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Volumn 269, Issue 22, 2002, Pages 5649-5658

The role of the second binding loop of the cysteine protease inhibitor, cystatin A (stefin A), in stabilizing complexes with target proteases is exerted predominantly by Leu73

Author keywords

Cathepsins; Cystatin; Cysteine proteases; Papain; Second binding loop

Indexed keywords

ASPARAGINE; CATHEPSIN B; CATHEPSIN L; CYSTATIN B; CYSTEINE PROTEINASE INHIBITOR; GLUTAMINE; LEUCINE; PAPAIN; PROLINE; PROTEINASE; STEFIN A;

EID: 0036436926     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03273.x     Document Type: Article
Times cited : (11)

References (55)
  • 1
    • 0002486962 scopus 로고
    • Cysteine proteinase inhibitors of the cystatin superfamily
    • Barrett, A.J. & Salvesen, G., eds. Elsevier, Amsterdam
    • Barrett, A.J., Rawlings, N.D., Davies, M.E., Machleidt, W., Salvesen, G. & Turk, V. (1986) Cysteine proteinase inhibitors of the cystatin superfamily. In Proteinase Inhibitors (Barrett, A.J. & Salvesen, G., eds), pp. 515-569. Elsevier, Amsterdam.
    • (1986) Proteinase Inhibitors , pp. 515-569
    • Barrett, A.J.1    Rawlings, N.D.2    Davies, M.E.3    Machleidt, W.4    Salvesen, G.5    Turk, V.6
  • 2
    • 0025817602 scopus 로고
    • The cystatins: Protein inhibitors of cysteine proteinases
    • Turk, V. & Bode, W. (1991) The cystatins: Protein inhibitors of cysteine proteinases. FEBS Lett. 285, 213-219.
    • (1991) FEBS Lett. , vol.285 , pp. 213-219
    • Turk, V.1    Bode, W.2
  • 4
    • 0030918546 scopus 로고    scopus 로고
    • Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors
    • Turk, B., Turk, V. & Turk, D. (1997) Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors. Biol. Chem. 378, 141-150.
    • (1997) Biol. Chem. , vol.378 , pp. 141-150
    • Turk, B.1    Turk, V.2    Turk, D.3
  • 7
    • 0032007523 scopus 로고    scopus 로고
    • Cystatin D, a natural salivary cysteine protease inhibitor, inhibits coronavirus replication at its physiologic concentration
    • Collins, A.R. & Grubb, A. (1998) Cystatin D, a natural salivary cysteine protease inhibitor, inhibits coronavirus replication at its physiologic concentration. Oral Microbiol. Immunol. 13, 59-61.
    • (1998) Oral Microbiol. Immunol. , vol.13 , pp. 59-61
    • Collins, A.R.1    Grubb, A.2
  • 8
    • 0031685364 scopus 로고    scopus 로고
    • Cysteine proteinases and their endogenous inhibitors: Target proteins for prognosis, diagnosis and therapy in cancer
    • Kos, J. & Lah, T.T. (1998) Cysteine proteinases and their endogenous inhibitors: Target proteins for prognosis, diagnosis and therapy in cancer. Oncol. Rep. 5, 1349-1361.
    • (1998) Oncol. Rep. , vol.5 , pp. 1349-1361
    • Kos, J.1    Lah, T.T.2
  • 9
    • 0035869563 scopus 로고    scopus 로고
    • Successful therapy of lethal murine visceral leishmaniasis with cystatin involves up-regulation of nitric oxide and a favorable T cell response
    • Das, L., Datta, N., Bandyopadhyay, S. & Das, P.K. (2001) Successful therapy of lethal murine visceral leishmaniasis with cystatin involves up-regulation of nitric oxide and a favorable T cell response. J. Immunol. 166, 4020-4028.
    • (2001) J. Immunol. , vol.166 , pp. 4020-4028
    • Das, L.1    Datta, N.2    Bandyopadhyay, S.3    Das, P.K.4
  • 10
    • 0034942372 scopus 로고    scopus 로고
    • Interactions of human lacrimal and salivary cystatins with adenovirus endo-peptidase
    • Ruzindana-Umunyana, A. & Weber, J.M. (2001) Interactions of human lacrimal and salivary cystatins with adenovirus endo-peptidase. Antiviral Res. 51, 203-214.
    • (2001) Antiviral Res. , vol.51 , pp. 203-214
    • Ruzindana-Umunyana, A.1    Weber, J.M.2
  • 11
    • 0035801514 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: Facts and opportunities
    • Turk, V., Turk, B. & Turk, D. (2001) Lysosomal cysteine pro-teases: facts and opportunities. EMBO J. 20, 4629-4633.
    • (2001) EMBO J. , vol.20 , pp. 4629-4633
    • Turk, V.1    Turk, B.2    Turk, D.3
  • 12
    • 0024066065 scopus 로고
    • The 2.0 Å X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases
    • Bode, W., Engh, R., Musil, D., Thiele, U., Huber, R., Karshikov, A., Brzin, J., Kos, J. & Turk, V. (1988) The 2.0 Å X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. EMBO J. 7, 2593-2599.
    • (1988) EMBO J. , vol.7 , pp. 2593-2599
    • Bode, W.1    Engh, R.2    Musil, D.3    Thiele, U.4    Huber, R.5    Karshikov, A.6    Brzin, J.7    Kos, J.8    Turk, V.9
  • 13
    • 0025301658 scopus 로고
    • The refined 2.4 Å 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. (1990) The refined 2.4 Å 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. 9, 1939-1947.
    • (1990) EMBO J. , vol.9 , 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
  • 14
    • 0024556990 scopus 로고
    • Kinetics of binding of chicken cystatin to papain
    • Björk, I., Alriksson, E. & Ylinenjärvi, K. (1989) Kinetics of binding of chicken cystatin to papain. Biochemistry 28, 1568-1573.
    • (1989) Biochemistry , vol.28 , pp. 1568-1573
    • Björk, I.1    Alriksson, E.2    Ylinenjärvi, K.3
  • 15
    • 0025057074 scopus 로고
    • Interaction between chicken cystatin and the cysteine proteinases actinidin, chymopapain A, and ficin
    • Björk, I. & Ylinenjärvi, K. (1990) Interaction between chicken cystatin and the cysteine proteinases actinidin, chymopapain A, and ficin. Biochemistry 29, 1770-1776.
    • (1990) Biochemistry , vol.29 , pp. 1770-1776
    • Björk, I.1    Ylinenjärvi, K.2
  • 16
    • 0026570448 scopus 로고
    • Interaction of recombinant human cystatin C with the cysteine proteinases papain and actinidin
    • Lindahl, P., Abrahamson, M. & Björk, I. (1992) Interaction of recombinant human cystatin C with the cysteine proteinases papain and actinidin. Biochem. J. 281, 49-55.
    • (1992) Biochem. J. , vol.281 , pp. 49-55
    • Lindahl, P.1    Abrahamson, M.2    Björk, I.3
  • 17
    • 0028258640 scopus 로고
    • Kinetics of inhibition of bovine cathepsin S by bovine stefin B
    • Turk, B., Colic, A., Stoka, V. & Turk, V. (1994) Kinetics of inhibition of bovine cathepsin S by bovine stefin B. FEBS Lett. 339, 155-159.
    • (1994) FEBS Lett. , vol.339 , pp. 155-159
    • Turk, B.1    Colic, A.2    Stoka, V.3    Turk, V.4
  • 18
    • 0029101752 scopus 로고
    • Characterization by spectroscopic, kinetic and equilibrium methods of the interaction between recombinant human cystatin A (stefin A) and cysteine proteinases
    • Pol, E., Olsson, S.L., Estrada, S., Prasthofer, T.W. & Björk, I. (1995) Characterization by spectroscopic, kinetic and equilibrium methods of the interaction between recombinant human cystatin A (stefin A) and cysteine proteinases. Biochem. J. 311, 275-282.
    • (1995) Biochem. J. , vol.311 , pp. 275-282
    • Pol, E.1    Olsson, S.L.2    Estrada, S.3    Prasthofer, T.W.4    Björk, I.5
  • 19
    • 0027731168 scopus 로고
    • The structures of native phosphorylated chicken cystatin and of a recombinant unphosphorylated variant in solution
    • Dieckmann, T., Mitschang, L., Hofmann, M., Kos, J., Turk, V., Auerswald, E.A., Jaenicke, R. & Oschkinat, H. (1993) The structures of native phosphorylated chicken cystatin and of a recombinant unphosphorylated variant in solution. J. Mol. Biol. 234, 1048-1059.
    • (1993) J. Mol. Biol. , vol.234 , pp. 1048-1059
    • Dieckmann, T.1    Mitschang, L.2    Hofmann, M.3    Kos, J.4    Turk, V.5    Auerswald, E.A.6    Jaenicke, R.7    Oschkinat, H.8
  • 22
    • 0028673327 scopus 로고
    • Families of cysteine peptidases
    • Rawlings, N.D. & Barrett, A.J. (1994) Families of cysteine peptidases. Methods Enzymol. 244, 461-486.
    • (1994) Methods Enzymol. , vol.244 , pp. 461-486
    • Rawlings, N.D.1    Barrett, A.J.2
  • 23
    • 0345310073 scopus 로고    scopus 로고
    • Revised definition of substrate binding sites of papain-like cysteine proteases
    • Turk, D., Guncar, G., Podobnik, M. & Turk, B. (1998) Revised definition of substrate binding sites of papain-like cysteine proteases. Biol. Chem. 379, 137-147.
    • (1998) Biol. Chem. , vol.379 , pp. 137-147
    • Turk, D.1    Guncar, G.2    Podobnik, M.3    Turk, B.4
  • 24
    • 0034615570 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: More than scavengers
    • Turk, B., Turk, D. & Turk, V. (2000) Lysosomal cysteine proteases: More than scavengers. Biochim. Biophys. Acta 1477, 98-111.
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 98-111
    • Turk, B.1    Turk, D.2    Turk, V.3
  • 26
    • 0032559423 scopus 로고    scopus 로고
    • Two-step mechanism of inhibition of cathepsin B by cystatin C due to displacement of the proteinase occluding loop
    • Nycander, M., Estrada, S., Mort, J.S., Abrahamson, M. & Björk, I. (1998) Two-step mechanism of inhibition of cathepsin B by cystatin C due to displacement of the proteinase occluding loop. FEBS Lett. 422, 61-64.
    • (1998) FEBS Lett. , vol.422 , pp. 61-64
    • Nycander, M.1    Estrada, S.2    Mort, J.S.3    Abrahamson, M.4    Björk, I.5
  • 27
    • 0034731319 scopus 로고    scopus 로고
    • Cystatin inhibition of cathepsin B requires dislocation of the proteinase occluding loop. Demonstration by release of loop anchoring through mutation of His110
    • Pavlova, A., Krupa, J.C., Mort, J.S., Abrahamson, M. & Björk, I. (2000) Cystatin inhibition of cathepsin B requires dislocation of the proteinase occluding loop. Demonstration by release of loop anchoring through mutation of His110. FEBS Lett. 487, 156-160.
    • (2000) FEBS Lett. , vol.487 , pp. 156-160
    • Pavlova, A.1    Krupa, J.C.2    Mort, J.S.3    Abrahamson, M.4    Björk, I.5
  • 28
    • 0028220189 scopus 로고
    • Differential changes in the association and dissociation rate constants for binding of cystatins to target proteinases occurring on N-terminal truncation of the inhibitors indicate that the interaction mechanism varies with different enzymes
    • Björk, I., Pol, E., Raub-Segall, E., Abrahamson, M., Rowan, A.D. & Mort, J.S. (1994) Differential changes in the association and dissociation rate constants for binding of cystatins to target proteinases occurring on N-terminal truncation of the inhibitors indicate that the interaction mechanism varies with different enzymes. Biochem. J. 299, 219-225.
    • (1994) Biochem. J. , vol.299 , pp. 219-225
    • Björk, I.1    Pol, E.2    Raub-Segall, E.3    Abrahamson, M.4    Rowan, A.D.5    Mort, J.S.6
  • 29
    • 0024570048 scopus 로고
    • Mechanism of inhibition of papain by chicken egg white cystatin. Inhibition constants of N-terminally truncated forms and cyanogen bromide fragments of the inhibitor
    • Machleidt, W., Thiele, U., Laber, B., Assfalg-Machleidt, I., Esterl, A., Wiegand, G., Kos, J., Turk, V. & Bode, W. (1989) Mechanism of inhibition of papain by chicken egg white cystatin. Inhibition constants of N-terminally truncated forms and cyanogen bromide fragments of the inhibitor. FEBS Lett. 243, 234-238.
    • (1989) FEBS Lett. , vol.243 , pp. 234-238
    • Machleidt, W.1    Thiele, U.2    Laber, B.3    Assfalg-Machleidt, I.4    Esterl, A.5    Wiegand, G.6    Kos, J.7    Turk, V.8    Bode, W.9
  • 30
    • 0025918732 scopus 로고
    • Molecular mechanism of inhibition of cysteine proteinases by their protein inhibitors: Kinetic studies with natural and recombinant variants of cystatins and stefins
    • Machleidt, W., Thiele, U., Assfalg-Machleidt, I., Forger, D. & Auerswald, E.A. (1991) Molecular mechanism of inhibition of cysteine proteinases by their protein inhibitors: Kinetic studies with natural and recombinant variants of cystatins and stefins. Biomed. Biochim. Acta 50, 613-620.
    • (1991) Biomed. Biochim. Acta , vol.50 , pp. 613-620
    • Machleidt, W.1    Thiele, U.2    Assfalg-Machleidt, I.3    Forger, D.4    Auerswald, E.A.5
  • 31
    • 0025964356 scopus 로고
    • Human cystatin C. Role of the N-terminal segment in the inhibition of human cysteine proteinases and in its inactivation by leucocyte elastase
    • Abrahamson, M., Mason, R.W., Hansson, H., Buttle, D.J., Grubb, A. & Ohlsson, K. (1991) Human cystatin C. Role of the N-terminal segment in the inhibition of human cysteine proteinases and in its inactivation by leucocyte elastase. Biochem. J. 273, 621-626.
    • (1991) Biochem. J. , vol.273 , pp. 621-626
    • Abrahamson, M.1    Mason, R.W.2    Hansson, H.3    Buttle, D.J.4    Grubb, A.5    Ohlsson, K.6
  • 32
    • 0026744734 scopus 로고
    • Characterization by rapid-kinetic and equilibrium methods of the interaction between N-terminally truncated forms of chicken cystatin and the cysteine proteinases papain and actinidin
    • Lindahl, P., Nycander, M., Ylinenjärvi, K., Pol, E. & Björk, I. (1992) Characterization by rapid-kinetic and equilibrium methods of the interaction between N-terminally truncated forms of chicken cystatin and the cysteine proteinases papain and actinidin. Biochem. J. 286, 165-171.
    • (1992) Biochem. J. , vol.286 , pp. 165-171
    • Lindahl, P.1    Nycander, M.2    Ylinenjärvi, K.3    Pol, E.4    Björk, I.5
  • 33
    • 0028968170 scopus 로고
    • Structural basis for the biological specificity of cystatin C. Identification of leucine 9 in the N-terminal binding region as a selectivity-conferring residue in the inhibition of mammalian cysteine peptidases
    • Hall, A., Håkansson, K., Mason, R.W., Grubb, A. & Abrahamson, M. (1995) Structural basis for the biological specificity of cystatin C. Identification of leucine 9 in the N-terminal binding region as a selectivity-conferring residue in the inhibition of mammalian cysteine peptidases. J. Biol. Chem. 270, 5115-5121.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5115-5121
    • Hall, A.1    Håkansson, K.2    Mason, R.W.3    Grubb, A.4    Abrahamson, M.5
  • 34
    • 0028903615 scopus 로고
    • Hairpin loop mutations of chicken cystatin have different effects on the inhibition of cathepsin B, cathepsin L and papain
    • Auerswald, E.A., Nägler, D.K., Assfalg-Machleidt, I., Stubbs, M.T., Machleidt, W. & Fritz, H. (1995) Hairpin loop mutations of chicken cystatin have different effects on the inhibition of cathepsin B, cathepsin L and papain. FEBS Lett. 361, 179-184.
    • (1995) FEBS Lett. , vol.361 , pp. 179-184
    • Auerswald, E.A.1    Nägler, D.K.2    Assfalg-Machleidt, I.3    Stubbs, M.T.4    Machleidt, W.5    Fritz, H.6
  • 35
    • 0033151771 scopus 로고    scopus 로고
    • The contribution of N-terminal region residues of cystatin A (stefin A) to the affinity and kinetics of inhibition of papain, cathepsin B, and cathepsin L
    • Estrada, S., Pavlova, A. & Björk, I. (1999) The contribution of N-terminal region residues of cystatin A (stefin A) to the affinity and kinetics of inhibition of papain, cathepsin B, and cathepsin L. Biochemistry 38, 7339-7345.
    • (1999) Biochemistry , vol.38 , pp. 7339-7345
    • Estrada, S.1    Pavlova, A.2    Björk, I.3
  • 36
    • 0034847170 scopus 로고    scopus 로고
    • Role of the single cysteine residue, Cys 3, of human and bovine cystatin B (stefin B) in the inhibition of cysteine proteinases
    • Pol, E. & Björk, I. (2001) Role of the single cysteine residue, Cys 3, of human and bovine cystatin B (stefin B) in the inhibition of cysteine proteinases. Protein Sci. 10, 1729-1738.
    • (2001) Protein Sci. , vol.10 , pp. 1729-1738
    • Pol, E.1    Björk, I.2
  • 37
    • 0039183718 scopus 로고    scopus 로고
    • Importance of the second binding loop and the C-terminal end of cystatin B (stefin B) for inhibition of cysteine proteinases
    • Pol, E. & Björk, I. (1999) Importance of the second binding loop and the C-terminal end of cystatin B (stefin B) for inhibition of cysteine proteinases. Biochemistry 38, 10519-10526.
    • (1999) Biochemistry , vol.38 , pp. 10519-10526
    • Pol, E.1    Björk, I.2
  • 38
    • 0032546591 scopus 로고    scopus 로고
    • The role of Gly-4 of human cystatin A (stefin A) in the binding of target proteinases. Characterization by kinetic and equilibrium methods of the interactions of cystatin A Gly-4 mutants with papain, cathepsin B, and cathepsin L
    • Estrada, S., Nycander, M., Hill, N.J., Craven, C.J., Waltho, J.P. & Björk, I. (1998) The role of Gly-4 of human cystatin A (stefin A) in the binding of target proteinases. Characterization by kinetic and equilibrium methods of the interactions of cystatin A Gly-4 mutants with papain, cathepsin B, and cathepsin L. Biochemistry 37, 7551-7560.
    • (1998) Biochemistry , vol.37 , pp. 7551-7560
    • Estrada, S.1    Nycander, M.2    Hill, N.J.3    Craven, C.J.4    Waltho, J.P.5    Björk, I.6
  • 39
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions
    • Higuchi, R., Krummel, B. & Saiki, R.K. (1988) A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions. Nucleic Acids Res. 16, 7351-7367.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 40
    • 0015385368 scopus 로고
    • Nonchromosomal antibiotic resistance in bacteria: Genetic transformation of Escherichia coli by R.-factor DNA
    • Cohen, S.N., Chang, A.C.Y. & Hsu, L. (1972) Nonchromosomal antibiotic resistance in bacteria: Genetic transformation of Escherichia coli by R.-factor DNA. Proc. Natl. Acad. Sci. USA 69, 2110-2114.
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 2110-2114
    • Cohen, S.N.1    Chang, A.C.Y.2    Hsu, L.3
  • 41
    • 0023801371 scopus 로고
    • Interaction of the cysteine proteinase inhibitor chicken cystatin with papain
    • Lindahl, P., Alriksson, E., Jörnvall, H. & Björk, I. (1988) Interaction of the cysteine proteinase inhibitor chicken cystatin with papain. Biochemistry 27, 5074-5082.
    • (1988) Biochemistry , vol.27 , pp. 5074-5082
    • Lindahl, P.1    Alriksson, E.2    Jörnvall, H.3    Björk, I.4
  • 43
  • 44
    • 0019765848 scopus 로고
    • Cathepsin B, cathepsin H, and cathepsin L
    • Barrett, A.J. & Kirschke, H. (1981) Cathepsin B, cathepsin H, and cathepsin L. Methods Enzymol. 80, 535-561.
    • (1981) Methods Enzymol. , vol.80 , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 45
    • 0022994613 scopus 로고
    • Species variants of cathepsin L and their immunological identification
    • Mason, R.W. (1986) Species variants of cathepsin L and their immunological identification. Biochem. J. 240, 285-288.
    • (1986) Biochem. J. , vol.240 , pp. 285-288
    • Mason, R.W.1
  • 46
    • 0025884209 scopus 로고
    • High-performance liquid chromatographic method for the simultaneous purification of cathepsins B, H and L from human liver
    • Dalet-Fumeron, V., Guinec, N. & Pagano, M. (1991) High-performance liquid chromatographic method for the simultaneous purification of cathepsins B, H and L from human liver. J. Chromatogr. 568, 55-68.
    • (1991) J. Chromatogr. , vol.568 , pp. 55-68
    • Dalet-Fumeron, V.1    Guinec, N.2    Pagano, M.3
  • 48
    • 0031473847 scopus 로고    scopus 로고
    • Swiss-Model and Swiss-Pdb Viewer: An environment for comparative protein modeling
    • Guex, N. & Peitsch, M.C. (1997) Swiss-Model and Swiss-Pdb Viewer: An environment for comparative protein modeling. Electrophoresis 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 49
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H. & von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 51
    • 77957062932 scopus 로고
    • Immunologic specificity and molecular structure
    • Karush, F. (1962) Immunologic specificity and molecular structure. Adv. Immunol. 2, 1-40.
    • (1962) Adv. Immunol. , vol.2 , pp. 1-40
    • Karush, F.1
  • 52
    • 0029776802 scopus 로고    scopus 로고
    • The importance of the second hairpin loop of cystatin C for proteinase binding. Characterization of the interaction of Trp-106 variants of the inhibitor with cysteine proteinases
    • Björk, I., Brieditis, I., Raub-Segall, E., Pol, E., Håkansson, K. & Abrahamson, M. (1996) The importance of the second hairpin loop of cystatin C for proteinase binding. Characterization of the interaction of Trp-106 variants of the inhibitor with cysteine proteinases. Biochemistry 35, 10720-10726.
    • (1996) Biochemistry , vol.35 , pp. 10720-10726
    • Björk, I.1    Brieditis, I.2    Raub-Segall, E.3    Pol, E.4    Håkansson, K.5    Abrahamson, M.6


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