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Volumn 8, Issue 3, 2013, Pages

SjAPI, the First Functionally Characterized Ascaris-Type Protease Inhibitor from Animal Venoms

Author keywords

[No Author keywords available]

Indexed keywords

ALANYLALANYLVALINE; BUTHUS MARTENSII ASCARIS TYPE PROTEASE INHIBITOR; CHAERILUS TRICOSTATUS ASCARIS TYPE PROTEASE INHIBITOR; CHYMOTRYPSIN A; COMPLEMENTARY DNA; CYSTEINE; ELASTASE; POLYPEPTIDE; PROTEINASE INHIBITOR; RECOMBINANT PROTEIN; RECOMBINANT SCORPIOPS JENDEKI ASCARIS TYPE PROTEASE INHIBITOR; SCORPION VENOM; SCORPIOPS JENDEKI ASCARIS TYPE PROTEASE INHIBITOR 2; SCORPIOPS JENDEKI ASCARIS TYPE PROTEASE INHIBITOR M1; SCORPIOPS JENDEKI ASCARIS TYPE PROTEASE INHIBITOR M2; SCORPIOPS JENDEKI ASCARIS TYPE PROTEASE INHIBITOR M3; SCORPIOPS JENDEKI ASCARIS TYPE PROTEASE INHIBITOR M4; SCORPIOPS JENDEKI ASCARIS TYPE PROTEASE INHIBITOR M5; SCORPIOPS JENDEKI ASCARIS TYPE PROTEASE INHIBITOR M6; SERINE PROTEINASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 84875341349     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0057529     Document Type: Article
Times cited : (38)

References (41)
  • 2
    • 84863115230 scopus 로고    scopus 로고
    • Nematode sperm maturation triggered by protease involves sperm-secreted serine protease inhibitor (Serpin)
    • Zhao Y, Sun W, Zhang P, Chi H, Zhang MJ, et al. (2012) Nematode sperm maturation triggered by protease involves sperm-secreted serine protease inhibitor (Serpin). Proc Natl Acad Sci U S A 109: 1542-1547.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 1542-1547
    • Zhao, Y.1    Sun, W.2    Zhang, P.3    Chi, H.4    Zhang, M.J.5
  • 3
    • 79951770643 scopus 로고    scopus 로고
    • Identification and characterization of a serine protease inhibitor with two trypsin inhibitor-like domains from the human hookworm Ancylostoma duodenale
    • Jin X, Deng L, Li H, Zhang Z, He Q, et al. (2011) Identification and characterization of a serine protease inhibitor with two trypsin inhibitor-like domains from the human hookworm Ancylostoma duodenale. Parasitol Res 108: 287-295.
    • (2011) Parasitol Res , vol.108 , pp. 287-295
    • Jin, X.1    Deng, L.2    Li, H.3    Zhang, Z.4    He, Q.5
  • 4
    • 38649083162 scopus 로고    scopus 로고
    • Multifaceted roles of human elafin and secretory leukocyte proteinase inhibitor (SLPI), two serine protease inhibitors of the chelonianin family
    • Moreau T, Baranger K, Dade S, Dallet-Choisy S, Guyot N, et al. (2008) Multifaceted roles of human elafin and secretory leukocyte proteinase inhibitor (SLPI), two serine protease inhibitors of the chelonianin family. Biochimie 90: 284-295.
    • (2008) Biochimie , vol.90 , pp. 284-295
    • Moreau, T.1    Baranger, K.2    Dade, S.3    Dallet-Choisy, S.4    Guyot, N.5
  • 5
    • 78149481863 scopus 로고    scopus 로고
    • C1 inhibitor, a multi-functional serine protease inhibitor
    • Davis AE 3rd, Lu F, Mejia P (2010) C1 inhibitor, a multi-functional serine protease inhibitor. Thromb Haemost 104: 886-893.
    • (2010) Thromb Haemost , vol.104 , pp. 886-893
    • Davis 3rd, A.E.1    Lu, F.2    Mejia, P.3
  • 6
    • 16844364124 scopus 로고    scopus 로고
    • A serine proteinase inhibitor isolated from Tamarindus indica seeds and its effects on the release of human neutrophil elastase
    • Fook JM, Macedo LL, Moura GE, Teixeira FM, Oliveira AS, et al. (2005) A serine proteinase inhibitor isolated from Tamarindus indica seeds and its effects on the release of human neutrophil elastase. Life Sci 76: 2881-2891.
    • (2005) Life Sci , vol.76 , pp. 2881-2891
    • Fook, J.M.1    Macedo, L.L.2    Moura, G.E.3    Teixeira, F.M.4    Oliveira, A.S.5
  • 7
    • 32644440584 scopus 로고    scopus 로고
    • Effect of trypsin inhibitor from Crotalaria pallida seeds on Callosobruchus maculatus (cowpea weevil) and Ceratitis capitata (fruit fly)
    • Gomes CE, Barbosa AE, Macedo LL, Pitanga JC, Moura FT, et al. (2005) Effect of trypsin inhibitor from Crotalaria pallida seeds on Callosobruchus maculatus (cowpea weevil) and Ceratitis capitata (fruit fly). Plant Physiol Biochem 43: 1095-1102.
    • (2005) Plant Physiol Biochem , vol.43 , pp. 1095-1102
    • Gomes, C.E.1    Barbosa, A.E.2    Macedo, L.L.3    Pitanga, J.C.4    Moura, F.T.5
  • 8
    • 0031440963 scopus 로고    scopus 로고
    • Isolation and amino acid sequences of two Kunitz-type protease inhibitors from the sea anemone Anthopleura aff. xanthogrammica
    • Minagawa S, Ishida M, Shimakura K, Nagashima Y, Shiomi K, (1997) Isolation and amino acid sequences of two Kunitz-type protease inhibitors from the sea anemone Anthopleura aff. xanthogrammica. Comp Biochem Physiol B Biochem Mol Biol 118: 381-386.
    • (1997) Comp Biochem Physiol B Biochem Mol Biol , vol.118 , pp. 381-386
    • Minagawa, S.1    Ishida, M.2    Shimakura, K.3    Nagashima, Y.4    Shiomi, K.5
  • 9
    • 13444263657 scopus 로고    scopus 로고
    • Taiwan cobra chymotrypsin inhibitor: cloning, functional expression and gene organization
    • Cheng YC, Yan FJ, Chang LS, (2005) Taiwan cobra chymotrypsin inhibitor: cloning, functional expression and gene organization. Biochim Biophys Acta 1747: 213-220.
    • (2005) Biochim Biophys Acta , vol.1747 , pp. 213-220
    • Cheng, Y.C.1    Yan, F.J.2    Chang, L.S.3
  • 10
    • 39649105868 scopus 로고    scopus 로고
    • A novel serine protease inhibitor from Bungarus fasciatus venom
    • Lu J, Yang H, Yu H, Gao W, Lai R, et al. (2008) A novel serine protease inhibitor from Bungarus fasciatus venom. Peptides 29: 369-374.
    • (2008) Peptides , vol.29 , pp. 369-374
    • Lu, J.1    Yang, H.2    Yu, H.3    Gao, W.4    Lai, R.5
  • 12
    • 0021453880 scopus 로고
    • The isoinhibitors of chymotrypsin/elastase from Ascaris lumbricoides: the primary structure
    • Babin DR, Peanasky RJ, Goos SM, (1984) The isoinhibitors of chymotrypsin/elastase from Ascaris lumbricoides: the primary structure. Arch Biochem Biophys 232: 143-161.
    • (1984) Arch Biochem Biophys , vol.232 , pp. 143-161
    • Babin, D.R.1    Peanasky, R.J.2    Goos, S.M.3
  • 14
    • 0021459593 scopus 로고
    • The isoinhibitors of chymotrypsin/elastase from Ascaris lumbricoides: isolation by affinity chromatography and association with the enzymes
    • Peanasky RJ, Bentz Y, Paulson B, Graham DL, Babin DR, (1984) The isoinhibitors of chymotrypsin/elastase from Ascaris lumbricoides: isolation by affinity chromatography and association with the enzymes. Arch Biochem Biophys 232: 127-134.
    • (1984) Arch Biochem Biophys , vol.232 , pp. 127-134
    • Peanasky, R.J.1    Bentz, Y.2    Paulson, B.3    Graham, D.L.4    Babin, D.R.5
  • 15
    • 0025060939 scopus 로고
    • Sequential resonance assignment and secondary structure determination of the Ascaris trypsin inhibitor, a member of a novel class of proteinase inhibitors
    • Gronenborn AM, Nilges M, Peanasky RJ, Clore GM, (1990) Sequential resonance assignment and secondary structure determination of the Ascaris trypsin inhibitor, a member of a novel class of proteinase inhibitors. Biochemistry 29: 183-189.
    • (1990) Biochemistry , vol.29 , pp. 183-189
    • Gronenborn, A.M.1    Nilges, M.2    Peanasky, R.J.3    Clore, G.M.4
  • 16
    • 0028773905 scopus 로고
    • The molecular structure of the complex of Ascaris chymotrypsin/elastase inhibitor with porcine elastase
    • Huang K, Strynadka NC, Bernard VD, Peanasky RJ, James MN, (1994) The molecular structure of the complex of Ascaris chymotrypsin/elastase inhibitor with porcine elastase. Structure 2: 679-689.
    • (1994) Structure , vol.2 , pp. 679-689
    • Huang, K.1    Strynadka, N.C.2    Bernard, V.D.3    Peanasky, R.J.4    James, M.N.5
  • 17
    • 0030063710 scopus 로고    scopus 로고
    • BSTI, a trypsin inhibitor from skin secretions of Bombina bombina related to protease inhibitors of nematodes
    • Mignogna G, Pascarella S, Wechselberger C, Hinterleitner C, Mollay C, et al. (1996) BSTI, a trypsin inhibitor from skin secretions of Bombina bombina related to protease inhibitors of nematodes. Protein Sci 5: 357-362.
    • (1996) Protein Sci , vol.5 , pp. 357-362
    • Mignogna, G.1    Pascarella, S.2    Wechselberger, C.3    Hinterleitner, C.4    Mollay, C.5
  • 18
    • 0034129479 scopus 로고    scopus 로고
    • NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1): structural similarity with Ascaris protease inhibitors
    • Cierpicki T, Bania J, Otlewski J, (2000) NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1): structural similarity with Ascaris protease inhibitors. Protein Sci 9: 976-984.
    • (2000) Protein Sci , vol.9 , pp. 976-984
    • Cierpicki, T.1    Bania, J.2    Otlewski, J.3
  • 19
    • 84859984930 scopus 로고    scopus 로고
    • Hg1, novel peptide inhibitor specific for Kv1.3 channels from first scorpion Kunitz-type potassium channel toxin family
    • Chen ZY, Hu YT, Yang WS, He YW, Feng J, et al. (2012) Hg1, novel peptide inhibitor specific for Kv1.3 channels from first scorpion Kunitz-type potassium channel toxin family. J Biol Chem 287: 13813-13821.
    • (2012) J Biol Chem , vol.287 , pp. 13813-13821
    • Chen, Z.Y.1    Hu, Y.T.2    Yang, W.S.3    He, Y.W.4    Feng, J.5
  • 20
    • 84856322933 scopus 로고    scopus 로고
    • Extreme diversity of scorpion venom peptides and proteins revealed by transcriptomic analysis: Implication for proteome evolution of scorpion venom arsenal
    • Ma Y, He Y, Zhao R, Wu Y, Li W, et al. (2011) Extreme diversity of scorpion venom peptides and proteins revealed by transcriptomic analysis: Implication for proteome evolution of scorpion venom arsenal. J Proteomics 75(5): 1563-1576.
    • (2011) J Proteomics , vol.75 , Issue.5 , pp. 1563-1576
    • Ma, Y.1    He, Y.2    Zhao, R.3    Wu, Y.4    Li, W.5
  • 21
    • 0033950727 scopus 로고    scopus 로고
    • Cloning and characterization of the cDNA sequences of two venom peptides from Chinese scorpion Buthus martensii Karsch (BmK)
    • Zeng XC, Li WX, Zhu SY, Peng F, Jiang DH, et al. (2000) Cloning and characterization of the cDNA sequences of two venom peptides from Chinese scorpion Buthus martensii Karsch (BmK). Toxicon 38: 893-899.
    • (2000) Toxicon , vol.38 , pp. 893-899
    • Zeng, X.C.1    Li, W.X.2    Zhu, S.Y.3    Peng, F.4    Jiang, D.H.5
  • 23
    • 49649113677 scopus 로고    scopus 로고
    • Structural basis of a potent peptide inhibitor designed for Kv1.3 channel, a therapeutic target of autoimmune disease
    • Han S, Yi H, Yin SJ, Chen ZY, Liu H, et al. (2008) Structural basis of a potent peptide inhibitor designed for Kv1.3 channel, a therapeutic target of autoimmune disease. J Biol Chem 283: 19058-19065.
    • (2008) J Biol Chem , vol.283 , pp. 19058-19065
    • Han, S.1    Yi, H.2    Yin, S.J.3    Chen, Z.Y.4    Liu, H.5
  • 24
    • 3042814574 scopus 로고    scopus 로고
    • Simulation of the interaction between ScyTx and small conductance calcium-activated potassium channel by docking and MM-PBSA
    • Wu Y, Cao Z, Yi H, Jiang D, Mao X, et al. (2004) Simulation of the interaction between ScyTx and small conductance calcium-activated potassium channel by docking and MM-PBSA. Biophys J 87: 105-112.
    • (2004) Biophys J , vol.87 , pp. 105-112
    • Wu, Y.1    Cao, Z.2    Yi, H.3    Jiang, D.4    Mao, X.5
  • 25
    • 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, et al. (2011) SdPI, the first functionally characterized Kunitz-type trypsin inhibitor from scorpion venom. PLoS One 6: e27548.
    • (2011) PLoS One , vol.6
    • Zhao, R.1    Dai, H.2    Qiu, S.3    Li, T.4    He, Y.5
  • 26
    • 38049061651 scopus 로고    scopus 로고
    • The crystal structure of guamerin in complex with chymotrypsin and the development of an elastase-specific inhibitor
    • Kim H, Chu TT, Kim DY, Kim DR, Nguyen CM, et al. (2008) The crystal structure of guamerin in complex with chymotrypsin and the development of an elastase-specific inhibitor. J Mol Biol 376: 184-192.
    • (2008) J Mol Biol , vol.376 , pp. 184-192
    • Kim, H.1    Chu, T.T.2    Kim, D.Y.3    Kim, D.R.4    Nguyen, C.M.5
  • 27
    • 0028773904 scopus 로고
    • High-resolution structure of Ascaris trypsin inhibitor in solution: direct evidence for a pH-induced conformational transition in the reactive site
    • Grasberger BL, Clore GM, Gronenborn AM, (1994) High-resolution structure of Ascaris trypsin inhibitor in solution: direct evidence for a pH-induced conformational transition in the reactive site. Structure 2: 669-678.
    • (1994) Structure , vol.2 , pp. 669-678
    • Grasberger, B.L.1    Clore, G.M.2    Gronenborn, A.M.3
  • 28
    • 34447640731 scopus 로고    scopus 로고
    • Active and exo-site inhibition of human factor Xa: structure of des-Gla factor Xa inhibited by NAP5, a potent nematode anticoagulant protein from Ancylostoma caninum
    • Rios-Steiner JL, Murakami MT, Tulinsky A, Arni RK, (2007) Active and exo-site inhibition of human factor Xa: structure of des-Gla factor Xa inhibited by NAP5, a potent nematode anticoagulant protein from Ancylostoma caninum. J Mol Biol 371: 774-786.
    • (2007) J Mol Biol , vol.371 , pp. 774-786
    • Rios-Steiner, J.L.1    Murakami, M.T.2    Tulinsky, A.3    Arni, R.K.4
  • 29
    • 0141539503 scopus 로고    scopus 로고
    • Purification of recombinant plasminogen activator inhibitor-1 in the active conformation by refolding from inclusion bodies
    • Lee HJ, Im H, (2003) Purification of recombinant plasminogen activator inhibitor-1 in the active conformation by refolding from inclusion bodies. Protein Expr Purif 31: 99-107.
    • (2003) Protein Expr Purif , vol.31 , pp. 99-107
    • Lee, H.J.1    Im, H.2
  • 30
    • 0042375854 scopus 로고    scopus 로고
    • Structure-function relationship of serine protease-protein inhibitor interaction
    • Otlewski J, Jaskolski M, Buczek O, Cierpicki T, Czapinska H, et al. (2001) Structure-function relationship of serine protease-protein inhibitor interaction. Acta Biochim Pol 48: 419-428.
    • (2001) Acta Biochim Pol , vol.48 , pp. 419-428
    • Otlewski, J.1    Jaskolski, M.2    Buczek, O.3    Cierpicki, T.4    Czapinska, H.5
  • 31
    • 0028863028 scopus 로고
    • Comparison of the accuracy of protein solution structures derived from conventional and network-edited NOESY data
    • Hoogstraten CG, Choe S, Westler WM, Markley JL, (1995) Comparison of the accuracy of protein solution structures derived from conventional and network-edited NOESY data. Protein Sci 4: 2289-2299.
    • (1995) Protein Sci , vol.4 , pp. 2289-2299
    • Hoogstraten, C.G.1    Choe, S.2    Westler, W.M.3    Markley, J.L.4
  • 32
    • 0030047628 scopus 로고    scopus 로고
    • Solution structure and backbone dynamics of recombinant Cucurbita maxima trypsin inhibitor-V determined by NMR spectroscopy
    • Liu J, Prakash O, Cai M, Gong Y, Huang Y, et al. (1996) Solution structure and backbone dynamics of recombinant Cucurbita maxima trypsin inhibitor-V determined by NMR spectroscopy. Biochemistry 35: 1516-1524.
    • (1996) Biochemistry , vol.35 , pp. 1516-1524
    • Liu, J.1    Prakash, O.2    Cai, M.3    Gong, Y.4    Huang, Y.5
  • 33
    • 0023652256 scopus 로고
    • Crystal and molecular structure of the serine proteinase inhibitor CI-2 from barley seeds
    • McPhalen CA, James MN, (1987) Crystal and molecular structure of the serine proteinase inhibitor CI-2 from barley seeds. Biochemistry 26: 261-269.
    • (1987) Biochemistry , vol.26 , pp. 261-269
    • McPhalen, C.A.1    James, M.N.2
  • 34
    • 80054909439 scopus 로고    scopus 로고
    • The P(2)' residue is a key determinant of mesotrypsin specificity: engineering a high-affinity inhibitor with anticancer activity
    • Salameh MA, Soares AS, Hockla A, Radisky DC, Radisky ES, (2011) The P(2)' residue is a key determinant of mesotrypsin specificity: engineering a high-affinity inhibitor with anticancer activity. Biochem J 440: 95-105.
    • (2011) Biochem J , vol.440 , pp. 95-105
    • Salameh, M.A.1    Soares, A.S.2    Hockla, A.3    Radisky, D.C.4    Radisky, E.S.5
  • 35
    • 0037447246 scopus 로고    scopus 로고
    • Engineering the proteolytic specificity of activated protein C improves its pharmacological properties
    • Berg DT, Gerlitz B, Shang J, Smith T, Santa P, et al. (2003) Engineering the proteolytic specificity of activated protein C improves its pharmacological properties. Proc Natl Acad Sci U S A 100: 4423-4428.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 4423-4428
    • Berg, D.T.1    Gerlitz, B.2    Shang, J.3    Smith, T.4    Santa, P.5
  • 36
    • 0032900897 scopus 로고    scopus 로고
    • Dynamic diversification from a putative common ancestor of scorpion toxins affecting sodium, potassium, and chloride channels
    • Froy O, Sagiv T, Poreh M, Urbach D, Zilberberg N, et al. (1999) Dynamic diversification from a putative common ancestor of scorpion toxins affecting sodium, potassium, and chloride channels. J Mol Evol 48: 187-196.
    • (1999) J Mol Evol , vol.48 , pp. 187-196
    • Froy, O.1    Sagiv, T.2    Poreh, M.3    Urbach, D.4    Zilberberg, N.5
  • 38
    • 52049091018 scopus 로고    scopus 로고
    • Isolation, expression and characterization of a novel dual serine protease inhibitor, OH-TCI, from king cobra venom
    • He YY, Liu SB, Lee WH, Qian JQ, Zhang Y, (2008) Isolation, expression and characterization of a novel dual serine protease inhibitor, OH-TCI, from king cobra venom. Peptides 29: 1692-1699.
    • (2008) Peptides , vol.29 , pp. 1692-1699
    • He, Y.Y.1    Liu, S.B.2    Lee, W.H.3    Qian, J.Q.4    Zhang, Y.5
  • 39
    • 79957597527 scopus 로고    scopus 로고
    • A bifunctional sea anemone peptide with Kunitz type protease and potassium channel inhibiting properties
    • Peigneur S, Billen B, Derua R, Waelkens E, Debaveye S, et al. (2011) A bifunctional sea anemone peptide with Kunitz type protease and potassium channel inhibiting properties. Biochem Pharmacol 82: 81-90.
    • (2011) Biochem Pharmacol , vol.82 , pp. 81-90
    • Peigneur, S.1    Billen, B.2    Derua, R.3    Waelkens, E.4    Debaveye, S.5
  • 40
    • 54849414437 scopus 로고    scopus 로고
    • Discovery of a distinct superfamily of Kunitz-type toxin (KTT) from tarantulas
    • Yuan CH, He QY, Peng K, Diao JB, Jiang LP, et al. (2008) Discovery of a distinct superfamily of Kunitz-type toxin (KTT) from tarantulas. PLoS One 3: e3414.
    • (2008) PLoS One , vol.3
    • Yuan, C.H.1    He, Q.Y.2    Peng, K.3    Diao, J.B.4    Jiang, L.P.5
  • 41
    • 54249105941 scopus 로고    scopus 로고
    • Surface sites for engineering allosteric control in proteins
    • Lee J, Natarajan M, Nashine VC, Socolich M, Vo T, et al. (2008) Surface sites for engineering allosteric control in proteins. Science 322: 438-442.
    • (2008) Science , vol.322 , pp. 438-442
    • Lee, J.1    Natarajan, M.2    Nashine, V.C.3    Socolich, M.4    Vo, T.5


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