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Volumn 35, Issue 1, 2003, Pages 61-78

Musarmins: Three single-chain ribosome-inactivating protein isoforms from bulbs of Muscari armeniacum L. and Miller

Author keywords

Inhibitors; Musarmins; Muscari armeniacum; N Glycosidase; Ribosome inactivating protein; rRNA; Translation

Indexed keywords

AMINO ACID DERIVATIVE; COMPLEMENTARY DNA; HYDROGEN PEROXIDE; ISOPROTEIN; MESSENGER RNA; MUSARMIN; RIBOSOME INACTIVATING PROTEIN; RNA 28S; SALICYLIC ACID; UNCLASSIFIED DRUG; UNTRANSLATED RNA; GLYCOSIDASE; PROTEIN SYNTHESIS INHIBITOR; VEGETABLE PROTEIN;

EID: 0037212289     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(02)00093-6     Document Type: Article
Times cited : (13)

References (36)
  • 1
    • 0030207043 scopus 로고    scopus 로고
    • The structure and function of ribosome-inactivating proteins
    • Hartley M.R., Chaddock J., Bonness M. The structure and function of ribosome-inactivating proteins. Trends Plant Sci. 1:1996;254-260.
    • (1996) Trends Plant Sci. , vol.1 , pp. 254-260
    • Hartley, M.R.1    Chaddock, J.2    Bonness, M.3
  • 4
    • 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. 288:2001;718-721.
    • (2001) Biochem. Biophys. Res. Commun. , vol.288 , pp. 718-721
    • Wang, H.X.1    Ng, T.B.2
  • 5
    • 0032581041 scopus 로고    scopus 로고
    • Shiga toxin attacks bacterial ribosomes as effectively as eukaryotic ribosomes
    • Suh J.K., Hovde C.J., Robertus J.D. Shiga toxin attacks bacterial ribosomes as effectively as eukaryotic ribosomes. Biochemistry. 37:1998;9394-9398.
    • (1998) Biochemistry , vol.37 , pp. 9394-9398
    • Suh, J.K.1    Hovde, C.J.2    Robertus, J.D.3
  • 7
    • 0034022958 scopus 로고    scopus 로고
    • A novel mechanism for inhibition of translation by pokeweed anti-viral protein: Depurination of the capped RNA template
    • Hudak K.A., Wang P., Tumer N.E. A novel mechanism for inhibition of translation by pokeweed anti-viral protein: depurination of the capped RNA template. RNA. 6:2000;369-380.
    • (2000) RNA , vol.6 , pp. 369-380
    • Hudak, K.A.1    Wang, P.2    Tumer, N.E.3
  • 8
    • 0034193439 scopus 로고    scopus 로고
    • Intrinsic ribonuclease activities in ribonuclease and ribosome-inactivating proteins from the seeds of bitter gourd
    • Fong W.P., Mock W.Y., Ng T.B. Intrinsic ribonuclease activities in ribonuclease and ribosome-inactivating proteins from the seeds of bitter gourd. Int. J. Biochem. Cell Biol. 32:2000;571-577.
    • (2000) Int. J. Biochem. Cell Biol. , vol.32 , pp. 571-577
    • Fong, W.P.1    Mock, W.Y.2    Ng, T.B.3
  • 9
    • 0028098025 scopus 로고
    • Ricin: Structure, mode of action, and some current applications
    • Lord J.M., Roberts L.M., Robertus J.D. Ricin: structure, mode of action, and some current applications. FASEB J. 8:1994;201-208.
    • (1994) FASEB J. , vol.8 , pp. 201-208
    • Lord, J.M.1    Roberts, L.M.2    Robertus, J.D.3
  • 11
    • 0035954240 scopus 로고    scopus 로고
    • Sensitivity of cancer cell lines to the novel non-toxic type 2 ribosome-inactivating protein Nigrin b
    • Muñoz R., Arias Y., Ferreras J.M., Jimenez P., Rojo M.A., Girbés T. Sensitivity of cancer cell lines to the novel non-toxic type 2 ribosome-inactivating protein Nigrin b. Cancer Lett. 167:2001;163-169.
    • (2001) Cancer Lett. , vol.167 , pp. 163-169
    • Muñoz, R.1    Arias, Y.2    Ferreras, J.M.3    Jimenez, P.4    Rojo, M.A.5    Girbés, T.6
  • 12
    • 0028369223 scopus 로고
    • Pokeweed anti-viral protein inactivates pokeweed ribosomes; Implication for the anti-viral mechanism
    • Bonness M., Ready M.P., Irvin J.D., Mabry T. Pokeweed anti-viral protein inactivates pokeweed ribosomes; implication for the anti-viral mechanism. Plant J. 5:1994;173-183.
    • (1994) Plant J. , vol.5 , pp. 173-183
    • Bonness, M.1    Ready, M.P.2    Irvin, J.D.3    Mabry, T.4
  • 14
    • 0027208585 scopus 로고
    • Broad-spectrum virus resistance in transgenic plants expressing pokeweed anti-viral protein
    • Lodge J.K., Kaniewski W., Tumer N. Broad-spectrum virus resistance in transgenic plants expressing pokeweed anti-viral protein. Proc. Natl. Acad. Sci. U.S.A. 90:1993;7089-7093.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 7089-7093
    • Lodge, J.K.1    Kaniewski, W.2    Tumer, N.3
  • 15
    • 0029987934 scopus 로고    scopus 로고
    • Activities associated with the presence of ribosome-inactivating proteins increase in senescent and stressed leaves
    • Stirpe F., Barbieri L., Gorini P., Valbonesi P., Bolognesi A., Polito L. Activities associated with the presence of ribosome-inactivating proteins increase in senescent and stressed leaves. FEBS Lett. 382:1996;309-312.
    • (1996) FEBS Lett. , vol.382 , pp. 309-312
    • Stirpe, F.1    Barbieri, L.2    Gorini, P.3    Valbonesi, P.4    Bolognesi, A.5    Polito, L.6
  • 20
    • 0019321718 scopus 로고
    • Rapid isolation of high molecular weight plant DNA
    • Murray M.G., Thompson W.F. Rapid isolation of high molecular weight plant DNA. Nucleic Acids Res. 8:1990;4321-4325.
    • (1990) Nucleic Acids Res. , vol.8 , pp. 4321-4325
    • Murray, M.G.1    Thompson, W.F.2
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0032031344 scopus 로고    scopus 로고
    • Presence of polymerized and free forms of the non-toxic type 2 ribosome-inactivating protein ebulin and a structurally-related new heterodimeric lectin in fruits of Sambucus ebulus L.
    • Citores L., de Benito F.M., Iglesias R., Ferreras J.M., Argüeso P., Jiménez P., Méndez E., Girbés T. Presence of polymerized and free forms of the non-toxic type 2 ribosome-inactivating protein ebulin and a structurally-related new heterodimeric lectin in fruits of Sambucus ebulus L. Planta. 204:1998;310-317.
    • (1998) Planta , vol.204 , pp. 310-317
    • Citores, L.1    De Benito, F.M.2    Iglesias, R.3    Ferreras, J.M.4    Argüeso, P.5    Jiménez, P.6    Méndez, E.7    Girbés, T.8
  • 26
    • 0033061571 scopus 로고    scopus 로고
    • Initiation of translation in prokaryotes and eukaryotes
    • Kozak M. Initiation of translation in prokaryotes and eukaryotes. Gene. 234:1999;187-208.
    • (1999) Gene , vol.234 , pp. 187-208
    • Kozak, M.1
  • 27
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H., Engelbrecht J., Brunak S., von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1997;1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 28
    • 0030749394 scopus 로고    scopus 로고
    • Type 1 ribosome-inactivating proteins are the most abundant proteins in iris (Iris hollandica var. Professor Blaauw) bulbs: Characterization and molecular cloning
    • Van Damme E.J., Barre A., Barbieri L., Valbonesi P., Rouge P., Van Leuven F., Stirpe F., Peumans W.J. Type 1 ribosome-inactivating proteins are the most abundant proteins in iris (Iris hollandica var. Professor Blaauw) bulbs: characterization and molecular cloning. Biochem. J. 324:1997;963-970.
    • (1997) Biochem. J. , vol.324 , pp. 963-970
    • Van Damme, E.J.1    Barre, A.2    Barbieri, L.3    Valbonesi, P.4    Rouge, P.5    Van Leuven, F.6    Stirpe, F.7    Peumans, W.J.8
  • 29
    • 0026063521 scopus 로고
    • Biochemical and molecular characterization of three barley seed proteins with anti-fungal properties
    • Leah R., Tommerup H., Svendsen I., Mundy J. Biochemical and molecular characterization of three barley seed proteins with anti-fungal properties. J. Biol. Chem. 266:1991;1564-1573.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1564-1573
    • Leah, R.1    Tommerup, H.2    Svendsen, I.3    Mundy, J.4
  • 30
    • 0027584743 scopus 로고
    • Nucleotide sequence of a genomic gene encoding tritin, a ribosome-inactivating protein from Triticum aestivum
    • Habuka N., Kataoka J., Miyano M., Tsuge H., Ago H., Noma M. Nucleotide sequence of a genomic gene encoding tritin, a ribosome-inactivating protein from Triticum aestivum. Plant Mol. Biol. 22:1993;171-176.
    • (1993) Plant Mol. Biol. , vol.22 , pp. 171-176
    • Habuka, N.1    Kataoka, J.2    Miyano, M.3    Tsuge, H.4    Ago, H.5    Noma, M.6
  • 31
    • 0022425912 scopus 로고
    • Nucleotide sequence of cloned cDNA coding for preproricin
    • Lamb F.I., Roberts L.M., Lord J.M. Nucleotide sequence of cloned cDNA coding for preproricin. Eur. J. Biochem. 148:1985;265-270.
    • (1985) Eur. J. Biochem. , vol.148 , pp. 265-270
    • Lamb, F.I.1    Roberts, L.M.2    Lord, J.M.3
  • 32
    • 0029620209 scopus 로고
    • Systematic delection analysis of ricin A-chain function
    • Munishkin A., Wool I.G. Systematic delection analysis of ricin A-chain function. J. Biol. Chem. 270:1995;30581-30587.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30581-30587
    • Munishkin, A.1    Wool, I.G.2
  • 34
    • 0027312493 scopus 로고
    • A genomic gene for MAP, a ribosome-inactivating protein from Mirabilis jalapa, contains an intron
    • Kataoka J., Miyano M., Habuka N., Masuta C., Koiwai A. A genomic gene for MAP, a ribosome-inactivating protein from Mirabilis jalapa, contains an intron. Nucleic Acids Res. 21:1993;1035.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1035
    • Kataoka, J.1    Miyano, M.2    Habuka, N.3    Masuta, C.4    Koiwai, A.5
  • 35
    • 0029140582 scopus 로고
    • Increased accumulation of trichosanthin in Trichosanthes kirilowii induced by microorganisms
    • Wong R.N.S., Mak N.K., Choi W.T., Law P.T.W. Increased accumulation of trichosanthin in Trichosanthes kirilowii induced by microorganisms. J. Exp. Bot. 46:1995;355-358.
    • (1995) J. Exp. Bot. , vol.46 , pp. 355-358
    • Wong, R.N.S.1    Mak, N.K.2    Choi, W.T.3    Law, P.T.W.4
  • 36
    • 0037086572 scopus 로고    scopus 로고
    • Cinnamomin, a type 2 ribosome-inactivating protein, is a storage protein in the seed of the Camphor tree (Cinnamomun camphora)
    • Liu R.S., Wei G.G., Yang Q., He W.J., Liu W.Y. Cinnamomin, a type 2 ribosome-inactivating protein, is a storage protein in the seed of the Camphor tree (Cinnamomun camphora). Biochem. J. 362:2002;659-663.
    • (2002) Biochem. J. , vol.362 , pp. 659-663
    • Liu, R.S.1    Wei, G.G.2    Yang, Q.3    He, W.J.4    Liu, W.Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.