) Arch. Biochem. Biophys , vol.231 , pp. 309-319
    • Nikai, T.1    Mori, N.2    Kishida, M.3    Sugihara, H.4    Tu, A.5
  • 43
    • 0028784498 scopus 로고
    • Characterization of a thermostable lysine-specific metalloendopep-tidase from the fruiting bodies of a basidiomycete Grifola frondosa
    • Nonaka, T., H. Ishikawa, Y. Tsumuraya, Y. Hashimoto, and N. Dohmae. 1995. Characterization of a thermostable lysine-specific metalloendopep-tidase from the fruiting bodies of a basidiomycete Grifola frondosa. J. Biochem. 118, 1014-1020.
    • (1995) J. Biochem , vol.118 , pp. 1014-1020
    • Nonaka, T.1    Ishikawa, H.2    Tsumuraya, Y.3    Hashimoto, Y.4    Dohmae, N.5
  • 44
    • 2042510390 scopus 로고    scopus 로고
    • Lonofibrase, a novel ?-fibrinogenase from Lonomia obliqua caterpillars
    • Pinto, A.F.M., R. Dobrovolski, A.B.G. Veiga, and J.A. Guimarães. 2004. Lonofibrase, a novel ?-fibrinogenase from Lonomia obliqua caterpillars. Thromb. Res. 113, 147-154.
    • (2004) Thromb. Res , vol.113 , pp. 147-154
    • Pinto, A.F.M.1    Dobrovolski, R.2    Veiga, A.B.G.3    Guimarães, J.A.4
  • 45
    • 5444250612 scopus 로고    scopus 로고
    • Phase I trial of cordycepin and deoxycoformycin in TdT-positive acute leukemia
    • Seldin, D., S.L.A. Urbano, R. McCaffrey, and F. Foss. 1997. Phase I trial of cordycepin and deoxycoformycin in TdT-positive acute leukemia. Blood 90, 246.
    • (1997) Blood , vol.90 , pp. 246
    • Seldin, D.1    Urbano, S.L.A.2    McCaffrey, R.3    Foss, F.4
  • 46
    • 0033395934 scopus 로고    scopus 로고
    • Purification and characterization of metalloproteases from Pleurotus sajor-caju
    • Shin, H.H. and H.S. Choi. 1999. Purification and characterization of metalloproteases from Pleurotus sajor-caju. J. Microbiol. Biotechnol. 9, 675-678.
    • (1999) J. Microbiol. Biotechnol , vol.9 , pp. 675-678
    • Shin, H.H.1    Choi, H.S.2
  • 47
    • 0032053249 scopus 로고    scopus 로고
    • Biochemical Characterization of Lebetase, a Direct-Acting Fibrinolytic Enzyme from Vipera Lebetina Snake Venom
    • Siigurkey, J., M. Samel, K. Tõnismägi, J. Subbi, E. Siigur, and A.T. Tu. 1998. Biochemical Characterization of Lebetase, a Direct-Acting Fibrinolytic Enzyme from Vipera Lebetina Snake Venom. Thromb. Res. 90, 39-49.
    • (1998) Thromb. Res , vol.90 , pp. 39-49
    • Siigurkey, J.1    Samel, M.2    Tõnismägi, K.3    Subbi, J.4    Siigur, E.5    Tu, A.T.6
  • 48
    • 0026590461 scopus 로고
    • Fibrinolysis relating substances in marine creatures
    • Sumi, H., N. Nakajima, and H. Mihara. 1992. Fibrinolysis relating substances in marine creatures. Comp. Biochem. Physiol. B. 102, 163-167.
    • (1992) Comp. Biochem. Physiol. B , vol.102 , pp. 163-167
    • Sumi, H.1    Nakajima, N.2    Mihara, H.3
  • 49
    • 0023656415 scopus 로고
    • A novel fibrinolytic enzyme (nattokinase) in the vegetable cheese Natto; a typical and popular soybean food in the Japanese diet
    • Sumi, H., H. Hamada, H. Tsushima, H. Mihara, and H. Muraki. 1987. A novel fibrinolytic enzyme (nattokinase) in the vegetable cheese Natto; a typical and popular soybean food in the Japanese diet. Experientia 43, 1110-1111.
    • (1987) Experientia , vol.43 , pp. 1110-1111
    • Sumi, H.1    Hamada, H.2    Tsushima, H.3    Mihara, H.4    Muraki, H.5
  • 50
    • 33947172918 scopus 로고    scopus 로고
    • nd edition. p. 1087-1095. In John Wiley and Sons, New York, USA.
    • nd edition. p. 1087-1095. In John Wiley and Sons, New York, USA.
  • 51
    • 0032917302 scopus 로고    scopus 로고
    • Therapeutic effects of substances occurring in higher Basidiomycetes mushrooms: A modern perspective
    • Wasser, S.P. and A.L. Weis. 1999. Therapeutic effects of substances occurring in higher Basidiomycetes mushrooms: a modern perspective. Crit. Rev. Immunol. 19, 65-96.
    • (1999) Crit. Rev. Immunol , vol.19 , pp. 65-96
    • Wasser, S.P.1    Weis, A.L.2
  • 53
    • 0034084877 scopus 로고    scopus 로고
    • Inhibitory effect of Cordyceps sinensis and Cordyceps militaris on human glomerular mesangial cell proliferation induced by native LDL
    • Wu, Z.L., X.X. Wang, and W.Y. Chen. 2000. Inhibitory effect of Cordyceps sinensis and Cordyceps militaris on human glomerular mesangial cell proliferation induced by native LDL. Cell Biochem. Funct. 18, 93-97.
    • (2000) Cell Biochem. Funct , vol.18 , pp. 93-97
    • Wu, Z.L.1    Wang, X.X.2    Chen, W.Y.3
  • 54
    • 20944449626 scopus 로고    scopus 로고
    • Medicinal mushroom modulators of molecular targets as cancer therapeutics
    • Zaidman, B.Z., M. Yassin, J. Mahajna, and S.P. Wasser. 2005. Medicinal mushroom modulators of molecular targets as cancer therapeutics. Appl. Microbiol. Biotechnol. 67, 453-468.
    • (2005) Appl. Microbiol. Biotechnol , vol.67 , pp. 453-468
    • Zaidman, B.Z.1    Yassin, M.2    Mahajna, J.3    Wasser, S.P.4
  • 55
    • 0037174818 scopus 로고    scopus 로고
    • Effect of cordycepin on interleukin-10 production of human peripheral blood mononuclear cells
    • Zhou, X.X., C.U. Meyer, P. Schmidtke, and F. Zepp. 2002. Effect of cordycepin on interleukin-10 production of human peripheral blood mononuclear cells. Eur. J. Pharmacol. 453, 309-317.
    • (2002) Eur. J. Pharmacol , vol.453 , pp. 309-317
    • Zhou, X.X.1    Meyer, C.U.2    Schmidtke, P.3    Zepp, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.