메뉴 건너뛰기




Volumn 248, Issue 1, 2005, Pages 23-30

ADAMs are present in fungi: Identification of two novel ADAM genes in Aspergillus fumigatus

Author keywords

ADAM; Aspergillus; Metalloprotease

Indexed keywords

A DISINTEGRIN AND METALLOPROTEASE A; A DISINTEGRIN AND METALLOPROTEASE B; ALBUMIN; CASEIN; METALLOPROTEINASE; UNCLASSIFIED DRUG;

EID: 20444466821     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.femsle.2005.05.017     Document Type: Article
Times cited : (10)

References (33)
  • 1
    • 0033817591 scopus 로고    scopus 로고
    • Remarkable roles of proteolysis on and beyond the cell surface
    • C.P. Blobel Remarkable roles of proteolysis on and beyond the cell surface Curr. Opin. Cell Biol. 12 2000 606 612
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 606-612
    • Blobel, C.P.1
  • 2
    • 0034141195 scopus 로고    scopus 로고
    • The ADAM gene family: Surface proteins with adhesion and protease activity
    • P. Primakoff, and D.G. Myles The ADAM gene family: surface proteins with adhesion and protease activity TIG 16 2000 83 87
    • (2000) TIG , vol.16 , pp. 83-87
    • Primakoff, P.1    Myles, D.G.2
  • 3
    • 0037224740 scopus 로고    scopus 로고
    • The ADAMs family of metalloproteases: Multidomain proteins with multiple functions
    • D.F. Seals, and S.A. Courtneidge The ADAMs family of metalloproteases: multidomain proteins with multiple functions Genes Dev. 17 2003 7 30
    • (2003) Genes Dev. , vol.17 , pp. 7-30
    • Seals, D.F.1    Courtneidge, S.A.2
  • 4
    • 0026471735 scopus 로고
    • Structure, function and evolutionary relationship of proteins containing a disintegrin domain
    • C.P. Blobel, and J.M. White Structure, function and evolutionary relationship of proteins containing a disintegrin domain Curr. Opin. Cell Biol. 4 1992 760 765
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 760-765
    • Blobel, C.P.1    White, J.M.2
  • 5
    • 0031698581 scopus 로고    scopus 로고
    • ADAMs: Focus on the protease domain
    • R.A. Black, and J.M. White ADAMs: focus on the protease domain Curr. Opin. Cell Biol. 10 1998 654 659
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 654-659
    • Black, R.A.1    White, J.M.2
  • 8
    • 0842308119 scopus 로고    scopus 로고
    • ADAM28 is activated by MMP-7 (matrilysin-1) and cleaves insulin-like growth factor binding protein-3
    • S. Mochizuki, M. Shimoda, T. Shiomi, Y. Fujii, and Y. Okada ADAM28 is activated by MMP-7 (matrilysin-1) and cleaves insulin-like growth factor binding protein-3 Biochem. Biophys. Res. Commun. 315 2004 79 84
    • (2004) Biochem. Biophys. Res. Commun. , vol.315 , pp. 79-84
    • Mochizuki, S.1    Shimoda, M.2    Shiomi, T.3    Fujii, Y.4    Okada, Y.5
  • 9
    • 0028146721 scopus 로고
    • A survey of furin substrate specificity using substrate phage display
    • D.J. Matthews, L.J. Goodman, C.M. Gorman, and J.A. Wells A survey of furin substrate specificity using substrate phage display Protein Sci. 3 1994 1197 1205
    • (1994) Protein Sci. , vol.3 , pp. 1197-1205
    • Matthews, D.J.1    Goodman, L.J.2    Gorman, C.M.3    Wells, J.A.4
  • 10
    • 0035430436 scopus 로고    scopus 로고
    • Regulation of the alpha-secretase ADAM10 by its prodomain and proprotein convertases
    • A. Anders, S. Gilbert, W. Garten, R. Postina, and F. Fahrenholz. Regulation of the alpha-secretase ADAM10 by its prodomain and proprotein convertases FASEB J. 15 2001 1837 1839
    • (2001) FASEB J. , vol.15 , pp. 1837-1839
    • Anders, A.1    Gilbert, S.2    Garten, W.3    Postina, R.4    Fahrenholz., F.5
  • 12
    • 0032741143 scopus 로고    scopus 로고
    • Metalloprotease-disintegrins: Modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding
    • J. Schlondorff, and C.P. Blobel Metalloprotease-disintegrins: modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding J. Cell Sci. 112 1999 3603 3617
    • (1999) J. Cell Sci. , vol.112 , pp. 3603-3617
    • Schlondorff, J.1    Blobel, C.P.2
  • 14
    • 0033933982 scopus 로고    scopus 로고
    • Meltrin gamma (ADAM-9) mediates cellular adhesion through alpha(6)beta(1)integrin, leading to a marked induction of fibroblast cell motility
    • D. Nath, P.M. Slocombe, A. Webster, P.E. Stephens, A.J. Docherty, and G. Murphy Meltrin gamma (ADAM-9) mediates cellular adhesion through alpha(6)beta(1)integrin, leading to a marked induction of fibroblast cell motility J. Cell Sci. 113 2000 2319 2328
    • (2000) J. Cell Sci. , vol.113 , pp. 2319-2328
    • Nath, D.1    Slocombe, P.M.2    Webster, A.3    Stephens, P.E.4    Docherty, A.J.5    Murphy, G.6
  • 15
    • 0034672264 scopus 로고    scopus 로고
    • Metalloprotease-disintegrin ADAM 12 binds to the SH3 domain of Src and activates Src tyrosine kinase in C2C12 cells
    • Q. Kang, Y. Cao, and A. Zolkiewska Metalloprotease-disintegrin ADAM 12 binds to the SH3 domain of Src and activates Src tyrosine kinase in C2C12 cells Biochem. J. 352 2000 883 892
    • (2000) Biochem. J. , vol.352 , pp. 883-892
    • Kang, Q.1    Cao, Y.2    Zolkiewska, A.3
  • 18
    • 0036133646 scopus 로고    scopus 로고
    • Tumor necrosis factor-α converting enzyme
    • R.A. Black Tumor necrosis factor-α converting enzyme Int J. Biochem. Cell Biol. 34 2002 1 5
    • (2002) Int J. Biochem. Cell Biol. , vol.34 , pp. 1-5
    • Black, R.A.1
  • 20
    • 0032540170 scopus 로고    scopus 로고
    • The metallo-disintegrin ADAM10 (MADM) from bovine kidney has type IV collagenase activity in vitro
    • M.I. Millichip, D.J. Dallas, E. Wu, S. Dale, and N. McKie The metallo-disintegrin ADAM10 (MADM) from bovine kidney has type IV collagenase activity in vitro Biochem. Biophys. Res. Commun. 245 1998 594 598
    • (1998) Biochem. Biophys. Res. Commun. , vol.245 , pp. 594-598
    • Millichip, M.I.1    Dallas, D.J.2    Wu, E.3    Dale, S.4    McKie, N.5
  • 21
    • 1242300153 scopus 로고    scopus 로고
    • ADAM family protein Mde10 is essential for development of spore envelopes in the fission yeast Schizosaccharomyces pombe
    • T. Nakamura, H. Abe, A. Hirata, and C. Shimoda ADAM family protein Mde10 is essential for development of spore envelopes in the fission yeast Schizosaccharomyces pombe Eukaryot. Cell 3 2004 27 39
    • (2004) Eukaryot. Cell , vol.3 , pp. 27-39
    • Nakamura, T.1    Abe, H.2    Hirata, A.3    Shimoda, C.4
  • 22
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • J.D. Thompson, T.J. Gibson, F. Plewniak, F. Jeanmougin, and D.G. Higgins The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools Nucleic Acids Res. 24 1997 4876 4882
    • (1997) Nucleic Acids Res. , vol.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 23
    • 0003437299 scopus 로고    scopus 로고
    • Distributed by the author. Department of Genome Sciences, University of Washington, Seattle.
    • Felsenstein, J. (2002) PHYLIP (Phylogeny Inference Package) version 3.6a3. Distributed by the author. Department of Genome Sciences, University of Washington, Seattle.
    • (2002) PHYLIP (Phylogeny Inference Package) Version 3.6a3
    • Felsenstein, J.1
  • 24
    • 1642340427 scopus 로고    scopus 로고
    • Identification of a novel class of annexin genes
    • V. Khalaj, L. Smith, J. Brookman, and D. Tuckwell Identification of a novel class of annexin genes FEBS Lett. 562 2004 79 86
    • (2004) FEBS Lett. , vol.562 , pp. 79-86
    • Khalaj, V.1    Smith, L.2    Brookman, J.3    Tuckwell, D.4
  • 25
    • 0036151793 scopus 로고    scopus 로고
    • Identification and analysis of collagen alpha 1(XXI), a novel member of the FACIT collagen family
    • D. Tuckwell Identification and analysis of collagen alpha 1(XXI), a novel member of the FACIT collagen family Matrix Biol. 21 2002 63 66
    • (2002) Matrix Biol. , vol.21 , pp. 63-66
    • Tuckwell, D.1
  • 26
    • 0036205377 scopus 로고    scopus 로고
    • TREE-PUZZLE: Maximum likelihood phylogenetic analysis using quartets and parallel computing
    • H.A. Schmidt, K. Strimmer, M. Vingron, and A. von Haeseler TREE-PUZZLE: maximum likelihood phylogenetic analysis using quartets and parallel computing Bioinformatics 18 2002 502 504
    • (2002) Bioinformatics , vol.18 , pp. 502-504
    • Schmidt, H.A.1    Strimmer, K.2    Vingron, M.3    Von Haeseler, A.4
  • 27
    • 0030203863 scopus 로고    scopus 로고
    • TreeView: An application to display phylogenetic trees on personal computers
    • R.D.M. Page TreeView: an application to display phylogenetic trees on personal computers Comput. Appl. Biosci. 12 1996 357 358
    • (1996) Comput. Appl. Biosci. , vol.12 , pp. 357-358
    • Page, R.D.M.1
  • 28
    • 0027403163 scopus 로고
    • A Coomassie brilliant blue G-250-based colorimetric assay for measuring activity of calpain and other proteases
    • M. Buroker-Kilgore, and K.W. Wang A Coomassie brilliant blue G-250-based colorimetric assay for measuring activity of calpain and other proteases Anal. Biochem. 208 1993 387 392
    • (1993) Anal. Biochem. , vol.208 , pp. 387-392
    • Buroker-Kilgore, M.1    Wang, K.W.2
  • 29
    • 0027515396 scopus 로고
    • Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'
    • W. Bode, F.X. Gomis-Ruth, and W. Stockler Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins' FEBS Lett. 331 1993 134 140
    • (1993) FEBS Lett. , vol.331 , pp. 134-140
    • Bode, W.1    Gomis-Ruth, F.X.2    Stockler, W.3
  • 30
    • 0034657228 scopus 로고    scopus 로고
    • Cloning and characterization of ADAM28: Evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28
    • L. Howard, R.A. Maciewicz, and C.P. Blobel Cloning and characterization of ADAM28: evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28 Biochem. J. 348 2000 21 27
    • (2000) Biochem. J. , vol.348 , pp. 21-27
    • Howard, L.1    MacIewicz, R.A.2    Blobel, C.P.3
  • 31
    • 0038056151 scopus 로고    scopus 로고
    • Shedding of membrane proteins by ADAM family proteases
    • M.L. Moss, and M.H. Lambert Shedding of membrane proteins by ADAM family proteases Essays Biochem. 38 2002 141 153
    • (2002) Essays Biochem. , vol.38 , pp. 141-153
    • Moss, M.L.1    Lambert, M.H.2
  • 32
    • 0042768002 scopus 로고    scopus 로고
    • Assays of matrix metalloproteinases (MMPs) and MMP inhibitors: Bioassays and immunoassays applicable to cell culture medium, serum, and synovial fluid
    • J.B. Catterall, and T.E. Cawston Assays of matrix metalloproteinases (MMPs) and MMP inhibitors: bioassays and immunoassays applicable to cell culture medium, serum, and synovial fluid Methods Mol. Biol. 225 2003 353 364
    • (2003) Methods Mol. Biol. , vol.225 , pp. 353-364
    • Catterall, J.B.1    Cawston, T.E.2
  • 33
    • 0032238025 scopus 로고    scopus 로고
    • Identification of matrix metalloproteinases (MMPs) in synovial fluid from patients with temporomandibular disorder
    • T. Kubota, E. Kubota, A. Matsumoto, Y. Kaway, H. Saito, Y. Mikuni-Takagaki, and S. Sato Identification of matrix metalloproteinases (MMPs) in synovial fluid from patients with temporomandibular disorder Eur. J. Oral Sci. 106 1998 992 999
    • (1998) Eur. J. Oral Sci. , vol.106 , pp. 992-999
    • Kubota, T.1    Kubota, E.2    Matsumoto, A.3    Kaway, Y.4    Saito, H.5    Mikuni-Takagaki, Y.6    Sato, S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.