메뉴 건너뛰기




Volumn 7, Issue 2, 2008, Pages 809-816

Proteome analysis of pitcher fluid of the carnivorous plant Nepenthes alata

Author keywords

Carnivorous plants; De novo sequencing; Nepenthes; PR protein; Proteome

Indexed keywords

1,3 BETA GLUCANASE; CHITINASE; THAUMATIN; XYLAN 1,4 BETA XYLOSIDASE;

EID: 39749087658     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr700566d     Document Type: Article
Times cited : (95)

References (27)
  • 2
    • 0006287726 scopus 로고    scopus 로고
    • The enduring controversies concerning the process of protein digestion in Nepenthes (Nepenaceae)
    • Frazier, C. K. The enduring controversies concerning the process of protein digestion in Nepenthes (Nepenaceae). Carnivorous Plant Newsletter 2000, 29, 56-61.
    • (2000) Carnivorous Plant Newsletter , vol.29 , pp. 56-61
    • Frazier, C.K.1
  • 3
    • 0000267820 scopus 로고
    • Reinigung der Proteinase aus Nepenthes-Kannensaft. (Purification of the proteinase from Nepenthes pitcher serection)
    • Steckelberg, R.; Lüttge, U.; Weigl, J. Reinigung der Proteinase aus Nepenthes-Kannensaft. (Purification of the proteinase from Nepenthes pitcher serection). Planta 1967, 76, 238-241.
    • (1967) Planta , vol.76 , pp. 238-241
    • Steckelberg, R.1    Lüttge, U.2    Weigl, J.3
  • 4
    • 0000100391 scopus 로고
    • Acid protease in Nepenthes: Partial purification and properties of the enzymes
    • Nakayama, S.; Amagase, S. Acid protease in Nepenthes: Partial purification and properties of the enzymes. Proc. Jpn. Acad. 1968, 44, 358-362.
    • (1968) Proc. Jpn. Acad , vol.44 , pp. 358-362
    • Nakayama, S.1    Amagase, S.2
  • 6
    • 0003135365 scopus 로고
    • Digestive enzymes secreted by the carnivorous plant Nepenthes macferlanei L
    • Tökés, Z. A.; Woon, W. C.; Chambers, S. M. Digestive enzymes secreted by the carnivorous plant Nepenthes macferlanei L. Planta 1974, 119, 39-46.
    • (1974) Planta , vol.119 , pp. 39-46
    • Tökés, Z.A.1    Woon, W.C.2    Chambers, S.M.3
  • 7
    • 0002510875 scopus 로고
    • Analysis of feeding mechanism in a pitcher of Nepenthes hybrida
    • Higashi, S.; Nakashima, A.; Ozaki, H.; Abe, M.; Uchiumi, T. Analysis of feeding mechanism in a pitcher of Nepenthes hybrida. J. Plant Res. 1993, 106, 47-54.
    • (1993) J. Plant Res , vol.106 , pp. 47-54
    • Higashi, S.1    Nakashima, A.2    Ozaki, H.3    Abe, M.4    Uchiumi, T.5
  • 8
    • 0015370532 scopus 로고
    • Digestive enzymes in the insectivorous plants: III. Acid proteases in the genus Nepenthes and Drosera peltata
    • Amagase, S. Digestive enzymes in the insectivorous plants: III. Acid proteases in the genus Nepenthes and Drosera peltata. J. Biochem. (Tokyo) 1972, 72, 73-81.
    • (1972) J. Biochem. (Tokyo) , vol.72 , pp. 73-81
    • Amagase, S.1
  • 9
    • 33747871549 scopus 로고    scopus 로고
    • Isolation and characterization of chitinase genes from pitchers of the carnivorous plant Nepenthes khasiana
    • Eilenberg, H.; Pnini-Cohen, S.; Schuster, S.; Movtchan, A.; Zilberstein, A. Isolation and characterization of chitinase genes from pitchers of the carnivorous plant Nepenthes khasiana. J. Exp. Bot. 2006, 57, 2775-2784.
    • (2006) J. Exp. Bot , vol.57 , pp. 2775-2784
    • Eilenberg, H.1    Pnini-Cohen, S.2    Schuster, S.3    Movtchan, A.4    Zilberstein, A.5
  • 12
  • 13
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko, A.; Wilm, M.; Vorm, O.; Mann, M. Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal. Chem. 1996, 68, 850-858.
    • (1996) Anal. Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 14
    • 0345791524 scopus 로고    scopus 로고
    • Proteomic analysis of rat liver peroxisome: Presence of peroxisome-specific isozyme of Lon protease
    • Kikuchi, M.; Hatano, N.; Yokota, S.; Shimozawa, N.; Imanaka, T.; Taniguchi, H. Proteomic analysis of rat liver peroxisome: Presence of peroxisome-specific isozyme of Lon protease. J. Biol. Chem. 2004, 279, 421-428.
    • (2004) J. Biol. Chem , vol.279 , pp. 421-428
    • Kikuchi, M.1    Hatano, N.2    Yokota, S.3    Shimozawa, N.4    Imanaka, T.5    Taniguchi, H.6
  • 16
    • 28444435561 scopus 로고    scopus 로고
    • Rapid and reliable method of extracting DNA and RNA from sweetpotato, Ipomoea batatas (L). Lam
    • Kim, S. H.; Hamada, T. Rapid and reliable method of extracting DNA and RNA from sweetpotato, Ipomoea batatas (L). Lam. Biotechnol. Lett. 2005, 27, 1841-1845.
    • (2005) Biotechnol. Lett , vol.27 , pp. 1841-1845
    • Kim, S.H.1    Hamada, T.2
  • 17
    • 0022454902 scopus 로고
    • A tobacco mosaic virus-induced tobacco protein is homologous to the sweet-tasting protein thaumatin
    • Cornelissen, B. J.; Hooft van Huijsduijnen, R. A.; Bol, J. F. A tobacco mosaic virus-induced tobacco protein is homologous to the sweet-tasting protein thaumatin. Nature 1986, 321, 531-532.
    • (1986) Nature , vol.321 , pp. 531-532
    • Cornelissen, B.J.1    Hooft van Huijsduijnen, R.A.2    Bol, J.F.3
  • 18
    • 0033179482 scopus 로고    scopus 로고
    • The families of pathogenesis-related protein, their activities, and comparative analysis of PR-1 type proteins
    • van Loon, L. C.; van Strien, E. A. The families of pathogenesis-related protein, their activities, and comparative analysis of PR-1 type proteins. Physiol. Mol. Plant Pathol. 1999, 55, 85-97.
    • (1999) Physiol. Mol. Plant Pathol , vol.55 , pp. 85-97
    • van Loon, L.C.1    van Strien, E.A.2
  • 19
    • 0002570240 scopus 로고
    • Regulation of changes in proteins and enzymes associated with active defense against virus infection
    • Wood, R. K. S, Ed, Plenum: New York
    • Van Loon, L. C. Regulation of changes in proteins and enzymes associated with active defense against virus infection. In Active Defence Mechanisms in Plants; Wood, R. K. S., Ed.; Plenum: New York, 1982; pp 247-273.
    • (1982) Active Defence Mechanisms in Plants , pp. 247-273
    • Van Loon, L.C.1
  • 20
    • 27944448231 scopus 로고
    • The major proteins in extracts of tobacco leaves that are responding hypersensitively to virus-infection
    • Pierpoint, W. S. The major proteins in extracts of tobacco leaves that are responding hypersensitively to virus-infection. Phytochemistry 1983, 22, 2691-2697.
    • (1983) Phytochemistry , vol.22 , pp. 2691-2697
    • Pierpoint, W.S.1
  • 21
    • 0001376743 scopus 로고
    • Pathogenesis-related proteins
    • van Loon, L. C. Pathogenesis-related proteins. Plant Mol. Biol. 1985, 4, 111-116.
    • (1985) Plant Mol. Biol , vol.4 , pp. 111-116
    • van Loon, L.C.1
  • 23
    • 0001324867 scopus 로고
    • Antifungal hydrolases in pea tissue. II. Inhibition of fungal growth by combinations of chitinase and β-1,3-glucanase
    • Mauch, F.; Mauch-Mani, B.; Boller, T. Antifungal hydrolases in pea tissue. II. Inhibition of fungal growth by combinations of chitinase and β-1,3-glucanase. Plant Physiol. 1988, 88, 936-942.
    • (1988) Plant Physiol , vol.88 , pp. 936-942
    • Mauch, F.1    Mauch-Mani, B.2    Boller, T.3
  • 24
    • 0032253808 scopus 로고    scopus 로고
    • Several thaumatin-like proteins bind to β-1,3-glucans
    • Trudel, J.; Grenier, J.; Potvin, C.; Asselin, A. Several thaumatin-like proteins bind to β-1,3-glucans. Plant Physiol. 1998, 118, 1431-1438.
    • (1998) Plant Physiol , vol.118 , pp. 1431-1438
    • Trudel, J.1    Grenier, J.2    Potvin, C.3    Asselin, A.4
  • 25
    • 0033180204 scopus 로고    scopus 로고
    • Some thaumatin-like proteins hydrolyse polymeric β-1,3-glucans
    • Grenier, J.; Potvin, C.; Trudel, J.; Asselin, A. Some thaumatin-like proteins hydrolyse polymeric β-1,3-glucans. Plant J. 1999, 19, 473-480.
    • (1999) Plant J , vol.19 , pp. 473-480
    • Grenier, J.1    Potvin, C.2    Trudel, J.3    Asselin, A.4
  • 26
    • 0030909499 scopus 로고    scopus 로고
    • Structual and evolutionary relationships among chitinases of flowering plants
    • Hamel, F.; Boivin, R.; Tremblay, C.; Bellemare, G. Structual and evolutionary relationships among chitinases of flowering plants. J. Mol. Evol. 1997, 44, 614-624.
    • (1997) J. Mol. Evol , vol.44 , pp. 614-624
    • Hamel, F.1    Boivin, R.2    Tremblay, C.3    Bellemare, G.4
  • 27
    • 0037297226 scopus 로고    scopus 로고
    • AtBXL1, a novel higher plant (Arabidopsis thaliana) putative β-xylosidase gene, is involved in secondary cell wall metabolism and plant development
    • Goujon, T.; Minie, Z.; El Amrani, A.; Lerouxel, O.; Aletti, E.; Lapierre, C.; Joseleau, J. P.; Jouanin, L. AtBXL1, a novel higher plant (Arabidopsis thaliana) putative β-xylosidase gene, is involved in secondary cell wall metabolism and plant development. Plant J. 2003, 33, 677-690.
    • (2003) Plant J , vol.33 , pp. 677-690
    • Goujon, T.1    Minie, Z.2    El Amrani, A.3    Lerouxel, O.4    Aletti, E.5    Lapierre, C.6    Joseleau, J.P.7    Jouanin, L.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.