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Volumn 23, Issue 4, 1999, Pages 433-436

Mutations in ELA2, encoding neutrophil elastase, define a 21-day biological clock in cyclic haematopoiesis

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 1 ANTITRYPSIN; LEUKOCYTE ELASTASE; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR;

EID: 0032757863     PISSN: 10614036     EISSN: None     Source Type: Journal    
DOI: 10.1038/70544     Document Type: Article
Times cited : (392)

References (23)
  • 1
    • 0032532631 scopus 로고    scopus 로고
    • Cyclical neutropenia and other periodic hematological disorders: A review of mechanisms and mathematical models
    • Haurie, C., Dale, D.C. & Mackey, M.C. Cyclical neutropenia and other periodic hematological disorders: a review of mechanisms and mathematical models. Blood 92, 2629-2640 (1998).
    • (1998) Blood , vol.92 , pp. 2629-2640
    • Haurie, C.1    Dale, D.C.2    Mackey, M.C.3
  • 2
    • 0030459532 scopus 로고    scopus 로고
    • Genetics, phenotype, and natural history of autosomal dominant cyclic hematopoiesis
    • Palmer, S.E., Stephens, K. & Dale, D.C. Genetics, phenotype, and natural history of autosomal dominant cyclic hematopoiesis. Am. J. Med. Genet. 66, 413-422 (1996).
    • (1996) Am. J. Med. Genet. , vol.66 , pp. 413-422
    • Palmer, S.E.1    Stephens, K.2    Dale, D.C.3
  • 3
    • 0023695353 scopus 로고
    • Cyclic neutropenia: A clinical review
    • Dale, D.C. & Hammond, W.P.T. Cyclic neutropenia: a clinical review. Blood Rev. 2, 178-185 (1988).
    • (1988) Blood Rev. , vol.2 , pp. 178-185
    • Dale, D.C.1    Hammond, W.P.T.2
  • 4
    • 0002346723 scopus 로고    scopus 로고
    • Leukocyte elastase
    • eds Barrett, A.J., Rawlings, N.D. & Woessner, J.F. Academic Press, San Diego
    • Bieth, J.G. Leukocyte elastase. in Handbook of Proteolytic Enzymes (eds Barrett, A.J., Rawlings, N.D. & Woessner, J.F.) 54-60 (Academic Press, San Diego, 1998).
    • (1998) Handbook of Proteolytic Enzymes , pp. 54-60
    • Bieth, J.G.1
  • 5
    • 0023856438 scopus 로고
    • Myelomonocytic cell lineage expression of the neutrophil elastase gene
    • Takahashi, H., Nukiwa, T., Basset, P. & Crystal, R.G. Myelomonocytic cell lineage expression of the neutrophil elastase gene. J. Biol. Chem. 263, 2543-2547 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 2543-2547
    • Takahashi, H.1    Nukiwa, T.2    Basset, P.3    Crystal, R.G.4
  • 6
    • 0028066779 scopus 로고
    • PEBP2/CBF, the murine homolog of the human myeloid AML1 and PEBP2 β/CBF β proto-oncoproteins, regulates the murine myeloperoxidase and neutrophil elastase genes in immature myeloid cells
    • Nuchprayoon, I. et al. PEBP2/CBF, the murine homolog of the human myeloid AML1 and PEBP2 β/CBF β proto-oncoproteins, regulates the murine myeloperoxidase and neutrophil elastase genes in immature myeloid cells. Mol. Cell. Biol. 14, 5558-5568 (1994).
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5558-5568
    • Nuchprayoon, I.1
  • 7
    • 0005237832 scopus 로고
    • Primary structure of human neutrophil elastase
    • Sinha, S. et al. Primary structure of human neutrophil elastase. Proc. Natl Acad. Sci. USA 84, 2228-2232 (1987).
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 2228-2232
    • Sinha, S.1
  • 8
    • 0033362102 scopus 로고    scopus 로고
    • Congenital end-plate acetylcholinesterase deficiency caused by a nonsense mutation and an A→G splice-donor-site mutation at position +3 of the collagenlike-tail-subunit gene (COLQ): How does G at position +3 result in aberrant splicing?
    • Ohno, K., Brengman, J.M., Felice, K.J., Cornblath, D.R. & Engel, A.G. Congenital end-plate acetylcholinesterase deficiency caused by a nonsense mutation and an A→G splice-donor-site mutation at position +3 of the collagenlike-tail-subunit gene (COLQ): how does G at position +3 result in aberrant splicing? Am. J. Hum. Genet. 65, 635-644 (1999).
    • (1999) Am. J. Hum. Genet. , vol.65 , pp. 635-644
    • Ohno, K.1    Brengman, J.M.2    Felice, K.J.3    Cornblath, D.R.4    Engel, A.G.5
  • 9
    • 0023723103 scopus 로고
    • Structure of the human neutrophil elastase gene
    • Takahashi, H. et al. Structure of the human neutrophil elastase gene. J. Biol. Chem. 263, 14739-14747 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 14739-14747
    • Takahashi, H.1
  • 10
    • 0024571818 scopus 로고
    • Human leukocyte and porcine pancreatic elastase: X-ray crystal structures, mechanism, substrate specificity, and mechanism-based inhibitors
    • Bode, W., Meyer, E. Jr & Powers, J.C. Human leukocyte and porcine pancreatic elastase: X-ray crystal structures, mechanism, substrate specificity, and mechanism-based inhibitors. Biochemistry 28, 1951-1963 (1989).
    • (1989) Biochemistry , vol.28 , pp. 1951-1963
    • Bode, W.1    Meyer E., Jr.2    Powers, J.C.3
  • 11
    • 0002451901 scopus 로고
    • Structure of human neutrophil elastase in complex with a peptide chloromethyl ketone inhibitor at 1.84-A resolution
    • Navia, M.A. et al. Structure of human neutrophil elastase in complex with a peptide chloromethyl ketone inhibitor at 1.84-A resolution. Proc. Natl Acad. Sci. USA 86, 7-11 (1989).
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 7-11
    • Navia, M.A.1
  • 12
    • 15444357089 scopus 로고    scopus 로고
    • Inhibition of human neutrophil elastase. 4. Design, synthesis, X-ray crystallographic analysis, and structure-activity relationships for a series of P2-modified, orally active peptidyl pentafluoroethyl ketones
    • Cregge, R.J. et al. Inhibition of human neutrophil elastase. 4. Design, synthesis, X-ray crystallographic analysis, and structure-activity relationships for a series of P2-modified, orally active peptidyl pentafluoroethyl ketones. J. Med. Chem. 41, 2461-2480 (1998).
    • (1998) J. Med. Chem. , vol.41 , pp. 2461-2480
    • Cregge, R.J.1
  • 13
    • 0031813817 scopus 로고    scopus 로고
    • Converting trypsin to elastase: Substitution of the S1 site and adjacent loops reconstitutes esterase specificity but not amidase activity
    • Hung, S.H. & Hedstrom, L. Converting trypsin to elastase: substitution of the S1 site and adjacent loops reconstitutes esterase specificity but not amidase activity. Protein Eng. 11, 669-673 (1998).
    • (1998) Protein Eng. , vol.11 , pp. 669-673
    • Hung, S.H.1    Hedstrom, L.2
  • 14
    • 0029808909 scopus 로고    scopus 로고
    • Modeling of serpin-protease complexes: Antithrombin-thrombin, α 1-antitrypsin (358Met→Arg)-thrombin, α 1-antitrypsin (358Met→Arg)-trypsin, and antitrypsin-elastase
    • Whisstock, J., Lesk, A.M. & Carrell, R. Modeling of serpin-protease complexes: antithrombin-thrombin, α 1-antitrypsin (358Met→Arg)-thrombin, α 1-antitrypsin (358Met→Arg)-trypsin, and antitrypsin-elastase. Proteins 26, 288-303 (1996).
    • (1996) Proteins , vol.26 , pp. 288-303
    • Whisstock, J.1    Lesk, A.M.2    Carrell, R.3
  • 16
    • 0029665226 scopus 로고    scopus 로고
    • Characterization of the P2′ and P3′ specificities of thrombin using fluorescence-quenched substrates and mapping of the subsites by mutagenesis
    • Le Bonniec, B.F. et al. Characterization of the P2′ and P3′ specificities of thrombin using fluorescence-quenched substrates and mapping of the subsites by mutagenesis. Biochemistry 35, 7114-7122 (1996).
    • (1996) Biochemistry , vol.35 , pp. 7114-7122
    • Le Bonniec, B.F.1
  • 17
    • 0031836105 scopus 로고    scopus 로고
    • Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis
    • Belaaouaj, A. et al. Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis. Nature Med. 4, 615-618 (1998).
    • (1998) Nature Med. , vol.4 , pp. 615-618
    • Belaaouaj, A.1
  • 19
    • 0033515887 scopus 로고    scopus 로고
    • Two distinct cytokines released from a human aminoacyl-tRNA synthetase
    • Wakasugi, K. & Schimmel, P. Two distinct cytokines released from a human aminoacyl-tRNA synthetase. Science 284, 147-151 (1999).
    • (1999) Science , vol.284 , pp. 147-151
    • Wakasugi, K.1    Schimmel, P.2
  • 20
    • 0030367937 scopus 로고    scopus 로고
    • Proteinase 3, the major autoantigen of Wegener's granulomatosis, enhances IL-8 production by endothelial cells in vitro
    • Berger, S.P. et al. Proteinase 3, the major autoantigen of Wegener's granulomatosis, enhances IL-8 production by endothelial cells in vitro. J. Am. Soc. Nephrol. 7, 694-701 (1996).
    • (1996) J. Am. Soc. Nephrol. , vol.7 , pp. 694-701
    • Berger, S.P.1
  • 23
    • 0029886532 scopus 로고    scopus 로고
    • Parametric and nonparametric linkage analysis: A unified multipoint approach
    • Kruglyak, L., Daly, M.J., Reeve-Daly, M.P. & Lander, E.S. Parametric and nonparametric linkage analysis: a unified multipoint approach. Am. J. Hum. Genet. 58, 1347-1363 (1996).
    • (1996) Am. J. Hum. Genet. , vol.58 , pp. 1347-1363
    • Kruglyak, L.1    Daly, M.J.2    Reeve-Daly, M.P.3    Lander, E.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.