메뉴 건너뛰기




Volumn 420, Issue 4, 2012, Pages 862-868

A structurally novel hemopexin fold protein of rice plays role in chlorophyll degradation

Author keywords

Chlorophyll degradation; Hemin; Hemopexin fold protein; OsHFP; Rice anther

Indexed keywords

CHLOROPHYLL; HEMIN; HEMOPEXIN; ORYZA SATIVA HEMOPEXIN FOLD PROTEIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 84859811135     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.03.089     Document Type: Article
Times cited : (10)

References (21)
  • 1
    • 33947654354 scopus 로고    scopus 로고
    • Hemopexin domains as multifunctional liganding modules in matrix metalloproteinases and other proteins
    • Piccard H., Van den Steen P.E., Opdenakker G. Hemopexin domains as multifunctional liganding modules in matrix metalloproteinases and other proteins. J. Leukoc. Biol. 2007, 81:870-892.
    • (2007) J. Leukoc. Biol. , vol.81 , pp. 870-892
    • Piccard, H.1    Van den Steen, P.E.2    Opdenakker, G.3
  • 2
    • 0036259938 scopus 로고    scopus 로고
    • Hemopexin: structure, function, and regulation
    • Tolosano E., Altruda F. Hemopexin: structure, function, and regulation. DNA Cell Biol. 2002, 21:297-306.
    • (2002) DNA Cell Biol. , vol.21 , pp. 297-306
    • Tolosano, E.1    Altruda, F.2
  • 5
    • 0029802271 scopus 로고    scopus 로고
    • Role of hemopexin in protection of low-density lipoprotein against hemoglobin-induced oxidation
    • Miller Y.I., Smith A., Morgan W.T., Shaklai N. Role of hemopexin in protection of low-density lipoprotein against hemoglobin-induced oxidation. Biochemistry 1996, 35:13112-13117.
    • (1996) Biochemistry , vol.35 , pp. 13112-13117
    • Miller, Y.I.1    Smith, A.2    Morgan, W.T.3    Shaklai, N.4
  • 6
    • 0023627387 scopus 로고
    • Nucleotide sequence and organization of the human S-protein gene: repeating peptide motifs in the " pexin" family and a model for their evolution
    • Jenne D., Stanley K.K. Nucleotide sequence and organization of the human S-protein gene: repeating peptide motifs in the " pexin" family and a model for their evolution. Biochemistry 1987, 26:6735-6742.
    • (1987) Biochemistry , vol.26 , pp. 6735-6742
    • Jenne, D.1    Stanley, K.K.2
  • 7
    • 0025813131 scopus 로고
    • Homology of placental protein 11 and pea seed albumin 2 with vitronectin
    • Jenne D. Homology of placental protein 11 and pea seed albumin 2 with vitronectin. Biochem. Biophys. Res. Commun. 1991, 176:1000-1006.
    • (1991) Biochem. Biophys. Res. Commun. , vol.176 , pp. 1000-1006
    • Jenne, D.1
  • 8
    • 40749094477 scopus 로고    scopus 로고
    • Combined metabolomic and genetic approaches reveal a link between the polyamine pathway and albumin 2 in developing pea seeds
    • Vigeolas H., Chinoy C., Zuther E., Blessington B., Geigenberger P., Domoney C. Combined metabolomic and genetic approaches reveal a link between the polyamine pathway and albumin 2 in developing pea seeds. Plant Physiol. 2008, 146:74-82.
    • (2008) Plant Physiol. , vol.146 , pp. 74-82
    • Vigeolas, H.1    Chinoy, C.2    Zuther, E.3    Blessington, B.4    Geigenberger, P.5    Domoney, C.6
  • 10
    • 79953100002 scopus 로고    scopus 로고
    • The Arabidopsis multistress regulator TSPO is a heme binding membrane protein and a potential scavenger of porphyrins via an autophagy-dependent degradation mechanism
    • Vanhee C., Zapotoczny G., Masquelier D., Ghislain M., Batoko H. The Arabidopsis multistress regulator TSPO is a heme binding membrane protein and a potential scavenger of porphyrins via an autophagy-dependent degradation mechanism. Plant Cell 2011, 23:785-805.
    • (2011) Plant Cell , vol.23 , pp. 785-805
    • Vanhee, C.1    Zapotoczny, G.2    Masquelier, D.3    Ghislain, M.4    Batoko, H.5
  • 11
    • 77950547509 scopus 로고    scopus 로고
    • Crystal structure and functional insights of hemopexin fold protein from grass pea
    • Gaur V., Qureshi I.A., Singh A., Chanana V., Salunke D.M. Crystal structure and functional insights of hemopexin fold protein from grass pea. Plant Physiol. 2010, 152:1842-1850.
    • (2010) Plant Physiol. , vol.152 , pp. 1842-1850
    • Gaur, V.1    Qureshi, I.A.2    Singh, A.3    Chanana, V.4    Salunke, D.M.5
  • 12
    • 79951485050 scopus 로고    scopus 로고
    • The structure of a haemopexin-fold protein from cow pea (Vigna unguiculata) suggests functional diversity of haemopexins in plants
    • Gaur V., Chanana V., Jain A., Salunke D.M. The structure of a haemopexin-fold protein from cow pea (Vigna unguiculata) suggests functional diversity of haemopexins in plants. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2011, 67:193-200.
    • (2011) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. , vol.67 , pp. 193-200
    • Gaur, V.1    Chanana, V.2    Jain, A.3    Salunke, D.M.4
  • 13
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994, 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 14
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restrains
    • Sali A., Blundell T.L. Comparative protein modelling by satisfaction of spatial restrains. J. Mol. Biol. 1993, 234:779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 16
    • 77949872681 scopus 로고    scopus 로고
    • Functional role of rice germin-like protein1 in regulation of plant height and disease resistance
    • Banerjee J., Maiti M.K. Functional role of rice germin-like protein1 in regulation of plant height and disease resistance. Biochem. Biophys. Res. Commun. 2010, 394:178-183.
    • (2010) Biochem. Biophys. Res. Commun. , vol.394 , pp. 178-183
    • Banerjee, J.1    Maiti, M.K.2
  • 17
    • 79952696237 scopus 로고    scopus 로고
    • Development of a transgenic hairy root system in jute (Corchorus capsularis L.) with gusA reporter gene through Agrobacterium rhizogenes mediated co-transformation
    • Chattopadhyay T., Roy S., Mitra A., Maiti M.K. Development of a transgenic hairy root system in jute (Corchorus capsularis L.) with gusA reporter gene through Agrobacterium rhizogenes mediated co-transformation. Plant Cell Rep. 2011, 30:485-493.
    • (2011) Plant Cell Rep. , vol.30 , pp. 485-493
    • Chattopadhyay, T.1    Roy, S.2    Mitra, A.3    Maiti, M.K.4
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantity of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantification of microgram quantity of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 0032825215 scopus 로고    scopus 로고
    • Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two beta-propeller domains
    • Paoli M., Anderson B.F., Baker H.M., Morgan W.T., Smith A., Baker E.N. Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two beta-propeller domains. Nat. Struct. Biol. 1999, 6:926-931.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 926-931
    • Paoli, M.1    Anderson, B.F.2    Baker, H.M.3    Morgan, W.T.4    Smith, A.5    Baker, E.N.6
  • 21
    • 0035895231 scopus 로고    scopus 로고
    • The Arabidopsis-accelerated cell death gene ACD2 encodes red chlorophyll catabolite reductase and suppresses the spread of disease symptoms
    • Mach J.M., Castillo A.R., Hoogstraten R., Greenberg J.T. The Arabidopsis-accelerated cell death gene ACD2 encodes red chlorophyll catabolite reductase and suppresses the spread of disease symptoms. Proc. Natl. Acad. Sci. USA 2001, 98:771-776.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 771-776
    • Mach, J.M.1    Castillo, A.R.2    Hoogstraten, R.3    Greenberg, J.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.