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Volumn 54, Issue 5, 2011, Pages

Isolation of recombinant cysteine dioxygenase protein from Trichophyton mentagrophytes

Author keywords

CDNA; Cysteine dioxygenase; Dermatophytes; Keratinolytic fungi; Recombinant protein

Indexed keywords

COMPLEMENTARY DNA; CYSTEINE; CYSTEINE DIOXYGENASE; CYSTEINE SULPHINATE; HISTONE; RECOMBINANT CYSTEINE DIOXYGENASE; RECOMBINANT PROTEIN; SULFINIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

EID: 80052792179     PISSN: 09337407     EISSN: 14390507     Source Type: Journal    
DOI: 10.1111/j.1439-0507.2010.01948.x     Document Type: Article
Times cited : (11)

References (23)
  • 1
    • 55149091122 scopus 로고    scopus 로고
    • Secreted proteases from dermatophytes
    • Monod M. Secreted proteases from dermatophytes. Mycopathologia 2008; 166: 285-94.
    • (2008) Mycopathologia , vol.166 , pp. 285-294
    • Monod, M.1
  • 2
    • 0024957560 scopus 로고
    • Biochemical mechanism of keratin degradation by the actinomycete Streptomyces fradiae and the fungus Microsporum gypseum- a comparison
    • Kunert J. Biochemical mechanism of keratin degradation by the actinomycete Streptomyces fradiae and the fungus Microsporum gypseum- a comparison. J Basic Microbiol 1989; 29: 597-604.
    • (1989) J Basic Microbiol , vol.29 , pp. 597-604
    • Kunert, J.1
  • 3
    • 0033809689 scopus 로고    scopus 로고
    • Physiology of keratinophilic fungi
    • Kushwaha RKS, Guarro J (eds), Bilbao: Revista Iberoamericana de Micología
    • Kunert J. Physiology of keratinophilic fungi. In: Kushwaha RKS, Guarro J (eds), Biology of Dermatophytes and Other Keratinophilic Fungi. Bilbao: Revista Iberoamericana de Micología, 2000: 77-85.
    • (2000) Biology of Dermatophytes and Other Keratinophilic Fungi , pp. 77-85
    • Kunert, J.1
  • 4
    • 32944454336 scopus 로고    scopus 로고
    • Regulation of cysteine dioxygenase degradation is mediated by intracellular cysteine levels and the ubiquitin-26 S proteasome system in the living rat
    • Dominy JE Jr, Hirschberger LL, Coloso RM, Stipanuk MH. Regulation of cysteine dioxygenase degradation is mediated by intracellular cysteine levels and the ubiquitin-26 S proteasome system in the living rat. Biochem J 2006; 394: 267-73.
    • (2006) Biochem J , vol.394 , pp. 267-273
    • Dominy Jr, J.E.1    Hirschberger, L.L.2    Coloso, R.M.3    Stipanuk, M.H.4
  • 5
    • 36849079937 scopus 로고    scopus 로고
    • The mechanism of cysteine oxygenation by cysteine dioxygenase enzymes
    • Aluri S, de Visser SP. The mechanism of cysteine oxygenation by cysteine dioxygenase enzymes. J Am Chem Soc 2007; 129: 14846-7.
    • (2007) J Am Chem Soc , vol.129 , pp. 14846-14847
    • Aluri, S.1    de Visser, S.P.2
  • 6
    • 34547758450 scopus 로고    scopus 로고
    • Cysteine dioxygenase: structure and mechanism
    • Joseph CA, Maroney MJ. Cysteine dioxygenase: structure and mechanism. Chem Commun 2007; 32: 3338-49.
    • (2007) Chem Commun , vol.32 , pp. 3338-3349
    • Joseph, C.A.1    Maroney, M.J.2
  • 8
    • 7944228774 scopus 로고    scopus 로고
    • Isolation and characterization of an immunogenic fragment of heat shock protein 60 from Trichophyton mentagrophytes
    • Raska M, Zemanova E, Kafkova L et al. Isolation and characterization of an immunogenic fragment of heat shock protein 60 from Trichophyton mentagrophytes. Mycoses 2004; 47: 482-90.
    • (2004) Mycoses , vol.47 , pp. 482-490
    • Raska, M.1    Zemanova, E.2    Kafkova, L.3
  • 9
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P, Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 1987; 162: 156-9.
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 10
    • 41449117230 scopus 로고    scopus 로고
    • Evaluation of the possible proteomic application of trypsin from Streptomyces griseus
    • Stosova T, Sebela M, Rehulka P, Sedo O, Havlis J, Zdrahal Z. Evaluation of the possible proteomic application of trypsin from Streptomyces griseus. Anal Biochem 2008; 376: 94-102.
    • (2008) Anal Biochem , vol.376 , pp. 94-102
    • Stosova, T.1    Sebela, M.2    Rehulka, P.3    Sedo, O.4    Havlis, J.5    Zdrahal, Z.6
  • 12
    • 0014018635 scopus 로고
    • Characteristics of the cysteine sulfinate-forming enzyme system in rat liver
    • Ewetz L, Sörbo B. Characteristics of the cysteine sulfinate-forming enzyme system in rat liver. Biochim Biophys Acta 1966; 128: 296-305.
    • (1966) Biochim Biophys Acta , vol.128 , pp. 296-305
    • Ewetz, L.1    Sörbo, B.2
  • 13
    • 0014669518 scopus 로고
    • Cystein oxygenase. II. Studies on the mechanism of the reaction with 18 oxygen
    • Lombardini JB, Singer TP, Boyer PD. Cystein oxygenase. II. Studies on the mechanism of the reaction with 18 oxygen. J Biol Chem 1969; 244: 1172-5.
    • (1969) J Biol Chem , vol.244 , pp. 1172-1175
    • Lombardini, J.B.1    Singer, T.P.2    Boyer, P.D.3
  • 14
    • 33746622949 scopus 로고    scopus 로고
    • Identification and characterization of bacterial cysteine dioxygenases: a new route of cysteine degradation for eubacteria
    • Dominy JE Jr, Simmons CR, Karplus PA, Gehring AM, Stipanuk MH. Identification and characterization of bacterial cysteine dioxygenases: a new route of cysteine degradation for eubacteria. J Bacteriol 2006; 188: 5561-9.
    • (2006) J Bacteriol , vol.188 , pp. 5561-5569
    • Dominy Jr, J.E.1    Simmons, C.R.2    Karplus, P.A.3    Gehring, A.M.4    Stipanuk, M.H.5
  • 15
    • 0017848886 scopus 로고
    • Rat liver cysteine dioxygenase (cysteine oxidase). Further purification, characterization, and analysis of the activation and inactivation
    • Yamaguchi K, Hosokawa Y, Kohashi N, Kori Y, Sakakibara S, Ueda I. Rat liver cysteine dioxygenase (cysteine oxidase). Further purification, characterization, and analysis of the activation and inactivation. J Biochem 1978; 83: 479-91.
    • (1978) J Biochem , vol.83 , pp. 479-491
    • Yamaguchi, K.1    Hosokawa, Y.2    Kohashi, N.3    Kori, Y.4    Sakakibara, S.5    Ueda, I.6
  • 16
    • 33745854127 scopus 로고    scopus 로고
    • Crystal structure of mammalian cysteine dioxygenase. A novel mononuclear iron center for cysteine thiol oxidation
    • Simmons CR, Liu Q, Huang Q et al. Crystal structure of mammalian cysteine dioxygenase. A novel mononuclear iron center for cysteine thiol oxidation. J Biol Chem 2006; 281: 18723-33.
    • (2006) J Biol Chem , vol.281 , pp. 18723-18733
    • Simmons, C.R.1    Liu, Q.2    Huang, Q.3
  • 17
    • 0742287185 scopus 로고    scopus 로고
    • Cupins: the most functionally diverse protein superfamily?
    • Dunwell JM, Purvis A, Khuri S. Cupins: the most functionally diverse protein superfamily? Phytochemistry 2004; 65: 7-17.
    • (2004) Phytochemistry , vol.65 , pp. 7-17
    • Dunwell, J.M.1    Purvis, A.2    Khuri, S.3
  • 18
    • 0037069364 scopus 로고    scopus 로고
    • Metabolic specialization associated with phenotypic switching in Candida albicans
    • Lan CY, Newport G, Murillo LA et al. Metabolic specialization associated with phenotypic switching in Candida albicans. Proc Natl Acad Sci USA 2002; 99: 14907-12.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14907-14912
    • Lan, C.Y.1    Newport, G.2    Murillo, L.A.3
  • 19
    • 0019506406 scopus 로고
    • Temperature- and cyclic nucleotide-induced phase transitions of Histoplasma capsulatum
    • Sacco M, Maresca B, Kumar BV, Kobayashi GS, Medoff G. Temperature- and cyclic nucleotide-induced phase transitions of Histoplasma capsulatum. J Bacteriol 1981; 146: 117-20.
    • (1981) J Bacteriol , vol.146 , pp. 117-120
    • Sacco, M.1    Maresca, B.2    Kumar, B.V.3    Kobayashi, G.S.4    Medoff, G.5
  • 20
    • 0020581235 scopus 로고
    • Purification and characterization of a cysteine dioxygenase from the yeast phase of Histoplasma capsulatum
    • Kumar V, Maresca B, Sacco M, Goewert R, Kobayashi GS, Medoff G. Purification and characterization of a cysteine dioxygenase from the yeast phase of Histoplasma capsulatum. Biochemistry 1983; 22: 762-8.
    • (1983) Biochemistry , vol.22 , pp. 762-768
    • Kumar, V.1    Maresca, B.2    Sacco, M.3    Goewert, R.4    Kobayashi, G.S.5    Medoff, G.6
  • 21
    • 33646087886 scopus 로고    scopus 로고
    • Expression, purification, and kinetic characterization of recombinant rat cysteine dioxygenase, a non-heme metalloenzyme necessary for regulation of cellular cysteine levels
    • Simmons CR, Hirschberger LL, Machi MS, Stipanuk MH. Expression, purification, and kinetic characterization of recombinant rat cysteine dioxygenase, a non-heme metalloenzyme necessary for regulation of cellular cysteine levels. Protein Expr Purif 2006; 47: 74-81.
    • (2006) Protein Expr Purif , vol.47 , pp. 74-81
    • Simmons, C.R.1    Hirschberger, L.L.2    Machi, M.S.3    Stipanuk, M.H.4
  • 22
    • 64549148454 scopus 로고    scopus 로고
    • The effect of post-translational and process-induced modifications on the multistage gas-phase fragmentation reactions of protonated peptides
    • Froelich JM, Reid GE. The effect of post-translational and process-induced modifications on the multistage gas-phase fragmentation reactions of protonated peptides. Comb Chem High Throughput Screen 2009; 12: 175-84.
    • (2009) Comb Chem High Throughput Screen , vol.12 , pp. 175-184
    • Froelich, J.M.1    Reid, G.E.2
  • 23
    • 23044505203 scopus 로고    scopus 로고
    • Oxidation of carboxyamidomethyl cysteine may add complexity to protein identification
    • Yague J, Nunez A, Boix M, Esteller M, Alfonso P, Casal JI. Oxidation of carboxyamidomethyl cysteine may add complexity to protein identification. Proteomics 2005; 5: 2761-8.
    • (2005) Proteomics , vol.5 , pp. 2761-2768
    • Yague, J.1    Nunez, A.2    Boix, M.3    Esteller, M.4    Alfonso, P.5    Casal, J.I.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.