메뉴 건너뛰기




Volumn 39, Issue 3, 2013, Pages 219-227

Structure and function of invertebrate Kunitz serine protease inhibitors

Author keywords

Invertebrates; Kunitz domain; Serine protease inhibitors

Indexed keywords

IMMUNOGLOBULIN E; SERINE PROTEINASE INHIBITOR; THROMBIN;

EID: 84871837913     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2012.10.005     Document Type: Review
Times cited : (107)

References (81)
  • 2
    • 0034924843 scopus 로고    scopus 로고
    • The contribution of proteinase inhibitors to immune defense
    • Armstrong P.B. The contribution of proteinase inhibitors to immune defense. Trends Immunol. 2001, 22:47-52.
    • (2001) Trends Immunol. , vol.22 , pp. 47-52
    • Armstrong, P.B.1
  • 8
    • 0026530977 scopus 로고
    • Natural protein proteinase inhibitors and their interaction with proteinases
    • Bode W., Huber R. Natural protein proteinase inhibitors and their interaction with proteinases. Eur. J. Biochem. 1992, 204:433-451.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 9
    • 0034615564 scopus 로고    scopus 로고
    • Structural basis of the endoproteinase-protein inhibitor interaction
    • Bode W., Huber R. Structural basis of the endoproteinase-protein inhibitor interaction. Biochim. Biophys. Acta 2000, 1477:241-252.
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 241-252
    • Bode, W.1    Huber, R.2
  • 12
    • 55849143256 scopus 로고    scopus 로고
    • Functional characterization and novel rickettsiostatic effects of a Kunitz-type serine protease inhibitor from the tick Dermacentor variabilis
    • Ceraul S.M., Dreher-Lesnick S.M., Mulenga A., Rahman M.S., Azad A.F. Functional characterization and novel rickettsiostatic effects of a Kunitz-type serine protease inhibitor from the tick Dermacentor variabilis. Infect. Immun. 2008, 76:5429-5435.
    • (2008) Infect. Immun. , vol.76 , pp. 5429-5435
    • Ceraul, S.M.1    Dreher-Lesnick, S.M.2    Mulenga, A.3    Rahman, M.S.4    Azad, A.F.5
  • 13
    • 84860295451 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic characterization of the N-terminal Kunitz domain of boophilin
    • Cereija T.B., Figueiredo A.C., de Sanctis D., Tanaka A.S., Pereira P.J.B. Crystallization and preliminary crystallographic characterization of the N-terminal Kunitz domain of boophilin. Acta Crystallogr. F 2012, 68:436-439.
    • (2012) Acta Crystallogr. F , vol.68 , pp. 436-439
    • Cereija, T.B.1    Figueiredo, A.C.2    de Sanctis, D.3    Tanaka, A.S.4    Pereira, P.J.B.5
  • 14
    • 2342419730 scopus 로고    scopus 로고
    • Structure-function analysis of the reactive site in the first Kunitz-type domain of human tissue factor pathway inhibitor-2
    • Chand H.S., Schmidt A.E., Bajaj S.P., Kisiel W. Structure-function analysis of the reactive site in the first Kunitz-type domain of human tissue factor pathway inhibitor-2. J. Biol. Chem. 2004, 279:17500-17507.
    • (2004) J. Biol. Chem. , vol.279 , pp. 17500-17507
    • Chand, H.S.1    Schmidt, A.E.2    Bajaj, S.P.3    Kisiel, W.4
  • 15
    • 1842431649 scopus 로고    scopus 로고
    • Molecular characterization of Ancylostoma ceylanicum Kunitz-type serine protease inhibitor: evidence for a role in hookworm-associated growth delay
    • Chu D., Bungiro R.D., Ibanez M., Harrison L.M., Campodonico E., Jones B.F., Mieszczanek J., Kuzmic P., Cappello M. Molecular characterization of Ancylostoma ceylanicum Kunitz-type serine protease inhibitor: evidence for a role in hookworm-associated growth delay. Infect. Immun. 2004, 72:2214-2221.
    • (2004) Infect. Immun. , vol.72 , pp. 2214-2221
    • Chu, D.1    Bungiro, R.D.2    Ibanez, M.3    Harrison, L.M.4    Campodonico, E.5    Jones, B.F.6    Mieszczanek, J.7    Kuzmic, P.8    Cappello, M.9
  • 18
    • 70350359468 scopus 로고    scopus 로고
    • Male-enriched transcription of genes encoding ASPs and Kunitz-type protease inhibitors in Ancylostoma species
    • Costa A.F., Gasser R.B., Dias S.R., Rabelo E.M. Male-enriched transcription of genes encoding ASPs and Kunitz-type protease inhibitors in Ancylostoma species. Mol. Cell Probes 2009, 23:298-303.
    • (2009) Mol. Cell Probes , vol.23 , pp. 298-303
    • Costa, A.F.1    Gasser, R.B.2    Dias, S.R.3    Rabelo, E.M.4
  • 19
    • 0016792887 scopus 로고
    • The two-disulphide intermediates and the folding pathway of reduced pancreatic trypsin inhibitor
    • Creighton T.E. The two-disulphide intermediates and the folding pathway of reduced pancreatic trypsin inhibitor. J. Mol. Biol. 1975, 95:167-199.
    • (1975) J. Mol. Biol. , vol.95 , pp. 167-199
    • Creighton, T.E.1
  • 20
    • 0033559558 scopus 로고    scopus 로고
    • Structural and energetic determinants of the S1-site specificity in serine proteases
    • Czapinska H., Otlewski J. Structural and energetic determinants of the S1-site specificity in serine proteases. Eur. J. Biochem. 1999, 260:571-595.
    • (1999) Eur. J. Biochem. , vol.260 , pp. 571-595
    • Czapinska, H.1    Otlewski, J.2
  • 21
    • 0034602930 scopus 로고    scopus 로고
    • High-resolution structure of bovine pancreatic trypsin inhibitor with altered binding loop sequence
    • Czapinska H., Otlewski J., Krzywda S., Sheldrick G.M., Jaskolski M. High-resolution structure of bovine pancreatic trypsin inhibitor with altered binding loop sequence. J. Mol. Biol. 2000, 295:1237-1249.
    • (2000) J. Mol. Biol. , vol.295 , pp. 1237-1249
    • Czapinska, H.1    Otlewski, J.2    Krzywda, S.3    Sheldrick, G.M.4    Jaskolski, M.5
  • 22
    • 0033952127 scopus 로고    scopus 로고
    • A survey of genes expressed in adults of the human hookworm, Necator americanus
    • Daub J., Loukas A., Pritchard D.I., Blaxter M. A survey of genes expressed in adults of the human hookworm, Necator americanus. Parasitology 2000, 120(Pt 2):171-184.
    • (2000) Parasitology , vol.120 , Issue.PART 2 , pp. 171-184
    • Daub, J.1    Loukas, A.2    Pritchard, D.I.3    Blaxter, M.4
  • 23
    • 0035940514 scopus 로고    scopus 로고
    • Genome-wide analysis of the Drosophila immune response by using oligonucleotide microarrays
    • De Gregorio E., Spellman P.T., Rubin G.M., Lemaitre B. Genome-wide analysis of the Drosophila immune response by using oligonucleotide microarrays. Proc. Natl. Acad. Sci. USA 2001, 98:12590-12595.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12590-12595
    • De Gregorio, E.1    Spellman, P.T.2    Rubin, G.M.3    Lemaitre, B.4
  • 25
    • 0024985345 scopus 로고
    • Peptide toxins and potassium channels
    • Dreyer F. Peptide toxins and potassium channels. Rev. Physiol. Biochem. Pharmacol. 1990, 115:93-136.
    • (1990) Rev. Physiol. Biochem. Pharmacol. , vol.115 , pp. 93-136
    • Dreyer, F.1
  • 27
    • 16544369169 scopus 로고    scopus 로고
    • Papilin, a novel component of basement membranes, in relation to ADAMTS metalloproteases and ECM development
    • Fessler J.H., Kramerova I., Kramerov A., Chen Y., Fessler L.I. Papilin, a novel component of basement membranes, in relation to ADAMTS metalloproteases and ECM development. Int. J. Biochem. Cell Biol. 2004, 36:1079-1084.
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 1079-1084
    • Fessler, J.H.1    Kramerova, I.2    Kramerov, A.3    Chen, Y.4    Fessler, L.I.5
  • 29
    • 0037093065 scopus 로고    scopus 로고
    • Ixolaris, a novel recombinant tissue factor pathway inhibitor (TFPI) from the salivary gland of the tick, Ixodes scapularis: identification of factor X and factor Xa as scaffolds for the inhibition of factor VIIa/tissue factor complex
    • Francischetti I.M., Valenzuela J.G., Andersen J.F., Mather T.N., Ribeiro J.M. Ixolaris, a novel recombinant tissue factor pathway inhibitor (TFPI) from the salivary gland of the tick, Ixodes scapularis: identification of factor X and factor Xa as scaffolds for the inhibition of factor VIIa/tissue factor complex. Blood 2002, 99:3602-3612.
    • (2002) Blood , vol.99 , pp. 3602-3612
    • Francischetti, I.M.1    Valenzuela, J.G.2    Andersen, J.F.3    Mather, T.N.4    Ribeiro, J.M.5
  • 30
    • 78651449678 scopus 로고    scopus 로고
    • Characterization of the anticoagulant protein Rhipilin-1 from the Rhipicephalus haemaphysaloides tick
    • Gao X., Shi L., Zhou Y., Cao J., Zhang H., Zhou J. Characterization of the anticoagulant protein Rhipilin-1 from the Rhipicephalus haemaphysaloides tick. J. Insect Physiol. 2011, 57:339-343.
    • (2011) J. Insect Physiol. , vol.57 , pp. 339-343
    • Gao, X.1    Shi, L.2    Zhou, Y.3    Cao, J.4    Zhang, H.5    Zhou, J.6
  • 33
    • 0034604364 scopus 로고    scopus 로고
    • Substitutions at the P(1) position in BPTI strongly affect the association energy with serine proteinases
    • Grzesiak A., Helland R., Smalas A.O., Krowarsch D., Dadlez M., Otlewski J. Substitutions at the P(1) position in BPTI strongly affect the association energy with serine proteinases. J. Mol. Biol. 2000, 301:205-217.
    • (2000) J. Mol. Biol. , vol.301 , pp. 205-217
    • Grzesiak, A.1    Helland, R.2    Smalas, A.O.3    Krowarsch, D.4    Dadlez, M.5    Otlewski, J.6
  • 34
    • 0034604364 scopus 로고    scopus 로고
    • Substitutions at the P1' position in BPTI strongly affect the association energy with serine proteinases
    • Grzesiak A., Helland R., Smalås A.O., Krowarsch D., Dadlez M., Otlewski J. Substitutions at the P1' position in BPTI strongly affect the association energy with serine proteinases. J. Mol. Biol. 2000, 301:205-217.
    • (2000) J. Mol. Biol. , vol.301 , pp. 205-217
    • Grzesiak, A.1    Helland, R.2    Smalås, A.O.3    Krowarsch, D.4    Dadlez, M.5    Otlewski, J.6
  • 35
    • 0037398198 scopus 로고    scopus 로고
    • Molecular cloning of a novel multidomain Kunitz-type proteinase inhibitor from the hookworm Ancylostoma caninum
    • Hawdon J.M., Datu B., Crowell M. Molecular cloning of a novel multidomain Kunitz-type proteinase inhibitor from the hookworm Ancylostoma caninum. J. Parasitol. 2003, 89:402-407.
    • (2003) J. Parasitol. , vol.89 , pp. 402-407
    • Hawdon, J.M.1    Datu, B.2    Crowell, M.3
  • 37
    • 44649086976 scopus 로고    scopus 로고
    • Ani s 1, the major allergen of Anisakis simplex: purification by affinity chromatography and functional expression in Escherichia coli
    • Kobayashi Y., Ishizaki S., Nagashima Y., Shiomi K. Ani s 1, the major allergen of Anisakis simplex: purification by affinity chromatography and functional expression in Escherichia coli. Parasitol. Int. 2008, 57:314-319.
    • (2008) Parasitol. Int. , vol.57 , pp. 314-319
    • Kobayashi, Y.1    Ishizaki, S.2    Nagashima, Y.3    Shiomi, K.4
  • 38
    • 57849159697 scopus 로고    scopus 로고
    • Identification of a thrombospondin-like immunodominant and phosphorylcholine-containing glycoprotein (GP300) in Dictyocaulus viviparus and related nematodes
    • Kooyman F.N.J., van Balkom B.W.M., de Vries E., van Putten J.P.M. Identification of a thrombospondin-like immunodominant and phosphorylcholine-containing glycoprotein (GP300) in Dictyocaulus viviparus and related nematodes. Mol. Biochem. Parasitol. 2009, 163:85-94.
    • (2009) Mol. Biochem. Parasitol. , vol.163 , pp. 85-94
    • Kooyman, F.N.J.1    van Balkom, B.W.M.2    de Vries, E.3    van Putten, J.P.M.4
  • 42
    • 85025382997 scopus 로고
    • Isolation from beef pancreas of crystalline trypsinogen, trypsin, a trypsin inhibitor, and an inhibitor-trypsin compound
    • Kunitz M., Northrop J.H. Isolation from beef pancreas of crystalline trypsinogen, trypsin, a trypsin inhibitor, and an inhibitor-trypsin compound. J. Gen. Physiol. 1936, 19:991-1007.
    • (1936) J. Gen. Physiol. , vol.19 , pp. 991-1007
    • Kunitz, M.1    Northrop, J.H.2
  • 44
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski M., Kato I. Protein inhibitors of proteinases. Annu. Rev. Biochem. 1980, 49:593-626.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 593-626
    • Laskowski, M.1    Kato, I.2
  • 46
    • 74449089420 scopus 로고    scopus 로고
    • Biochemical characterization of a Kunitz type inhibitor similar to dendrotoxins produced by Rhipicephalus (Boophilus) microplus (Acari: Ixodidae) hemocytes
    • Lima C.A., Torquato R.J., Sasaki S.D., Justo G.Z., Tanaka A.S. Biochemical characterization of a Kunitz type inhibitor similar to dendrotoxins produced by Rhipicephalus (Boophilus) microplus (Acari: Ixodidae) hemocytes. Vet. Parasitol. 2010, 167:279-287.
    • (2010) Vet. Parasitol. , vol.167 , pp. 279-287
    • Lima, C.A.1    Torquato, R.J.2    Sasaki, S.D.3    Justo, G.Z.4    Tanaka, A.S.5
  • 49
    • 0023138380 scopus 로고
    • Mutants of bovine pancreatic trypsin inhibitor lacking cysteines 14 and 38 can fold properly
    • Marks C.B., Naderi H., Kosen P.A., Kuntz I.D., Anderson S. Mutants of bovine pancreatic trypsin inhibitor lacking cysteines 14 and 38 can fold properly. Science 1987, 235:1370-1373.
    • (1987) Science , vol.235 , pp. 1370-1373
    • Marks, C.B.1    Naderi, H.2    Kosen, P.A.3    Kuntz, I.D.4    Anderson, S.5
  • 50
    • 0034703067 scopus 로고    scopus 로고
    • A broad spectrum Kunitz type serine protease inhibitor secreted by the hookworm Ancylostoma ceylanicum
    • Milstone A.M., Harrison L.M., Bungiro R.D., Kuzmic P., Cappello M. A broad spectrum Kunitz type serine protease inhibitor secreted by the hookworm Ancylostoma ceylanicum. J. Biol. Chem. 2000, 275:29391-29399.
    • (2000) J. Biol. Chem. , vol.275 , pp. 29391-29399
    • Milstone, A.M.1    Harrison, L.M.2    Bungiro, R.D.3    Kuzmic, P.4    Cappello, M.5
  • 53
    • 0028063054 scopus 로고
    • Characterization of the serine protease and serine protease inhibitor from the tissue-penetrating nematode Anisakis simplex
    • Morris S.R., Sakanari J.A. Characterization of the serine protease and serine protease inhibitor from the tissue-penetrating nematode Anisakis simplex. J. Biol. Chem. 1994, 269:27650-27656.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27650-27656
    • Morris, S.R.1    Sakanari, J.A.2
  • 54
    • 0034771748 scopus 로고    scopus 로고
    • Identification of four small molecular mass proteins in the silk of Bombyx mori
    • Nirmala X., Mita K., Vanisree V., Zurovec M., Sehnal F. Identification of four small molecular mass proteins in the silk of Bombyx mori. Insect Mol. Biol. 2001, 10:437-445.
    • (2001) Insect Mol. Biol. , vol.10 , pp. 437-445
    • Nirmala, X.1    Mita, K.2    Vanisree, V.3    Zurovec, M.4    Sehnal, F.5
  • 56
    • 33646796713 scopus 로고    scopus 로고
    • Biosynthesis and enzymology of the Caenorhabditis elegans cuticle: identification and characterization of a novel serine protease inhibitor
    • Page A.P., McCormack G., Birnie A.J. Biosynthesis and enzymology of the Caenorhabditis elegans cuticle: identification and characterization of a novel serine protease inhibitor. Int. J. Parasitol. 2006, 36:681-689.
    • (2006) Int. J. Parasitol. , vol.36 , pp. 681-689
    • Page, A.P.1    McCormack, G.2    Birnie, A.J.3
  • 57
  • 58
    • 0030729481 scopus 로고    scopus 로고
    • Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold
    • Perona J.J., Craik C.S. Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold. J. Biol. Chem. 1997, 272:29987-29990.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29987-29990
    • Perona, J.J.1    Craik, C.S.2
  • 59
    • 0033613817 scopus 로고    scopus 로고
    • Evolutionary trace analysis of the Kunitz/BPTI family of proteins: functional divergence may have been based on conformational adjustment
    • Pritchard L., Dufton M.J. Evolutionary trace analysis of the Kunitz/BPTI family of proteins: functional divergence may have been based on conformational adjustment. J. Mol. Biol. 1999, 285:1589-1607.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1589-1607
    • Pritchard, L.1    Dufton, M.J.2
  • 60
    • 58149469498 scopus 로고    scopus 로고
    • Improved insights into the transcriptomes of the human hookworm Necator americanus - fundamental and biotechnological implications
    • Rabelo E.M., Hall R.S., Loukas A., Cooper L., Hu M., Ranganathan S., Gasser R.B. Improved insights into the transcriptomes of the human hookworm Necator americanus - fundamental and biotechnological implications. Biotechnol. Adv. 2009, 27:122-132.
    • (2009) Biotechnol. Adv. , vol.27 , pp. 122-132
    • Rabelo, E.M.1    Hall, R.S.2    Loukas, A.3    Cooper, L.4    Hu, M.5    Ranganathan, S.6    Gasser, R.B.7
  • 61
    • 35448980829 scopus 로고    scopus 로고
    • Differential protein expression in ovaries of uninfected and Babesia-infected southern cattle ticks, Rhipicephalus (Boophilus) microplus
    • Rachinsky A., Guerrero F.D., Scoles G.A. Differential protein expression in ovaries of uninfected and Babesia-infected southern cattle ticks, Rhipicephalus (Boophilus) microplus. Insect Biochem. Mol. Biol. 2007, 37:1291-1308.
    • (2007) Insect Biochem. Mol. Biol. , vol.37 , pp. 1291-1308
    • Rachinsky, A.1    Guerrero, F.D.2    Scoles, G.A.3
  • 62
    • 84859426282 scopus 로고    scopus 로고
    • MEROPS: the database of proteolytic enzymes, their substrates and inhibitors
    • Rawlings N.D., Barrett A.J., Bateman A. MEROPS: the database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res. 2012, 40:D343-D350.
    • (2012) Nucleic Acids Res. , vol.40
    • Rawlings, N.D.1    Barrett, A.J.2    Bateman, A.3
  • 63
    • 1642464622 scopus 로고    scopus 로고
    • Evolutionary families of peptidase inhibitors
    • Rawlings N.D., Tolle D.P., Barrett A.J. Evolutionary families of peptidase inhibitors. Biochem. J. 2004, 378:705-716.
    • (2004) Biochem. J. , vol.378 , pp. 705-716
    • Rawlings, N.D.1    Tolle, D.P.2    Barrett, A.J.3
  • 65
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson J.S. The anatomy and taxonomy of protein structure. Adv. Protein Chem. 1981, 34:167-339.
    • (1981) Adv. Protein Chem. , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 67
    • 30944444115 scopus 로고    scopus 로고
    • An unexpected inhibitory activity of Kunitz-type serine proteinase inhibitor derived from Boophilus microplus trypsin inhibitor on cathepsin L
    • Sasaki S.D., Cotrin S.S., Carmona A.K., Tanaka A.S. An unexpected inhibitory activity of Kunitz-type serine proteinase inhibitor derived from Boophilus microplus trypsin inhibitor on cathepsin L. Biochem. Biophys. Res. Commun. 2006, 341:266-272.
    • (2006) Biochem. Biophys. Res. Commun. , vol.341 , pp. 266-272
    • Sasaki, S.D.1    Cotrin, S.S.2    Carmona, A.K.3    Tanaka, A.S.4
  • 68
    • 0014211618 scopus 로고
    • On the size of the active site in proteases I. Papain
    • Schechter I., Berger A. On the size of the active site in proteases I. Papain. Biochem. Biophys. Res. Commun. 1967, 27:157-162.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 72
    • 0013838236 scopus 로고
    • Enzymically catalyzed disulfide interchange in randomly cross-linked soybean trypsin inhibitor
    • Steiner R.F., De Lorenzo F., Anfinsen C.B. Enzymically catalyzed disulfide interchange in randomly cross-linked soybean trypsin inhibitor. J. Biol. Chem. 1965, 240:4648-4651.
    • (1965) J. Biol. Chem. , vol.240 , pp. 4648-4651
    • Steiner, R.F.1    De Lorenzo, F.2    Anfinsen, C.B.3
  • 73
    • 71549132727 scopus 로고    scopus 로고
    • The kunitz domain protein BLI-5 plays a functionally conserved role in cuticle formation in a diverse range of nematodes
    • Stepek G., McCormack G., Page A.P. The kunitz domain protein BLI-5 plays a functionally conserved role in cuticle formation in a diverse range of nematodes. Mol. Biochem. Parasitol. 2010, 169:1-11.
    • (2010) Mol. Biochem. Parasitol. , vol.169 , pp. 1-11
    • Stepek, G.1    McCormack, G.2    Page, A.P.3
  • 74
    • 0028912561 scopus 로고
    • The clot thickens: clues provided by thrombin structure
    • Stubbs M.T., Bode W. The clot thickens: clues provided by thrombin structure. Trends Biochem. Sci. 1995, 20:23-28.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 23-28
    • Stubbs, M.T.1    Bode, W.2
  • 75
    • 84857551964 scopus 로고    scopus 로고
    • Simukunin from the salivary glands of the black fly Simulium vittatum inhibits enzymes that regulate clotting and inflammatory responses
    • Tsujimoto H., Kotsyfakis M., Francischetti I.M., Eum J.H., Strand M.R., Champagne D.E. Simukunin from the salivary glands of the black fly Simulium vittatum inhibits enzymes that regulate clotting and inflammatory responses. PLoS One 2012, 7:e29964.
    • (2012) PLoS One , vol.7
    • Tsujimoto, H.1    Kotsyfakis, M.2    Francischetti, I.M.3    Eum, J.H.4    Strand, M.R.5    Champagne, D.E.6
  • 77
    • 80052521105 scopus 로고    scopus 로고
    • Deep small RNA sequencing from the nematode Ascaris reveals conservation, functional diversification, and novel developmental profiles
    • Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J., Davis R.E. Deep small RNA sequencing from the nematode Ascaris reveals conservation, functional diversification, and novel developmental profiles. Genome Res. 2011, 21:1462-1477.
    • (2011) Genome Res. , vol.21 , pp. 1462-1477
    • Wang, J.1    Czech, B.2    Crunk, A.3    Wallace, A.4    Mitreva, M.5    Hannon, G.J.6    Davis, R.E.7
  • 79
    • 0025375504 scopus 로고
    • Tick anticoagulant peptide (TAP) is a novel inhibitor of blood coagulation factor Xa
    • Waxman L., Smith D., Arcuri K., Vlasuk G. Tick anticoagulant peptide (TAP) is a novel inhibitor of blood coagulation factor Xa. Science 1990, 248:593-596.
    • (1990) Science , vol.248 , pp. 593-596
    • Waxman, L.1    Smith, D.2    Arcuri, K.3    Vlasuk, G.4
  • 81
    • 80555154427 scopus 로고    scopus 로고
    • SdPI, the first functionally characterized Kunitz-type trypsin inhibitor from scorpion venom
    • Zhao R., Dai H., Qiu S., Li T., He Y., Ma Y., Chen Z., Wu Y., Li W., Cao Z. SdPI, the first functionally characterized Kunitz-type trypsin inhibitor from scorpion venom. PLoS One 2011, 6:e27548.
    • (2011) PLoS One , vol.6
    • Zhao, R.1    Dai, H.2    Qiu, S.3    Li, T.4    He, Y.5    Ma, Y.6    Chen, Z.7    Wu, Y.8    Li, W.9    Cao, Z.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.