메뉴 건너뛰기




Volumn 108, Issue 6, 1996, Pages 473-484

Hypothesis for a serine proteinase-like domain at the COOH terminus of slowpoke calcium-activated potassium channels

Author keywords

bovine pancreatic trypsin inhibitor; planar bilayer; sequence alignment; sequence homology; single channel recording

Indexed keywords

APROTININ; CALCIUM CHANNEL; SERINE PROTEINASE;

EID: 0030466438     PISSN: 00221295     EISSN: None     Source Type: Journal    
DOI: 10.1085/jgp.108.6.473     Document Type: Article
Times cited : (20)

References (83)
  • 2
    • 0028328469 scopus 로고
    • Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases
    • Allaire, M., M.M. Chernaia, B.A. Malcolm, and M.N.G. James. 1994. Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases. Nature (Lond.). 369:72-76.
    • (1994) Nature (Lond.) , vol.369 , pp. 72-76
    • Allaire, M.1    Chernaia, M.M.2    Malcolm, B.A.3    James, M.N.G.4
  • 5
    • 0026413976 scopus 로고
    • A component of calcium-activated potassium channels encoded by the Drosophila slo locus
    • Atkinson, N.S., G.A. Robertson, and B. Ganetzky. 1991. A component of calcium-activated potassium channels encoded by the Drosophila slo locus. Science (Wash. DC). 253:551-555.
    • (1991) Science (Wash. DC) , vol.253 , pp. 551-555
    • Atkinson, N.S.1    Robertson, G.A.2    Ganetzky, B.3
  • 6
    • 0000686943 scopus 로고
    • Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: Structural and functional implications
    • Bazan, J.F., and R.J. Fletterick. 1988. Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications. Proc. Natl. Acad. Sci. USA. 85:7872-7876.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7872-7876
    • Bazan, J.F.1    Fletterick, R.J.2
  • 7
    • 0015506036 scopus 로고
    • A model for the association of bovine pancreatic trypsin inhibitor with chymotrypsin and trypsin
    • Blow, D.M., C.S. Wright, D. Kukla, A. Rühlmann, W. Steigmann, and R. Huber. 1972. A model for the association of bovine pancreatic trypsin inhibitor with chymotrypsin and trypsin. J. Mol. Biol. 69:137-144.
    • (1972) J. Mol. Biol. , vol.69 , pp. 137-144
    • Blow, D.M.1    Wright, C.S.2    Kukla, D.3    Rühlmann, A.4    Steigmann, W.5    Huber, R.6
  • 8
    • 0018781771 scopus 로고
    • The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. II. The binding of the pancreatic trypsin inhibitor and of isoleucine-valine and of sequentially related peptides to trypsinogen and to p-guanidobenzoate-trypsinogen
    • Bode, W. 1979. The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. II. The binding of the pancreatic trypsin inhibitor and of isoleucine-valine and of sequentially related peptides to trypsinogen and to p-guanidobenzoate-trypsinogen. J. Mol. Biol. 127:357-374.
    • (1979) J. Mol. Biol. , vol.127 , pp. 357-374
    • Bode, W.1
  • 9
    • 0026530977 scopus 로고
    • Natural protein proteinase inhibitors and their interaction with proteinases
    • Bode, W., and R. Huber. 1992. Natural protein proteinase inhibitors and their interaction with proteinases. Eur. J. Biochem. 204: 433-451.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 10
    • 0016741380 scopus 로고
    • The single calcium-binding site of crystalline bovine β-trypsin
    • Bode, W., and P. Schwager. 1975. The single calcium-binding site of crystalline bovine β-trypsin. FEBS Lett. 56:139-143.
    • (1975) FEBS Lett. , vol.56 , pp. 139-143
    • Bode, W.1    Schwager, P.2
  • 11
    • 0017893796 scopus 로고
    • The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen-pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 Å resolution
    • Bode, W., P. Schwager, and R. Huber. 1978. The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen-pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 Å resolution. J. Mol. Biol. 118:99-112.
    • (1978) J. Mol. Biol. , vol.118 , pp. 99-112
    • Bode, W.1    Schwager, P.2    Huber, R.3
  • 13
    • 0026575435 scopus 로고
    • Regulation of arterial tone by activation of calcium-dependent potassium channels
    • Brayden, J.E., and M.T. Nelson. 1992. Regulation of arterial tone by activation of calcium-dependent potassium channels. Science (Wash. DC). 256:532-535.
    • (1992) Science (Wash. DC) , vol.256 , pp. 532-535
    • Brayden, J.E.1    Nelson, M.T.2
  • 14
    • 0027161159 scopus 로고
    • mSlo, a complex mouse gene encoding "maxi" calcium-activated potassium channels
    • Butler, A., S. Tsunoda, D.P. McCobb, A. Wei, and L. Salkoff. 1993. mSlo, a complex mouse gene encoding "maxi" calcium-activated potassium channels. Science (Wash. DC). 261:221-224.
    • (1993) Science (Wash. DC) , vol.261 , pp. 221-224
    • Butler, A.1    Tsunoda, S.2    McCobb, D.P.3    Wei, A.4    Salkoff, L.5
  • 15
    • 0022237839 scopus 로고
    • Dynamic and structural properties of the calcium binding site of bovine serine proteases and their zymogens. A multinuclear nuclear magnetic resonance and stopped-flow study
    • Chiancone, E., T. Drakenberg, O. Teleman, and S. Forsen. 1985. Dynamic and structural properties of the calcium binding site of bovine serine proteases and their zymogens. A multinuclear nuclear magnetic resonance and stopped-flow study. J. Mol. Biol. 185:201-207.
    • (1985) J. Mol. Biol. , vol.185 , pp. 201-207
    • Chiancone, E.1    Drakenberg, T.2    Teleman, O.3    Forsen, S.4
  • 16
    • 0016708122 scopus 로고
    • Principles of protein-protein recognition
    • Chothia, C., and J. Janin. 1975. Principles of protein-protein recognition. Nature (Lond.). 256:705-708.
    • (1975) Nature (Lond.) , vol.256 , pp. 705-708
    • Chothia, C.1    Janin, J.2
  • 17
    • 0020485895 scopus 로고
    • Orthogonal packing of β-pleated sheets in proteins
    • Chothia, C., and J. Janin. 1982. Orthogonal packing of β-pleated sheets in proteins. Biochemistry. 21:3955-3965.
    • (1982) Biochemistry , vol.21 , pp. 3955-3965
    • Chothia, C.1    Janin, J.2
  • 18
    • 0018110116 scopus 로고
    • Prediction of the secondary structures of proteins from their amino acid sequence
    • Chou, P.Y., and G.D. Fasman. 1978. Prediction of the secondary structures of proteins from their amino acid sequence. Adv. Enzymol. 47:45-148.
    • (1978) Adv. Enzymol. , vol.47 , pp. 45-148
    • Chou, P.Y.1    Fasman, G.D.2
  • 19
    • 0019873323 scopus 로고
    • Refined crystal structure of γ-chymotrypsin at 1.9 Å resolution: Comparison with other pancreatic serine proteases
    • Cohen, G.H., E.W. Silverton, and D.R. Davies. 1981. Refined crystal structure of γ-chymotrypsin at 1.9 Å resolution: comparison with other pancreatic serine proteases. J. Mol. Biol. 148:449-479.
    • (1981) J. Mol. Biol. , vol.148 , pp. 449-479
    • Cohen, G.H.1    Silverton, E.W.2    Davies, D.R.3
  • 21
    • 0025266744 scopus 로고
    • Searching through sequence databases
    • Doolittle, R.F. 1990. Searching through sequence databases. Methods Enzymol. 183:99-110.
    • (1990) Methods Enzymol. , vol.183 , pp. 99-110
    • Doolittle, R.F.1
  • 22
    • 0029006062 scopus 로고
    • The multiplicity of domains in proteins
    • Doolittle, R.F. 1995. The multiplicity of domains in proteins. Annu. Rev. Biochem. 64:287-314.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 287-314
    • Doolittle, R.F.1
  • 23
    • 0026773754 scopus 로고
    • Atomic scale structure and functional models of voltage-gated potassium channels
    • Durell, S.R., and H.R. Guy. 1992. Atomic scale structure and functional models of voltage-gated potassium channels. Biophys. J. 62: 238-250.
    • (1992) Biophys. J. , vol.62 , pp. 238-250
    • Durell, S.R.1    Guy, H.R.2
  • 25
    • 0023084055 scopus 로고
    • Progressive sequence alignment as a prerequisite to correct phylogenetic trees
    • Feng, D.F., and R.F. Doolittle. 1987. Progressive sequence alignment as a prerequisite to correct phylogenetic trees. J. Mol. Evol. 25:351-360.
    • (1987) J. Mol. Evol. , vol.25 , pp. 351-360
    • Feng, D.F.1    Doolittle, R.F.2
  • 26
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
    • Gamier, J., D.J. Osguthorpe, and B. Robson. 1978. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120:97-120.
    • (1978) J. Mol. Biol. , vol.120 , pp. 97-120
    • Gamier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 28
    • 0024495898 scopus 로고
    • Cysteine proteases of positive strand RNA viruses and chymotrypsin-like serine proteases. A distinct protein superfamily with a common structural fold
    • Gorbalenya, A.E., A.P. Donchenko, V.M. Blinov, and E.V. Koonin. 1989. Cysteine proteases of positive strand RNA viruses and chymotrypsin-like serine proteases. A distinct protein superfamily with a common structural fold. FEBS Lett. 243:103-114.
    • (1989) FEBS Lett. , vol.243 , pp. 103-114
    • Gorbalenya, A.E.1    Donchenko, A.P.2    Blinov, V.M.3    Koonin, E.V.4
  • 29
    • 0025363116 scopus 로고
    • Superfamily of UvrA-related NTP-binding proteins. Implications for rational classification of recombination/repair systems
    • Gorbalenya, A.E., and E.V. Koonin. 1990. Superfamily of UvrA-related NTP-binding proteins. Implications for rational classification of recombination/repair systems. J. Mol. Biol. 213:583-591.
    • (1990) J. Mol. Biol. , vol.213 , pp. 583-591
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 30
    • 0025287330 scopus 로고
    • Comparative modeling methods: Application to the family of mammalian serine proteases
    • Greer, J. 1990. Comparative modeling methods: application to the family of mammalian serine proteases. Proteins Struct. funct. Genet. 7:317-334.
    • (1990) Proteins Struct. Funct. Genet. , vol.7 , pp. 317-334
    • Greer, J.1
  • 31
    • 0026320025 scopus 로고
    • Comparative modeling of homologous proteins
    • Greer, J. 1991. Comparative modeling of homologous proteins. Methods Enzymol. 202:239-252.
    • (1991) Methods Enzymol. , vol.202 , pp. 239-252
    • Greer, J.1
  • 32
    • 0023502221 scopus 로고
    • Kinetic basis for insensitivity to tetrodotoxin and saxitoxin in sodium channels of canine heart and denervated rat skeletal muscle
    • Guo, X., A. Uehara, A. Ravindran, S.H. Bryant, S. Hall, and E. Moczydlowski. 1987. Kinetic basis for insensitivity to tetrodotoxin and saxitoxin in sodium channels of canine heart and denervated rat skeletal muscle. Biochemistry. 26:7546-7556.
    • (1987) Biochemistry , vol.26 , pp. 7546-7556
    • Guo, X.1    Uehara, A.2    Ravindran, A.3    Bryant, S.H.4    Hall, S.5    Moczydlowski, E.6
  • 33
    • 0025938869 scopus 로고
    • Characterization of the DNF15S2 locus on human chromosome 3: Identification of a gene coding for four kringle domains with homology to hepatocyte growth factor
    • Han, S., L.A. Stuart, and S.J. Friezner Degen. 1991. Characterization of the DNF15S2 locus on human chromosome 3: identification of a gene coding for four kringle domains with homology to hepatocyte growth factor. Biochemistry. 30:9768-9780.
    • (1991) Biochemistry , vol.30 , pp. 9768-9780
    • Han, S.1    Stuart, L.A.2    Friezner Degen, S.J.3
  • 36
    • 0022429411 scopus 로고
    • Amino acid sequence of bovine protein Z: A vitamin K-dependent serine protease homolog
    • Højrup, P., M.S. Jensen, and T.E. Petersen. 1985. Amino acid sequence of bovine protein Z: a vitamin K-dependent serine protease homolog. FEBS Lett. 184:333-338.
    • (1985) FEBS Lett. , vol.184 , pp. 333-338
    • Højrup, P.1    Jensen, M.S.2    Petersen, T.E.3
  • 37
    • 0016291686 scopus 로고
    • Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Crystallographic refinement at 1.9 A resolution
    • Huber, R., D. Kukla, W. Bode, P. Schwager, K. Bartels, J. Deisenhofer, and W. Steigmann. 1974. Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Crystallographic refinement at 1.9 A resolution. J. Mol. Biol. 89:73-101.
    • (1974) J. Mol. Biol. , vol.89 , pp. 73-101
    • Huber, R.1    Kukla, D.2    Bode, W.3    Schwager, P.4    Bartels, K.5    Deisenhofer, J.6    Steigmann, W.7
  • 38
    • 0020306559 scopus 로고
    • Complete amino acid sequence of streptokinase and its homology with serine proteases
    • Jackson, K.W., and J. Tang. 1982. Complete amino acid sequence of streptokinase and its homology with serine proteases. Biochemistry. 21:6620-6625.
    • (1982) Biochemistry. , vol.21 , pp. 6620-6625
    • Jackson, K.W.1    Tang, J.2
  • 39
    • 0017257628 scopus 로고
    • Stability and specificity of protein-protein interactions: The case of the trypsin-trypsin inhibitor complexes
    • Janin, J., and C. Chothia. 1976. Stability and specificity of protein-protein interactions: the case of the trypsin-trypsin inhibitor complexes. J. Mol. Biol. 100:197-211.
    • (1976) J. Mol. Biol. , vol.100 , pp. 197-211
    • Janin, J.1    Chothia, C.2
  • 40
    • 0025123333 scopus 로고
    • The structure of protein-protein recognition sites
    • Janin, J., and C. Chothia. 1990. The structure of protein-protein recognition sites. J. Biol. Chem. 265:16027-16030.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16027-16030
    • Janin, J.1    Chothia, C.2
  • 41
    • 0025259313 scopus 로고
    • Methods for assessing the statistical significance of molecular sequence features by using general scoring schemes
    • Karlin, S., and S.F. Altschul. 1990. Methods for assessing the statistical significance of molecular sequence features by using general scoring schemes. Proc. Natl. Acad. Sci. USA. 87:2264-22687.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2264-22687
    • Karlin, S.1    Altschul, S.F.2
  • 44
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski, M., and I. Kato. 1980. Protein inhibitors of proteinases. Annu. Rev. Biochem. 49:593-626.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 593-626
    • Laskowski, M.1    Kato, I.2
  • 48
    • 0025644364 scopus 로고
    • Mapping the receptor site for charybdoloxin, a port-blocking potassium channel inhibitor
    • MacKinnon, R., L. Heginbotham, and T. Abramson. 1990. Mapping the receptor site for charybdoloxin, a port-blocking potassium channel inhibitor. Neuron. 5:1-10.
    • (1990) Neuron. , vol.5 , pp. 1-10
    • MacKinnon, R.1    Heginbotham, L.2    Abramson, T.3
  • 49
    • 84977303841 scopus 로고
    • The geometry of the reactive site and of the peptide groups in trypsin, trypsinogen and its complexes with inhibitors
    • Marquart, M., J. Walter, J. Deisenhofer, W. Bode, and R Huber. 1983. The geometry of the reactive site and of the peptide groups in trypsin, trypsinogen and its complexes with inhibitors. Acta Crystallogr. 839:480-490.
    • (1983) Acta Crystallogr. , vol.839 , pp. 480-490
    • Marquart, M.1    Walter, J.2    Deisenhofer, J.3    Bode, W.4    Huber, R.5
  • 50
    • 0028609781 scopus 로고
    • + channel β subunits belong to an NAD(P)H-dependent oxidoreductase superfamily
    • + channel β subunits belong to an NAD(P)H-dependent oxidoreductase superfamily. Cell. 79:1133-1135.
    • (1994) Cell , vol.79 , pp. 1133-1135
    • McCormack, T.1    McCormack, K.2
  • 51
    • 0028983387 scopus 로고
    • + channel-blocking peptides
    • + channel-blocking peptides. Neuron. 15:5-10.
    • (1995) Neuron. , vol.15 , pp. 5-10
    • Miller, C.1
  • 53
    • 12644280096 scopus 로고
    • Structural requirements of bovine pancreatic trypsin inhibitor for production of substates in maxi K(Ca) channels
    • Abstr.
    • Moss, G.W.J., D. Laheru, S. Wooden, D.P. Goldenberg, and E. Moczydlowski. 1991. Structural requirements of bovine pancreatic trypsin inhibitor for production of substates in maxi K(Ca) channels. Biophys. J. 59:79a. (Abstr.).
    • (1991) Biophys. J. , vol.59
    • Moss, G.W.J.1    Laheru, D.2    Wooden, S.3    Goldenberg, D.P.4    Moczydlowski, E.5
  • 54
    • 0030299989 scopus 로고    scopus 로고
    • An evolutionarily conserved binding site for serine proteinase inhibitors in large conductance calcium-activated potassium channels
    • In press
    • Moss, G.W.J., J. Marshall, M. Morabito, J.R. Howe, and E.G. Moczydlowski. 1996. An evolutionarily conserved binding site for serine proteinase inhibitors in large conductance calcium-activated potassium channels. Biochemistry. In press.
    • (1996) Biochemistry
    • Moss, G.W.J.1    Marshall, J.2    Morabito, M.3    Howe, J.R.4    Moczydlowski, E.G.5
  • 55
    • 4243163391 scopus 로고
    • Cloning of a maxi Ca-activated K-channel from bovine aortic smooth muscle. Sensitivity to a Kunitz inhibitor
    • Abstr.
    • Moss, G.W.J., J. Marshall, M. Morabito, E. Moczydlowski, and J. Howe. 1995. Cloning of a maxi Ca-activated K-channel from bovine aortic smooth muscle. Sensitivity to a Kunitz inhibitor. Biophys J. 68:A29. (Abstr.).
    • (1995) Biophys J. , vol.68
    • Moss, G.W.J.1    Marshall, J.2    Morabito, M.3    Moczydlowski, E.4    Howe, J.5
  • 56
    • 0030040324 scopus 로고    scopus 로고
    • + channel: Evidence for a fluctuating barrier mechanism
    • + channel: evidence for a fluctuating barrier mechanism. J. Gen. Physiol. 107: 47-68.
    • (1996) J. Gen. Physiol. , vol.107 , pp. 47-68
    • Moss, G.W.J.1    Moczydlowski, E.2
  • 57
    • 0000668333 scopus 로고
    • Reconstitution of excitable cell membrane structure in vitro
    • Mueller, P., D. Rudin, H.T. Tien, and W.C. Wescott. 1962. Reconstitution of excitable cell membrane structure in vitro. Circulation. 26:1167-1171.
    • (1962) Circulation , vol.26 , pp. 1167-1171
    • Mueller, P.1    Rudin, D.2    Tien, H.T.3    Wescott, W.C.4
  • 58
    • 0015216974 scopus 로고
    • The binding of hemoglobin to haptoglobin and its relation to subunit dissociation of hemoglobin
    • Nagel, R.I.., and Q.H. Gibson. 1971. The binding of hemoglobin to haptoglobin and its relation to subunit dissociation of hemoglobin. J. Biol. Chem. 246:69-73.
    • (1971) J. Biol. Chem. , vol.246 , pp. 69-73
    • Nagel, R.I.1    Gibson, Q.H.2
  • 60
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequences of two proteins
    • Needleman, S.B., and C.D. Wunsch. 1970. A general method applicable to the search for similarities in the amino acid sequences of two proteins. J. Mol. Biol. 48:443-453.
    • (1970) J. Mol. Biol. , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.D.2
  • 62
    • 0022367735 scopus 로고
    • Proteolytic enzymes, past and present
    • Neurath, H. 1985. Proteolytic enzymes, past and present. Fed. Proc. 44:2907-2913.
    • (1985) Fed. Proc. , vol.44 , pp. 2907-2913
    • Neurath, H.1
  • 63
    • 0026326273 scopus 로고
    • Predicting protein secondary structure based on amino acid sequence
    • Nishikawa, K., and T. Noguchi. 1991. Predicting protein secondary structure based on amino acid sequence. Methods Enzymol. 202: 31-44.
    • (1991) Methods Enzymol. , vol.202 , pp. 31-44
    • Nishikawa, K.1    Noguchi, T.2
  • 66
    • 0027196503 scopus 로고
    • Binding of bovine pancreatic trypsin inhibitor to heparin binding protein/ CAP37/azurocidin: Interaction between a Kunitz-type inhibitor and a proteolytically inactive serine proteinase homologue
    • Petersen, L.C., J.J. Birktoft, and H. Flodgaard. 1993. Binding of bovine pancreatic trypsin inhibitor to heparin binding protein/ CAP37/azurocidin: interaction between a Kunitz-type inhibitor and a proteolytically inactive serine proteinase homologue. Eur. J. Biochem. 214:271-279.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 271-279
    • Petersen, L.C.1    Birktoft, J.J.2    Flodgaard, H.3
  • 68
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson, J.S. 1981. The anatomy and taxonomy of protein structure. Adv. Protein Chem. 34:167-339.
    • (1981) Adv. Protein Chem. , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 69
    • 0015901579 scopus 로고
    • Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Crystal structure determination and stereochemistry of the contact region
    • Rühlmann, A., D. Kukla, P. Schwager, K. Bartels, and R. Huber. 1973. Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Crystal structure determination and stereochemistry of the contact region. J. Mol. Biol. 77:417-436.
    • (1973) J. Mol. Biol. , vol.77 , pp. 417-436
    • Rühlmann, A.1    Kukla, D.2    Schwager, P.3    Bartels, K.4    Huber, R.5
  • 70
    • 0028982831 scopus 로고
    • 2+-binding site in the serine protease domain of human factor VIIa and its role in tissue factor binding and development of catalytic activity
    • 2+-binding site in the serine protease domain of human factor VIIa and its role in tissue factor binding and development of catalytic activity. J. Biol Chem. 270:15523-15530.
    • (1995) J. Biol Chem. , vol.270 , pp. 15523-15530
    • Sabharwal, A.K.1    Birktoft, J.J.2    Gorka, J.3    Wildgoose, P.4    Petersen, L.C.5    Bajaj, S.P.6
  • 73
    • 0028178520 scopus 로고
    • Tetraethylammonium block of slowpoke calcium-activated potassium channels expressed in Xenopus oocytes: Evidence for tetrameric channel formation
    • Shen, K.-Z., A. Lagrutta, N.W. Davies, N.B. Standen, J.P. Adelman, and R.A. North. 1994. Tetraethylammonium block of slowpoke calcium-activated potassium channels expressed in Xenopus oocytes: evidence for tetrameric channel formation. Pflüg. Arch. 426:440-445.
    • (1994) Pflüg. Arch. , vol.426 , pp. 440-445
    • Shen, K.-Z.1    Lagrutta, A.2    Davies, N.W.3    Standen, N.B.4    Adelman, J.P.5    North, R.A.6
  • 75
    • 0028912561 scopus 로고
    • The clot thickens: Clues provided by thrombin structure
    • Stubbs, M.T., and W. Bode. 1995. The clot thickens: clues provided by thrombin structure. Trends Biochem. Sci. 20:23-28.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 23-28
    • Stubbs, M.T.1    Bode, W.2
  • 76
    • 0027474021 scopus 로고
    • Refined structure of sindbis virus core protein and comparison with other chymotrypsin-like serine proteinase structures
    • Tong, L., G. Wengler, and M.G. Rossman. 1993. Refined structure of sindbis virus core protein and comparison with other chymotrypsin-like serine proteinase structures. J. Mol. Biol. 230:228-247.
    • (1993) J. Mol. Biol. , vol.230 , pp. 228-247
    • Tong, L.1    Wengler, G.2    Rossman, M.G.3
  • 78
    • 0029114464 scopus 로고
    • Molecular mechanism for ligand discrimination of cyclic nucleotide-gated channels
    • Yarnum, M.D., K.D. Black, and W.N. Zagotta. 1995. Molecular mechanism for ligand discrimination of cyclic nucleotide-gated channels. Neuron. 15:019-625.
    • (1995) Neuron. , vol.15 , pp. 19-625
    • Yarnum, M.D.1    Black, K.D.2    Zagotta, W.N.3
  • 79
    • 0015387337 scopus 로고
    • Trypsin-pancreatic trypsin inhibitor association. Dynamics of the interaction and role of disulfide bridges
    • Vincent, J.-P., and M. Lazdunski. 1972. Trypsin-pancreatic trypsin inhibitor association. Dynamics of the interaction and role of disulfide bridges. Biochemistry. 11:2967-2977.
    • (1972) Biochemistry , vol.11 , pp. 2967-2977
    • Vincent, J.-P.1    Lazdunski, M.2
  • 80
    • 0015813659 scopus 로고
    • The interaction between α-chymotrypsin and pancreatic trypsin inhibitor (Kunitz inhibitor). Kinetic and thermodynamic properties
    • Vincent, J.-P., and M. Lazdunski. 1973. The interaction between α-chymotrypsin and pancreatic trypsin inhibitor (Kunitz inhibitor). Kinetic and thermodynamic properties. Eur. J. Biochem. 38:365-372.
    • (1973) Eur. J. Biochem. , vol.38 , pp. 365-372
    • Vincent, J.-P.1    Lazdunski, M.2
  • 81
    • 0017277533 scopus 로고
    • Pre-existence of the active site in zymogens, the interaction of trypsinogen with the basic pancreatic trypsin inhibitor (Kunitz)
    • Vincent, J.P., and M. Lazdunski. 1976. Pre-existence of the active site in zymogens, the interaction of trypsinogen with the basic pancreatic trypsin inhibitor (Kunitz). FEBS Lett. 63:240-244.
    • (1976) FEBS Lett. , vol.63 , pp. 240-244
    • Vincent, J.P.1    Lazdunski, M.2
  • 82
    • 0021930156 scopus 로고
    • Bovine chymotrypsinogen A: X-ray crystal structure analysis and refinement of a new crystal form at 1.8 Å resolution
    • Wang, D., W. Bode, and R Huber. 1985. Bovine chymotrypsinogen A: x-ray crystal structure analysis and refinement of a new crystal form at 1.8 Å resolution. J. Mol. Biol. 185:595-624.
    • (1985) J. Mol. Biol. , vol.185 , pp. 595-624
    • Wang, D.1    Bode, W.2    Huber, R.3
  • 83
    • 0028965140 scopus 로고
    • Unraveling the modular design of glutaniate-gated ion channels
    • Wo, Z.G., and R.E. Oswald. 1995. Unraveling the modular design of glutaniate-gated ion channels. Trends Neurosa. 18:161-168.
    • (1995) Trends Neurosa. , vol.18 , pp. 161-168
    • Wo, Z.G.1    Oswald, R.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.