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Volumn 239, Issue 2, 1999, Pages 325-331

Isolation and mapping of a human lung-specific gene, TSA1902, encoding a novel chitinase family member

Author keywords

Chitinase; Differential display; Lung specific gene

Indexed keywords

CHITINASE;

EID: 0032735186     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(99)00394-7     Document Type: Article
Times cited : (28)

References (27)
  • 2
    • 0028108580 scopus 로고
    • Complementary deoxyribonucleic acid cloning and molecular characterization of an estrogen-dependent human oviductal glycoprotein
    • Arias E.B., Verhage H.G., Jaffe R.C. Complementary deoxyribonucleic acid cloning and molecular characterization of an estrogen-dependent human oviductal glycoprotein. Biol. Reprod. 51:1994;685-694.
    • (1994) Biol. Reprod. , vol.51 , pp. 685-694
    • Arias, E.B.1    Verhage, H.G.2    Jaffe, R.C.3
  • 5
    • 0026709204 scopus 로고
    • What's new in chitinase research?
    • Flach J., Pilet P.-E., Jolles P. What's new in chitinase research? Experientia. 48:1992;701-716.
    • (1992) Experientia , vol.48 , pp. 701-716
    • Flach, J.1    Pilet, P.-E.2    Jolles, P.3
  • 7
    • 0027505001 scopus 로고
    • Human cartilage gp-39, a major secretory product of articular chondrocytes and synovial cells, is a mammalian member of a chitinase protein family
    • Hakala B.E., White C., Recklies A.D. Human cartilage gp-39, a major secretory product of articular chondrocytes and synovial cells, is a mammalian member of a chitinase protein family. J. Biol. Chem. 268:1993;25803-25810.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25803-25810
    • Hakala, B.E.1    White, C.2    Recklies, A.D.3
  • 8
    • 0031826040 scopus 로고    scopus 로고
    • SOSUI: Classification and secondary structure prediction system for membrane proteins
    • Hirokawa T., Boon-Chieng S., Mitaku S. SOSUI: classification and secondary structure prediction system for membrane proteins. Bioinformatics. 14:1998;378-379.
    • (1998) Bioinformatics , vol.14 , pp. 378-379
    • Hirokawa, T.1    Boon-Chieng, S.2    Mitaku, S.3
  • 10
    • 0029765534 scopus 로고    scopus 로고
    • Isolation and sequence of a novel human chondrocyte protein related to mammalian members of the chitinase protein family
    • Hu B., Trinh K., Figueira W.F., Price P.A. Isolation and sequence of a novel human chondrocyte protein related to mammalian members of the chitinase protein family. J. Biol. Chem. 271:1996;19415-19420.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19415-19420
    • Hu, B.1    Trinh, K.2    Figueira, W.F.3    Price, P.A.4
  • 12
    • 0026002418 scopus 로고
    • Chitinase is required for cell separation during growth of Saccharomyces cerevisiae
    • Kuranda M.J., Robbins P.W. Chitinase is required for cell separation during growth of Saccharomyces cerevisiae. J. Biol. Chem. 266:1991;19758-19767.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19758-19767
    • Kuranda, M.J.1    Robbins, P.W.2
  • 13
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:1982;105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 14
    • 0026674886 scopus 로고
    • Differential display of eukaryotic messenger RNA by means of the polymerase chain reaction
    • Liang P., Pardee A.B. Differential display of eukaryotic messenger RNA by means of the polymerase chain reaction. Science. 257:1992;967-971.
    • (1992) Science , vol.257 , pp. 967-971
    • Liang, P.1    Pardee, A.B.2
  • 15
    • 0028063457 scopus 로고
    • Neu and ras initiate murine mammary tumors that share genetic markers generally absent in c-myc and int-2-initiated tumors
    • Morrison B.W., Leder P. neu and ras initiate murine mammary tumors that share genetic markers generally absent in c-myc and int-2-initiated tumors. Oncogene. 9:1994;3417-3426.
    • (1994) Oncogene , vol.9 , pp. 3417-3426
    • Morrison, B.W.1    Leder, P.2
  • 16
    • 0003447671 scopus 로고
    • R.A.A. Muzzarelli, C. Jeuniaux, & G.W. Gooday. New York: Plenum Press
    • Muzzarelli R.A.A., Jeuniaux C., Gooday G.W. Chitin in Nature and Technology. 1986;Plenum Press, New York.
    • (1986) Chitin in Nature and Technology
  • 17
    • 0030248629 scopus 로고    scopus 로고
    • Isolation of three testis-specific genes (TSA303, TSA806, TSA903) by a differential mRNA display method
    • Ozaki K., Kuroki T., Hayashi S., Nakamura Y. Isolation of three testis-specific genes (TSA303, TSA806, TSA903) by a differential mRNA display method. Genomics. 36:1996;316-319.
    • (1996) Genomics , vol.36 , pp. 316-319
    • Ozaki, K.1    Kuroki, T.2    Hayashi, S.3    Nakamura, Y.4
  • 19
    • 0032529242 scopus 로고    scopus 로고
    • Isolation and characterization of a novel human lung-specific gene homologous to lysosomal membrane glycoproteins 1 and 2: Significantly increased expression in cancers of various tissues
    • Ozaki K., Nagata M., Suzuki M., Fujiwara T., Ueda K., Miyoshi Y., Takahashi E., Nakamura Y. Isolation and characterization of a novel human lung-specific gene homologous to lysosomal membrane glycoproteins 1 and 2: significantly increased expression in cancers of various tissues. Cancer Res. 58:1998;3499-3503.
    • (1998) Cancer Res. , vol.58 , pp. 3499-3503
    • Ozaki, K.1    Nagata, M.2    Suzuki, M.3    Fujiwara, T.4    Ueda, K.5    Miyoshi, Y.6    Takahashi, E.7    Nakamura, Y.8
  • 20
    • 0032518453 scopus 로고    scopus 로고
    • Chitotriosidase, a chitinase, and the 39-kDa human cartilage glycoprotein, a chitin-binding lectin, are homologues of family 18 glycosyl hydrolases secreted by human macrophages
    • Renkema G.H., Boot R.G., Au F.L., Donker-Koopman W.E., Strijland A., Muijsers A.O., Hrebicek M., Aerts J.M.F.G. Chitotriosidase, a chitinase, and the 39-kDa human cartilage glycoprotein, a chitin-binding lectin, are homologues of family 18 glycosyl hydrolases secreted by human macrophages. Eur. J. Biochem. 251:1998;504-509.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 504-509
    • Renkema, G.H.1    Boot, R.G.2    Au, F.L.3    Donker-Koopman, W.E.4    Strijland, A.5    Muijsers, A.O.6    Hrebicek, M.7    Aerts, J.M.F.G.8
  • 21
    • 0001194009 scopus 로고
    • Plant and bacterial chitinases differ in antifungal activity
    • Roberts W.K., Selitrennikoff C.P. Plant and bacterial chitinases differ in antifungal activity. J. Gen. Microbiol. 134:1988;169-176.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 169-176
    • Roberts, W.K.1    Selitrennikoff, C.P.2
  • 22
    • 0001519173 scopus 로고
    • Plant chitinases are potent inhibitors of fungal growth
    • Schlumbaum A., Mauch F., Vögeli U., Boller T. Plant chitinases are potent inhibitors of fungal growth. Nature. 324:1986;365-367.
    • (1986) Nature , vol.324 , pp. 365-367
    • Schlumbaum, A.1    Mauch, F.2    Vögeli, U.3    Boller, T.4
  • 24
    • 0030665155 scopus 로고    scopus 로고
    • Characterization of a novel gut-specific chitinase gene from the human malaria vector Anopheles gambiae
    • Shen Z., Jacobs-Lorena M. Characterization of a novel gut-specific chitinase gene from the human malaria vector Anopheles gambiae. J. Biol. Chem. 272:1997;28895-28900.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28895-28900
    • Shen, Z.1    Jacobs-Lorena, M.2
  • 25
    • 0031669733 scopus 로고    scopus 로고
    • Intracellular chitinase gene from Rhizopus oligosporus: Molecular cloning and characterization
    • Takaya N., Yamazaki D., Horiuchi H., Ohta A., Takagi M. Intracellular chitinase gene from Rhizopus oligosporus: molecular cloning and characterization. Microbiology. 144:1998;2647-2654.
    • (1998) Microbiology , vol.144 , pp. 2647-2654
    • Takaya, N.1    Yamazaki, D.2    Horiuchi, H.3    Ohta, A.4    Takagi, M.5
  • 26
    • 0027216435 scopus 로고
    • Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity
    • Watanabe T., Kobori K., Miyashita K., Fujii T., Sakai H., Uchida M., Tanaka H. Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity. J. Biol. Chem. 268:1993;18567-18572.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18567-18572
    • Watanabe, T.1    Kobori, K.2    Miyashita, K.3    Fujii, T.4    Sakai, H.5    Uchida, M.6    Tanaka, H.7
  • 27
    • 0028713479 scopus 로고
    • Site-directed mutagenesis of the Asp-197 and Asp-202 residues in chitinase A1 of Bacillus circulans WL-12
    • Watanabe T., Uchida M., Kobori K., Tanaka H. Site-directed mutagenesis of the Asp-197 and Asp-202 residues in chitinase A1 of Bacillus circulans WL-12. Biosci. Biotechnol. Biochem. 58:1994;2283-2285.
    • (1994) Biosci. Biotechnol. Biochem. , vol.58 , pp. 2283-2285
    • Watanabe, T.1    Uchida, M.2    Kobori, K.3    Tanaka, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.