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Volumn 12, Issue 5, 2011, Pages 341-347

Plant protein proteinase inhibitors: Structure and mechanism of inhibition

Author keywords

Plant protein proteinase inhibitor; Reactive site loop; Standard mechanism; Three dimensional structure

Indexed keywords

APROTININ; BOWMAN BIRK INHIBITOR; CARBOXYPEPTIDASE; CARBOXYPEPTIDASE INHIBITOR; CYSTATIN; CYSTEINE PROTEINASE; CYSTEINE PROTEINASE INHIBITOR; ENZYME INHIBITOR; HELIX LOOP HELIX PROTEIN; KNOTTIN; PROTEINASE INHIBITOR; SERINE PROTEINASE; TRYPSIN INHIBITOR; UNCLASSIFIED DRUG; CERAL PROTEINASE INHIBITOR; POTATO 1 INHIBITOR; POTATO II INHIBITOR; RAPESEED PROTEINASE INHIBITOR; SERINE PROTEINASE INHIBITOR; SUNFLOWER TRYPSIN INHIBITOR; VEGETABLE PROTEIN;

EID: 84855322586     PISSN: 13892037     EISSN: 18755550     Source Type: Journal    
DOI: 10.2174/138920311796391124     Document Type: Review
Times cited : (51)

References (61)
  • 2
    • 84855318964 scopus 로고    scopus 로고
    • U.S. National Library of Medicine, Accessed March, 2010
    • U.S. National Library of Medicine. PubMed. http://www.ncbi.nlmnih.gov/sites/entrez?db=pubmed (Accessed March, 2010).
    • PubMed
  • 4
    • 0342445397 scopus 로고    scopus 로고
    • What can the structures of enzymeinhibitor complexes tell us about the structures of enzyme substrate complexes?
    • Laskowski, M.J.; Qasim, M.A. What can the structures of enzymeinhibitor complexes tell us about the structures of enzyme substrate complexes? Biochim. Biophys. Acta, 2000, 1477(1), 324-337.
    • (2000) Biochim. Biophys. Acta , vol.1477 , Issue.1 , pp. 324-337
    • Laskowski, M.J.1    Qasim, M.A.2
  • 5
    • 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(2), 433-451.
    • (1992) Eur. J. Biochem , vol.204 , Issue.2 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 7
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski, M.J.; Kato, I. Protein inhibitors of proteinases. Annu. Rev. Biochem., 1980, 49, 593-626.
    • (1980) Annu. Rev. Biochem , vol.49 , pp. 593-626
    • Laskowski, M.J.1    Kato, I.2
  • 12
    • 0022371307 scopus 로고
    • Turkey ovomucoid third domain inhibits eight different serine proteinases of varied specificity on the same . . .Leu18-Glu19 . . . reactive site
    • Ardelt, W.; Laskowski, M.J. Turkey ovomucoid third domain inhibits eight different serine proteinases of varied specificity on the same . . .Leu18-Glu19 . . . reactive site. Biochemistry, 1985, 24(20), 5313-5320.
    • (1985) Biochemistry , vol.24 , Issue.20 , pp. 5313-5320
    • Ardelt, W.1    Laskowski, M.J.2
  • 13
    • 0036678453 scopus 로고    scopus 로고
    • A clogged gutter mechanism for protease inhibitors
    • Radisky, E.S.; Koshland, D.E.J. A clogged gutter mechanism for protease inhibitors. Proc. Natl. Acad. Sci. USA, 2002, 99(16), 10316-10321.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.16 , pp. 10316-10321
    • Radisky, E.S.1    Koshland, D.E.J.2
  • 14
    • 0025769768 scopus 로고
    • Effect of single amino acid replacements on the thermodynamics of the reactive site peptide bond hydrolysis in ovomucoid third domain
    • Ardelt, W.; Laskowski, M.J. Effect of single amino acid replacements on the thermodynamics of the reactive site peptide bond hydrolysis in ovomucoid third domain. J. Mol. Biol., 1991, 220(4), 1041-1053.
    • (1991) J. Mol. Biol , vol.220 , Issue.4 , pp. 1041-1053
    • Ardelt, W.1    Laskowski, M.J.2
  • 15
    • 0037441484 scopus 로고    scopus 로고
    • Structure and dynamics of the potato carboxypeptidase inhibitor by 1H and 15N NMR
    • Gonzlez, C.; Neira, J.L.; Ventura, S.; Bronsoms, S.; Rico, M.; Avils, F.X. Structure and dynamics of the potato carboxypeptidase inhibitor by 1H and 15N NMR. Proteins, 2003, 50(3), 410-422.
    • (2003) Proteins , vol.50 , Issue.3 , pp. 410-422
    • Gonzlez, C.1    Neira, J.L.2    Ventura, S.3    Bronsoms, S.4    Rico, M.5    Avils, F.X.6
  • 16
    • 0023475020 scopus 로고
    • Threedimensional structure of potato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics
    • Clore, G.M.; Gronenborn, A.M.; Nilges, M.; Ryan, C.A. Threedimensional structure of potato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics. Biochemistry, 1987, 26(24), 8012-8023.
    • (1987) Biochemistry , vol.26 , Issue.24 , pp. 8012-8023
    • Clore, G.M.1    Gronenborn, A.M.2    Nilges, M.3    Ryan, C.A.4
  • 17
    • 0020491126 scopus 로고
    • Refined crystal structure of the potato inhibitor complex of carboxypeptidase A at 2.5 A resolution
    • Rees, D.C.; Lipscomb, W.N. Refined crystal structure of the potato inhibitor complex of carboxypeptidase A at 2.5 A resolution. J. Mol. Biol., 1982, 160(3), 475-498.
    • (1982) J. Mol. Biol , vol.160 , Issue.3 , pp. 475-498
    • Rees, D.C.1    Lipscomb, W.N.2
  • 18
    • 0034615567 scopus 로고    scopus 로고
    • Metallocarboxypeptidases and their protein inhibitors. Structure, function and biomedical properties
    • Vendrell, J.; Querol, E.; Avilés, F.X. Metallocarboxypeptidases and their protein inhibitors. Structure, function and biomedical properties. Biochim. Biophys. Acta, 2000, 1477(2), 284-298.
    • (2000) Biochim. Biophys. Acta , vol.1477 , Issue.2 , pp. 284-298
    • Vendrell, J.1    Querol, E.2    Avilés, F.X.3
  • 19
    • 0025301658 scopus 로고
    • The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: A novel type of proteinase inhibitor interaction
    • Stubbs, M.T.; Laber, B.; Bode, W.; Huber, R.; Jerala, R.; Lenarcic, B.; Turk, V. The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction. EMBO J., 1990, 9(6), 1939-1947.
    • (1990) EMBO J , vol.9 , Issue.6 , pp. 1939-1947
    • Stubbs, M.T.1    Laber, B.2    Bode, W.3    Huber, R.4    Jerala, R.5    Lenarcic, B.6    Turk, V.7
  • 20
    • 70349327661 scopus 로고    scopus 로고
    • Action of plant proteinase inhibitors on enzymes of physiopathological importance
    • Oliva, M.L.; Sampaio, M.U. Action of plant proteinase inhibitors on enzymes of physiopathological importance. An. Acad. Bras. Cienc., 2009, 81(3), 615-621.
    • (2009) An. Acad. Bras. Cienc , vol.81 , Issue.3 , pp. 615-621
    • Oliva, M.L.1    Sampaio, M.U.2
  • 21
    • 0016318618 scopus 로고
    • Mode of action of soybean trypsin inhibitor (Kunitz) as a model for specific protein-protein interactions
    • Blow, D.M.; Janin, J.; Sweet, R.M. Mode of action of soybean trypsin inhibitor (Kunitz) as a model for specific protein-protein interactions. Nature, 1974, 249(452), 54-57.
    • (1974) Nature , vol.249 , Issue.452 , pp. 54-57
    • Blow, D.M.1    Janin, J.2    Sweet, R.M.3
  • 22
    • 0016174105 scopus 로고
    • Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6-A resolution
    • Sweet, R.M.; Wright, H.T.; Janin, J.; Chothia, C.H.; Blow, D.M. Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6-A resolution. Biochemistry, 1974, 13(20), 4212-4228.
    • (1974) Biochemistry , vol.13 , Issue.20 , pp. 4212-4228
    • Sweet, R.M.1    Wright, H.T.2    Janin, J.3    Chothia, C.H.4    Blow, D.M.5
  • 23
    • 74149093016 scopus 로고    scopus 로고
    • Cloning, sequence analysis and crystal structure determination of a miraculin-like protein from Murraya koenigii
    • Gahloth, D.; Selvakumar, P.; Shee, C.; Kumar, P.; Sharma, A.K. Cloning, sequence analysis and crystal structure determination of a miraculin-like protein from Murraya koenigii. Arch. Biochem. Biophys., 2010, 494(1), 15-22.
    • (2010) Arch. Biochem. Biophys , vol.494 , Issue.1 , pp. 15-22
    • Gahloth, D.1    Selvakumar, P.2    Shee, C.3    Kumar, P.4    Sharma, A.K.5
  • 24
    • 70350355110 scopus 로고    scopus 로고
    • The ternary structure of the double-headed arrowhead protease inhibitor API-A complexed with two trypsins reveals a novel reactive site conformation
    • Bao, R.; Zhou, C.Z.; Jiang, C.; Lin, S.X.; Chi, C.W.; Chen, Y. The ternary structure of the double-headed arrowhead protease inhibitor API-A complexed with two trypsins reveals a novel reactive site conformation. J. Biol. Chem., 2009, 284(39), 26676-26684.
    • (2009) J. Biol. Chem , vol.284 , Issue.39 , pp. 26676-26684
    • Bao, R.1    Zhou, C.Z.2    Jiang, C.3    Lin, S.X.4    Chi, C.W.5    Chen, Y.6
  • 26
    • 26844473090 scopus 로고    scopus 로고
    • Kunitz-type Bauhinia bauhinioides inhibitors devoid of disulfide bridges: Isolation of the cDNAs, heterologous expression and structural studies
    • Arajo, A.P.; Hansen, D.; Vieira, D.F.; Oliveira, C.; Santana, L.A.; Beltramini, L.M.; Sampaio, C.A.; Sampaio, M.U.; Oliva, M.L. Kunitz-type Bauhinia bauhinioides inhibitors devoid of disulfide bridges: isolation of the cDNAs, heterologous expression and structural studies. Biol. Chem., 2005, 386(6), 561-568.
    • (2005) Biol. Chem , vol.386 , Issue.6 , pp. 561-568
    • Arajo, A.P.1    Hansen, D.2    Vieira, D.F.3    Oliveira, C.4    Santana, L.A.5    Beltramini, L.M.6    Sampaio, C.A.7    Sampaio, M.U.8    Oliva, M.L.9
  • 27
    • 0242432550 scopus 로고    scopus 로고
    • Inhouse phase determination of the lima bean trypsin inhibitor: A lowresolution sulfur-SAD case
    • Debreczeni, J.E.; Bunkczi, G.; Girmann, B.; Sheldrick, G.M. Inhouse phase determination of the lima bean trypsin inhibitor: a lowresolution sulfur-SAD case. Acta Cryst. D Biol. Crystallogr., 2003, 59(2), 393-395.
    • (2003) Acta Cryst. D Biol. Crystallogr , vol.59 , Issue.2 , pp. 393-395
    • Debreczeni, J.E.1    Bunkczi, G.2    Girmann, B.3    Sheldrick, G.M.4
  • 28
    • 34748915798 scopus 로고    scopus 로고
    • Bowman-Birk protease inhibitor from the seeds of Vigna unguiculata forms a highly stable dimeric structure
    • Rao, K.N.; Suresh, C.G. Bowman-Birk protease inhibitor from the seeds of Vigna unguiculata forms a highly stable dimeric structure. Biochim. Biophys. Acta, 2007, 1774(10), 1264-1273.
    • (2007) Biochim. Biophys. Acta , vol.1774 , Issue.10 , pp. 1264-1273
    • Rao, K.N.1    Suresh, C.G.2
  • 29
    • 0029658121 scopus 로고    scopus 로고
    • Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution. Structural peculiarities in a folded protein conformation
    • Voss, R.H.; Ermler, U.; Essen, L.O.; Wenzl, G.; Kim, Y.M.; Flecker, P. Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution. Structural peculiarities in a folded protein conformation. Eur. J. Biochem., 1996, 242(1), 122-131.
    • (1996) Eur. J. Biochem , vol.242 , Issue.1 , pp. 122-131
    • Voss, R.H.1    Ermler, U.2    Essen, L.O.3    Wenzl, G.4    Kim, Y.M.5    Flecker, P.6
  • 30
    • 33747399034 scopus 로고    scopus 로고
    • Inhibitory properties and solution structure of a potent Bowman-Birk protease inhibitor from lentil (Lens culinaris, L) seeds
    • Ragg, E.M.; Galbusera, V.; Scarafoni, A.; Negri, A.; Tedeschi, G.; Consonni, A.; Sessa, F.; Duranti, M. Inhibitory properties and solution structure of a potent Bowman-Birk protease inhibitor from lentil (Lens culinaris, L) seeds. FEBS J., 2006, 273(17), 4024-4039.
    • (2006) FEBS J , vol.273 , Issue.17 , pp. 4024-4039
    • Ragg, E.M.1    Galbusera, V.2    Scarafoni, A.3    Negri, A.4    Tedeschi, G.5    Consonni, A.6    Sessa, F.7    Duranti, M.8
  • 31
    • 0037452941 scopus 로고    scopus 로고
    • Anticarcinogenic Bowman Birk inhibitor isolated from snail medic seeds (Medicago scutellata): Solution structure and analysis of selfassociation behavior
    • Catalano, M.; Ragona, L.; Molinari, H.; Tava, A.; Zetta, L. Anticarcinogenic Bowman Birk inhibitor isolated from snail medic seeds (Medicago scutellata): solution structure and analysis of selfassociation behavior. Biochemistry, 2003, 42(10), 2836-2846.
    • (2003) Biochemistry , vol.42 , Issue.10 , pp. 2836-2846
    • Catalano, M.1    Ragona, L.2    Molinari, H.3    Tava, A.4    Zetta, L.5
  • 32
    • 0026551660 scopus 로고
    • Three-dimensional structure of soybean trypsin/chymotrypsin Bowman-Birk inhibitor in solution
    • Werner, M.H.; Wemmer, D.E. Three-dimensional structure of soybean trypsin/chymotrypsin Bowman-Birk inhibitor in solution. Biochemistry, 1992, 31(4), 999-1010.
    • (1992) Biochemistry , vol.31 , Issue.4 , pp. 999-1010
    • Werner, M.H.1    Wemmer, D.E.2
  • 33
    • 0027409046 scopus 로고
    • The 0.25-nm X-ray structure of the Bowman-Birk-type inhibitor from mung bean in ternary complex with porcine trypsin
    • Lin, G.; Bode, W.; Huber, R.; Chi, C.W.; Engh, R.A. The 0.25-nm X-ray structure of the Bowman-Birk-type inhibitor from mung bean in ternary complex with porcine trypsin. Eur. J. Biochem., 1993, 212(2), 549-555.
    • (1993) Eur. J. Biochem , vol.212 , Issue.2 , pp. 549-555
    • Lin, G.1    Bode, W.2    Huber, R.3    Chi, C.W.4    Engh, R.A.5
  • 34
    • 33847785970 scopus 로고    scopus 로고
    • Crystal structure of the Bowman-Birk Inhibitor from Vigna unguiculata seeds in complex with beta-trypsin at 1.55 A resolution and its structural properties in association with proteinases
    • Barbosa, J.A.; Silva, L.P.; Teles, R.C.; Esteves, G.F.; Azevedo, R.B.; Ventura, M.M.; de Freitas, S.M. Crystal structure of the Bowman-Birk Inhibitor from Vigna unguiculata seeds in complex with beta-trypsin at 1.55 A resolution and its structural properties in association with proteinases. Biophys. J., 2007, 92(5), 1638-1650.
    • (2007) Biophys. J , vol.92 , Issue.5 , pp. 1638-1650
    • Barbosa, J.A.1    Silva, L.P.2    Teles, R.C.3    Esteves, G.F.4    Azevedo, R.B.5    Ventura, M.M.6    de Freitas, S.M.7
  • 35
    • 33947319328 scopus 로고    scopus 로고
    • Crystal structure of the anticarcinogenic Bowman-Birk inhibitor from snail medic (Medicago scutellata) seeds complexed with bovine trypsin
    • Capaldi, S.; Perduca, M.; Faggion, B.; Carrizo, M.E.; Tava, A.; Ragona, L.; Monaco, H.L. Crystal structure of the anticarcinogenic Bowman-Birk inhibitor from snail medic (Medicago scutellata) seeds complexed with bovine trypsin. J. Struct. Biol., 2007, 158(1), 71-79.
    • (2007) J. Struct. Biol , vol.158 , Issue.1 , pp. 71-79
    • Capaldi, S.1    Perduca, M.2    Faggion, B.3    Carrizo, M.E.4    Tava, A.5    Ragona, L.6    Monaco, H.L.7
  • 36
    • 4644349431 scopus 로고    scopus 로고
    • Crystal structure of the Bowman-Birk inhibitor from barley seeds in ternary complex with porcine trypsin
    • Park, E.Y.; Kim, J.A.; Kim, H.W.; Kim, Y.S.; Song, H.K. Crystal structure of the Bowman-Birk inhibitor from barley seeds in ternary complex with porcine trypsin. J. Mol. Biol., 2004, 343(1), 173-186.
    • (2004) J. Mol. Biol , vol.343 , Issue.1 , pp. 173-186
    • Park, E.Y.1    Kim, J.A.2    Kim, H.W.3    Kim, Y.S.4    Song, H.K.5
  • 37
  • 38
    • 0034607547 scopus 로고    scopus 로고
    • Crystal structure of cancer chemopreventive Bowman-Birk inhibitor in ternary complex with bovine trypsin at 2.3 A resolution. Structural basis of Janus-faced serine protease inhibitor specificity
    • Koepke, J.; Ermler, U.; Warkentin, E.; Wenzl, G.; Flecker, P. Crystal structure of cancer chemopreventive Bowman-Birk inhibitor in ternary complex with bovine trypsin at 2.3 A resolution. Structural basis of Janus-faced serine protease inhibitor specificity. J. Mol. Biol., 2000, 298(3), 477-491.
    • (2000) J. Mol. Biol , vol.298 , Issue.3 , pp. 477-491
    • Koepke, J.1    Ermler, U.2    Warkentin, E.3    Wenzl, G.4    Flecker, P.5
  • 39
    • 0001483373 scopus 로고    scopus 로고
    • Dimeric crystal structure of a Bowman-Birk protease inhibitor from pea seeds
    • Li de la Sierra, I.; Quillien, L.; Flecker, P.; Gueguen, J.; Brunie, S. Dimeric crystal structure of a Bowman-Birk protease inhibitor from pea seeds. J. Mol. Biol., 1999, 285(3), 1195-207.
    • (1999) J. Mol. Biol , vol.285 , Issue.3 , pp. 1195-1207
    • de la Li Sierra, I.1    Quillien, L.2    Flecker, P.3    Gueguen, J.4    Brunie, S.5
  • 40
    • 0035902766 scopus 로고    scopus 로고
    • Solution structures by 1H NMR of the novel cyclic trypsin inhibitor SFTI-1 from sunflower seeds and an acyclic permutant
    • Korsinczky, M.L.; Schirra, H.J.; Rosengren, K.J.; West, J.; Condie, B.A.; Otvos, L.; Anderson, M.A.; Craik, D.J. Solution structures by 1H NMR of the novel cyclic trypsin inhibitor SFTI-1 from sunflower seeds and an acyclic permutant. J. Mol. Biol., 2001, 311(3), 579-591.
    • (2001) J. Mol. Biol , vol.311 , Issue.3 , pp. 579-591
    • Korsinczky, M.L.1    Schirra, H.J.2    Rosengren, K.J.3    West, J.4    Condie, B.A.5    Otvos, L.6    Anderson, M.A.7    Craik, D.J.8
  • 41
    • 25444487484 scopus 로고    scopus 로고
    • Discovery, structural determination, and putative processing of the precursor protein that produces the cyclic trypsin inhibitor sunflower trypsin inhibitor 1
    • Mulvenna, J.; Foley, F.; Craik, D. Discovery, structural determination, and putative processing of the precursor protein that produces the cyclic trypsin inhibitor sunflower trypsin inhibitor 1. J. Biol. Chem., 2005, 280(37), 32245-32253.
    • (2005) J. Biol. Chem , vol.280 , Issue.37 , pp. 32245-32253
    • Mulvenna, J.1    Foley, F.2    Craik, D.3
  • 42
    • 0023729499 scopus 로고
    • Structural comparison of two serine proteinase-protein inhibitor complexes: Eglin-c-subtilisin Carlsberg and CI-2-subtilisin Novo
    • McPhalen, C.A.; James, M.N.G. Structural comparison of two serine proteinase-protein inhibitor complexes: eglin-c-subtilisin Carlsberg and CI-2-subtilisin Novo. Biochemistry, 1988, 27(17), 6582-6598.
    • (1988) Biochemistry , vol.27 , Issue.17 , pp. 6582-6598
    • McPhalen, C.A.1    James, M.N.G.2
  • 43
    • 0023652256 scopus 로고
    • Crystal and molecular structure of the serine proteinase inhibitor CI-2 from barley seeds
    • McPhalen, C.A.; James, M.N.G. Crystal and molecular structure of the serine proteinase inhibitor CI-2 from barley seeds. Biochemistry, 1987, 26(1), 261-269.
    • (1987) Biochemistry , vol.26 , Issue.1 , pp. 261-269
    • McPhalen, C.A.1    James, M.N.G.2
  • 44
    • 0023398103 scopus 로고
    • Comparison of the solution and Xray structures of barley serine proteinase inhibitor 2
    • Clore, G.M.; Gronenborn, A.M.; James, M.N.G.; Kjaer, M.; McPhalen, C.A.; Poulsen, F.M. Comparison of the solution and Xray structures of barley serine proteinase inhibitor 2. Protein Eng., 1987, 1(4), 313-318.
    • (1987) Protein Eng , vol.1 , Issue.4 , pp. 313-318
    • Clore, G.M.1    Gronenborn, A.M.2    James, M.N.G.3    Kjaer, M.4    McPhalen, C.A.5    Poulsen, F.M.6
  • 45
    • 21444454700 scopus 로고    scopus 로고
    • Structure and folding of potato type II proteinase inhibitors: Circular permutation and intramolecular domain swapping
    • Schirra, H.J.; Craik, D.J. Structure and folding of potato type II proteinase inhibitors: circular permutation and intramolecular domain swapping. Protein Pept. Lett., 2005, 12(5), 421-431.
    • (2005) Protein Pept. Lett , vol.12 , Issue.5 , pp. 421-431
    • Schirra, H.J.1    Craik, D.J.2
  • 46
    • 0043234212 scopus 로고    scopus 로고
    • Unbound Form of Tomato Inhibitor-II Reveals Interdomain Flexibility and Conformational Variability In the Reactive Site Loops
    • Barrette-Ng, I.H.; Ng, K.K.; Cherney, M.M.; Pearce, G.; Ghani, U.; Ryan, C.A.; James, M.N.G. Unbound form of tomato inhibitor-II reveals interdomain flexibility and conformational variability in the reactive site loops. J. Biol. Chem., 2003, 278(33), 31391-31400.
    • (2003) J. Biol. Chem , vol.278 , Issue.33 , pp. 31391-31400
    • Barrette-Ng, I.H.1    Ng, K.K.2    Cherney, M.M.3    Pearce, G.4    Ghani, U.5    Ryan, C.A.6    James, M.N.G.7
  • 47
    • 0038267164 scopus 로고    scopus 로고
    • Structural basis of inhibition revealed by a 1:2 complex of the two-headed tomato inhibitor-II and subtilisin Carlsberg
    • Barrette-Ng, I.H.; Ng, K.K.; Cherney, M.M.; Pearce, G.; Ryan, C.A.; James, M.N.G. Structural basis of inhibition revealed by a 1:2 complex of the two-headed tomato inhibitor-II and subtilisin Carlsberg. J. Biol. Chem., 2003, 278(26), 24062-24071.
    • (2003) J. Biol. Chem , vol.278 , Issue.26 , pp. 24062-24071
    • Barrette-Ng, I.H.1    Ng, K.K.2    Cherney, M.M.3    Pearce, G.4    Ryan, C.A.5    James, M.N.G.6
  • 48
    • 0032480808 scopus 로고    scopus 로고
    • Structural determinants of the bifunctional corn Hageman factor inhibitor: X-ray crystal structure at 1.95 A resolution
    • Behnke, C.A.; Yee, V.C.; Trong, I.L.; Pedersen, L.C.; Stenkamp, R.E.; Kim, S.S.; Reeck, G.R.; Teller, D.C. Structural determinants of the bifunctional corn Hageman factor inhibitor: X-ray crystal structure at 1.95 A resolution. Biochemistry, 1998, 37(44), 15277-15288.
    • (1998) Biochemistry , vol.37 , Issue.44 , pp. 15277-15288
    • Behnke, C.A.1    Yee, V.C.2    Trong, I.L.3    Pedersen, L.C.4    Stenkamp, R.E.5    Kim, S.S.6    Reeck, G.R.7    Teller, D.C.8
  • 49
    • 0034098039 scopus 로고    scopus 로고
    • Structure of the bifunctional inhibitor of trypsin and alpha-amylase from ragi seeds at 2.2 A resolution
    • Gourinath, S.; Alam, N.; Srinivasan, A.; Betzel, C.; Singh, T.P. Structure of the bifunctional inhibitor of trypsin and alpha-amylase from ragi seeds at 2.2 A resolution. Acta Crystallogr. D Biol. Crystallogr., 2000, 56(3), 287-293.
    • (2000) Acta Crystallogr. D Biol. Crystallogr , vol.56 , Issue.3 , pp. 287-293
    • Gourinath, S.1    Alam, N.2    Srinivasan, A.3    Betzel, C.4    Singh, T.P.5
  • 50
    • 0032528247 scopus 로고    scopus 로고
    • A novel strategy for inhibition of alpha-amylases: Yellow meal worm alpha-amylase in complex with the Ragi bifunctional inhibitor at 2.5 A resolution
    • Strobl, S.; Maskos, K.; Wiegand, G.; Huber, R.; Gomis-Ruth, F.X.; Glockshuber, R. A novel strategy for inhibition of alpha-amylases: yellow meal worm alpha-amylase in complex with the Ragi bifunctional inhibitor at 2.5 A resolution. Structure, 1998, 6(7), 911-921.
    • (1998) Structure , vol.6 , Issue.7 , pp. 911-921
    • Strobl, S.1    Maskos, K.2    Wiegand, G.3    Huber, R.4    Gomis-Ruth, F.X.5    Glockshuber, R.6
  • 51
    • 34948872162 scopus 로고    scopus 로고
    • An unusual helix-turnhelix protease inhibitory motif in a novel trypsin inhibitor from seeds of Veronica (Veronica hederifolia L.)
    • Conners, R.; Konarev, A.V.; Forsyth, J.; Lovegrove, A.; Marsh, J.; Joseph-Horne, T.; Shewry, P.; Brady, R. L. An unusual helix-turnhelix protease inhibitory motif in a novel trypsin inhibitor from seeds of Veronica (Veronica hederifolia L.). J. Biol. Chem., 2007, 282(38), 27760-27768.
    • (2007) J. Biol. Chem , vol.282 , Issue.38 , pp. 27760-27768
    • Conners, R.1    Konarev, A.V.2    Forsyth, J.3    Lovegrove, A.4    Marsh, J.5    Joseph-Horne, T.6    Shewry, P.7    Brady, R.L.8
  • 52
    • 0037108093 scopus 로고    scopus 로고
    • NMR solution structure of ATTp, an Arabidopsis thaliana trypsin inhibitor
    • Zhao, Q.; Chae, Y.K.; Markley, J.L. NMR solution structure of ATTp, an Arabidopsis thaliana trypsin inhibitor. Biochemistry, 2002, 41(41), 12284-12296.
    • (2002) Biochemistry , vol.41 , Issue.41 , pp. 12284-12296
    • Zhao, Q.1    Chae, Y.K.2    Markley, J.L.3
  • 55
    • 70349583511 scopus 로고    scopus 로고
    • Discovery, structure and biological activities of cyclotides
    • Daly, N.L.; Rosengren, K.J.; Craik, D.J. Discovery, structure and biological activities of cyclotides. Adv Drug Deliv. Rev., 2009, 61(11), 918-930.
    • (2009) Adv Drug Deliv. Rev , vol.61 , Issue.11 , pp. 918-930
    • Daly, N.L.1    Rosengren, K.J.2    Craik, D.J.3
  • 57
    • 77957902701 scopus 로고    scopus 로고
    • Discovery and applications of the plant cyclotides
    • Craik, D.J. Discovery and applications of the plant cyclotides. Toxicon, 2010.
    • (2010) Toxicon
    • Craik, D.J.1
  • 58
    • 0035933743 scopus 로고    scopus 로고
    • Circular proteins in plants: Solution structure of a novel macrocyclic trypsin inhibitor from Momordica cochinchinensis
    • Felizmenio-Quimio, M.E.; Daly, N.L.; Craik, D.J. Circular proteins in plants: solution structure of a novel macrocyclic trypsin inhibitor from Momordica cochinchinensis. J. Biol. Chem., 2001, 276(25), 22875-22882.
    • (2001) J. Biol. Chem , vol.276 , Issue.25 , pp. 22875-22882
    • Felizmenio-Quimio, M.E.1    Daly, N.L.2    Craik, D.J.3
  • 61
    • 66449110019 scopus 로고    scopus 로고
    • Characterization of Solanum tuberosum multicystatin and its structural comparison with other cystatins
    • Nissen, M.S.; Kumar, G.N.; Youn, B.; Knowles, D.B.; Lam, K.S.; Ballinger, W.J.; Knowles, N.R.; Kang, C. Characterization of Solanum tuberosum multicystatin and its structural comparison with other cystatins. Plant Cell, 2009, 21(3), 861-875.
    • (2009) Plant Cell , vol.21 , Issue.3 , pp. 861-875
    • Nissen, M.S.1    Kumar, G.N.2    Youn, B.3    Knowles, D.B.4    Lam, K.S.5    Ballinger, W.J.6    Knowles, N.R.7    Kang, C.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.