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Volumn 246, Issue 2, 1995, Pages 273-283

Alignment/phylogeny of the papain superfamily of cysteine proteases

Author keywords

Cysteine protease; Evolution; Papain superfamily; Phylogeny; Sequence alignment

Indexed keywords


EID: 0028923541     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1994.0083     Document Type: Article
Times cited : (358)

References (63)
  • 2
    • 0019156319 scopus 로고
    • Structure of actinidin, after refinement at 1.7 A Resolution
    • Baker, E. N. (1980). Structure of actinidin, after refinement at 1.7 A Resolution. J. Mol. Biol. 141, 441-484.
    • (1980) J. Mol. Biol. , vol.141 , pp. 441-484
    • Baker, E.N.1
  • 4
    • 0026580016 scopus 로고
    • Isolation and sequence of the granulin precursor cDNA from human bone marrow reveals tandem cysteine-rich granulin domains
    • Bhandari, V., Palfree, R. G. E. & Bateman, A. (1992). Isolation and sequence of the granulin precursor cDNA from human bone marrow reveals tandem cysteine-rich granulin domains. Proc. Nat. Acad. Sci, U.S.A. 89, 1715-1719.
    • (1992) Proc. Nat. Acad. Sci, U.S.A. , vol.89 , pp. 1715-1719
    • Bhandari, V.1    Palfree, R.G.E.2    Bateman, A.3
  • 5
    • 77956868548 scopus 로고
    • Cysteine proteinases
    • Neuberger, A. & Brocklehurst, K., Elsevier Biomedical Press, Amsterdam
    • Brocklehurst, K., Willenbrock, F. & Salih, E. (1987). Cysteine proteinases. In Hydrolytic Enzymes (Neuberger, A. & Brocklehurst, K., eds), pp. 39-158, Elsevier Biomedical Press, Amsterdam.
    • (1987) Hydrolytic Enzymes , pp. 39-158
    • Brocklehurst, K.1    Willenbrock, F.2    Salih, E.3
  • 6
    • 0026559860 scopus 로고
    • Increased expression of cathepsins L and B and decreased activity of their inhibitors in metastatic ras-transformed NIH 3T3 cells
    • Chambers, A. F., Colella, R., Denhardt, D. T. & Wilson, S. M. (1992). Increased expression of cathepsins L and B and decreased activity of their inhibitors in metastatic ras-transformed NIH 3T3 cells. Mol. Carcinogen. 5, 238-245.
    • (1992) Mol. Carcinogen. , vol.5 , pp. 238-245
    • Chambers, A.F.1    Colella, R.2    Denhardt, D.T.3    Wilson, S.M.4
  • 7
    • 0027176566 scopus 로고
    • Testins are structurally related to the mouse cysteine proteinase precursor but devoid of any protease/anti-protease activity
    • Cheng, C. Y., Morris, I. & Bardin, C. W. (1993). Testins are structurally related to the mouse cysteine proteinase precursor but devoid of any protease/anti-protease activity. Biochem. Biophys. Res. Commun. 191, 224-231.
    • (1993) Biochem. Biophys. Res. Commun. , vol.191 , pp. 224-231
    • Cheng, C.Y.1    Morris, I.2    Bardin, C.W.3
  • 8
    • 0027048269 scopus 로고
    • MALIGNED: A multiple sequence alignment editor
    • Clark, S. P. (1992). MALIGNED: a multiple sequence alignment editor. Comput. Appl. Biosci. 8, 535-538.
    • (1992) Comput. Appl. Biosci. , vol.8 , pp. 535-538
    • Clark, S.P.1
  • 9
    • 0024382970 scopus 로고
    • Functional evolutionary divergence of proteolytic enzymes and their inhibitors
    • Creighton, T. E. & Darby N. J. (1989). Functional evolutionary divergence of proteolytic enzymes and their inhibitors. Trends Biochem. Sci. 14, 319-324.
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 319-324
    • Creighton, T.E.1    Darby, N.J.2
  • 10
    • 0025831476 scopus 로고
    • Calcium-activated neutral protease (Calpain) system: Structure, function and regulation
    • Croall, D. E. & Demartino, G. N. (1991). Calcium-activated neutral protease (calpain) system: structure, function and regulation. Physiol. Rev. 71, 813-847.
    • (1991) Physiol. Rev. , vol.71 , pp. 813-847
    • Croall, D.E.1    Demartino, G.N.2
  • 12
    • 0024390094 scopus 로고
    • Similar amino acid sequences revisited
    • Doolittle, R. F. (1989). Similar amino acid sequences revisited. Trends Biochem. Sci. 14, 244-245.
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 244-245
    • Doolittle, R.F.1
  • 13
    • 0024418527 scopus 로고
    • Estimating the prokaryote-eukaryote divergence time from protein sequences
    • Fernholm, B., Bremer, K. & Jornvall, H., Elsevier Science Publishers B.V., Amsterdam
    • Doolittle, R. F., Anderson, K. L. & Feng, D.-F. (1989). Estimating the prokaryote-eukaryote divergence time from protein sequences. In The Hierarchy of Life (Fernholm, B., Bremer, K. & Jornvall, H., eds), pp. 73-85, Elsevier Science Publishers B.V., Amsterdam.
    • (1989) The Hierarchy of Life , pp. 73-85
    • Doolittle, R.F.1    Erson, K.L.2    Feng, D.-F.3
  • 14
    • 0027499191 scopus 로고
    • BLH1 codes for a yeast thiol aminopeptidase, the equivalent of mammalian bleomycin hydrolase
    • Enenkel, C. & Wolf, D. H. (1993). BLH1 codes for a yeast thiol aminopeptidase, the equivalent of mammalian bleomycin hydrolase. J. Biol. Chem. 268, 7036-7043.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7036-7043
    • Enenkel, C.1    Wolf, D.H.2
  • 15
    • 0000461280 scopus 로고
    • Confidence limits on phylogenies: An approach using the bootstrap
    • Felsenstein, J. (1985). Confidence limits on phylogenies: an approach using the bootstrap. Evolution, 39, 783-791.
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 16
    • 0024152983 scopus 로고
    • Phylogenies from molecular sequences: Inference and reliability
    • Felsenstein, J. (1988). Phylogenies from molecular sequences: inference and reliability Annu. Rev. Genet. 22, 521-565.
    • (1988) Annu. Rev. Genet , vol.22 , pp. 521-565
    • Felsenstein, J.1
  • 17
    • 0003437299 scopus 로고
    • version 3.5c, Distributed by the author, Department of Genetics, University of Washington, Seattle
    • Felsenstein, J. (1993). PHYLIP (Phylogeny Inference Package) version 3.5c, Distributed by the author, Department of Genetics, University of Washington, Seattle.
    • (1993) PHYLIP (Phylogeny Inference Package)
    • Felsenstein, J.1
  • 18
    • 0025025261 scopus 로고
    • Progressive alignment and phylogenetic tree construction of protein sequences
    • Feng, D.-F. & Doolittle, R. F. (1990). Progressive alignment and phylogenetic tree construction of protein sequences. Methods Enzymol. 183, 375-387.
    • (1990) Methods Enzymol , vol.183 , pp. 375-387
    • Feng, D.-F.1    Doolittle, R.F.2
  • 19
    • 0002521151 scopus 로고
    • The usefulness of amino-acid and nucleotide sequences in evolutionary studies
    • Fitch, W. M. & Margoliash, E. (1971). The usefulness of amino-acid and nucleotide sequences in evolutionary studies. Evol. Biol. 4, 67-109.
    • (1971) Evol. Biol. , vol.4 , pp. 67-109
    • Fitch, W.M.1    Margoliash, E.2
  • 20
    • 0026952853 scopus 로고
    • Temporal and spatial expression of a thiolprotease gene during pea ovary senescence, and its regulation by gibberellin
    • Granelli, A., Harris, N., Pisabarro, A. G. & Carbonell, J. (1992). Temporal and spatial expression of a thiolprotease gene during pea ovary senescence, and its regulation by gibberellin. Plant J. 2, 907-915.
    • (1992) Plant J , vol.2 , pp. 907-915
    • Granelli, A.1    Harris, N.2    Pisabarro, A.G.3    Carbonell, J.4
  • 21
    • 0019888748 scopus 로고
    • Comparative model-building of the mammalian serine proteases
    • Greer, J. (1981). Comparative model-building of the mammalian serine proteases. J. Mol. Biol. 153, 1027-1042.
    • (1981) J. Mol. Biol. , vol.153 , pp. 1027-1042
    • Greer, J.1
  • 22
    • 0026661928 scopus 로고
    • Characterization of recombinant rat cathepsin B and nonglycosylated mutants expressed in yeast
    • Hasnain, S., Hirama, T., Tam, A. & Mort, J. S. (1992). Characterization of recombinant rat cathepsin B and nonglycosylated mutants expressed in yeast. J. Biol. Chem. 267, 4713-4721.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4713-4721
    • Hasnain, S.1    Hirama, T.2    Tam, A.3    Mort, J.S.4
  • 23
    • 0025342577 scopus 로고
    • Unified approach to alignment and phylogenies
    • Hein, J. (1990). Unified approach to alignment and phylogenies. Methods Enzymol. 183, 626-645.
    • (1990) Methods Enzymol , vol.183 , pp. 626-645
    • Hein, J.1
  • 24
    • 0020484334 scopus 로고
    • Crystal and molecular structure of the sulfhydryl protease calotropin DI at 3.2 A Resolution
    • Heinemann, U., Pal, G. P., Hilgenfeld, R. & Saenger, W. (1982). Crystal and molecular structure of the sulfhydryl protease calotropin DI at 3.2 A Resolution. J. Mol. Biol. 161, 591-606.
    • (1982) J. Mol. Biol. , vol.161 , pp. 591-606
    • Heinemann, U.1    Pal, G.P.2    Hilgenfeld, R.3    Saenger, W.4
  • 25
    • 0017814689 scopus 로고
    • Studies of a calcium-activated neutral protease from chicken skeletal muscle: I. Purification and characterization
    • Ishiura, S., Murofushi, H., Suzuki, K. & Imahori, K. (1978). Studies of a calcium-activated neutral protease from chicken skeletal muscle: I. Purification and characterization. J. Biochem. 84, 225-230.
    • (1978) J. Biochem. , vol.84 , pp. 225-230
    • Ishiura, S.1    Murofushi, H.2    Suzuki, K.3    Imahori, K.4
  • 26
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometric features
    • Kabsch, W. & Sander, C. (1983). Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometric features. Biopolymers 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 28
    • 0022429212 scopus 로고
    • Thiol proteases: Comparative studies based on the high-resolution structures of papain and actinidin, and on amino acid sequence information for cathepsins B and H, and stem bromelain
    • Kamphuis, I. G., Drenth, J. & Baker, E. N. (1985). Thiol proteases: comparative studies based on the high-resolution structures of papain and actinidin, and on amino acid sequence information for cathepsins B and H, and stem bromelain. J. Mol. Biol. 182, 317-329.
    • (1985) J. Mol. Biol. , vol.182 , pp. 317-329
    • Kamphuis, I.G.1    Drenth, J.2    Baker, E.N.3
  • 29
    • 0026613365 scopus 로고
    • The early evolution of eukaryotes: A geological perspective
    • Knoll, A. H. (1992). The early evolution of eukaryotes: a geological perspective. Science, 256, 622-627.
    • (1992) Science , vol.256 , pp. 622-627
    • Knoll, A.H.1
  • 30
    • 0025465440 scopus 로고
    • Hormonal regulation, processing, and secretion of cysteine proteinases in barley aleurone layers
    • Koehler, S. M. & Ho, T.-H. D. (1990). Hormonal regulation, processing, and secretion of cysteine proteinases in barley aleurone layers. Plant Cell, 2, 769-783.
    • (1990) Plant Cell , vol.2 , pp. 769-783
    • Koehler, S.M.1    Ho, T.-H.D.2
  • 32
    • 0025961761 scopus 로고
    • Tracing origins with molecular sequences: Metazoan and eukaryotic beginnings
    • Lake, J. A. (1991). Tracing origins with molecular sequences: metazoan and eukaryotic beginnings. Trends Biochem. Sci. 16, 46-50.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 46-50
    • Lake, J.A.1
  • 33
    • 0026001237 scopus 로고
    • Molecular cloning of three cDNAs that encode cysteine proteinases in the digestive gland of the American lobster (Homarus americanus)
    • Laycock, M. V., MacKay R. M., Di Fruscio, M. & Gallant, J. W. (1991). Molecular cloning of three cDNAs that encode cysteine proteinases in the digestive gland of the American lobster (Homarus americanus). FEBS Letters, 292, 115-120.
    • (1991) FEBS Letters , vol.292 , pp. 115-120
    • Laycock, M.V.1    Mackay, R.M.2    Di Fruscio, M.3    Gallant, J.W.4
  • 34
    • 0027539308 scopus 로고
    • Nucleotide sequence of a cDNA clone encoding tomato (Lycopersicon esculentum) cysteine proteinase
    • Linthorst, H. J. M., van der Does, C., van Kan, J. A. L. & Bol, J. F. (1993). Nucleotide sequence of a cDNA clone encoding tomato (Lycopersicon esculentum) cysteine proteinase. Plant Physiol. 101, 705-706.
    • (1993) Plant Physiol , vol.101 , pp. 705-706
    • Linthorst, H.J.M.1    Van Der Does, C.2    Van Kan, J.A.L.3    Bol, J.F.4
  • 35
    • 0024287196 scopus 로고
    • Affinity purification and biochemical characterization of histolysin, the major cysteine proteinase of
    • Luaces, A. L. & Barrett, A. J. (1988). Affinity purification and biochemical characterization of histolysin, the major cysteine proteinase of Entamoeba histolytica. Biochem. J. 250, 903-909.
    • (1988) Entamoeba Histolytica. Biochem. J , vol.250 , pp. 903-909
    • Luaces, A.L.1    Barrett, A.J.2
  • 36
    • 0024596636 scopus 로고
    • Parasite proteases
    • McKerrow, J. H. (1989). Parasite proteases. Expt. Parasitol. 68, 111-115.
    • (1989) Expt. Parasitol. , vol.68 , pp. 111-115
    • McKerrow, J.H.1
  • 37
    • 0025817139 scopus 로고
    • Cysteine proteinase inhibitors and bleomycin-sensitive and -resistant cells
    • Morris, G., Mistry J. S., Jani, J. P., Sebti, S. M. & Lazo, J. S. (1991). Cysteine proteinase inhibitors and bleomycin-sensitive and -resistant cells. Biochem. Pharmacol. 41, 1559-1566.
    • (1991) Biochem. Pharmacol. , vol.41 , pp. 1559-1566
    • Morris, G.1    Mistry, J.S.2    Jani, J.P.3    Sebti, S.M.4    Lazo, J.S.5
  • 38
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • Munro, S. & Pelham, H. R. B. (1987). A C-terminal signal prevents secretion of luminal ER proteins. Cell, 48, 899-907.
    • (1987) Cell , vol.48 , pp. 899-907
    • Munro, S.1    Pelham, H.R.B.2
  • 39
    • 0024674263 scopus 로고
    • Rapid determination of sequence variations in actinidin isolated from Actinidia chinensis (Var. Hayward) using fast atom bombardment mapping mass spectrometry and gas phase microsequencing
    • Naylor, S., Ang, S.-G., Williams, D. H., Moore, C. H. & Walsh, K. (1989). Rapid determination of sequence variations in actinidin isolated from Actinidia chinensis (var. Hayward) using fast atom bombardment mapping mass spectrometry and gas phase microsequencing. Biomed. Env. Mass Spectrom. 18, 424-428.
    • (1989) Biomed. Env. Mass Spectrom. , vol.18 , pp. 424-428
    • Naylor, S.1    Ang, S.-G.2    Williams, D.H.3    Moore, C.H.4    Walsh, K.5
  • 40
    • 0021273620 scopus 로고
    • Evolution of proteolytic enzymes
    • Neurath, H. (1984). Evolution of proteolytic enzymes. Science, 224, 350-357.
    • (1984) Science , vol.224 , pp. 350-357
    • Neurath, H.1
  • 41
    • 0009107534 scopus 로고
    • Proteinases of trichomonads and Giardia
    • Coombs, G. H. & North, M. J., Taylor & Francis, New York
    • North, M. J. (1991). Proteinases of trichomonads and Giardia. In Biochemical Protozoology (Coombs, G. H. & North, M. J., eds), pp. 234-244, Taylor & Francis, New York.
    • (1991) Biochemical Protozoology , pp. 234-244
    • North, M.J.1
  • 42
    • 0021749729 scopus 로고
    • Evolutionary origin of a calcium-dependent protease by fusion of genes for a thiol protease and a calcium-binding protein?
    • Ohno, S., Emori, Y., Imajoh, S., Kawasaki, H., Kisaragi, M. & Suzuki, K. (1984). Evolutionary origin of a calcium-dependent protease by fusion of genes for a thiol protease and a calcium-binding protein? Nature (London), 312, 566-570.
    • (1984) Nature (London) , vol.312 , pp. 566-570
    • Ohno, S.1    Emori, Y.2    Imajoh, S.3    Kawasaki, H.4    Kisaragi, M.5    Suzuki, K.6
  • 43
    • 0024398377 scopus 로고
    • Characterization of a thiol proteinase in Giardia lamblia
    • Parenti, D. M. (1989). Characterization of a thiol proteinase in Giardia lamblia. J. Infect. Dis. 160, 1076-1080.
    • (1989) J. Infect. Dis , vol.160 , pp. 1076-1080
    • Parenti, D.M.1
  • 44
    • 0027092035 scopus 로고
    • Sequence analysis, tissue distribution, and expression of rat cathepsin S
    • Petanceska, S. & Devi, L. (1992). Sequence analysis, tissue distribution, and expression of rat cathepsin S. J. Biol. Chem. 267, 26038-26043.
    • (1992) J. Biol. Chem. , vol.267 , pp. 26038-26043
    • Petanceska, S.1    Devi, L.2
  • 47
    • 0344223030 scopus 로고
    • Analysis of the expression of two genes of Dictyostelium discoideum which code for developmentally regulated cysteine proteinases
    • Presse, F., Bogdanovsky-Sequeval, D., Mathieu, M. & Felenbok, B. (1986). Analysis of the expression of two genes of Dictyostelium discoideum which code for developmentally regulated cysteine proteinases. Mol. Gen. Genet. 203, 333-340.
    • (1986) Mol. Gen. Genet. , vol.203 , pp. 333-340
    • Presse, F.1    Bogdanovsky-Sequeval, D.2    Mathieu, M.3    Felenbok, B.4
  • 48
    • 0025995711 scopus 로고
    • The expression of cathepsin B and other lysosomal proteinases in normal tissues and in tumors. Biomed. Biochim
    • Qian, F., Chan, S. J., Gong, Q., Bajkowski, A. S., Steiner, D. F. & Frankfater, A. (1991). The expression of cathepsin B and other lysosomal proteinases in normal tissues and in tumors. Biomed. Biochim. Acta, 50, 531-540.
    • (1991) Acta , vol.50 , pp. 531-540
    • Qian, F.1    Chan, S.J.2    Gong, Q.3    Bajkowski, A.S.4    Steiner, D.F.5    Frankfater, A.6
  • 50
    • 0001427425 scopus 로고
    • Inhibitors of cysteine proteinases
    • Barrett, A. J. & Salvesen, G., Elsevier, Amsterdam
    • Rich, D. H. (1986). Inhibitors of cysteine proteinases. In Proteinase Inhibitors (Barrett, A. J. & Salvesen, G., eds), pp. 153-178, Elsevier, Amsterdam.
    • (1986) Proteinase Inhibitors , pp. 153-178
    • Rich, D.H.1
  • 51
    • 0027512171 scopus 로고
    • Inhibition of a Plasmodium vinckei cysteine proteinase cures murine malaria
    • Rosenthal, P. J., Lee, G. K. & Smith, R. E. (1993). Inhibition of a Plasmodium vinckei cysteine proteinase cures murine malaria. J. Clin. Invest. 91, 1052-1056.
    • (1993) J. Clin. Invest. , vol.91 , pp. 1052-1056
    • Rosenthal, P.J.1    Lee, G.K.2    Smith, R.E.3
  • 52
    • 0026664252 scopus 로고
    • Rat procathepsin B: Proteolytic processing to the mature form, in vitro
    • Rowan, A. D., Mason, P., Mach, L. & Mort, J. S. (1992). Rat procathepsin B: proteolytic processing to the mature form, in vitro. J. Biol. Chem. 267, 15993-15999.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15993-15999
    • Rowan, A.D.1    Mason, P.2    Mach, L.3    Mort, J.S.4
  • 53
    • 0001213953 scopus 로고
    • Simultaneous comparison of three or more sequences related by a tree
    • Sankoff, D. & Kruskal, J. B., Addison-Wesley Publishing Co., Inc., Reading, MA
    • Sankoff, D. & Cedergreen, R. J. (1983). Simultaneous comparison of three or more sequences related by a tree. In Time Warps, String Edits, and Macromolecules: The Theory and Practice of Sequence Comparison (Sankoff, D. & Kruskal, J. B., eds), pp. 253-261, Addison-Wesley Publishing Co., Inc., Reading, MA.
    • (1983) Time Warps, String Edits, and Macromolecules: The Theory and Practice of Sequence Comparison , pp. 253-261
    • Sankoff, D.1    Cedergreen, R.J.2
  • 54
    • 0001540727 scopus 로고
    • Analysis of mRNAs that accumulate in response to low temperature identifies a thiol protease gene in tomato
    • Schaffer, M. A. & Fischer, R. L. (1988). Analysis of mRNAs that accumulate in response to low temperature identifies a thiol protease gene in tomato. Plant Physiol. 87, 431-436.
    • (1988) Plant Physiol , vol.87 , pp. 431-436
    • Schaffer, M.A.1    Fischer, R.L.2
  • 55
    • 0026527758 scopus 로고
    • Pattern-induced multi-sequence alignment (PIMA) algorithm employing secondary structure-dependent gap penalties for use in comparative protein modelling
    • Smith, R. F. & Smith, T. F. (1992). Pattern-induced multi-sequence alignment (PIMA) algorithm employing secondary structure-dependent gap penalties for use in comparative protein modelling. Protein Eng. 5, 35-41.
    • (1992) Protein Eng , vol.5 , pp. 35-41
    • Smith, R.F.1    Smith, T.F.2
  • 56
    • 0026282909 scopus 로고
    • Early evolution and the origin of eukaryotes
    • Sogin, M. L. (1991). Early evolution and the origin of eukaryotes. Curr. Opinion Genet. Develop. 1, 457-463.
    • (1991) Curr. Opinion Genet. Develop. , vol.1 , pp. 457-463
    • Sogin, M.L.1
  • 58
    • 0001140522 scopus 로고
    • Phylogeny reconstruction
    • Hillis, D. M. & Moritz, C., Sinauer Associates, Inc., Sunderland, MA
    • Swofford, D. L. & Olsen, G. J. (1990). Phylogeny reconstruction. In Molecular Systematics (Hillis, D. M. & Moritz, C., eds), pp. 411-501, Sinauer Associates, Inc., Sunderland, MA.
    • (1990) Molecular Systematics , pp. 411-501
    • Swofford, D.L.1    Olsen, G.J.2
  • 60
    • 0026095842 scopus 로고
    • Molecular cloning and gibberellin-induced expression of multiple cysteine proteinases of rice seeds (Oryzains)
    • Watanabe, H., Abe, K., Emori, Y., Hosoyama, H. & Arai, S. (1991). Molecular cloning and gibberellin-induced expression of multiple cysteine proteinases of rice seeds (Oryzains). J. Biol. Chem. 266, 16897-16902.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16897-16902
    • Watanabe, H.1    Abe, K.2    Emori, Y.3    Hosoyama, H.4    Arai, S.5
  • 61
    • 0026216355 scopus 로고
    • Degradation of T-cell receptor chains in the endoplasmic reticulum is inhibited by inhibitors of cysteine proteases
    • Wileman, T., Kane, L. P. & Terhorst, C. (1991). Degradation of T-cell receptor chains in the endoplasmic reticulum is inhibited by inhibitors of cysteine proteases. Cell Regulat. 2, 753-765.
    • (1991) Cell Regulat , vol.2 , pp. 753-765
    • Wileman, T.1    Kane, L.P.2    Terhorst, C.3
  • 62
    • 0025800635 scopus 로고
    • Suboptimal sequence alignment in molecluar biology: Alignment with error analysis
    • Zuker, M. (1991). Suboptimal sequence alignment in molecluar biology: alignment with error analysis. J. Mol. Biol. 221, 403-420.
    • (1991) J. Mol. Biol. , vol.221 , pp. 403-420
    • Zuker, M.1
  • 63
    • 0024557588 scopus 로고
    • The alignment of protein structures in three dimensions
    • Zuker, M. & Somorjai, R. L. (1989). The alignment of protein structures in three dimensions. Bull. Math. Biol. 51, 55-78.
    • (1989) Bull. Math. Biol. , vol.51 , pp. 55-78
    • Zuker, M.1    Somorjai, R.L.2


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