메뉴 건너뛰기




Volumn 408, Issue 1, 2011, Pages 9-17

Ancylostoma ceylanicum excretory-secretory protein 2 adopts a netrin-like fold and defines a novel family of nematode proteins

Author keywords

crystal structure; cytokine decoy receptor; hookworm parasite; immunosuppressor; vaccine candidate

Indexed keywords

ANCYLOSTOMA CEYLANICUM EXCRETORY SECRETORY PROTEIN 2; COLLAGENASE 3; COMPLEMENT COMPONENT C3; COMPLEMENT COMPONENT C5; GELATINASE A; GELATINASE B; HELMINTH PROTEIN; INTERSTITIAL COLLAGENASE; MACROPHAGE ELASTASE; MATRILYSIN; MATRIX METALLOPROTEINASE 14; NETRIN; NEUTROPHIL COLLAGENASE; STROMELYSIN; STROMELYSIN 2; TISSUE INHIBITOR OF METALLOPROTEINASE; TISSUE INHIBITOR OF METALLOPROTEINASE 1; TISSUE INHIBITOR OF METALLOPROTEINASE 3; UNCLASSIFIED DRUG;

EID: 79953236271     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.02.033     Document Type: Article
Times cited : (14)

References (68)
  • 2
    • 2142711132 scopus 로고    scopus 로고
    • Cellular responses and cytokine production in post-treatment hookworm patients from an endemic area in Brazil
    • DOI 10.1111/j.1365-2249.2004.02449.x
    • Geiger S.M., Massara C.L., Bethony J., Soboslay P.T., and Correa-Oliveira R. Cellular responses and cytokine production in post-treatment hookworm patients from an endemic area in Brazil Clin. Exp. Immunol. 136 2004 334 340 (Pubitemid 38543454)
    • (2004) Clinical and Experimental Immunology , vol.136 , Issue.2 , pp. 334-340
    • Geiger, S.M.1    Massara, C.L.2    Bethony, J.3    Soboslay, P.T.4    Correa-Oliveira, R.5
  • 4
    • 0141576694 scopus 로고    scopus 로고
    • Immune regulation by helminth parasites: Cellular and molecular mechanisms
    • DOI 10.1038/nri1183
    • Maizels R.M., and Yazdanbakhsh M. Immune regulation by helminth parasites: cellular and molecular mechanisms Nat. Rev., Immunol. 3 2003 733 744 (Pubitemid 41070814)
    • (2003) Nature Reviews Immunology , vol.3 , Issue.9 , pp. 733-744
    • Maizels, R.M.1    Yazdanbakhsh, M.2
  • 6
    • 77949526953 scopus 로고    scopus 로고
    • Understanding human-Plasmodium falciparum immune interactions uncovers the immunological role of worms
    • Roussilhon C., Brasseur P., Agnamey P., Perignon J.L., and Druilhe P. Understanding human-Plasmodium falciparum immune interactions uncovers the immunological role of worms PLoS One 5 2010 e9309
    • (2010) PLoS One , vol.5 , pp. 9309
    • Roussilhon, C.1    Brasseur, P.2    Agnamey, P.3    Perignon, J.L.4    Druilhe, P.5
  • 7
    • 0034235378 scopus 로고    scopus 로고
    • Good worms or bad worms: Do worm infections affect the epidemiological patterns of other diseases?
    • Bundy D., Sher A., and Michael E. Good worms or bad worms: do worm infections affect the epidemiological patterns of other diseases? Parasitol. Today 16 2000 273 274
    • (2000) Parasitol. Today , vol.16 , pp. 273-274
    • Bundy, D.1    Sher, A.2    Michael, E.3
  • 8
    • 0142120238 scopus 로고    scopus 로고
    • T-lymphocyte subsets in patients with hookworm infection in Zaria, Nigeria
    • Onyemelukwe G.C., and Musa B.O. T-lymphocyte subsets in patients with hookworm infection in Zaria, Nigeria Afr. J. Med. Med. Sci. 30 2001 255 259
    • (2001) Afr. J. Med. Med. Sci. , vol.30 , pp. 255-259
    • Onyemelukwe, G.C.1    Musa, B.O.2
  • 9
    • 42449084148 scopus 로고    scopus 로고
    • Efficacy of current drugs against soil-transmitted helminth infections: Systematic review and meta-analysis
    • DOI 10.1001/jama.299.16.1937
    • Keiser J., and Utzinger J. Efficacy of current drugs against soil-transmitted helminth infections: systematic review and meta-analysis JAMA, J. Am. Med. Assoc. 299 2008 1937 1948 (Pubitemid 351574924)
    • (2008) JAMA - Journal of the American Medical Association , vol.299 , Issue.16 , pp. 1937-1948
    • Keiser, J.1    Utzinger, J.2
  • 10
    • 6044246292 scopus 로고    scopus 로고
    • Monitoring drug efficacy and early detection of drug resistance in human soil-transmitted nematodes: A pressing public health agenda for helminth control
    • DOI 10.1016/j.ijpara.2004.08.001, PII S0020751904001651
    • Albonico M., Engels D., and Savioli L. Monitoring drug efficacy and early detection of drug resistance in human soil-transmitted nematodes: a pressing public health agenda for helminth control Int. J. Parasitol. 34 2004 1205 1210 (Pubitemid 39382392)
    • (2004) International Journal for Parasitology , vol.34 , Issue.11 , pp. 1205-1210
    • Albonico, M.1    Engels, D.2    Savioli, L.3
  • 11
    • 0023229213 scopus 로고
    • Do hookworms elicit protective immunity in man?
    • DOI 10.1016/0169-4758(87)90060-3
    • Behnke J.M. Do hookworms elicit protective immunity in man? Parasitol. Today 3 1987 200 206 (Pubitemid 17128432)
    • (1987) Parasitology Today , vol.3 , Issue.7 , pp. 200-206
    • Behnke, J.M.1
  • 12
    • 0034767749 scopus 로고    scopus 로고
    • Immune responses in hookworm infections
    • DOI 10.1128/CMR.14.4.689-703.2001
    • Loukas A., and Prociv P. Immune responses in hookworm infections Clin. Microbiol. Rev. 14 2001 689 703 table of contents (Pubitemid 32979627)
    • (2001) Clinical Microbiology Reviews , vol.14 , Issue.4 , pp. 689-703
    • Loukas, A.1    Prociv, P.2
  • 14
    • 0029014045 scopus 로고
    • Ancylostoma caninum anticoagulant peptide: A hookworm-derived inhibitor of human coagulation factor Xa
    • Cappello M., Vlasuk G.P., Bergum P.W., Huang S., and Hotez P.J. Ancylostoma caninum anticoagulant peptide: a hookworm-derived inhibitor of human coagulation factor Xa Proc. Natl Acad. Sci. USA 92 1995 6152 6156
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 6152-6156
    • Cappello, M.1    Vlasuk, G.P.2    Bergum, P.W.3    Huang, S.4    Hotez, P.J.5
  • 15
    • 0038015446 scopus 로고    scopus 로고
    • Isolation and molecular cloning of a secreted hookworm platelet inhibitor from adult Ancylostoma caninum
    • DOI 10.1016/S0166-6851(03)00121-X
    • Del Valle A., Jones B.F., Harrison L.M., Chadderdon R.C., and Cappello M. Isolation and molecular cloning of a secreted hookworm platelet inhibitor from adult Ancylostoma caninum Mol. Biochem. Parasitol. 129 2003 167 177 (Pubitemid 36794569)
    • (2003) Molecular and Biochemical Parasitology , vol.129 , Issue.2 , pp. 167-177
    • Del Valle, A.1    Jones, B.F.2    Harrison, L.M.3    Chadderdon, R.C.4    Cappello, M.5
  • 17
    • 0035078139 scopus 로고    scopus 로고
    • A calreticulin-like molecule from the human hookworm Necator americanus interacts with C1q and the cytoplasmic signalling domains of some integrins
    • DOI 10.1046/j.1365-3024.2001.00366.x
    • Kasper G., Brown A., Eberl M., Vallar L., Kieffer N., and Berry C. A calreticulin-like molecule from the human hookworm Necator americanus interacts with C1q and the cytoplasmic signalling domains of some integrins Parasite Immunol. 23 2001 141 152 (Pubitemid 32231916)
    • (2001) Parasite Immunology , vol.23 , Issue.3 , pp. 141-152
    • Kasper, G.1    Brown, A.2    Eberl, M.3    Vallar, L.4    Kieffer, N.5    Berry, C.6    Girdwood, K.7    Eggleton, P.8    Quinnell, R.9    Pritchard, D.I.10
  • 18
    • 0037242769 scopus 로고    scopus 로고
    • Ac-FAR-1, a 20 kDa fatty acid- and retinol-binding protein secreted by adult Ancylostoma caninum hookworms: Gene transcription pattern, ligand binding properties and structural characterisation
    • DOI 10.1016/S0166-6851(02)00253-0, PII S0166685102002530
    • Basavaraju S., Zhan B., Kennedy M.W., Liu Y., Hawdon J., and Hotez P.J. Ac-FAR-1, a 20 kDa fatty acid- and retinol-binding protein secreted by adult Ancylostoma caninum hookworms: gene transcription pattern, ligand binding properties and structural characterisation Mol. Biochem. Parasitol. 126 2003 63 71 (Pubitemid 36124012)
    • (2003) Molecular and Biochemical Parasitology , vol.126 , Issue.1 , pp. 63-71
    • Basavaraju, S.1    Zhan, B.2    Kennedy, M.W.3    Liu, Y.4    Hawdon, J.5    Hotez, P.J.6
  • 20
    • 0034703067 scopus 로고    scopus 로고
    • A broad spectrum Kunitz type serine protease inhibitor secreted by the hookworm Ancylostoma ceylanicum
    • DOI 10.1074/jbc.M002715200
    • Milstone A.M., Harrison L.M., Bungiro R.D., Kuzmic P., and Cappello M. A broad spectrum Kunitz type serine protease inhibitor secreted by the hookworm Ancylostoma ceylanicum J. Biol. Chem. 275 2000 29391 29399 (Pubitemid 32043812)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.38 , pp. 29391-29399
    • Milstone, A.M.1    Harrison, L.M.2    Bungiro, R.D.3    Kuzmic, P.4    Cappello, M.5
  • 23
    • 77949329252 scopus 로고    scopus 로고
    • The hookworm tissue inhibitor of metalloproteases (Ac-TMP-1) modifies dendritic cell function and induces generation of CD4 and CD8 suppressor T cells
    • Cuellar C., Wu W., and Mendez S. The hookworm tissue inhibitor of metalloproteases (Ac-TMP-1) modifies dendritic cell function and induces generation of CD4 and CD8 suppressor T cells PLoS Negl. Trop. Dis. 3 2009 e439
    • (2009) PLoS Negl. Trop. Dis. , vol.3 , pp. 439
    • Cuellar, C.1    Wu, W.2    Mendez, S.3
  • 24
    • 54049129199 scopus 로고    scopus 로고
    • Molecular cloning and characterization of Ac-TMP-2, a tissue inhibitor of metalloproteinase secreted by adult Ancylostoma caninum
    • Zhan B., Gupta R., Wong S.P., Bier S., Jiang D., Goud G., and Hotez P. Molecular cloning and characterization of Ac-TMP-2, a tissue inhibitor of metalloproteinase secreted by adult Ancylostoma caninum Mol. Biochem. Parasitol. 162 2008 142 148
    • (2008) Mol. Biochem. Parasitol. , vol.162 , pp. 142-148
    • Zhan, B.1    Gupta, R.2    Wong, S.P.3    Bier, S.4    Jiang, D.5    Goud, G.6    Hotez, P.7
  • 25
    • 6444227382 scopus 로고    scopus 로고
    • Hookworm infection: New developments and prospects for control
    • DOI 10.1097/00001432-200410000-00006
    • Bungiro R., and Cappello M. Hookworm infection: new developments and prospects for control Curr. Opin. Infect. Dis. 17 2004 421 426 (Pubitemid 39407372)
    • (2004) Current Opinion in Infectious Diseases , vol.17 , Issue.5 , pp. 421-426
    • Bungiro, R.1    Cappello, M.2
  • 26
    • 33750157972 scopus 로고    scopus 로고
    • Hookworm vaccines: past, present, and future
    • DOI 10.1016/S1473-3099(06)70630-2, PII S1473309906706302
    • Loukas A., Bethony J., Brooker S., and Hotez P. Hookworm vaccines: past, present, and future Lancet Infect. Dis. 6 2006 733 741 (Pubitemid 44601993)
    • (2006) Lancet Infectious Diseases , vol.6 , Issue.11 , pp. 733-741
    • Loukas, A.1    Bethony, J.2    Brooker, S.3    Hotez, P.4
  • 27
    • 1842484056 scopus 로고    scopus 로고
    • Purification and Molecular Cloning of and Immunization with Ancylostoma ceylanicum Excretory-Secretory Protein 2, An Immunoreactive Protein Produced by Adult Hookworms
    • DOI 10.1128/IAI.72.4.2203-2213.2004
    • Bungiro R.D. Jr, Solis C.V., Harrison L.M., and Cappello M. Purification and molecular cloning of and immunization with Ancylostoma ceylanicum excretory-secretory protein 2, an immunoreactive protein produced by adult hookworms Infect. Immun. 72 2004 2203 2213 (Pubitemid 38419935)
    • (2004) Infection and Immunity , vol.72 , Issue.4 , pp. 2203-2213
    • Bungiro Jr., R.D.1    Solis, C.V.2    Harrison, L.M.3    Cappello, M.4
  • 29
    • 41949131667 scopus 로고    scopus 로고
    • Mucosal antibody responses in experimental hookworm infection
    • DOI 10.1111/j.1365-3024.2008.01023.x
    • Bungiro R.D. Jr, Sun T., Harrison L.M., Shoemaker C.B., and Cappello M. Mucosal antibody responses in experimental hookworm infection Parasite Immunol. 30 2008 293 303 (Pubitemid 351514546)
    • (2008) Parasite Immunology , vol.30 , Issue.5 , pp. 293-303
    • Bungiro Jr., R.D.1    Sun, T.2    Harrison, L.M.3    Shoemaker, C.B.4    Cappello, M.5
  • 30
    • 0037314068 scopus 로고    scopus 로고
    • TopDraw: A sketchpad for protein structure topology cartoons
    • DOI 10.1093/bioinformatics/19.2.311
    • Bond C.S. TopDraw: a sketchpad for protein structure topology cartoons Bioinformatics 19 2003 311 312 (Pubitemid 36181928)
    • (2003) Bioinformatics , vol.19 , Issue.2 , pp. 311-312
    • Bond, C.S.1
  • 32
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 33
  • 34
    • 4644366388 scopus 로고    scopus 로고
    • HKL2MAP: A graphical user interface for macromolecular phasing with SHELX programs
    • Pape T., and Schneider T.R. HKL2MAP: a graphical user interface for macromolecular phasing with SHELX programs J. Appl. Crystallogr. 37 2004 843 844
    • (2004) J. Appl. Crystallogr. , vol.37 , pp. 843-844
    • Pape, T.1    Schneider, T.R.2
  • 35
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building. 1. Tracing protein chains
    • DOI 10.1107/S0907444906022116
    • Cowtan K. The Buccaneer software for automated model building. 1. Tracing protein chains Acta Crystallogr., Sect. D: Biol. Crystallogr. 62 2006 1002 1011 (Pubitemid 44337374)
    • (2006) Acta Crystallographica Section D: Biological Crystallography , vol.62 , Issue.9 , pp. 1002-1011
    • Cowtan, K.1
  • 36
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallogr., Sect. D: Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763
  • 41
    • 56649103902 scopus 로고    scopus 로고
    • Searching protein structure databases with DaliLite v.3
    • DOI 10.1093/bioinformatics/btn507
    • Holm L., Kaariainen S., Rosenstrom P., and Schenkel A. Searching protein structure databases with DaliLite v.3 Bioinformatics 24 2008 2780 2781 (Pubitemid 352722625)
    • (2008) Bioinformatics , vol.24 , Issue.23 , pp. 2780-2781
    • Holm, L.1    Kaariainen, S.2    Rosenstrom, P.3    Schenkel, A.4
  • 44
    • 31344458952 scopus 로고    scopus 로고
    • Structure and function of matrix metalloproteinases and TIMPs
    • DOI 10.1016/j.cardiores.2005.12.002, PII S0008636305005651
    • Nagase H., Visse R., and Murphy G. Structure and function of matrix metalloproteinases and TIMPs Cardiovasc. Res. 69 2006 562 573 (Pubitemid 43139720)
    • (2006) Cardiovascular Research , vol.69 , Issue.3 , pp. 562-573
    • Nagase, H.1    Visse, R.2    Murphy, G.3
  • 47
    • 77954827231 scopus 로고    scopus 로고
    • The intrinsic protein flexibility of endogenous protease inhibitor TIMP-1 controls its binding interface and affects its function
    • Grossman M., Tworowski D., Dym O., Lee M.H., Levy Y., Murphy G., and Sagi I. The intrinsic protein flexibility of endogenous protease inhibitor TIMP-1 controls its binding interface and affects its function Biochemistry 49 2010 6184 6192
    • (2010) Biochemistry , vol.49 , pp. 6184-6192
    • Grossman, M.1    Tworowski, D.2    Dym, O.3    Lee, M.H.4    Levy, Y.5    Murphy, G.6    Sagi, I.7
  • 48
    • 33846675236 scopus 로고    scopus 로고
    • Flexibility and Variability of TIMP Binding: X-ray Structure of the Complex Between Collagenase-3/MMP-13 and TIMP-2
    • DOI 10.1016/j.jmb.2006.11.072, PII S0022283606016317
    • Maskos K., Lang R., Tschesche H., and Bode W. Flexibility and variability of TIMP binding: X-ray structure of the complex between collagenase-3/MMP-13 and TIMP-2 J. Mol. Biol. 366 2007 1222 1231 (Pubitemid 46188638)
    • (2007) Journal of Molecular Biology , vol.366 , Issue.4 , pp. 1222-1231
    • Maskos, K.1    Lang, R.2    Tschesche, H.3    Bode, W.4
  • 49
    • 0038723727 scopus 로고    scopus 로고
    • Global orientation of bound MMP-3 and N-TIMP-1 in solution via residual dipolar couplings
    • DOI 10.1021/bi034545s
    • Arumugam S., and Van Doren S.R. Global orientation of bound MMP-3 and N-TIMP-1 in solution via residual dipolar couplings Biochemistry 42 2003 7950 7958 (Pubitemid 36807712)
    • (2003) Biochemistry , vol.42 , Issue.26 , pp. 7950-7958
    • Arumugam, S.1    Van Doren, S.R.2
  • 50
    • 48749094943 scopus 로고    scopus 로고
    • Structural determinants of the ADAM inhibition by TIMP-3: Crystal structure of the TACE-N-TIMP-3 complex
    • Wisniewska M., Goettig P., Maskos K., Belouski E., Winters D., and Hecht R. Structural determinants of the ADAM inhibition by TIMP-3: crystal structure of the TACE-N-TIMP-3 complex J. Mol. Biol. 381 2008 1307 1319
    • (2008) J. Mol. Biol. , vol.381 , pp. 1307-1319
    • Wisniewska, M.1    Goettig, P.2    Maskos, K.3    Belouski, E.4    Winters, D.5    Hecht, R.6
  • 51
    • 0035980017 scopus 로고    scopus 로고
    • Tyrosine 36 plays a critical role in the interaction of the AB loop of tissue inhibitor of metalloproteinases-2 with matrix metalloproteinase-14
    • Williamson R.A., Hutton M., Vogt G., Rapti M., Knauper V., Carr M.D., and Murphy G. Tyrosine 36 plays a critical role in the interaction of the AB loop of tissue inhibitor of metalloproteinases-2 with matrix metalloproteinase-14 J. Biol. Chem. 276 2001 32966 32970
    • (2001) J. Biol. Chem. , vol.276 , pp. 32966-32970
    • Williamson, R.A.1    Hutton, M.2    Vogt, G.3    Rapti, M.4    Knauper, V.5    Carr, M.D.6    Murphy, G.7
  • 52
    • 33847258857 scopus 로고    scopus 로고
    • Molecular cloning and characterization of Ac-MTP-2, an astacin-like metalloprotease released by adult Ancylostoma caninum
    • Feng J., Zhan B., Liu Y., Liu S., Williamson A., and Goud G. Molecular cloning and characterization of Ac-MTP-2, an astacin-like metalloprotease released by adult Ancylostoma caninum Mol. Biochem. Parasitol. 152 2007 132 138
    • (2007) Mol. Biochem. Parasitol. , vol.152 , pp. 132-138
    • Feng, J.1    Zhan, B.2    Liu, Y.3    Liu, S.4    Williamson, A.5    Goud, G.6
  • 53
    • 0036318078 scopus 로고    scopus 로고
    • Molecular cloning and purification of Ac-TMP, a developmentally regulated putative tissue inhibitor of metalloprotease released in relative abundance by adult Ancylostoma hookworms
    • Zhan B., Badamchian M., Meihua B., Ashcom J., Feng J., and Hawdon J. Molecular cloning and purification of Ac-TMP, a developmentally regulated putative tissue inhibitor of metalloprotease released in relative abundance by adult Ancylostoma hookworms Am. J. Trop. Med. Hyg. 66 2002 238 244 (Pubitemid 34756090)
    • (2002) American Journal of Tropical Medicine and Hygiene , vol.66 , Issue.3 , pp. 238-244
    • Zhan, B.1    Badamchian, M.2    Meihua, B.3    Ashcom, J.4    Feng, J.5    Hawdon, J.6    Shuhua, X.7    Hotez, P.J.8
  • 54
    • 5444259851 scopus 로고    scopus 로고
    • The complement system in regulation of adaptive immunity
    • DOI 10.1038/ni1113
    • Carroll M.C. The complement system in regulation of adaptive immunity Nat. Immunol. 5 2004 981 986 (Pubitemid 41057714)
    • (2004) Nature Immunology , vol.5 , Issue.10 , pp. 981-986
    • Carroll, M.C.1
  • 56
    • 58849109079 scopus 로고    scopus 로고
    • 3D structure of the C3bB complex provides insights into the activation and regulation of the complement alternative pathway convertase
    • Torreira E., Tortajada A., Montes T., Rodriguez de Cordoba S., and Llorca O. 3D structure of the C3bB complex provides insights into the activation and regulation of the complement alternative pathway convertase Proc. Natl Acad. Sci. USA 106 2009 882 887
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 882-887
    • Torreira, E.1    Tortajada, A.2    Montes, T.3    Rodriguez De Cordoba, S.4    Llorca, O.5
  • 57
    • 69249220131 scopus 로고    scopus 로고
    • Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex
    • Janssen B.J., Gomes L., Koning R.I., Svergun D.I., Koster A.J., and Fritzinger D.C. Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex EMBO J. 28 2009 2469 2478
    • (2009) EMBO J. , vol.28 , pp. 2469-2478
    • Janssen, B.J.1    Gomes, L.2    Koning, R.I.3    Svergun, D.I.4    Koster, A.J.5    Fritzinger, D.C.6
  • 58
    • 24644502532 scopus 로고    scopus 로고
    • Investigating hookworm genomes by comparative analysis of two Ancylostoma species
    • Mitreva M., McCarter J.P., Arasu P., Hawdon J., Martin J., and Dante M. Investigating hookworm genomes by comparative analysis of two Ancylostoma species BMC Genomics 6 2005 58
    • (2005) BMC Genomics , vol.6 , pp. 58
    • Mitreva, M.1    McCarter, J.P.2    Arasu, P.3    Hawdon, J.4    Martin, J.5    Dante, M.6
  • 59
    • 0037519264 scopus 로고    scopus 로고
    • The NTR module: Domains of netrins, secreted frizzled related proteins, and type I procollagen C-proteinase enhancer protein are homologous with tissue inhibitors of metalloproteases
    • Banyai L., and Patthy L. The NTR module: domains of netrins, secreted frizzled related proteins, and type I procollagen C-proteinase enhancer protein are homologous with tissue inhibitors of metalloproteases Protein Sci. 8 1999 1636 1642 (Pubitemid 29379945)
    • (1999) Protein Science , vol.8 , Issue.8 , pp. 1636-1642
    • Banyai, L.1    Patthy, L.2
  • 60
    • 14844284571 scopus 로고    scopus 로고
    • TIMP-2: An endogenous inhibitor of angiogenesis
    • DOI 10.1016/j.molmed.2005.01.007
    • Stetler-Stevenson W.G., and Seo D.W. TIMP-2: an endogenous inhibitor of angiogenesis Trends Mol. Med. 11 2005 97 103 (Pubitemid 40348986)
    • (2005) Trends in Molecular Medicine , vol.11 , Issue.3 , pp. 97-103
    • Stetler-Stevenson, W.G.1    Seo, D.-W.2
  • 64
    • 70350208780 scopus 로고    scopus 로고
    • The evolutionary conundrum of pathogen mimicry
    • Elde N.C., and Malik H.S. The evolutionary conundrum of pathogen mimicry Nat. Rev. Microbiol. 7 2009 787 797
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 787-797
    • Elde, N.C.1    Malik, H.S.2
  • 65
    • 10544256181 scopus 로고    scopus 로고
    • Control of C. elegans larval development by neuronal expression of a TGF-β homolog
    • DOI 10.1126/science.274.5291.1389
    • Ren P., Lim C.S., Johnsen R., Albert P.S., Pilgrim D., and Riddle D.L. Control of C. elegans larval development by neuronal expression of a TGF-β homolog Science 274 1996 1389 1391 (Pubitemid 26391466)
    • (1996) Science , vol.274 , Issue.5291 , pp. 1389-1391
    • Ren, P.1    Lim, C.-S.2    Johnsen, R.3    Albert, P.S.4    Pilgrim, D.5    Riddle, D.L.6
  • 66
    • 0035980651 scopus 로고    scopus 로고
    • Macrophage migration inhibitory factor (mif) transcription is significantly elevated in Caenorhabditis elegans dauer larvae
    • DOI 10.1016/S0378-1119(01)00706-5, PII S0378111901007065
    • Marson A.L., Tarr D.E., and Scott A.L. Macrophage migration inhibitory factor (mif) transcription is significantly elevated in Caenorhabditis elegans dauer larvae Gene 278 2001 53 62 (Pubitemid 33055779)
    • (2001) Gene , vol.278 , Issue.1-2 , pp. 53-62
    • Marson, A.L.1    Tarr, D.EllenK.2    Scott, A.L.3
  • 67
    • 0344178160 scopus 로고    scopus 로고
    • Identification of a TRAF (TNF receptor-associated factor) gene in Caenorhabditis elegans
    • DOI 10.1007/PL00006423
    • Wajant H., Muhlenbeck F., and Scheurich P. Identification of a TRAF (TNF receptor-associated factor) gene in Caenorhabditis elegans J. Mol. Evol. 47 1998 656 662 (Pubitemid 29008767)
    • (1998) Journal of Molecular Evolution , vol.47 , Issue.6 , pp. 656-662
    • Wajant, H.1    Muhlenbeck, F.2    Scheurich, P.3
  • 68
    • 0027525104 scopus 로고
    • The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme
    • DOI 10.1016/0092-8674(93)90485-9
    • Yuan J., Shaham S., Ledoux S., Ellis H.M., and Horvitz H.R. The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme Cell 75 1993 641 652 (Pubitemid 23346363)
    • (1993) Cell , vol.75 , Issue.4 , pp. 641-652
    • Yuan, J.1    Shaham, S.2    Ledoux, S.3    Ellis, H.M.4    Horvitz, H.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.