메뉴 건너뛰기




Volumn 11, Issue 1, 2010, Pages 37-53

Recent progress in research on ribosome inactivating proteins

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA MOMORCHARIN; BENINCASIN; BETA KIRILOWIN; BETA MOMORCHARIN; BETA TRICHOSANTHIN; CALCAELIN; CHARANTIN; CHARYBDIN; COCHININ B; DIZOCILPINE; HERBACEOUS AGENT; IMMUNOTOXIN; KIRILOWIN; LUFFACULIN; LUFFACYLIN; LUFFANGULIN; LUFFIN; MOMORDIN; MOMORGROSVIN; MOSCHIN; NEOTRICHOCANTIN; NEUROTOXIN; PISAVIN; RIBOSOME INACTIVATING PROTEIN; RIBOSOME INACTIVATING PROTEIN 1; SAPORIN; TEXANIN; TRICHOKIRIN S; TRICHOSANTHIN; UNCLASSIFIED DRUG; UNINDEXED DRUG; VEGETABLE PROTEIN;

EID: 77950166344     PISSN: 13892037     EISSN: None     Source Type: Journal    
DOI: 10.2174/138920310790274662     Document Type: Review
Times cited : (65)

References (190)
  • 1
    • 15944368960 scopus 로고    scopus 로고
    • Recent advances in trichosanthin, a ribosome-inactivating protein with multiple pharmacological properties
    • Shaw, P.C.; Lee, K.M.; Wong, K.B. Recent advances in trichosanthin, a ribosome-inactivating protein with multiple pharmacological properties. Toxicon. 2005, 45(6), 683-689.
    • (2005) Toxicon , vol.45 , Issue.6 , pp. 683-689
    • Shaw, P.C.1    Lee, K.M.2    Wong, K.B.3
  • 2
    • 35348926040 scopus 로고    scopus 로고
    • Lipid transfer proteins from Brassica campestris and mung bean surpass mung bean chitinase in exploitability
    • Lin, P.; Xia, L.; Wong, J.H.; Ng, T.B.; Ye, X.; Wang, S.; Shi, X. Lipid transfer proteins from Brassica campestris and mung bean surpass mung bean chitinase in exploitability. J. Pept. Sci., 2007, 13(10), 642-648.
    • (2007) J. Pept. Sci , vol.13 , Issue.10 , pp. 642-648
    • Lin, P.1    Xia, L.2    Wong, J.H.3    Ng, T.B.4    Ye, X.5    Wang, S.6    Shi, X.7
  • 4
    • 40749104862 scopus 로고    scopus 로고
    • A Bowman-Birk trypsin inhibitor with antiproliferative activity from Hokkaido large black soybeans
    • Ho, V.S.; Ng, T.B. A Bowman-Birk trypsin inhibitor with antiproliferative activity from Hokkaido large black soybeans. J. Pept. Sci., 2008, 14(3), 278-282.
    • (2008) J. Pept. Sci , vol.14 , Issue.3 , pp. 278-282
    • Ho, V.S.1    Ng, T.B.2
  • 5
    • 57349188418 scopus 로고    scopus 로고
    • Novel insights on the mechanism of action of alpha-amylase inhibitors from the plant defensin family
    • Pelegrini, P.B.; Lay, F.T.; Murad, A.M.; Anderson, M.A.; Franco, O.L. Novel insights on the mechanism of action of alpha-amylase inhibitors from the plant defensin family. Proteins, 2008, 73(3), 719-729.
    • (2008) Proteins , vol.73 , Issue.3 , pp. 719-729
    • Pelegrini, P.B.1    Lay, F.T.2    Murad, A.M.3    Anderson, M.A.4    Franco, O.L.5
  • 7
    • 38449085362 scopus 로고    scopus 로고
    • Uses of plant lectins in bio-science and biomedicine
    • Pusztai, A.; Bardocz, S.; Ewen, S.W. Uses of plant lectins in bio-science and biomedicine. Front Biosci., 2008, 13, 1130-1140.
    • (2008) Front Biosci , vol.13 , pp. 1130-1140
    • Pusztai, A.1    Bardocz, S.2    Ewen, S.W.3
  • 10
    • 54849415693 scopus 로고    scopus 로고
    • Isolation and purification of ribosome-inactivating proteins from bitter melon seeds by ion exchange chromatographic columns in series]
    • Wang, B.; Shi, X.; Guo, C.; Ye, X.; Wang, Z.; Rao, P. Isolation and purification of ribosome-inactivating proteins from bitter melon seeds by ion exchange chromatographic columns in series] Se Pu, 2004, 22(5), 543-546.
    • (2004) Se Pu , vol.22 , Issue.5 , pp. 543-546
    • Wang, B.1    Shi, X.2    Guo, C.3    Ye, X.4    Wang, Z.5    Rao, P.6
  • 11
    • 33947110305 scopus 로고    scopus 로고
    • The non-toxic A subunit of Shiga toxin type 1 prevents replication of bovine immunodeficiency virus in infected cells
    • Ferens, WA.; Hovde, C.J. The non-toxic A subunit of Shiga toxin type 1 prevents replication of bovine immunodeficiency virus in infected cells. Virus Res., 2007, 125(1), 29-41.
    • (2007) Virus Res , vol.125 , Issue.1 , pp. 29-41
    • Ferens, W.A.1    Hovde, C.J.2
  • 12
    • 0023181362 scopus 로고
    • The immunosuppressive activities of two abortifacient proteins isolated from the seeds of bitter melon (Momordica charantia)
    • Leung, S.O.; Yeung, H.W.; Leung, K.N. The immunosuppressive activities of two abortifacient proteins isolated from the seeds of bitter melon (Momordica charantia). Immunopharmacology, 1987, 13(3), 159-171.
    • (1987) Immunopharmacology , vol.13 , Issue.3 , pp. 159-171
    • Leung, S.O.1    Yeung, H.W.2    Leung, K.N.3
  • 13
    • 33747229123 scopus 로고    scopus 로고
    • Ribosome-inactivating proteins: Progress and problems
    • Review
    • Stirpe, F.; Battelli, M.G. Ribosome-inactivating proteins: progress and problems. Cell Mol. Life Sci., 2006, 63(16), 1850-1866. Review.
    • (2006) Cell Mol. Life Sci , vol.63 , Issue.16 , pp. 1850-1866
    • Stirpe, F.1    Battelli, M.G.2
  • 15
    • 3042613317 scopus 로고    scopus 로고
    • Description, distribution, activity and phylogenetic relationship of ribosome-inactivating proteins in plants, fungi and bacteria
    • Girbés T, Ferreras JM, Arias FJ, Stirpe F. Description, distribution, activity and phylogenetic relationship of ribosome-inactivating proteins in plants, fungi and bacteria. Mini Rev. Med. Chem., 2004, 4(5), 461-476.
    • (2004) Mini Rev. Med. Chem , vol.4 , Issue.5 , pp. 461-476
    • Girbés, T.1    Ferreras, J.M.2    Arias, F.J.3    Stirpe, F.4
  • 16
    • 3042658236 scopus 로고    scopus 로고
    • The structure of ribosome inactivating proteins
    • Robertus, J.D.; Monzingo, A.F. The structure of ribosome inactivating proteins. Mini Rev. Med. Chem., 2004, 4, 477-486.
    • (2004) Mini Rev. Med. Chem , vol.4 , pp. 477-486
    • Robertus, J.D.1    Monzingo, A.F.2
  • 17
    • 3042515159 scopus 로고    scopus 로고
    • Cytotoxicity and toxicity to animals and humans of ribosome-inactivating proteins
    • Battelli, M.G. Cytotoxicity and toxicity to animals and humans of ribosome-inactivating proteins. Mini Rev. Med. Chem., 2004, 4(5), 513-521.
    • (2004) Mini Rev. Med. Chem , vol.4 , Issue.5 , pp. 513-521
    • Battelli, M.G.1
  • 18
    • 3042609680 scopus 로고    scopus 로고
    • Ribosome-inactivating, proteins: Entry into mammalian cells and intracellular routing
    • Roberts, L.M.; Lord, J.M.; Ribosome-inactivating, proteins: entry into mammalian cells and intracellular routing. Mini Rev. Med. Chem., 2004, 4, 505-512.
    • (2004) Mini Rev. Med. Chem , vol.4 , pp. 505-512
    • Roberts, L.M.1    Lord, J.M.2
  • 19
    • 10744226691 scopus 로고    scopus 로고
    • Substrate binding and catalysis in trichosanthin occur in different sites as revealed by the complex structures of several E85 mutants
    • Guo, Q.; Zhou, W.; Too, H.M.; Li, J.; Liu, Y.; Bartlam, M.; Dong, Y.; Wong, K.B.; Shaw, P.C.; Rao, Z.; Substrate binding and catalysis in trichosanthin occur in different sites as revealed by the complex structures of several E85 mutants. Protein Eng., 2003, 16(6), 391-396.
    • (2003) Protein Eng , vol.16 , Issue.6 , pp. 391-396
    • Guo, Q.1    Zhou, W.2    Too, H.M.3    Li, J.4    Liu, Y.5    Bartlam, M.6    Dong, Y.7    Wong, K.B.8    Shaw, P.C.9    Rao, Z.10
  • 20
    • 0030019277 scopus 로고    scopus 로고
    • Wong, R.N.; Dong, T.X.; Ng, T.B.; Choi, W.T.; Yeung, H.W. alpha-Kirilowin, a novel ribosome-inactivating protein from seeds of Trichosanthes kirilowii (family Cucurbitaceae): a comparison with beta-kirilowin and other related proteins. Int. J. Pept. Protein Res., 1996, 47(1-2), 103-109.
    • Wong, R.N.; Dong, T.X.; Ng, T.B.; Choi, W.T.; Yeung, H.W. alpha-Kirilowin, a novel ribosome-inactivating protein from seeds of Trichosanthes kirilowii (family Cucurbitaceae): a comparison with beta-kirilowin and other related proteins. Int. J. Pept. Protein Res., 1996, 47(1-2), 103-109.
  • 21
    • 0028291183 scopus 로고
    • Isolation and characterization of a novel ribosome-inactivating protein, betakirilowin, from the seeds of Trichosanthes kirilowii
    • Dong, T.X.; Ng, T.B.; Yeung, H.W., Wong, R.N. Isolation and characterization of a novel ribosome-inactivating protein, betakirilowin, from the seeds of Trichosanthes kirilowii. Biochem. Biophys. Res. Commun., 1994, 199(1), 387-393.
    • (1994) Biochem. Biophys. Res. Commun , vol.199 , Issue.1 , pp. 387-393
    • Dong, T.X.1    Ng, T.B.2    Yeung, H.W.3    Wong, R.N.4
  • 22
    • 0032759183 scopus 로고    scopus 로고
    • Role of Arg163 in the N-glycosidase activity of neo-trichosanthin
    • Li, H.G.; Xu, S.Z.; Wu, S.; Yan, L.; Li, J.H.; Wong, R.N.; Shi, Q.L.; Dong, Y.C. Role of Arg163 in the N-glycosidase activity of neo-trichosanthin. Protein Eng., 1999, 12(11), 999-1004.
    • (1999) Protein Eng , vol.12 , Issue.11 , pp. 999-1004
    • Li, H.G.1    Xu, S.Z.2    Wu, S.3    Yan, L.4    Li, J.H.5    Wong, R.N.6    Shi, Q.L.7    Dong, Y.C.8
  • 23
    • 0023120604 scopus 로고
    • Beta-trichosanthin: A new abortifacient protein from the Chinese drug, wangua, Trichosanthes cucumeroides
    • Yeung, H.W.; Li, W.W. Beta-trichosanthin: a new abortifacient protein from the Chinese drug, wangua, Trichosanthes cucumeroides. Int. J. Pept. Protein Res., 1987, 29(3), 289-292.
    • (1987) Int. J. Pept. Protein Res , vol.29 , Issue.3 , pp. 289-292
    • Yeung, H.W.1    Li, W.W.2
  • 24
    • 0035808199 scopus 로고    scopus 로고
    • Isolation and characterization of a new ribosome inactivating protein, momorgrosvin, from seeds of the monk's fruit Momordica grosvenorii
    • Tsang, K.Y.; Ng, T.B. Isolation and characterization of a new ribosome inactivating protein, momorgrosvin, from seeds of the monk's fruit Momordica grosvenorii. Life Sci., 2001, 68(7), 773-784.
    • (2001) Life Sci , vol.68 , Issue.7 , pp. 773-784
    • Tsang, K.Y.1    Ng, T.B.2
  • 25
    • 0026648952 scopus 로고
    • Two proteins with ribosome- inactivating, cytotoxic and abortifacient activities from seeds of Luffa cylindrica roem (Cucurbitaceae)
    • Ng, T.B.; Wong, R.N.; Yeung, H.W. Two proteins with ribosome- inactivating, cytotoxic and abortifacient activities from seeds of Luffa cylindrica roem (Cucurbitaceae). Biochem. Int., 1992, 27(2), 197-207.
    • (1992) Biochem. Int , vol.27 , Issue.2 , pp. 197-207
    • Ng, T.B.1    Wong, R.N.2    Yeung, H.W.3
  • 26
    • 0035824775 scopus 로고    scopus 로고
    • Purification of allivin, a novel antifungal protein from bulbs of the round-cloved garlic
    • Wang, H.X.; Ng, T.B. Purification of allivin, a novel antifungal protein from bulbs of the round-cloved garlic. Life Sci., 2001, 70(3), 357-365.
    • (2001) Life Sci , vol.70 , Issue.3 , pp. 357-365
    • Wang, H.X.1    Ng, T.B.2
  • 27
    • 33745245990 scopus 로고    scopus 로고
    • Isolation, characterization, sequencing and crystal structure of charybdin, a type 1 ribosome-inactivating protein from Charybdis maritima agg
    • Touloupakis, E.;Gessmann, R.; Kavelaki, K.; Christofakis, E.; Petratos, K.; Ghanotakis, D.F. Isolation, characterization, sequencing and crystal structure of charybdin, a type 1 ribosome-inactivating protein from Charybdis maritima agg. FEBS J., 2006, 273(12), 2684-2692.
    • (2006) FEBS J , vol.273 , Issue.12 , pp. 2684-2692
    • Touloupakis, E.1    Gessmann, R.2    Kavelaki, K.3    Christofakis, E.4    Petratos, K.5    Ghanotakis, D.F.6
  • 28
    • 33748751006 scopus 로고    scopus 로고
    • Sequence determination of lychnin, a type 1 ribosome-inactivating protein from Lychnis chalcedonica seeds
    • Chambery, A.; de Donatom, A.; Bolognesi, A.; Polito, L.; Stirpe, F.; Parente A. Sequence determination of lychnin, a type 1 ribosome-inactivating protein from Lychnis chalcedonica seeds. Biol. Chem., 2006, 387(9), 1261-1266.
    • (2006) Biol. Chem , vol.387 , Issue.9 , pp. 1261-1266
    • Chambery, A.1    de Donatom, A.2    Bolognesi, A.3    Polito, L.4    Stirpe, F.5    Parente, A.6
  • 29
    • 33747879020 scopus 로고    scopus 로고
    • Purification, characterization and cloning of antiviral/ ribosome inactivating protein from Amaranthus tricolor leaves
    • Roy, S.; Sadhana, P.; Begum, M.; Kumar, S.; Lodha, M.L.; Kapoor, H.C. Purification, characterization and cloning of antiviral/ ribosome inactivating protein from Amaranthus tricolor leaves. Phytochemistry, 2006, 67(17), 1865-1873.
    • (2006) Phytochemistry , vol.67 , Issue.17 , pp. 1865-1873
    • Roy, S.1    Sadhana, P.2    Begum, M.3    Kumar, S.4    Lodha, M.L.5    Kapoor, H.C.6
  • 30
  • 31
    • 33847399669 scopus 로고    scopus 로고
    • Invariant Ser211 is involved in the catalysis of PD-L4, type I RIP from Phytolacca dioica leaves
    • Chambery, A.; Pisante, M.; Di Maro, A.; Di Zazzo, E.; Ruvo, M.; Costantini, S.; Colonna, G.; Parente, A. Invariant Ser211 is involved in the catalysis of PD-L4, type I RIP from Phytolacca dioica leaves. Proteins, 2007, 67(1), 209-218.
    • (2007) Proteins , vol.67 , Issue.1 , pp. 209-218
    • Chambery, A.1    Pisante, M.2    Di Maro, A.3    Di Zazzo, E.4    Ruvo, M.5    Costantini, S.6    Colonna, G.7    Parente, A.8
  • 33
    • 33847634392 scopus 로고    scopus 로고
    • a novel ribosome-inactivating protein from the seeds of Momordica cochinchinensis
    • Chuethong, J.; Oda, K.; Sakurai, H.; Saiki, I.; Leelamanit, W.; Cochinin, B. a novel ribosome-inactivating protein from the seeds of Momordica cochinchinensis. Biol. Pharm. Bull., 2007, 30(3), 428-432.
    • (2007) Biol. Pharm. Bull , vol.30 , Issue.3 , pp. 428-432
    • Chuethong, J.1    Oda, K.2    Sakurai, H.3    Saiki, I.4    Leelamanit, W.5    Cochinin, B.6
  • 34
    • 34248579289 scopus 로고    scopus 로고
    • Isolation and characterization of ribosome-inactivating proteins from Cucurbitaceae
    • Zhang, D.; Halaweish, F.T. Isolation and characterization of ribosome-inactivating proteins from Cucurbitaceae. Chem. Biodivers., 2007, 4(3), 431-442.
    • (2007) Chem. Biodivers , vol.4 , Issue.3 , pp. 431-442
    • Zhang, D.1    Halaweish, F.T.2
  • 35
    • 38449105302 scopus 로고    scopus 로고
    • Xu, L.; Wang, Y.; Wang, L.; Gao, Y.; An, C. TYchi, a novel chitinase with RNA N-glycosidase and anti-tumor activities. Front Biosci., 2008, 13, 3127-3135.
    • Xu, L.; Wang, Y.; Wang, L.; Gao, Y.; An, C. TYchi, a novel chitinase with RNA N-glycosidase and anti-tumor activities. Front Biosci., 2008, 13, 3127-3135.
  • 37
    • 45049084882 scopus 로고    scopus 로고
    • Novel role for pectin methylesterase in Arabidopsis: A new function showing ribosome-inactivating protein (RIP) activity
    • De-la-Peña, C.; Badri, D.V.; Vivanco, J.M. Novel role for pectin methylesterase in Arabidopsis: a new function showing ribosome-inactivating protein (RIP) activity. Biochim. Biophys. Acta, 2008, 1780(5), 773-783.
    • (2008) Biochim. Biophys. Acta , vol.1780 , Issue.5 , pp. 773-783
    • De-la-Peña, C.1    Badri, D.V.2    Vivanco, J.M.3
  • 38
    • 41649094796 scopus 로고    scopus 로고
    • Cloning and expression of antiviral/ribosome-inactivating protein from Bougainvillea x buttiana
    • Choudhary, N.; Kapoor, H.C.; Lodha, M.L. Cloning and expression of antiviral/ribosome-inactivating protein from Bougainvillea x buttiana. J. Biosci., 2008, 33(1), 91-101.
    • (2008) J. Biosci , vol.33 , Issue.1 , pp. 91-101
    • Choudhary, N.1    Kapoor, H.C.2    Lodha, M.L.3
  • 39
    • 0028236694 scopus 로고
    • Luffin-S-a small novel ribosome-inactivating protein from Luffa cylindrica. Characterization and mechanism studies
    • Gao, W.; Ling, J.; Zhong, X.; Liu, W.; Zhang, R.; Yang, H.; Cao, H.; Zhang, Z. Luffin-S-a small novel ribosome-inactivating protein from Luffa cylindrica. Characterization and mechanism studies. FEBS Lett., 1994, 347(2-3), 257-260.
    • (1994) FEBS Lett , vol.347 , Issue.2-3 , pp. 257-260
    • Gao, W.1    Ling, J.2    Zhong, X.3    Liu, W.4    Zhang, R.5    Yang, H.6    Cao, H.7    Zhang, Z.8
  • 40
    • 0030569510 scopus 로고    scopus 로고
    • Characterization of the enzymatic mechanism of gamma-momorcharin, a novel ribosome-inactivating protein with lower molecular weight of 11,500 purified from the seeds of bitter gourd (Momordica charantia)
    • Pu, Z.; Lu, B.Y.; Liu, W.Y.; Jin, S.W. Characterization of the enzymatic mechanism of gamma-momorcharin, a novel ribosome-inactivating protein with lower molecular weight of 11,500 purified from the seeds of bitter gourd (Momordica charantia). Biochem. Biophys. Res. Commun., 1996, 229(1), 287-294.
    • (1996) Biochem. Biophys. Res. Commun , vol.229 , Issue.1 , pp. 287-294
    • Pu, Z.1    Lu, B.Y.2    Liu, W.Y.3    Jin, S.W.4
  • 41
    • 0037059572 scopus 로고    scopus 로고
    • Wang, H.; Ng, T.B. Luffangulin, a novel ribosome inactivating peptide from ridge gourd (Luffa acutangula) seeds. Life Sci., 2002, 70(8), 899-906.
    • Wang, H.; Ng, T.B. Luffangulin, a novel ribosome inactivating peptide from ridge gourd (Luffa acutangula) seeds. Life Sci., 2002, 70(8), 899-906.
  • 42
    • 0035996833 scopus 로고    scopus 로고
    • Isolation and characterization of luffacylin, a ribosome inactivating peptide with anti-fungal activity from sponge gourd (Luffa cylindrica) seeds
    • Parkash, A.; Ng, T.B.; Tso, W.W. Isolation and characterization of luffacylin, a ribosome inactivating peptide with anti-fungal activity from sponge gourd (Luffa cylindrica) seeds. Peptides, 2002, 23(6), 1019-1024.
    • (2002) Peptides , vol.23 , Issue.6 , pp. 1019-1024
    • Parkash, A.1    Ng, T.B.2    Tso, W.W.3
  • 43
    • 0036226097 scopus 로고    scopus 로고
    • Purification and characterization of charantin, a napin-like ribosome-inactivating peptide from bitter gourd (Momordica charantia) seeds
    • Parkash, A.; Ng, T.B.; Tso, W.W. Purification and characterization of charantin, a napin-like ribosome-inactivating peptide from bitter gourd (Momordica charantia) seeds. J. Pept. Res., 2002, 59(5), 197-202.
    • (2002) J. Pept. Res , vol.59 , Issue.5 , pp. 197-202
    • Parkash, A.1    Ng, T.B.2    Tso, W.W.3
  • 44
    • 0036422777 scopus 로고    scopus 로고
    • Purification and characterization of moschins, arginine-glutamate-rich proteins with translation inhibiting activity from brown pumpkin (Cucurbita moschata) seeds
    • Ng, T.B.; Parkash, A.; Tso, W.W. Purification and characterization of moschins, arginine-glutamate-rich proteins with translation inhibiting activity from brown pumpkin (Cucurbita moschata) seeds. Protein Expr. Purif., 2002, 26(1), 9-13.
    • (2002) Protein Expr. Purif , vol.26 , Issue.1 , pp. 9-13
    • Ng, T.B.1    Parkash, A.2    Tso, W.W.3
  • 45
    • 0037258691 scopus 로고    scopus 로고
    • Purification and characterization of alpha- and beta-benincasins, arginine/glutamate-rich peptides with translation-inhibiting activity from wax gourd seeds
    • Ng, T.B.; Parkash, A.; Tso, W.W. Purification and characterization of alpha- and beta-benincasins, arginine/glutamate-rich peptides with translation-inhibiting activity from wax gourd seeds. Peptides, 2003, 24(1), 11-6.
    • (2003) Peptides , vol.24 , Issue.1 , pp. 11-16
    • Ng, T.B.1    Parkash, A.2    Tso, W.W.3
  • 46
    • 0347594322 scopus 로고    scopus 로고
    • Purification and characterization of trichokirin-S1, a novel ribosomeinactivating peptide from seeds of Trichosanthes kirilowii
    • Li, F.; Yang, X.X.; Hu, W.G.; Xia, H.C.; Li, Z.; Zhang, Z.C. Purification and characterization of trichokirin-S1, a novel ribosomeinactivating peptide from seeds of Trichosanthes kirilowii Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2003, 35(9), 841-846.
    • (2003) Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai) , vol.35 , Issue.9 , pp. 841-846
    • Li, F.1    Yang, X.X.2    Hu, W.G.3    Xia, H.C.4    Li, Z.5    Zhang, Z.C.6
  • 47
    • 0034644716 scopus 로고    scopus 로고
    • Wang, H.X.; Ng, T.B. Lagenin, a novel ribosome-inactivating protein with ribonucleolytic activity from bottle gourd (Lagenaria siceraria) seeds. Life Sci., 2000, 67(21), 2631-2638.
    • Wang, H.X.; Ng, T.B. Lagenin, a novel ribosome-inactivating protein with ribonucleolytic activity from bottle gourd (Lagenaria siceraria) seeds. Life Sci., 2000, 67(21), 2631-2638.
  • 48
    • 0036417228 scopus 로고    scopus 로고
    • Ng, T.B.; Parkash, A. Hispin, a novel ribosome inactivating protein with antifungal activity from hairy melon seeds. Protein Expr. Purif., 2002, 26(2), 211-217.
    • Ng, T.B.; Parkash, A. Hispin, a novel ribosome inactivating protein with antifungal activity from hairy melon seeds. Protein Expr. Purif., 2002, 26(2), 211-217.
  • 49
    • 0032501473 scopus 로고    scopus 로고
    • Purification and characterization of novel ribosome inactivating proteins, alpha- and beta-pisavins, from seeds of the garden pea Pisum sativum
    • Lam, S.S.; Wang, H.; Ng, T.B. Purification and characterization of novel ribosome inactivating proteins, alpha- and beta-pisavins, from seeds of the garden pea Pisum sativum. Biochem. Biophys. Res. Commun., 1998, 253(1), 135-142.
    • (1998) Biochem. Biophys. Res. Commun , vol.253 , Issue.1 , pp. 135-142
    • Lam, S.S.1    Wang, H.2    Ng, T.B.3
  • 50
    • 0037362020 scopus 로고    scopus 로고
    • Ng, T.B.; Lam, Y.W.; Wang, H. Calcaelin, a new protein with translation-inhibiting, antiproliferative and antimitogenic activities from the mosaic puffball mushroom Calvatia caelata. Planta Med., 2003, 69(3), 212-217.
    • Ng, T.B.; Lam, Y.W.; Wang, H. Calcaelin, a new protein with translation-inhibiting, antiproliferative and antimitogenic activities from the mosaic puffball mushroom Calvatia caelata. Planta Med., 2003, 69(3), 212-217.
  • 51
    • 0034488562 scopus 로고    scopus 로고
    • Wang, H.X.; Ng, T.B. Flammulin: a novel ribosome-inactivating protein from fruiting bodies of the winter mushroom Flammulina velutipes. Biochem. Cell Biol., 2000, 78(6), 699-702.
    • Wang, H.X.; Ng, T.B. Flammulin: a novel ribosome-inactivating protein from fruiting bodies of the winter mushroom Flammulina velutipes. Biochem. Cell Biol., 2000, 78(6), 699-702.
  • 52
    • 0035937399 scopus 로고    scopus 로고
    • Isolation and characterization of velutin, a novel low-molecular-weight ribosome-inactivating protein from winter mushroom (Flammulina velutipes) fruiting bodies
    • Wang, H.; Ng, T.B. Isolation and characterization of velutin, a novel low-molecular-weight ribosome-inactivating protein from winter mushroom (Flammulina velutipes) fruiting bodies. Life Sci., 2001, 68(18), 2151-2158.
    • (2001) Life Sci , vol.68 , Issue.18 , pp. 2151-2158
    • Wang, H.1    Ng, T.B.2
  • 53
    • 0034804852 scopus 로고    scopus 로고
    • Lam, S.K.; Ng, T.B. Hypsin, a novel thermostable ribosome-inactivating protein with antifungal and antiproliferative activities from fruiting bodies of the edible mushroom Hypsizigus marmoreus. Biochem. Biophys. Res. Commun., 2001, 285(4), 1071-1075.
    • Lam, S.K.; Ng, T.B. Hypsin, a novel thermostable ribosome-inactivating protein with antifungal and antiproliferative activities from fruiting bodies of the edible mushroom Hypsizigus marmoreus. Biochem. Biophys. Res. Commun., 2001, 285(4), 1071-1075.
  • 54
    • 0035884010 scopus 로고    scopus 로고
    • First simultaneous isolation of a ribosome inactivating protein and an antifungal protein from a mushroom (Lyophyllum shimeji) together with evidence for synergism of their antifungal effects
    • Lam, S.K.; Ng, T.B. First simultaneous isolation of a ribosome inactivating protein and an antifungal protein from a mushroom (Lyophyllum shimeji) together with evidence for synergism of their antifungal effects. Arch. Biochem. Biophys., 2001, 393(2), 271-280.
    • (2001) Arch. Biochem. Biophys , vol.393 , Issue.2 , pp. 271-280
    • Lam, S.K.1    Ng, T.B.2
  • 55
    • 57249115911 scopus 로고    scopus 로고
    • Wong, J.H.; Wang, H.X.; Ng, T.B. Marmorin, a new ribosome inactivating protein with antiproliferative and HIV-1 reverse transcriptase inhibitory activities from the mushroom Hypsizigus marmoreus. Appl. Mircrobiol. Biotechnol., 2008, 81(4), 669-674.
    • Wong, J.H.; Wang, H.X.; Ng, T.B. Marmorin, a new ribosome inactivating protein with antiproliferative and HIV-1 reverse transcriptase inhibitory activities from the mushroom Hypsizigus marmoreus. Appl. Mircrobiol. Biotechnol., 2008, 81(4), 669-674.
  • 56
    • 0035798226 scopus 로고    scopus 로고
    • Isolation of pleuturegin, a novel ribosome-inactivating protein from fresh sclerotia of the edible mushroom Pleurotus tuber-regium
    • Wang, H.X.; Ng, T.B. Isolation of pleuturegin, a novel ribosome-inactivating protein from fresh sclerotia of the edible mushroom Pleurotus tuber-regium. Biochem. Biophys. Res. Commun., 2001, 288(3), 718-721.
    • (2001) Biochem. Biophys. Res. Commun , vol.288 , Issue.3 , pp. 718-721
    • Wang, H.X.1    Ng, T.B.2
  • 57
    • 0042026112 scopus 로고    scopus 로고
    • Isolation and Characterization of a type 1 ribosome-inactivating protein from fruiting bodies of the edible mushroom (Volvariella volvacea)
    • Yao, Q.Z.; Yu, M.M.; Ooi, L.S.; Ng, T.B.; Chang, S.T.; Sun, S.S.; Ooi, V.E. Isolation and Characterization of a type 1 ribosome-inactivating protein from fruiting bodies of the edible mushroom (Volvariella volvacea). J. Agric. Food Chem., 1998, 46(2), 788-792.
    • (1998) J. Agric. Food Chem , vol.46 , Issue.2 , pp. 788-792
    • Yao, Q.Z.1    Yu, M.M.2    Ooi, L.S.3    Ng, T.B.4    Chang, S.T.5    Sun, S.S.6    Ooi, V.E.7
  • 58
    • 0028144743 scopus 로고    scopus 로고
    • Lin, A.; Lee, T.M.; Rern, J.C. Tricholin, a new antifungal agent from Trichoderma viride, and its action in biological control of Rhizoctonia solani. J. Antibiot. (Tokyo), 1994, 47(7), 799-805.
    • Lin, A.; Lee, T.M.; Rern, J.C. Tricholin, a new antifungal agent from Trichoderma viride, and its action in biological control of Rhizoctonia solani. J. Antibiot. (Tokyo), 1994, 47(7), 799-805.
  • 60
    • 0027981963 scopus 로고
    • Purification and characterization of a ribonuclease from Aspergillus giganteus IFO 5818, the gigantin. Immunological and enzymic comparison with alphasarcin
    • Salvarelli, S.; Muñoz, S.; Conde, F.P. Purification and characterization of a ribonuclease from Aspergillus giganteus IFO 5818, the gigantin. Immunological and enzymic comparison with alphasarcin. Eur. J. Biochem., 1994, 225(1), 243-251.
    • (1994) Eur. J. Biochem , vol.225 , Issue.1 , pp. 243-251
    • Salvarelli, S.1    Muñoz, S.2    Conde, F.P.3
  • 61
    • 0037442015 scopus 로고    scopus 로고
    • Suppression of NF-kappa B activation and proinflammatory cytokine expression by Shiga toxin-producing Escherichia coli
    • Hauf, N.; Caraborty, T. Suppression of NF-kappa B activation and proinflammatory cytokine expression by Shiga toxin-producing Escherichia coli. J. Immunol., 2003, 170, 2074-2082.
    • (2003) J. Immunol , vol.170 , pp. 2074-2082
    • Hauf, N.1    Caraborty, T.2
  • 62
    • 34248590284 scopus 로고    scopus 로고
    • X-ray sequence and crystal structure of luffaculin 1, a novel type 1 ribosome-inactivating protein
    • Hou, X.; Chen, M.; Chen, L.; Meehan, E.J.; Xie, J.; Huang, M. X-ray sequence and crystal structure of luffaculin 1, a novel type 1 ribosome-inactivating protein. BMC Struct. Biol., 2007, 7, 29.
    • (2007) BMC Struct. Biol , vol.7 , pp. 29
    • Hou, X.1    Chen, M.2    Chen, L.3    Meehan, E.J.4    Xie, J.5    Huang, M.6
  • 63
    • 0034141384 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of luffaculin, a ribosome-inactivating protein from sponge-gourd seeds
    • Ma, Q.; Yao, G.; Wu, S.; Li, H.; Li, J.; Dong, Y. Crystallization and preliminary X-ray analysis of luffaculin, a ribosome-inactivating protein from sponge-gourd seeds. Acta Crystallogr. D Biol. Crystallogr., 2000, 56(Pt 2), 185-186.
    • (2000) Acta Crystallogr. D Biol. Crystallogr , vol.56 , Issue.PART 2 , pp. 185-186
    • Ma, Q.1    Yao, G.2    Wu, S.3    Li, H.4    Li, J.5    Dong, Y.6
  • 64
    • 34147106119 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of PD-L1, a highly glycosylated ribosome inactivating protein with DNase activity
    • Ruggieroa, A.; Chambery, A.; Di Maro, A.; Mastroianni, A.; Parente, A.; Berisio, R. Crystallization and preliminary X-ray diffraction analysis of PD-L1, a highly glycosylated ribosome inactivating protein with DNase activity. Protein Pept. Lett., 2007, 14(4), 407-409.
    • (2007) Protein Pept. Lett , vol.14 , Issue.4 , pp. 407-409
    • Ruggieroa, A.1    Chambery, A.2    Di Maro, A.3    Mastroianni, A.4    Parente, A.5    Berisio, R.6
  • 65
    • 33846023062 scopus 로고    scopus 로고
    • Ruggiero, A.; Chambery, A.; Di, Maro. A.; Pisante, M.; Parente, A.; Berisio, R. Crystallization and preliminary X-ray diffraction analysis of PD-L4, a ribosome inactivating protein from Phytolacca dioica L. leaves. Protein Pept. Lett., 2007, 14(1), 97-100.
    • Ruggiero, A.; Chambery, A.; Di, Maro. A.; Pisante, M.; Parente, A.; Berisio, R. Crystallization and preliminary X-ray diffraction analysis of PD-L4, a ribosome inactivating protein from Phytolacca dioica L. leaves. Protein Pept. Lett., 2007, 14(1), 97-100.
  • 66
    • 33748178290 scopus 로고    scopus 로고
    • Pokeweed antiviral protein depurinates the sarcin/ricin loop of the rRNA prior to binding of aminoacyl-tRNA to the ribosomal A-site
    • Mansouri, S.; Nourollahzadeh, E.; Hudak, K.A. Pokeweed antiviral protein depurinates the sarcin/ricin loop of the rRNA prior to binding of aminoacyl-tRNA to the ribosomal A-site. RNA, 2006, 12(9), 1683-1692.
    • (2006) RNA , vol.12 , Issue.9 , pp. 1683-1692
    • Mansouri, S.1    Nourollahzadeh, E.2    Hudak, K.A.3
  • 67
    • 34249778366 scopus 로고    scopus 로고
    • Roday, S.; Saen-oon, S.; Schramm, V.L. Vinyldeoxyadenosine in a sarcin-ricin RNA loop and its binding to ricin toxin a-chain. Biochemistry, 2007, 46(21), 6169-6182.
    • Roday, S.; Saen-oon, S.; Schramm, V.L. Vinyldeoxyadenosine in a sarcin-ricin RNA loop and its binding to ricin toxin a-chain. Biochemistry, 2007, 46(21), 6169-6182.
  • 68
    • 33644854446 scopus 로고    scopus 로고
    • A novel interaction of pokeweed antiviral protein with translation initiation factors 4G and iso4G: A potential indirect mechanism to access viral RNAs
    • Wang, M.; Hudak, K.A. A novel interaction of pokeweed antiviral protein with translation initiation factors 4G and iso4G: a potential indirect mechanism to access viral RNAs. Nucleic Acids Res., 2006, 4, 174-181.
    • (2006) Nucleic Acids Res , vol.4 , pp. 174-181
    • Wang, M.1    Hudak, K.A.2
  • 69
    • 33847383363 scopus 로고    scopus 로고
    • The C-terminus of pokeweed antiviral protein has distinct roles in transport to the cytosol, ribosome depurination and cytotoxicity
    • Baykal, U.; Tumer, N.E. The C-terminus of pokeweed antiviral protein has distinct roles in transport to the cytosol, ribosome depurination and cytotoxicity. Plant J., 2007, 49(6), 995-1007.
    • (2007) Plant J , vol.49 , Issue.6 , pp. 995-1007
    • Baykal, U.1    Tumer, N.E.2
  • 70
    • 42749094248 scopus 로고    scopus 로고
    • Pokeweed antiviral protein region Gly209-Lys225 is critical for RNA N-glycosidase activity of the prokaryotic ribosome
    • Nagasawa, Y.; Fujii,K.; Yoshikawa, T.; Kobayashi, Y.; Kondo, T. Pokeweed antiviral protein region Gly209-Lys225 is critical for RNA N-glycosidase activity of the prokaryotic ribosome. Phytochemistry, 2008, 69(8), 1653-1660.
    • (2008) Phytochemistry , vol.69 , Issue.8 , pp. 1653-1660
    • Nagasawa, Y.1    Fujii, K.2    Yoshikawa, T.3    Kobayashi, Y.4    Kondo, T.5
  • 71
    • 40849106335 scopus 로고    scopus 로고
    • The C-terminal end of P proteins mediates ribosome inactivation by trichosanthin but does not affect the pokeweed antiviral protein activity
    • Ayub, M.J.; Smulski, C.R.; Ma, K.W.; Levin, M.J.; Shaw, P.C.; Wong, K.B. The C-terminal end of P proteins mediates ribosome inactivation by trichosanthin but does not affect the pokeweed antiviral protein activity. Biochem. Biophys. Res. Commun., 2008, 369(2), 314-319
    • (2008) Biochem. Biophys. Res. Commun , vol.369 , Issue.2 , pp. 314-319
    • Ayub, M.J.1    Smulski, C.R.2    Ma, K.W.3    Levin, M.J.4    Shaw, P.C.5    Wong, K.B.6
  • 72
    • 34247135324 scopus 로고    scopus 로고
    • Interaction between trichosanthin, a ribosome-inactivating protein, and the ribosomal stalk protein P2 by chemical shift perturbation and mutagenesis analyses
    • Chan, D.S.; Chu, L.O.; Lee, K.M.; Too, P.H.; Ma, K.W.; Sze, K.H.; Zhu, G.; Shaw, P.C.; Wong, K.B. Interaction between trichosanthin, a ribosome-inactivating protein, and the ribosomal stalk protein P2 by chemical shift perturbation and mutagenesis analyses. Nucleic Acids Res., 2007, 35(5), 1660-1672.
    • (2007) Nucleic Acids Res , vol.35 , Issue.5 , pp. 1660-1672
    • Chan, D.S.1    Chu, L.O.2    Lee, K.M.3    Too, P.H.4    Ma, K.W.5    Sze, K.H.6    Zhu, G.7    Shaw, P.C.8    Wong, K.B.9
  • 73
    • 57349096048 scopus 로고    scopus 로고
    • Low numbers of intestinal Shiga toxin-producing E. coli correlate with a poor prognosis in sheep infected with bovine leukemia virus
    • Ferens, W.A.; Haruna, J.; Cobbold, R.; Hovde, C.J. Low numbers of intestinal Shiga toxin-producing E. coli correlate with a poor prognosis in sheep infected with bovine leukemia virus. J. Vet. Sci., 2008, 9(4), 375-379.
    • (2008) J. Vet. Sci , vol.9 , Issue.4 , pp. 375-379
    • Ferens, W.A.1    Haruna, J.2    Cobbold, R.3    Hovde, C.J.4
  • 74
    • 34548348189 scopus 로고    scopus 로고
    • Evidence for the importance of electrostatics in the function of two distinct families of ribosome inactivating toxins
    • Korennykh, A.V.; Correll, C.C.; Piccirilli, J.A. Evidence for the importance of electrostatics in the function of two distinct families of ribosome inactivating toxins. RNA, 2007, 13(9), 1391-1396.
    • (2007) RNA , vol.13 , Issue.9 , pp. 1391-1396
    • Korennykh, A.V.1    Correll, C.C.2    Piccirilli, J.A.3
  • 75
    • 39549084730 scopus 로고    scopus 로고
    • Expression and purification of cysteine introduced recombinant saporin
    • Günhan, E.; Swe, M.; Palazoglu, M.; Voss, J.C.; Chalupa, L.M. Expression and purification of cysteine introduced recombinant saporin. Protein Expr. Purif. 2008, 58(2), 203-209.
    • (2008) Protein Expr. Purif , vol.58 , Issue.2 , pp. 203-209
    • Günhan, E.1    Swe, M.2    Palazoglu, M.3    Voss, J.C.4    Chalupa, L.M.5
  • 76
    • 43049120195 scopus 로고    scopus 로고
    • RIP and RALyase cleave the sarcin/ricin domain, a critical domain for ribosome function, during senescence of wheat coleoptiles
    • Sawasaki, T.; Nishihara, M.; Endo, Y. RIP and RALyase cleave the sarcin/ricin domain, a critical domain for ribosome function, during senescence of wheat coleoptiles. Biochem. Biophys. Res. Commun., 2008, 370(4), 561-565.
    • (2008) Biochem. Biophys. Res. Commun , vol.370 , Issue.4 , pp. 561-565
    • Sawasaki, T.1    Nishihara, M.2    Endo, Y.3
  • 77
    • 34548139406 scopus 로고    scopus 로고
    • Expression of a ribosome-inactivating protein gene in bitter melon is induced by Sphaerotheca fuliginea and abiotic stimuli
    • Xu, J.; Wang, H.; Fan, J. Expression of a ribosome-inactivating protein gene in bitter melon is induced by Sphaerotheca fuliginea and abiotic stimuli. Biotechnol. Lett., 2007, 29(10), 1605-1610.
    • (2007) Biotechnol. Lett , vol.29 , Issue.10 , pp. 1605-1610
    • Xu, J.1    Wang, H.2    Fan, J.3
  • 78
    • 38349193455 scopus 로고    scopus 로고
    • Transgenic tobacco plants with ribosome inactivating protein gene cassin from Cassia occidentalis and their resistance to tobacco mosaic virus
    • Ruan, X.L.; Liu, L.F.; Li, H.P.; Transgenic tobacco plants with ribosome inactivating protein gene cassin from Cassia occidentalis and their resistance to tobacco mosaic virus. Zhi Wu Sheng Li Yu Fen Zi Sheng Wu Xue Xue Bao. 2007, 33(6), 517-523.
    • (2007) Zhi Wu Sheng Li Yu Fen Zi Sheng Wu Xue Xue Bao , vol.33 , Issue.6 , pp. 517-523
    • Ruan, X.L.1    Liu, L.F.2    Li, H.P.3
  • 79
    • 41749112638 scopus 로고    scopus 로고
    • Ribonuclease, deoxy-ribonuclease, and antiviral activity of Escherichia coli-expressed Bougainvillea xbuttiana antiviral protein
    • Choudhary, N.L.; Yadav, O.P.; Lodha, M.L. Ribonuclease, deoxy-ribonuclease, and antiviral activity of Escherichia coli-expressed Bougainvillea xbuttiana antiviral protein. Biochemistry (Mosc), 2008, 73(3), 273-277.
    • (2008) Biochemistry (Mosc) , vol.73 , Issue.3 , pp. 273-277
    • Choudhary, N.L.1    Yadav, O.P.2    Lodha, M.L.3
  • 80
    • 33746889828 scopus 로고    scopus 로고
    • Trichosanthin suppresses the elevation of p38 MAPK, and Bcl-2 induced by HSV-1 infection in Vero cells
    • Huang, H.; Chan, H.; Wang, Y.Y.; Ouyang, D.Y.; Zheng, Y.T.; Tam, S.C. Trichosanthin suppresses the elevation of p38 MAPK, and Bcl-2 induced by HSV-1 infection in Vero cells. Life Sci., 2006, 79(13), 1287-1292.
    • (2006) Life Sci , vol.79 , Issue.13 , pp. 1287-1292
    • Huang, H.1    Chan, H.2    Wang, Y.Y.3    Ouyang, D.Y.4    Zheng, Y.T.5    Tam, S.C.6
  • 81
    • 33745638511 scopus 로고    scopus 로고
    • Protective effects of trichosanthin in Herpes simplex virus-1 encephalitis in mice
    • Chen, G.F.; Huang, W.G.; Chen, F.Y.; Shan, J.L.; Protective effects of trichosanthin in Herpes simplex virus-1 encephalitis in mice. Zhongguo Dang Dai Er Ke Za Zhi, 2006, 8(3), 239-241.
    • (2006) Zhongguo Dang Dai Er Ke Za Zhi , vol.8 , Issue.3 , pp. 239-241
    • Chen, G.F.1    Huang, W.G.2    Chen, F.Y.3    Shan, J.L.4
  • 82
    • 28144457267 scopus 로고    scopus 로고
    • An inhibitor of c-Jun N-terminal kinases (CEP-11004) counteracts the anti-HIV-1 action of trichosanthin
    • Ouyang, D.Y.; Chan, H.; Wang, Y.Y.; Huang, H.; Tam, S.C.; Zheng, Y.T. An inhibitor of c-Jun N-terminal kinases (CEP-11004) counteracts the anti-HIV-1 action of trichosanthin. Biochem. Biophys. Res. Commun., 2006, 339(1), 25-29.
    • (2006) Biochem. Biophys. Res. Commun , vol.339 , Issue.1 , pp. 25-29
    • Ouyang, D.Y.1    Chan, H.2    Wang, Y.Y.3    Huang, H.4    Tam, S.C.5    Zheng, Y.T.6
  • 83
    • 33646067140 scopus 로고    scopus 로고
    • Y55 and D78 are crucial amino acid residues of a new IgE epitope on trichosanthin
    • Zhang, X.Y.; Wu, Y.; Yan, J.Y.; Gao, Y.; Wang, Y.; Mi, S.L.; An, C.C. Y55 and D78 are crucial amino acid residues of a new IgE epitope on trichosanthin. Biochem. Biophys. Res. Commun., 2006, 343(4), 1251-1256.
    • (2006) Biochem. Biophys. Res. Commun , vol.343 , Issue.4 , pp. 1251-1256
    • Zhang, X.Y.1    Wu, Y.2    Yan, J.Y.3    Gao, Y.4    Wang, Y.5    Mi, S.L.6    An, C.C.7
  • 85
    • 33749360551 scopus 로고    scopus 로고
    • Mapping the antigenic determinants and reducing the immunogenicity of trichosanthin by site-directed mutagenesis
    • An, Q.; Wei, S.; Mu, S.; Zhang, X.; Lei, Y.; Zhang, W.; Jia, N.; Cheng, X.; Fan, A.; Li, Z.; Xu, Z. Mapping the antigenic determinants and reducing the immunogenicity of trichosanthin by site-directed mutagenesis. J. Biomed. Sci., 2006, 13(5), 637-643.
    • (2006) J. Biomed. Sci , vol.13 , Issue.5 , pp. 637-643
    • An, Q.1    Wei, S.2    Mu, S.3    Zhang, X.4    Lei, Y.5    Zhang, W.6    Jia, N.7    Cheng, X.8    Fan, A.9    Li, Z.10    Xu, Z.11
  • 86
    • 1642488142 scopus 로고    scopus 로고
    • Trichosanthin induces leakage and membrane fusion of liposome
    • Xia, X.F.; Zhang, F.; Shaw, P.C.; Sui, S.F. Trichosanthin induces leakage and membrane fusion of liposome. IUBMB Life, 2003, 55, 681-687.
    • (2003) IUBMB Life , vol.55 , pp. 681-687
    • Xia, X.F.1    Zhang, F.2    Shaw, P.C.3    Sui, S.F.4
  • 89
    • 38349065412 scopus 로고    scopus 로고
    • Effects of ibotenate and 192IgG-saporin lesions of the nucleus basalis magnocellularis/ substantia innominata on spontaneous sleep and wake states and on recovery sleep after sleep deprivation in rats
    • Kaur, S.; Junek, A.; Black, M.A.; Semba, K. Effects of ibotenate and 192IgG-saporin lesions of the nucleus basalis magnocellularis/ substantia innominata on spontaneous sleep and wake states and on recovery sleep after sleep deprivation in rats. J. Neurosci., 2008, 28(2), 491-504.
    • (2008) J. Neurosci , vol.28 , Issue.2 , pp. 491-504
    • Kaur, S.1    Junek, A.2    Black, M.A.3    Semba, K.4
  • 90
    • 33744789973 scopus 로고    scopus 로고
    • Purkinje cell loss by OX7-saporin impairs acquisition and extinction of eyeblink conditioning
    • Nolan, B.C.; Freeman, J.H. Purkinje cell loss by OX7-saporin impairs acquisition and extinction of eyeblink conditioning. Learn Mem., 2006, 13(3), 359-365.
    • (2006) Learn Mem , vol.13 , Issue.3 , pp. 359-365
    • Nolan, B.C.1    Freeman, J.H.2
  • 91
    • 36448945106 scopus 로고    scopus 로고
    • The role of the nucleus basalis of Meynert and reticular thalamic nucleus in pathogenesis of genetically determined absence epilepsy in rats: A lesion study
    • Berdiev, R.K.; Chepurnov, S.A.; Veening, J.G.; Chepurnova, N.E.; van Luijtelaar, G. The role of the nucleus basalis of Meynert and reticular thalamic nucleus in pathogenesis of genetically determined absence epilepsy in rats: a lesion study. Brain Res., 2007, 1185, 266-274.
    • (2007) Brain Res , vol.1185 , pp. 266-274
    • Berdiev, R.K.1    Chepurnov, S.A.2    Veening, J.G.3    Chepurnova, N.E.4    van Luijtelaar, G.5
  • 92
    • 33947255084 scopus 로고    scopus 로고
    • Combined damage to entorhinal cortex and cholinergic basal forebrain neurons, two early neurodegenerative features accompanying Alzheimer's disease: Effects on locomotor activity and memory functions in rats
    • Traissard, N.; Herbeaux, K.; Cosquer, B.; Jeltsch, H.; Ferry, B.; Galani, R.; Pernon, A.; Majchrzak, M.; Cassel, J.C. Combined damage to entorhinal cortex and cholinergic basal forebrain neurons, two early neurodegenerative features accompanying Alzheimer's disease: effects on locomotor activity and memory functions in rats. Neuropsychopharmacology, 2007, 32(4), 851-871.
    • (2007) Neuropsychopharmacology , vol.32 , Issue.4 , pp. 851-871
    • Traissard, N.1    Herbeaux, K.2    Cosquer, B.3    Jeltsch, H.4    Ferry, B.5    Galani, R.6    Pernon, A.7    Majchrzak, M.8    Cassel, J.C.9
  • 93
    • 33748325777 scopus 로고    scopus 로고
    • Long-term effects of neonatal basal forebrain cholinergic lesions on radial maze learning and impulsivity in rats
    • Scattoni, M.L.; Adriani, W.; Calamandrei, G.; Laviola, G.; Ricceri, L. Long-term effects of neonatal basal forebrain cholinergic lesions on radial maze learning and impulsivity in rats. Behav. Pharmacol., 2006, 17(5-6), 517-524.
    • (2006) Behav. Pharmacol , vol.17 , Issue.5-6 , pp. 517-524
    • Scattoni, M.L.1    Adriani, W.2    Calamandrei, G.3    Laviola, G.4    Ricceri, L.5
  • 94
    • 33748875466 scopus 로고    scopus 로고
    • Basal forebrain cholinergic lesions reduce heat shock protein 72 response but not pathology induced by the NMDA antagonist MK-801 in the rat cingulate cortex
    • Willis, C.L.; Ray, D.E.; Marshall, H.; Elliot, G.; Evans, J.G.; Kind, C.N. Basal forebrain cholinergic lesions reduce heat shock protein 72 response but not pathology induced by the NMDA antagonist MK-801 in the rat cingulate cortex. Neurosci. Lett., 2006, 407(2), 112-117.
    • (2006) Neurosci. Lett , vol.407 , Issue.2 , pp. 112-117
    • Willis, C.L.1    Ray, D.E.2    Marshall, H.3    Elliot, G.4    Evans, J.G.5    Kind, C.N.6
  • 95
    • 33744470103 scopus 로고    scopus 로고
    • Selective lesions of the nucleus basalis magnocellularis impair cognitive flexibility
    • Cabrera, S.M., Chavez, C.M.; Corley, S.R.; Kitto, M.R.; Butt, A.E. Selective lesions of the nucleus basalis magnocellularis impair cognitive flexibility. Behav. Neurosci., 2006; 120(2), 298-306.
    • (2006) Behav. Neurosci , vol.120 , Issue.2 , pp. 298-306
    • Cabrera, S.M.1    Chavez, C.M.2    Corley, S.R.3    Kitto, M.R.4    Butt, A.E.5
  • 96
    • 33744476430 scopus 로고    scopus 로고
    • Effect of nucleus basalis magnocellularis cholinergic lesions on fear-like and anxiety-like behavior
    • Knox, D.; Berntson, G.G. Effect of nucleus basalis magnocellularis cholinergic lesions on fear-like and anxiety-like behavior. Behav. Neurosci., 2006, 120(2), 307-312.
    • (2006) Behav. Neurosci , vol.120 , Issue.2 , pp. 307-312
    • Knox, D.1    Berntson, G.G.2
  • 97
    • 33646561257 scopus 로고    scopus 로고
    • Aversive stimulus attenuates impairment of acquisition in a delayed match to position T-maze task caused by a selective lesion of septo-hippocampal cholinergic projections
    • Fitz, N.F.; Gibbs, R.B.; Johnson, D.A. Aversive stimulus attenuates impairment of acquisition in a delayed match to position T-maze task caused by a selective lesion of septo-hippocampal cholinergic projections. Brain Res. Bull., 2006, 69(6), 660-665.
    • (2006) Brain Res. Bull , vol.69 , Issue.6 , pp. 660-665
    • Fitz, N.F.1    Gibbs, R.B.2    Johnson, D.A.3
  • 98
    • 33748751956 scopus 로고    scopus 로고
    • Lack of localization of 5-HT6 receptors on cholinergic neurons: Implication of multiple neurotransmitter systems in 5-HT6 receptor-mediated acetylcholine release
    • Marcos, B.; Gil-Bea, F.J.; Hirst, W.D.; García-Alloza, M.; Ramírez, M.J. Lack of localization of 5-HT6 receptors on cholinergic neurons: implication of multiple neurotransmitter systems in 5-HT6 receptor-mediated acetylcholine release. Eur. J. Neurosci., 2006, 24(5), 1299-1306.
    • (2006) Eur. J. Neurosci , vol.24 , Issue.5 , pp. 1299-1306
    • Marcos, B.1    Gil-Bea, F.J.2    Hirst, W.D.3    García-Alloza, M.4    Ramírez, M.J.5
  • 99
    • 33846070104 scopus 로고    scopus 로고
    • Long-term effects of immunotoxic cholinergic lesions in the septum on acquisition of the cone-field task and noncognitive measures in rats
    • van der Staay, F.J.; Bouger, P.; Lehmann, O.; Lazarus, C.; Cosquer, B.; Koenig, J.; Stump, V.; Cassel, J.C. Long-term effects of immunotoxic cholinergic lesions in the septum on acquisition of the cone-field task and noncognitive measures in rats. Hippocampus, 2006, 16(12), 1061-1079.
    • (2006) Hippocampus , vol.16 , Issue.12 , pp. 1061-1079
    • van der Staay, F.J.1    Bouger, P.2    Lehmann, O.3    Lazarus, C.4    Cosquer, B.5    Koenig, J.6    Stump, V.7    Cassel, J.C.8
  • 101
    • 35448937166 scopus 로고    scopus 로고
    • Selective immunolesion of cholinergic neurons leads to long-term changes in 5-HT2A receptor levels in hippocampus and frontal cortex
    • Severino, M.; Pedersen, A.F.; Trajkovska, V.; Christensen, E.; Lohals, R.; Veng, L.M.; Knudsen, G.M.; Aznar, S. Selective immunolesion of cholinergic neurons leads to long-term changes in 5-HT2A receptor levels in hippocampus and frontal cortex. Neurosci. Lett., 2007, 428(1), 47-51.
    • (2007) Neurosci. Lett , vol.428 , Issue.1 , pp. 47-51
    • Severino, M.1    Pedersen, A.F.2    Trajkovska, V.3    Christensen, E.4    Lohals, R.5    Veng, L.M.6    Knudsen, G.M.7    Aznar, S.8
  • 102
    • 38149098258 scopus 로고    scopus 로고
    • Up-regulation of cation-independent mannose 6-phosphate receptor and endosomal-lysosomal markers in surviving neurons after 192-IgG-saporin administrations into the adult rat brain
    • Hawkes, C.; Kabogo, D.; Amritraj, A.; Kar, S. Up-regulation of cation-independent mannose 6-phosphate receptor and endosomal-lysosomal markers in surviving neurons after 192-IgG-saporin administrations into the adult rat brain. Am. J. Pathol., 2006, 169(4), 1140-1154.
    • (2006) Am. J. Pathol , vol.169 , Issue.4 , pp. 1140-1154
    • Hawkes, C.1    Kabogo, D.2    Amritraj, A.3    Kar, S.4
  • 103
    • 34249314004 scopus 로고    scopus 로고
    • Cholinergic lesions produce task-selective effects on delayed matching to position and configural association learning related to response pattern and strategy
    • Gibbs, R.B.; Johnson, D.A.; Cholinergic lesions produce task-selective effects on delayed matching to position and configural association learning related to response pattern and strategy. Neurobiol. Learn Mem., 2007, 88(1), 19-32.
    • (2007) Neurobiol. Learn Mem , vol.88 , Issue.1 , pp. 19-32
    • Gibbs, R.B.1    Johnson, D.A.2
  • 104
    • 36749100867 scopus 로고    scopus 로고
    • Tait, D.S.; Brown, V.J. Lesions of the basal forebrain impair reversal learning but not shifting of attentional set in rats. Behav. Brain Res., 2008, 87,100-108.
    • Tait, D.S.; Brown, V.J. Lesions of the basal forebrain impair reversal learning but not shifting of attentional set in rats. Behav. Brain Res., 2008, 87,100-108.
  • 105
    • 33947251331 scopus 로고    scopus 로고
    • Selective cholinergic depletion of the hippocampus spares both behaviorally induced Arc transcription and spatial learning and memory
    • Fletcher, B.R.; Baxter, M.G.; Guzowski, J.F.; Shapiro, M.L.; Rapp, P.R. Selective cholinergic depletion of the hippocampus spares both behaviorally induced Arc transcription and spatial learning and memory. Hippocampus, 2007, 17(3), 227-234.
    • (2007) Hippocampus , vol.17 , Issue.3 , pp. 227-234
    • Fletcher, B.R.1    Baxter, M.G.2    Guzowski, J.F.3    Shapiro, M.L.4    Rapp, P.R.5
  • 106
    • 33846869280 scopus 로고    scopus 로고
    • Lesions to the nucleus basalis magnocellularis lower performance but do not block the retention of a previously acquired learning set
    • Bailey, A.M.; Lee, J.M. Lesions to the nucleus basalis magnocellularis lower performance but do not block the retention of a previously acquired learning set. Brain Res., 2007, 1136(1), 110-121.
    • (2007) Brain Res , vol.1136 , Issue.1 , pp. 110-121
    • Bailey, A.M.1    Lee, J.M.2
  • 108
    • 33747161263 scopus 로고    scopus 로고
    • Secondary hyperalgesia in the monoarthritic rat is mediated by GABAB and NK1 receptors of spinal dorsal horn neurons: A behavior and c-fos study
    • Castro, A.R.; Pinto, M.; Lima, D.; Tavares, I. Secondary hyperalgesia in the monoarthritic rat is mediated by GABAB and NK1 receptors of spinal dorsal horn neurons: a behavior and c-fos study. Neuroscience, 2006, 141(4), 2087-2095.
    • (2006) Neuroscience , vol.141 , Issue.4 , pp. 2087-2095
    • Castro, A.R.1    Pinto, M.2    Lima, D.3    Tavares, I.4
  • 109
    • 34047271295 scopus 로고    scopus 로고
    • Spinal NK-1 receptor expressing neurons mediate opioid-induced hyperalgesia and antinociceptive tolerance via activation of descending pathways
    • Vera-Portocarrero, L.P.; Zhang, E.T.; King, T.; Ossipov, M.H.; Vanderah, T.W.; Lai, J.; Porreca, F. Spinal NK-1 receptor expressing neurons mediate opioid-induced hyperalgesia and antinociceptive tolerance via activation of descending pathways. Pain, 2007, 129(1-2), 35-45.
    • (2007) Pain , vol.129 , Issue.1-2 , pp. 35-45
    • Vera-Portocarrero, L.P.1    Zhang, E.T.2    King, T.3    Ossipov, M.H.4    Vanderah, T.W.5    Lai, J.6    Porreca, F.7
  • 110
    • 33750455483 scopus 로고    scopus 로고
    • Ablation of NK1 receptor bearing neurons in the nucleus of the solitary tract blunts cardiovascular reflexes in awake rats
    • Abdala, A.P.; Schoorlemmer, G.H.; Colombari, E. Ablation of NK1 receptor bearing neurons in the nucleus of the solitary tract blunts cardiovascular reflexes in awake rats. Brain Res., 2006, 1119, 165-173.
    • (2006) Brain Res , vol.1119 , pp. 165-173
    • Abdala, A.P.1    Schoorlemmer, G.H.2    Colombari, E.3
  • 111
    • 33845751991 scopus 로고    scopus 로고
    • Substance P-saporin down-regulates substance P receptor immunoreactive sensory dorsal root ganglion neurons innervating the lumbar intervertebral discs in rats
    • Ohtori, S.; Inoue, G.; Koshi, T.; Ito, T.; Doya, H.; Moriya, H.; Takahashi, K. Substance P-saporin down-regulates substance P receptor immunoreactive sensory dorsal root ganglion neurons innervating the lumbar intervertebral discs in rats. Spine. 2006, 31(26), 2987-2991.
    • (2006) Spine , vol.31 , Issue.26 , pp. 2987-2991
    • Ohtori, S.1    Inoue, G.2    Koshi, T.3    Ito, T.4    Doya, H.5    Moriya, H.6    Takahashi, K.7
  • 112
    • 41949122732 scopus 로고    scopus 로고
    • Wiley, R.G. Substance P receptor-expressing dorsal horn neurons: lessons from the targeted cytotoxin, substance P-saporin. Pain, 2008, 136, 7-10.
    • Wiley, R.G. Substance P receptor-expressing dorsal horn neurons: lessons from the targeted cytotoxin, substance P-saporin. Pain, 2008, 136, 7-10.
  • 113
    • 33847106367 scopus 로고    scopus 로고
    • From anxiety to autism: Spectrum of abnormal social behaviors modeled by progressive disruption of inhibitory neuronal function in the basolateral amygdala in Wistar rats
    • Truitt, W.A.; Sajdyk, T.J.; Dietrich, A.D.; Oberlin, B.; McDougle, C.J.; Shekhar, A. From anxiety to autism: spectrum of abnormal social behaviors modeled by progressive disruption of inhibitory neuronal function in the basolateral amygdala in Wistar rats. Psychopharmacology (Berl), 2007, 191(1), 07-18.
    • (2007) Psychopharmacology (Berl) , vol.191 , Issue.1 , pp. 07-18
    • Truitt, W.A.1    Sajdyk, T.J.2    Dietrich, A.D.3    Oberlin, B.4    McDougle, C.J.5    Shekhar, A.6
  • 114
    • 33947306096 scopus 로고    scopus 로고
    • Targeted deletion of neurokinin-1 receptor expressing nucleus tractus solitarii neurons precludes somatosensory depression of arterial baroreceptor-heart rate reflex
    • Potts, J.T.; Fong, A.Y.; Anguelov, P.I.; Lee, S.; McGovern, D.; Grias, I. Targeted deletion of neurokinin-1 receptor expressing nucleus tractus solitarii neurons precludes somatosensory depression of arterial baroreceptor-heart rate reflex. Neuroscience, 2007, 145(3), 1168-1181.
    • (2007) Neuroscience , vol.145 , Issue.3 , pp. 1168-1181
    • Potts, J.T.1    Fong, A.Y.2    Anguelov, P.I.3    Lee, S.4    McGovern, D.5    Grias, I.6
  • 115
    • 34248160137 scopus 로고    scopus 로고
    • Anti-nociceptive effects of selectively destroying substance P receptor-expressing dorsal horn neurons using [Sar9,Met(O2)11]-substance P-saporin: Behavioral and anatomical analyses
    • Wiley, R.G.; Kline, R.H.; 4th, Vierck, C.J.; Jr. Anti-nociceptive effects of selectively destroying substance P receptor-expressing dorsal horn neurons using [Sar9,Met(O2)11]-substance P-saporin: behavioral and anatomical analyses. Neuroscience, 2007, 146(3), 1333-1345.
    • (2007) Neuroscience , vol.146 , Issue.3 , pp. 1333-1345
    • Wiley, R.G.1    Kline 4th, R.H.2    Vierck Jr., C.J.3
  • 116
    • 34347347061 scopus 로고    scopus 로고
    • Ketanserin-induced baroreflex enhancement in spontaneously hypertensive rats depends on central 5-HT(2A) receptors
    • Shen, F.M.; Wang, J.; Ni, C.R.; Yu, J.G.; Wang, W.Z.; Su, D.F. Ketanserin-induced baroreflex enhancement in spontaneously hypertensive rats depends on central 5-HT(2A) receptors. Clin. Exp. Pharmacol. Physiol., 2007, 34(8), 702-707.
    • (2007) Clin. Exp. Pharmacol. Physiol , vol.34 , Issue.8 , pp. 702-707
    • Shen, F.M.1    Wang, J.2    Ni, C.R.3    Yu, J.G.4    Wang, W.Z.5    Su, D.F.6
  • 117
    • 33744518427 scopus 로고    scopus 로고
    • Descending facilitation from the rostral ventromedical medulla maintains visceral pain in rats with experimental panccreatitis
    • Vera-Portocarero, L.P.; Xie, J.Y.; Kowal, J.; Ossipor, M.H.; King, T.; Porreca, F. Descending facilitation from the rostral ventromedical medulla maintains visceral pain in rats with experimental panccreatitis. Gastroenterology, 2006, 130, 2155-2164.
    • (2006) Gastroenterology , vol.130 , pp. 2155-2164
    • Vera-Portocarero, L.P.1    Xie, J.Y.2    Kowal, J.3    Ossipor, M.H.4    King, T.5    Porreca, F.6
  • 118
    • 38149121526 scopus 로고    scopus 로고
    • Selective ablation of GABA neurons in the ventral tegmental area increases spontaneous locomotor activity
    • Shank, E.J.; Seitz, P.K.; Bubar, M.J.; Stutz, S.J.; Cunningham, K.A. Selective ablation of GABA neurons in the ventral tegmental area increases spontaneous locomotor activity. Behav. Neurosci., 2007, 121(6), 1224-1233.
    • (2007) Behav. Neurosci , vol.121 , Issue.6 , pp. 1224-1233
    • Shank, E.J.1    Seitz, P.K.2    Bubar, M.J.3    Stutz, S.J.4    Cunningham, K.A.5
  • 119
    • 33750621066 scopus 로고    scopus 로고
    • Pedrino, G.R.; Maurino, I.; de Almeida, Colombari, D.S.; Cravo, S.L.; Role of catecholaminergic neurones of the caudal ventrolateral medulla in cardiovascular responses induced by acute changes in circulating in rats. Exp. Physiol., 2006, 91 (6), 995-1005.
    • Pedrino, G.R.; Maurino, I.; de Almeida, Colombari, D.S.; Cravo, S.L.; Role of catecholaminergic neurones of the caudal ventrolateral medulla in cardiovascular responses induced by acute changes in circulating volume in rats. Exp. Physiol., 2006, 91 (6), 995-1005.
  • 120
    • 33845361644 scopus 로고    scopus 로고
    • Selective depletion of cortical noradrenaline by anti-dopamine beta-hydroxylase-saporin impairs attentional function and enhances the effects of guanfacine in the rat
    • Milstein, J.A.; Lehmann, O.; Theobald, D.E.; Dalley, J.W.; Robbins, T.W. Selective depletion of cortical noradrenaline by anti-dopamine beta-hydroxylase-saporin impairs attentional function and enhances the effects of guanfacine in the rat. Psychopharmacology (Berl), 2007, 190(1), 51-63.
    • (2007) Psychopharmacology (Berl) , vol.190 , Issue.1 , pp. 51-63
    • Milstein, J.A.1    Lehmann, O.2    Theobald, D.E.3    Dalley, J.W.4    Robbins, T.W.5
  • 121
    • 39849085999 scopus 로고    scopus 로고
    • Selective impairment of the cerebellar C1 module involved in rat hindlimb control reduces step-dependent modulation of cutaneous reflexes
    • Pijpers, H.; Winkelman, B.R.; Bronsing, R.; Ruigrok, T.J. Selective impairment of the cerebellar C1 module involved in rat hindlimb control reduces step-dependent modulation of cutaneous reflexes. J. Neurosci., 2008, 28, 2179-2189.
    • (2008) J. Neurosci , vol.28 , pp. 2179-2189
    • Pijpers, H.1    Winkelman, B.R.2    Bronsing, R.3    Ruigrok, T.J.4
  • 122
    • 38049026855 scopus 로고    scopus 로고
    • Different neuronal toxicity of single-chain ribosome-inactivating proteins on the rat retina
    • Sha, O.; Kwong, W.H.; Pang Cho, E.Y.; Wai Yew, D.T; Ng, T.B. Different neuronal toxicity of single-chain ribosome-inactivating proteins on the rat retina. Toxicon, 2008, 51(1), 45-53.
    • (2008) Toxicon , vol.51 , Issue.1 , pp. 45-53
    • Sha, O.1    Kwong, W.H.2    Pang Cho, E.Y.3    Wai Yew, D.T.4    Ng, T.B.5
  • 123
    • 29144444375 scopus 로고    scopus 로고
    • Structure-activity-relationship of saponins to enhance toxic effects of agrostin
    • Melzig, M.F.; Hebestreit, P.; Gaidi, G.; Lacaille-Dubois, M.A. Structure-activity-relationship of saponins to enhance toxic effects of agrostin. Planta Med., 2005, 71(11), 1088-1090.
    • (2005) Planta Med , vol.71 , Issue.11 , pp. 1088-1090
    • Melzig, M.F.1    Hebestreit, P.2    Gaidi, G.3    Lacaille-Dubois, M.A.4
  • 124
    • 33751112726 scopus 로고    scopus 로고
    • The differential catalytic activity of ribosome-inactivating proteins saporin 5 and 6 is due to a single substitution at position 162
    • Ghosh, P.; Batra, J.K. The differential catalytic activity of ribosome-inactivating proteins saporin 5 and 6 is due to a single substitution at position 162. Biochem. J., 2006, 400(1), 99-104.
    • (2006) Biochem. J , vol.400 , Issue.1 , pp. 99-104
    • Ghosh, P.1    Batra, J.K.2
  • 126
    • 33344459356 scopus 로고    scopus 로고
    • Photochemically stimulated drug delivery increases the cytotoxicity and specificity of EGF-saporin
    • Weyergang, A.; Selbo, P.K.; Berg, K. Photochemically stimulated drug delivery increases the cytotoxicity and specificity of EGF-saporin. J. Control Rel., 2006, 111(1-2), 165-173.
    • (2006) J. Control Rel , vol.111 , Issue.1-2 , pp. 165-173
    • Weyergang, A.1    Selbo, P.K.2    Berg, K.3
  • 128
    • 33645224029 scopus 로고    scopus 로고
    • The saponin-mediated enhanced uptake of targeted saporin-based drugs is strongly dependent on the saponin structure
    • Bachran, C.; Sutherland, M.; Heisler, I.; Hebestreit, P.; Melzig, M.F.; Fuchs, H. The saponin-mediated enhanced uptake of targeted saporin-based drugs is strongly dependent on the saponin structure. Exp. Biol. Med. (Maywood), 2006, 231(4), 412-420.
    • (2006) Exp. Biol. Med. (Maywood) , vol.231 , Issue.4 , pp. 412-420
    • Bachran, C.1    Sutherland, M.2    Heisler, I.3    Hebestreit, P.4    Melzig, M.F.5    Fuchs, H.6
  • 129
    • 34247371925 scopus 로고    scopus 로고
    • Targeted delivery and enhanced cytotoxicity of cetuximab-saporin by photochemical internalization in EGFR-positive cancer cells
    • Yip, W.L.; Weyergang, A.; Berg, K.; Tønnesen, H.H.; Selbo, P.K. Targeted delivery and enhanced cytotoxicity of cetuximab-saporin by photochemical internalization in EGFR-positive cancer cells. Mol. Pharm., 2007, 4(2), 241-251.
    • (2007) Mol. Pharm , vol.4 , Issue.2 , pp. 241-251
    • Yip, W.L.1    Weyergang, A.2    Berg, K.3    Tønnesen, H.H.4    Selbo, P.K.5
  • 130
    • 33745138505 scopus 로고    scopus 로고
    • The anti-CD20 antibody rituximab augments the immunospecific therapeutic effectiveness of an anti-CD19 immunotoxin directed against human B-cell lymphoma
    • Flavell, D.J.; Warnes, S.L.; Bryson, C.J.; Field, S.A.; Noss, A.L.; Packham, G.; Flavell, S.U. The anti-CD20 antibody rituximab augments the immunospecific therapeutic effectiveness of an anti-CD19 immunotoxin directed against human B-cell lymphoma. Br. J. Haematol., 2006, 134(2), 157-170.
    • (2006) Br. J. Haematol , vol.134 , Issue.2 , pp. 157-170
    • Flavell, D.J.1    Warnes, S.L.2    Bryson, C.J.3    Field, S.A.4    Noss, A.L.5    Packham, G.6    Flavell, S.U.7
  • 133
    • 34548444675 scopus 로고    scopus 로고
    • Lipopolyamine treatment increases the efficacy of intoxication with saporin and an anticancer saporin conjugate
    • Geden, S.E.; Gardner, R.A.; Fabbrini, M.S.; Ohashi, M.; Phanstiel, IV O.; Teter, K. Lipopolyamine treatment increases the efficacy of intoxication with saporin and an anticancer saporin conjugate. FEBS J., 2007, 274(18), 4825-4836.
    • (2007) FEBS J , vol.274 , Issue.18 , pp. 4825-4836
    • Geden, S.E.1    Gardner, R.A.2    Fabbrini, M.S.3    Ohashi, M.4    Phanstiel, I.O.5    Teter, K.6
  • 134
    • 36749004368 scopus 로고    scopus 로고
    • Conjugation of an anti transferrin receptor IgG3-avidin fusion protein with biotinylated saporin results in significant enhancement of its cytotoxicity against malignant hematopoietic cells
    • Daniels, T.R.; Ng, P.P.; Delgado, T.; Lynch, M.R.; Schiller, G.; Helguera, G.; Penichet, M.L. Conjugation of an anti transferrin receptor IgG3-avidin fusion protein with biotinylated saporin results in significant enhancement of its cytotoxicity against malignant hematopoietic cells. Mol. Cancer Ther., 2007, 6(11), 2995-3008.
    • (2007) Mol. Cancer Ther , vol.6 , Issue.11 , pp. 2995-3008
    • Daniels, T.R.1    Ng, P.P.2    Delgado, T.3    Lynch, M.R.4    Schiller, G.5    Helguera, G.6    Penichet, M.L.7
  • 135
    • 51849151811 scopus 로고    scopus 로고
    • Enhanced cytotoxicity of saporin by polyamidoamine dendrimer conjugation and photochemical internalization
    • Lai, P.S.; Pai, C.L.; Peng, C.L.; Shieh, M.J.; Berg, K.; Lou, P.J. Enhanced cytotoxicity of saporin by polyamidoamine dendrimer conjugation and photochemical internalization. J. Biomed. Mater. Res. A, 2008, 87(1), 147-155.
    • (2008) J. Biomed. Mater. Res. A , vol.87 , Issue.1 , pp. 147-155
    • Lai, P.S.1    Pai, C.L.2    Peng, C.L.3    Shieh, M.J.4    Berg, K.5    Lou, P.J.6
  • 136
    • 34147119204 scopus 로고    scopus 로고
    • Selective deletion of antigenspecific CD8+ T cells by MHC class I tetramers coupled to the type I ribosome-inactivating protein saporin
    • Hess, P.R.; Barnes, C.; Woolard, M.D.; Johnson, M.D.; Cullen, J.M.; Collins, E.J.; Frelinger, J.A. Selective deletion of antigenspecific CD8+ T cells by MHC class I tetramers coupled to the type I ribosome-inactivating protein saporin. Blood, 2007, 109(8), 3300-3307.
    • (2007) Blood , vol.109 , Issue.8 , pp. 3300-3307
    • Hess, P.R.1    Barnes, C.2    Woolard, M.D.3    Johnson, M.D.4    Cullen, J.M.5    Collins, E.J.6    Frelinger, J.A.7
  • 137
    • 33847130982 scopus 로고    scopus 로고
    • Truncations of gelonin lead to a reduction in its cytotoxicity
    • Li, Z.; Qu, Y.; Li, H.; Yuan, J. Truncations of gelonin lead to a reduction in its cytotoxicity. Toxicology, 2007, 231(2-3), 129-136.
    • (2007) Toxicology , vol.231 , Issue.2-3 , pp. 129-136
    • Li, Z.1    Qu, Y.2    Li, H.3    Yuan, J.4
  • 138
    • 33845314445 scopus 로고    scopus 로고
    • Inhibition of prostate tumor growth and bone remodeling by the vascular targeting agent VEGF121/rGel
    • Mohamedali, K.A.; Poblenz, A.T.; Sikes, C.R.; Navone, N.M.; Thorpe, P.E.; Darnay, B.G.; Rosenblum, M.G. Inhibition of prostate tumor growth and bone remodeling by the vascular targeting agent VEGF121/rGel. Cancer Res., 2006, 66(22), 10919-10928.
    • (2006) Cancer Res , vol.66 , Issue.22 , pp. 10919-10928
    • Mohamedali, K.A.1    Poblenz, A.T.2    Sikes, C.R.3    Navone, N.M.4    Thorpe, P.E.5    Darnay, B.G.6    Rosenblum, M.G.7
  • 139
    • 34247208168 scopus 로고    scopus 로고
    • Hsu, A.R.; Cai,W.; Veeravagu, A.; Mohamedali, K.A.; Chen, K.; Kim, S.; Vogel, H, Hou, L.C.;Tse, V.; Rosenblum, M.G.; Chen, X.. Multimodality molecular imaging of glioblastoma growth inhibition with vasculature-targeting fusion toxin VEGF121/rGel. J. Nucl. Med., 2007, 48(3), 445-454.
    • Hsu, A.R.; Cai,W.; Veeravagu, A.; Mohamedali, K.A.; Chen, K.; Kim, S.; Vogel, H, Hou, L.C.;Tse, V.; Rosenblum, M.G.; Chen, X.. Multimodality molecular imaging of glioblastoma growth inhibition with vasculature-targeting fusion toxin VEGF121/rGel. J. Nucl. Med., 2007, 48(3), 445-454.
  • 140
    • 33947274774 scopus 로고    scopus 로고
    • The growth factor fusion construct containing B-lymphocyte stimulator (BLyS) and the toxin rGel induces apoptosis specifically in BAFF-R-positive CLL cells
    • Nimmanapalli, R.; Lyu, M.A.; Du, M.; Keating, M.J.; Rosenblum, M.G.; Gandhi, V. The growth factor fusion construct containing B-lymphocyte stimulator (BLyS) and the toxin rGel induces apoptosis specifically in BAFF-R-positive CLL cells. Blood, 2007, 109(6), 2557-2564.
    • (2007) Blood , vol.109 , Issue.6 , pp. 2557-2564
    • Nimmanapalli, R.1    Lyu, M.A.2    Du, M.3    Keating, M.J.4    Rosenblum, M.G.5    Gandhi, V.6
  • 141
    • 33847415945 scopus 로고    scopus 로고
    • The rGel/BLyS fusion toxin specifically targets malignant B cells expressing the BLyS receptors BAFF-R, TACI, and BCMA
    • Lyu, M.A.; Cheung, L.H.; Hittelman, W.N.; Marks, J.W.; Aguiar, R.C.; Rosenblum M.G. The rGel/BLyS fusion toxin specifically targets malignant B cells expressing the BLyS receptors BAFF-R, TACI, and BCMA. Mol. Cancer Ther., 2007, 6(2), 460-470.
    • (2007) Mol. Cancer Ther , vol.6 , Issue.2 , pp. 460-470
    • Lyu, M.A.1    Cheung, L.H.2    Hittelman, W.N.3    Marks, J.W.4    Aguiar, R.C.5    Rosenblum, M.G.6
  • 143
    • 33845528947 scopus 로고    scopus 로고
    • PKC inhibition is involved in trichosanthin-induced apoptosis in human chronic myeloid leukemia cell line K562
    • Li, J.; Xia, X.; Nie, H.; Smith, M.A.; Zhu, X. PKC inhibition is involved in trichosanthin-induced apoptosis in human chronic myeloid leukemia cell line K562. Biochim. Biophys. Acta, 2007, 1770(1), 63-70.
    • (2007) Biochim. Biophys. Acta , vol.1770 , Issue.1 , pp. 63-70
    • Li, J.1    Xia, X.2    Nie, H.3    Smith, M.A.4    Zhu, X.5
  • 144
    • 45549089880 scopus 로고    scopus 로고
    • Elicitor-dependent expression of the ribosome-inactivating protein beetin is developmentally regulated
    • Iglesias, R.; Pérez, Y.; Citores, L.; Ferreras, J.M.; Méndez, E.; Girbés, T. Elicitor-dependent expression of the ribosome-inactivating protein beetin is developmentally regulated. J. Exp. Bot., 2008, 59(6), 1215-1223.
    • (2008) J. Exp. Bot , vol.59 , Issue.6 , pp. 1215-1223
    • Iglesias, R.1    Pérez, Y.2    Citores, L.3    Ferreras, J.M.4    Méndez, E.5    Girbés, T.6
  • 145
    • 34249686013 scopus 로고    scopus 로고
    • In vitro and in vivo toxicity of type 2 ribosome-inactivating proteins lanceolin and stenodactylin on glial and neuronal cells
    • Monti, B., D'Alessandro, C.; Farini, V.; Bolognesi, A.; Polazzi, E.; Contestabile, A.; Stirpe, F.; Battelli, M.G. In vitro and in vivo toxicity of type 2 ribosome-inactivating proteins lanceolin and stenodactylin on glial and neuronal cells. Neurotoxicology, 2007, 28(3), 637-644.
    • (2007) Neurotoxicology , vol.28 , Issue.3 , pp. 637-644
    • Monti, B.1    D'Alessandro, C.2    Farini, V.3    Bolognesi, A.4    Polazzi, E.5    Contestabile, A.6    Stirpe, F.7    Battelli, M.G.8
  • 147
    • 33751422748 scopus 로고    scopus 로고
    • Cloning and expression of the B chain of volkensin, type 2 ribosome inactivating protein from Adenia volkensii harms: Co-folding with the A chain for heterodimer reconstitution
    • Chambery, A.; Severino, V.; Stirpe, F.; Parente, A. Cloning and expression of the B chain of volkensin, type 2 ribosome inactivating protein from Adenia volkensii harms: co-folding with the A chain for heterodimer reconstitution. Protein Expr. Purif., 2007, 51(2), 209-215.
    • (2007) Protein Expr. Purif , vol.51 , Issue.2 , pp. 209-215
    • Chambery, A.1    Severino, V.2    Stirpe, F.3    Parente, A.4
  • 148
    • 38949218389 scopus 로고    scopus 로고
    • Isolation and characterization of four type 2 ribosome inactivating pulchellin isoforms from Abrus pulchellus seeds
    • Castilho, P.V.; Goto, L.S.; Roberts, L.M.; Araújo, A.P. Isolation and characterization of four type 2 ribosome inactivating pulchellin isoforms from Abrus pulchellus seeds. FEBS J., 2008, 275(5), 948-959.
    • (2008) FEBS J , vol.275 , Issue.5 , pp. 948-959
    • Castilho, P.V.1    Goto, L.S.2    Roberts, L.M.3    Araújo, A.P.4
  • 149
    • 33845927350 scopus 로고    scopus 로고
    • Structure-function analysis and insights into the reduced toxicity of Abrus precatorius agglutinin I in relation to abrin
    • Bagaria, A.; Surendranath, K.; Ramagopal, U.A.; Ramakumar, S.; Karande, A.A., Structure-function analysis and insights into the reduced toxicity of Abrus precatorius agglutinin I in relation to abrin. J. Biol. Chem., 2006, 281(45), 34465-34474.
    • (2006) J. Biol. Chem , vol.281 , Issue.45 , pp. 34465-34474
    • Bagaria, A.1    Surendranath, K.2    Ramagopal, U.A.3    Ramakumar, S.4    Karande, A.A.5
  • 150
    • 33845649761 scopus 로고    scopus 로고
    • Identification and characterization of riproximin, a new type II ribosome-inactivating protein with antineoplastic activity from Ximenia americana
    • Voss, C.; Eyol, E.; Frank, M.; von der Lieth, C.W.; Berger, M.R. Identification and characterization of riproximin, a new type II ribosome-inactivating protein with antineoplastic activity from Ximenia americana. FASEB J., 2006, 20(8), 1194-1196.
    • (2006) FASEB J , vol.20 , Issue.8 , pp. 1194-1196
    • Voss, C.1    Eyol, E.2    Frank, M.3    von der Lieth, C.W.4    Berger, M.R.5
  • 151
    • 33750162506 scopus 로고    scopus 로고
    • Molecular cloning and functional identification of a ribosome inactivating/ antiviral protein from leaves of post-flowering stage of Celosia cristata and its expression in E. coli
    • Begam, M.; Kumar, S.; Roy, S.; Campanella, J.J.; Kapoor, H.C. Molecular cloning and functional identification of a ribosome inactivating/ antiviral protein from leaves of post-flowering stage of Celosia cristata and its expression in E. coli. Phytochemistry, 2006, 67, 2441-2449.
    • (2006) Phytochemistry , vol.67 , pp. 2441-2449
    • Begam, M.1    Kumar, S.2    Roy, S.3    Campanella, J.J.4    Kapoor, H.C.5
  • 153
    • 20144364945 scopus 로고    scopus 로고
    • Crystal structure of himalayan mistletoe ribosome-inactivating protein reveals the presence of a natural inhibitor and a new functionally active sugar-binding site
    • Mishra, V.; Bilgrami, S.; Sharma, R.S.; Kaur, P.; Yadav, S.; Krauspenhaar, R.; Betzel, C.; Voelter, W.; Babu, C.R.; Singh, T.P. Crystal structure of himalayan mistletoe ribosome-inactivating protein reveals the presence of a natural inhibitor and a new functionally active sugar-binding site. J. Biol. Chem., 2005, 280(21), 20712-20721.
    • (2005) J. Biol. Chem , vol.280 , Issue.21 , pp. 20712-20721
    • Mishra, V.1    Bilgrami, S.2    Sharma, R.S.3    Kaur, P.4    Yadav, S.5    Krauspenhaar, R.6    Betzel, C.7    Voelter, W.8    Babu, C.R.9    Singh, T.P.10
  • 154
    • 33745969531 scopus 로고    scopus 로고
    • Detection of ricin and other ribosome-inactivating proteins by an immuno-polymerase chain reaction assay
    • Lubelli, C.; Chatgilialoglu, A.; Bolognesi, A.; Strocchi, P.; Colombatti, M.; Stirpe, F. Detection of ricin and other ribosome-inactivating proteins by an immuno-polymerase chain reaction assay. Anal. Biochem., 2006, 355(1), 102-109.
    • (2006) Anal. Biochem , vol.355 , Issue.1 , pp. 102-109
    • Lubelli, C.1    Chatgilialoglu, A.2    Bolognesi, A.3    Strocchi, P.4    Colombatti, M.5    Stirpe, F.6
  • 155
    • 39049100378 scopus 로고    scopus 로고
    • Cinnamomin: Separation, crystallization and preliminary X-ray diffraction study
    • Wang, T.; Zou, Y.S.; Zhu, D.W.; Azzi, A.; Liu, W.Y.; Lin, S.X. Cinnamomin: separation, crystallization and preliminary X-ray diffraction study. Amino Acids, 2008, 34(2), 239-243.
    • (2008) Amino Acids , vol.34 , Issue.2 , pp. 239-243
    • Wang, T.1    Zou, Y.S.2    Zhu, D.W.3    Azzi, A.4    Liu, W.Y.5    Lin, S.X.6
  • 156
    • 0034737565 scopus 로고    scopus 로고
    • Theorystal structure of saporin S06 from Saponarica officinalis and its interaction with the ribosome
    • Savino, C.; Federici, L.; Ippoliti, R.; Lendaro, E.; Tsernoglou, D. Theorystal structure of saporin S06 from Saponarica officinalis and its interaction with the ribosome FEBS Lett., 2000, 470, 239-243.
    • (2000) FEBS Lett , vol.470 , pp. 239-243
    • Savino, C.1    Federici, L.2    Ippoliti, R.3    Lendaro, E.4    Tsernoglou, D.5
  • 157
    • 0028177695 scopus 로고
    • The N-glycosidase mechanism of ribosome-inactivating proteins implied by crystal structures of alpha-momorcharin
    • Ren, J.; Wang, Y.; Dong, Y.; Stuart, D.I. The N-glycosidase mechanism of ribosome-inactivating proteins implied by crystal structures of alpha-momorcharin. Structure, 1994, 2(1), 7-16.
    • (1994) Structure , vol.2 , Issue.1 , pp. 7-16
    • Ren, J.1    Wang, Y.2    Dong, Y.3    Stuart, D.I.4
  • 158
    • 0028205798 scopus 로고
    • Crystal structure of momordin, a type I ribosome inactivating protein from the seeds of Momordica charantia
    • Husain, J.; Tickle, I.J.; Wood, S.P. Crystal structure of momordin, a type I ribosome inactivating protein from the seeds of Momordica charantia. FEBS Lett., 1994, 342(2), 154-158.
    • (1994) FEBS Lett , vol.342 , Issue.2 , pp. 154-158
    • Husain, J.1    Tickle, I.J.2    Wood, S.P.3
  • 159
    • 36849033327 scopus 로고    scopus 로고
    • Elderberry bark lectins evolved to recognize Neu5Ac alpha2,6Gal/ GalNAc sequence from a Gal/GalNAc binding lectin through the substitution of amino-acid residues critical for the binding to sialic acid
    • Kaku, H.; Kaneko, H.; Minamihara, N.; Iwata, K.; Jordan, E.T.; Rojo, M.A.; Minami-Ishii, N.; Minami, E.; Hisajima, S.; Shibuya, N. Elderberry bark lectins evolved to recognize Neu5Ac alpha2,6Gal/ GalNAc sequence from a Gal/GalNAc binding lectin through the substitution of amino-acid residues critical for the binding to sialic acid. J. Biochem., 2007, 142(3), 393-401.
    • (2007) J. Biochem , vol.142 , Issue.3 , pp. 393-401
    • Kaku, H.1    Kaneko, H.2    Minamihara, N.3    Iwata, K.4    Jordan, E.T.5    Rojo, M.A.6    Minami-Ishii, N.7    Minami, E.8    Hisajima, S.9    Shibuya, N.10
  • 160
    • 33846017593 scopus 로고    scopus 로고
    • Cytotoxicity of an ebulin 1-anti-human CD105 immunotoxin on mouse of fibroblast (L929) and rat myoblasts (L6E9) cells expressing human CD105
    • Benitez, J.; Ferreras, J.M.; Munoz, R.; Arias, Y.; Iglesias, R.; Cordoba-Diaz, M.; deVillar, R.; Girbes, T. Cytotoxicity of an ebulin 1-anti-human CD105 immunotoxin on mouse of fibroblast (L929) and rat myoblasts (L6E9) cells expressing human CD105. Med. Chem., 2005, 1, 65-70.
    • (2005) Med. Chem , vol.1 , pp. 65-70
    • Benitez, J.1    Ferreras, J.M.2    Munoz, R.3    Arias, Y.4    Iglesias, R.5    Cordoba-Diaz, M.6    deVillar, R.7    Girbes, T.8
  • 161
    • 34548224573 scopus 로고    scopus 로고
    • Targeting a marker of the tumour neovasculature using a novel antihuman CD105-immunotoxin containing the non-toxic type 2 ribosome-inactivating protein nigrin b
    • Muñoz, R.; Arias, Y.; Ferreras, J.M.; Rojo, M.A.; Gayoso, M.J.; Nocito, M.; Benitez, J.; Jiménez, P.; Bernabéu, C.; Girbés, T. Targeting a marker of the tumour neovasculature using a novel antihuman CD105-immunotoxin containing the non-toxic type 2 ribosome-inactivating protein nigrin b. Cancer Lett., 2007, 256(1), 73-80.
    • (2007) Cancer Lett , vol.256 , Issue.1 , pp. 73-80
    • Muñoz, R.1    Arias, Y.2    Ferreras, J.M.3    Rojo, M.A.4    Gayoso, M.J.5    Nocito, M.6    Benitez, J.7    Jiménez, P.8    Bernabéu, C.9    Girbés, T.10
  • 162
    • 33745200074 scopus 로고    scopus 로고
    • The lower cytotoxicity of cinnamomin (a type II RIP) is due to its B-chain
    • Wang, B.Z.; Zou, W.G.; Liu, W.Y.; Liu, X.Y. The lower cytotoxicity of cinnamomin (a type II RIP) is due to its B-chain. Arch. Biochem. Biophys., 2006, 451(1), 91-96.
    • (2006) Arch. Biochem. Biophys , vol.451 , Issue.1 , pp. 91-96
    • Wang, B.Z.1    Zou, W.G.2    Liu, W.Y.3    Liu, X.Y.4
  • 163
    • 34447336107 scopus 로고    scopus 로고
    • Viscum album agglutinin-I induces degradation of cytoskeletal proteins in leukaemia PLB-985 cells differentiated toward neutrophils: Cleavage of non-muscle myosin heavy chain-IIA by caspases
    • Lavastre, V.; Binet, F.; Moisan, E.; Chiasson, S.; Girard, D. Viscum album agglutinin-I induces degradation of cytoskeletal proteins in leukaemia PLB-985 cells differentiated toward neutrophils: cleavage of non-muscle myosin heavy chain-IIA by caspases. Br. J. Haematol., 2007, 138(4), 545-554.
    • (2007) Br. J. Haematol , vol.138 , Issue.4 , pp. 545-554
    • Lavastre, V.1    Binet, F.2    Moisan, E.3    Chiasson, S.4    Girard, D.5
  • 164
    • 33645805238 scopus 로고    scopus 로고
    • Quality of life is improved in breast cancer patients by Standardised Mistletoe Extract PS76A2 during chemotherapy and follow-up: A randomised, placebo-controlled, double-blind, multicentre clinical trial
    • Semiglazov, V.F.; Stepula, V.V.; Dudov, A.; Schnitker, J.; Mengs, U. Quality of life is improved in breast cancer patients by Standardised Mistletoe Extract PS76A2 during chemotherapy and follow-up: a randomised, placebo-controlled, double-blind, multicentre clinical trial. Anticancer Res., 2006, 26(2B), 1519-1529.
    • (2006) Anticancer Res , vol.26 , Issue.2 B , pp. 1519-1529
    • Semiglazov, V.F.1    Stepula, V.V.2    Dudov, A.3    Schnitker, J.4    Mengs, U.5
  • 165
    • 33847624711 scopus 로고    scopus 로고
    • The proteasome inhibitor bortezomib augments anti-proliferative effects of mistletoe lectin-I and the PPAR-gamma agonist rosiglitazone in human melanoma cells
    • Freudlsperger, C.; Thies, A.; Pfüller, U.; Schumacher, U. The proteasome inhibitor bortezomib augments anti-proliferative effects of mistletoe lectin-I and the PPAR-gamma agonist rosiglitazone in human melanoma cells. Anticancer Res., 2007, 27(1A), 207-213.
    • (2007) Anticancer Res , vol.27 , Issue.1 A , pp. 207-213
    • Freudlsperger, C.1    Thies, A.2    Pfüller, U.3    Schumacher, U.4
  • 166
    • 38049015487 scopus 로고    scopus 로고
    • Low-dose mistletoe lectin-I reduces melanoma growth and spread in a scid mouse xenograft model
    • Thies, A.; Dautel, P.; Meyer, A.; Pfüller, U.; Schumacher, U. Low-dose mistletoe lectin-I reduces melanoma growth and spread in a scid mouse xenograft model. Br. J. Cancer, 2008, 98(1), 106-112.
    • (2008) Br. J. Cancer , vol.98 , Issue.1 , pp. 106-112
    • Thies, A.1    Dautel, P.2    Meyer, A.3    Pfüller, U.4    Schumacher, U.5
  • 167
    • 34347261003 scopus 로고    scopus 로고
    • Mechanisms involved in Korean mistletoe lectin-induced apoptosis of cancer cells
    • Khil, L.Y.; Kim, W.; Lyu, S.; Park, W.B.; Yoon, J.W.; Jun, H.S. Mechanisms involved in Korean mistletoe lectin-induced apoptosis of cancer cells. World J. Gastroenterol., 2007, 13(20), 2811-2818.
    • (2007) World J. Gastroenterol , vol.13 , Issue.20 , pp. 2811-2818
    • Khil, L.Y.1    Kim, W.2    Lyu, S.3    Park, W.B.4    Yoon, J.W.5    Jun, H.S.6
  • 168
    • 33847648144 scopus 로고    scopus 로고
    • Cytotoxic activity and absence of tumor growth stimulation of standardized mistletoe extracts in human tumor models in vitro
    • Kelter, G.; Schierholz, J.M.; Fischer, I.U.; Fiebig, H.H. Cytotoxic activity and absence of tumor growth stimulation of standardized mistletoe extracts in human tumor models in vitro. Anticancer Res., 2007, 27(1A), 223-233.
    • (2007) Anticancer Res , vol.27 , Issue.1 A , pp. 223-233
    • Kelter, G.1    Schierholz, J.M.2    Fischer, I.U.3    Fiebig, H.H.4
  • 169
    • 29844438773 scopus 로고    scopus 로고
    • Suppression of growth of tumour cell lines in vitro and tumours in vivo by mistletoe lectins
    • Review
    • Pryme, I.F.; Bardocz, S.; Pusztai, A.; Ewen, S.W. Suppression of growth of tumour cell lines in vitro and tumours in vivo by mistletoe lectins. Histol. Histopathol., 2006, 21(3), 285-299. Review.
    • (2006) Histol. Histopathol , vol.21 , Issue.3 , pp. 285-299
    • Pryme, I.F.1    Bardocz, S.2    Pusztai, A.3    Ewen, S.W.4
  • 170
    • 46249099436 scopus 로고    scopus 로고
    • A neutralizing antibody to the a chain of abrin inhibits abrin toxicity both in vitro and in vivo
    • Surendranath, K.; Karande, A.A. A neutralizing antibody to the a chain of abrin inhibits abrin toxicity both in vitro and in vivo. Clin. Vaccine Immunol., 2008, 15(5), 737-743.
    • (2008) Clin. Vaccine Immunol , vol.15 , Issue.5 , pp. 737-743
    • Surendranath, K.1    Karande, A.A.2
  • 171
    • 33745937021 scopus 로고    scopus 로고
    • Immunologic effects of mistletoe lectins: A placebo-controlled study in healthy subjects
    • Huber, R.; Rostock, M.; Goedl, R.; Lüdtke, R.; Urech, K.; Klein, R. Immunologic effects of mistletoe lectins: a placebo-controlled study in healthy subjects. J. Soc. Integr. Oncol., 2006, 4, 3-7.
    • (2006) J. Soc. Integr. Oncol , vol.4 , pp. 3-7
    • Huber, R.1    Rostock, M.2    Goedl, R.3    Lüdtke, R.4    Urech, K.5    Klein, R.6
  • 172
    • 39849103338 scopus 로고    scopus 로고
    • Korean mistletoe lectin (KML-IIU) and its subchains induce nitric oxide (NO) production in murine macrophage cells
    • Kang, T.B.; Yoo, Y.C.; Lee, K.H.; Yoon, H.S.; Her, E.; Kim, J.B.; Song, S.K. Korean mistletoe lectin (KML-IIU) and its subchains induce nitric oxide (NO) production in murine macrophage cells. J. Biomed. Sci., 2008, 15(2), 197-204.
    • (2008) J. Biomed. Sci , vol.15 , Issue.2 , pp. 197-204
    • Kang, T.B.1    Yoo, Y.C.2    Lee, K.H.3    Yoon, H.S.4    Her, E.5    Kim, J.B.6    Song, S.K.7
  • 173
    • 33646905629 scopus 로고    scopus 로고
    • Immunoglobulin A antibodies against ricin A and B subunits protect epithelial cells from ricin intoxication
    • Mantis, N.J.; McGuinness, C.R.; Sonuyi, O.; Edwards, G.; Farrant, S.A. Immunoglobulin A antibodies against ricin A and B subunits protect epithelial cells from ricin intoxication. Infect. Immun., 2006, 74(6), 3455-3462.
    • (2006) Infect. Immun , vol.74 , Issue.6 , pp. 3455-3462
    • Mantis, N.J.1    McGuinness, C.R.2    Sonuyi, O.3    Edwards, G.4    Farrant, S.A.5
  • 174
    • 0034018978 scopus 로고    scopus 로고
    • Toxicity of cinnamomin-a new type II ribosome-inactivating protein to boll-worm and mosquito
    • Zhou, X.; Li, X.D.; Yuan, J.Z.; Tang, Z.H.; Liu, W.Y. Toxicity of cinnamomin-a new type II ribosome-inactivating protein to boll-worm and mosquito. Insect Biochem. Mol. Bio., 2000, 30, 259-264.
    • (2000) Insect Biochem. Mol. Bio , vol.30 , pp. 259-264
    • Zhou, X.1    Li, X.D.2    Yuan, J.Z.3    Tang, Z.H.4    Liu, W.Y.5
  • 175
    • 39049175574 scopus 로고    scopus 로고
    • Bioassays for insecticidal activity of iris ribosome-inactivating proteins expressed in tobacco
    • Shahidi Noghabi, S.; Van Damme, E.; Smagghe, G. Bioassays for insecticidal activity of iris ribosome-inactivating proteins expressed in tobacco. Commun. Agric. Appl. Biol. Sci., 2006, 71(1), 285-289.
    • (2006) Commun. Agric. Appl. Biol. Sci , vol.71 , Issue.1 , pp. 285-289
    • Shahidi Noghabi, S.1    Van Damme, E.2    Smagghe, G.3
  • 176
    • 33748806597 scopus 로고    scopus 로고
    • An activity-dependent assay for ricin and related RNA N-glycosidases based on electrochemiluminescence
    • Keener, W.K.; Rivera, V.R.,Young, C.C.; Poli, M.A. An activity-dependent assay for ricin and related RNA N-glycosidases based on electrochemiluminescence. Anal. Biochem., 2006, 357(2), 200-207.
    • (2006) Anal. Biochem , vol.357 , Issue.2 , pp. 200-207
    • Keener, W.K.1    Rivera, V.R.2    Young, C.C.3    Poli, M.A.4
  • 177
    • 34548052258 scopus 로고    scopus 로고
    • Solvent-assisted trypsin digestion of ricin for forensic identification by LCESI MS/MS
    • Ostin, A.; Bergstrom, T.; Fredriksson, S.A.; Nilsson, C. Solvent-assisted trypsin digestion of ricin for forensic identification by LCESI MS/MS. Anal. Chem., 2007, 79, 6271-6278.
    • (2007) Anal. Chem , vol.79 , pp. 6271-6278
    • Ostin, A.1    Bergstrom, T.2    Fredriksson, S.A.3    Nilsson, C.4
  • 178
    • 33845660041 scopus 로고    scopus 로고
    • Improvement of an enzyme linked lectin assay to determine recombinant mistletoe lectin I
    • Hussein, F.; Daniels, R. Improvement of an enzyme linked lectin assay to determine recombinant mistletoe lectin I. J. Pharm. Biomed. Anal., 2007, 43(2), 758-762.
    • (2007) J. Pharm. Biomed. Anal , vol.43 , Issue.2 , pp. 758-762
    • Hussein, F.1    Daniels, R.2
  • 179
    • 33745969531 scopus 로고    scopus 로고
    • Detection of ricin and other ribosome-inactivating proteins by an immuno-polymerase chain reaction assay
    • Lubelli, C.; Chatgilialoglu, A.; Bolognesi, A.; Strocchi, P.; Colombatti, M.; Stirpe, F. Detection of ricin and other ribosome-inactivating proteins by an immuno-polymerase chain reaction assay. Anal. Biochem., 2006, 355(1), 102-109.
    • (2006) Anal. Biochem , vol.355 , Issue.1 , pp. 102-109
    • Lubelli, C.1    Chatgilialoglu, A.2    Bolognesi, A.3    Strocchi, P.4    Colombatti, M.5    Stirpe, F.6
  • 180
    • 35548984395 scopus 로고    scopus 로고
    • Structural-function study of maize ribosome-inactivating protein: Implications for the internal inactivation region and the sole glutamate in the active site
    • Mak AN, Wong YT, An YJ, Cha SS, Sze KH, Au SW, Wong KB, Shaw PC. Structural-function study of maize ribosome-inactivating protein: implications for the internal inactivation region and the sole glutamate in the active site. Nucleic Acids Res., 2007, 35(18), 6259-6267.
    • (2007) Nucleic Acids Res , vol.35 , Issue.18 , pp. 6259-6267
    • Mak, A.N.1    Wong, Y.T.2    An, Y.J.3    Cha, S.S.4    Sze, K.H.5    Au, S.W.6    Wong, K.B.7    Shaw, P.C.8
  • 182
    • 33645998090 scopus 로고    scopus 로고
    • Relative activity of a tobacco hybrid expressing high levels of a tobacco anionic peroxidase and maize ribosome-inactivating protein against Helicoverpa zea and Lasioderma serricorne
    • Dowd, P.F.; Holmes, R.A.; Pinkerton, T.S.; Johnson, E.T.; Lagrimini, L.M.; Boston, R.S. Relative activity of a tobacco hybrid expressing high levels of a tobacco anionic peroxidase and maize ribosome-inactivating protein against Helicoverpa zea and Lasioderma serricorne. J. Agric. Food Chem., 2006, 54(7), 2629-2634.
    • (2006) J. Agric. Food Chem , vol.54 , Issue.7 , pp. 2629-2634
    • Dowd, P.F.1    Holmes, R.A.2    Pinkerton, T.S.3    Johnson, E.T.4    Lagrimini, L.M.5    Boston, R.S.6
  • 183
    • 0033978465 scopus 로고    scopus 로고
    • Anti-HIV and anti-tumor protein MAP30, a 30 kDa single-strand type-I RIP, shares similar secondary structure and beta-sheet topology with the A chain of ricin, a type-II RIP
    • Wang, H.X.; Jacob, J.; Wingfield, P.T.; Palmer, I.; Stahl, S.J.; Kaufman, J.D.; Huang, P.L.; Lee-Huang, S.; Torchia, D.A. Anti-HIV and anti-tumor protein MAP30, a 30 kDa single-strand type-I RIP, shares similar secondary structure and beta-sheet topology with the A chain of ricin, a type-II RIP. Protein Sci., 2000, 9, 138-144.
    • (2000) Protein Sci , vol.9 , pp. 138-144
    • Wang, H.X.1    Jacob, J.2    Wingfield, P.T.3    Palmer, I.4    Stahl, S.J.5    Kaufman, J.D.6    Huang, P.L.7    Lee-Huang, S.8    Torchia, D.A.9
  • 184
    • 0036399242 scopus 로고    scopus 로고
    • Isolation and enzymatic characterization of lamjapin, the first ribosome-inactivating protein from cryptogamic algal plant (Laminaria japonica A)
    • Liu, R.S.; Yang, J.H.; Liu, W.Y. Isolation and enzymatic characterization of lamjapin, the first ribosome-inactivating protein from cryptogamic algal plant (Laminaria japonica A). Eur. J. Biochem., 2002, 269, 4746-4752.
    • (2002) Eur. J. Biochem , vol.269 , pp. 4746-4752
    • Liu, R.S.1    Yang, J.H.2    Liu, W.Y.3
  • 185
    • 67650167717 scopus 로고    scopus 로고
    • Purification and characterization of a novel ribosome-inactivating protein from seeds of Trichosanthes kirilowii Maxim
    • Shu, S.H.; Xie, G.Z.; Guo, X.L.; Wang, M. Purification and characterization of a novel ribosome-inactivating protein from seeds of Trichosanthes kirilowii Maxim. Protein Expr. Purif., 2009, 67(2): 120-125.
    • (2009) Protein Expr. Purif , vol.67 , Issue.2 , pp. 120-125
    • Shu, S.H.1    Xie, G.Z.2    Guo, X.L.3    Wang, M.4
  • 186
    • 0033533392 scopus 로고    scopus 로고
    • Proteolytic fragments of anti-HIV and anti-tumor proteins MAP30 and GAP31 are biologically active
    • Huang, P.L.; Sun, Y.; Chen, H.C.; Kung, H.F.; Lee-Huang, S. Proteolytic fragments of anti-HIV and anti-tumor proteins MAP30 and GAP31 are biologically active. Biochem. Biophys. Res. Commun., 1999, 262(3), 615-623.
    • (1999) Biochem. Biophys. Res. Commun , vol.262 , Issue.3 , pp. 615-623
    • Huang, P.L.1    Sun, Y.2    Chen, H.C.3    Kung, H.F.4    Lee-Huang, S.5
  • 188
    • 32644474374 scopus 로고    scopus 로고
    • Novel immunotoxin: A fusion protein consisting of gelonin and an acetylcholine receptor fragment as a potential immunotherapeutic agent for the treatment of myasthenia gravis
    • Hossann, M.; Li, Z.; Shi, Y.; Kreilinger, U.; Büttner, J.; Vogel, P.D.; Yuan, J.; Wise, J.G.; Trommer, W.E. Novel immunotoxin: a fusion protein consisting of gelonin and an acetylcholine receptor fragment as a potential immunotherapeutic agent for the treatment of myasthenia gravis. Protein Expr. Purif., 2006, 46(1), 73-84.
    • (2006) Protein Expr. Purif , vol.46 , Issue.1 , pp. 73-84
    • Hossann, M.1    Li, Z.2    Shi, Y.3    Kreilinger, U.4    Büttner, J.5    Vogel, P.D.6    Yuan, J.7    Wise, J.G.8    Trommer, W.E.9
  • 189
    • 65649100180 scopus 로고    scopus 로고
    • A novel sorting strategy of trichosanthin for hijacking human immunodeficiency virus type 1
    • Zhao, W.L.; Zhang, F.; Feng, D.; Wu, J.; Chen, S.; Sui, S.F. A novel sorting strategy of trichosanthin for hijacking human immunodeficiency virus type 1. Biochem. Biophys. Res. Commun., 2009, 384(3), 347-351.
    • (2009) Biochem. Biophys. Res. Commun , vol.384 , Issue.3 , pp. 347-351
    • Zhao, W.L.1    Zhang, F.2    Feng, D.3    Wu, J.4    Chen, S.5    Sui, S.F.6
  • 190
    • 0037411183 scopus 로고    scopus 로고
    • He, W.J.; Liu, W.Y. Cinnamomin: a multifunctional type II ribosome-inactivating protein. Int. J. Biochem. Cell Biol., 2003, 35, 1021-1027.
    • He, W.J.; Liu, W.Y. Cinnamomin: a multifunctional type II ribosome-inactivating protein. Int. J. Biochem. Cell Biol., 2003, 35, 1021-1027.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.