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Volumn 6, Issue 1, 1997, Pages 5-12

Friends and relations of the cystatin superfamily - New members and their evolution

Author keywords

cystatins; cysteine protease inhibitors; evolution; fetuins; kininogens; TGF receptor II

Indexed keywords

CYSTATIN; FETUIN; KININOGEN; TRANSFORMING GROWTH FACTOR BETA RECEPTOR;

EID: 0031013054     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060102     Document Type: Review
Times cited : (148)

References (101)
  • 1
    • 0023657047 scopus 로고
    • Molecular cloning of a cysteine proteinase inhibitor of rice (oryzacystatin). Homology with animal cystatins and transient expression in the ripening process of rice seeds
    • Abe K, Emori Y, Kondo H, Suzuki K, Arai S. 1987. Molecular cloning of a cysteine proteinase inhibitor of rice (oryzacystatin). Homology with animal cystatins and transient expression in the ripening process of rice seeds. J Biol Chem 262:16793-16797.
    • (1987) J Biol Chem , vol.262 , pp. 16793-16797
    • Abe, K.1    Emori, Y.2    Kondo, H.3    Suzuki, K.4    Arai, S.5
  • 2
    • 0026497716 scopus 로고
    • Com kernel cysteine proteinase inhibitor as a novel cystatin superfamily member of plant origin. Molecular cloning and expression studies
    • Abe M, Abe K, Kuroda M, Arai S. 1992. Com kernel cysteine proteinase inhibitor as a novel cystatin superfamily member of plant origin. Molecular cloning and expression studies. Eur J Biochem 209:933-937.
    • (1992) Eur J Biochem , vol.209 , pp. 933-937
    • Abe, M.1    Abe, K.2    Kuroda, M.3    Arai, S.4
  • 3
    • 0026589838 scopus 로고
    • Invariant chain can function as a chaperone protein for class II major histocompatibility complex molecules
    • Anderson MS, Miller J. 1992. Invariant chain can function as a chaperone protein for class II major histocompatibility complex molecules. Proc Natl Acad Sci USA 89:2282-2286.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2282-2286
    • Anderson, M.S.1    Miller, J.2
  • 4
    • 0024589261 scopus 로고
    • 2HS-glycoprotein and the repeating double disulfide bonds in the domain structure
    • 2HS-glycoprotein and the repeating double disulfide bonds in the domain structure. Biochim Biophys Acta 994:195-199.
    • (1989) Biochim Biophys Acta , vol.994 , pp. 195-199
    • Araki, T.1    Yoshioka, Y.2    Schmid, K.3
  • 6
    • 0030028342 scopus 로고    scopus 로고
    • Hybrids of chicken cystatin with human kininogen domain 2 sequences exhibit novel inhibition of calpain, improved inhibition of actinidin and impaired inhibition of papain, cathepsin L and cathepsin B
    • Auerswald EA, Naegler DK, Gross S, Assfalg-Machleidt I, Stubbs MT, Eckerskora C, Machleidt W, Fritz H. 1996. Hybrids of chicken cystatin with human kininogen domain 2 sequences exhibit novel inhibition of calpain, improved inhibition of actinidin and impaired inhibition of papain, cathepsin L and cathepsin B. Eur J Biochem 235:534-542.
    • (1996) Eur J Biochem , vol.235 , pp. 534-542
    • Auerswald, E.A.1    Naegler, D.K.2    Gross, S.3    Assfalg-Machleidt, I.4    Stubbs, M.T.5    Eckerskora, C.6    Machleidt, W.7    Fritz, H.8
  • 7
    • 77957034551 scopus 로고
    • Cystatin, the egg white inhibitor of cysteine proteinases
    • Barrett AJ. 1981. Cystatin, the egg white inhibitor of cysteine proteinases. Methods Enzymol 80:771-778.
    • (1981) Methods Enzymol , vol.80 , pp. 771-778
    • Barrett, A.J.1
  • 8
    • 0025695557 scopus 로고
    • Isolation and molecular cloning of transferrin from the tobacco hornworm, Manduca sexta. Sequence similarity to the vertebrate transferrins
    • Bartfeld NS, Law JH. 1990. Isolation and molecular cloning of transferrin from the tobacco hornworm, Manduca sexta. Sequence similarity to the vertebrate transferrins. J Biol Chem 265:21684-21691.
    • (1990) J Biol Chem , vol.265 , pp. 21684-21691
    • Bartfeld, N.S.1    Law, J.H.2
  • 9
    • 0024066065 scopus 로고
    • The 2.0 A 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 A 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
  • 10
    • 0025028813 scopus 로고
    • Mechanism of interaction of cysteine proteinases and their protein inhibitors as compared to the serine proteinase-inhibitor interaction
    • Bode W, Engh R, Musil D, Laber B, Stubbs M, Huber R, Turk V. 1990. Mechanism of interaction of cysteine proteinases and their protein inhibitors as compared to the serine proteinase-inhibitor interaction. Biol Chem Hoppe-Seyler 371(Suppl):111-118.
    • (1990) Biol Chem Hoppe-Seyler , vol.371 , Issue.SUPPL. , pp. 111-118
    • Bode, W.1    Engh, R.2    Musil, D.3    Laber, B.4    Stubbs, M.5    Huber, R.6    Turk, V.7
  • 11
    • 0024248764 scopus 로고
    • Transferrin: Evolution and genetic regulation of expression
    • Bowman BH, Yang FM, Adrian GS. 1988. Transferrin: Evolution and genetic regulation of expression. Adv Genet 25:1-38.
    • (1988) Adv Genet , vol.25 , pp. 1-38
    • Bowman, B.H.1    Yang, F.M.2    Adrian, G.S.3
  • 12
    • 0000375790 scopus 로고
    • Structure of bovine serum albumin
    • Brown JR. 1976a. Structure of bovine serum albumin. Fed Proc 34:591.
    • (1976) Fed Proc , vol.34 , pp. 591
    • Brown, J.R.1
  • 13
    • 0016989611 scopus 로고
    • Structural origins of mammalian albumin
    • Brown JR. 1976b. Structural origins of mammalian albumin. Fed Proc 35:2141-2144.
    • (1976) Fed Proc , vol.35 , pp. 2141-2144
    • Brown, J.R.1
  • 14
    • 0026513599 scopus 로고
    • The nucleotide and deduced amino acid structures of sheep and pig fetuin. Common structural features of the mammalian fetuin family
    • Brown WM, Christie DL, Dziegielewska KM, Nawratil P, Saunders NR, Müller-Esterl W. 1992a. The nucleotide and deduced amino acid structures of sheep and pig fetuin. Common structural features of the mammalian fetuin family. Eur J Biochem 205:321-331.
    • (1992) Eur J Biochem , vol.205 , pp. 321-331
    • Brown, W.M.1    Christie, D.L.2    Dziegielewska, K.M.3    Nawratil, P.4    Saunders, N.R.5    Müller-Esterl, W.6
  • 16
    • 0027440812 scopus 로고
    • The use of tributylphosphine and 4-(aminosulfonyl)-7-fluoro-2,1,3-benzoxadiazole in the study of protein sulfhydryls and disulfides
    • Chin CC, Wold F. 1993. The use of tributylphosphine and 4-(aminosulfonyl)-7-fluoro-2,1,3-benzoxadiazole in the study of protein sulfhydryls and disulfides. Anal Biochem 214:128-134.
    • (1993) Anal Biochem , vol.214 , pp. 128-134
    • Chin, C.C.1    Wold, F.2
  • 18
    • 0026794191 scopus 로고
    • The structure and expression of the genes for T-kininogen in the rat
    • Cole TJ, Schreiber G. 1992. The structure and expression of the genes for T-kininogen in the rat. Agents Actions Suppl 38:292-299.
    • (1992) Agents Actions Suppl , vol.38 , pp. 292-299
    • Cole, T.J.1    Schreiber, G.2
  • 19
    • 0027328796 scopus 로고
    • Isolation and characterization of the chicken cystatin-encoding gene: Mapping transcription start point and polyadenylation sites
    • Colella R, Bird JW. 1993. Isolation and characterization of the chicken cystatin-encoding gene: Mapping transcription start point and polyadenylation sites. Gene 130:175-181.
    • (1993) Gene , vol.130 , pp. 175-181
    • Colella, R.1    Bird, J.W.2
  • 20
    • 0026502909 scopus 로고
    • Structure, organization and regulation of a rat cysteine proteinase inhibitor-encoding gene
    • Cox JL, Shaw PA. 1992. Structure, organization and regulation of a rat cysteine proteinase inhibitor-encoding gene. Gene 110:175-180.
    • (1992) Gene , vol.110 , pp. 175-180
    • Cox, J.L.1    Shaw, P.A.2
  • 21
    • 0025081249 scopus 로고
    • Sequence analysis, and chromosomal localization of a gene encoding a cystatin-like protein from Drosophila melanogaster
    • Delbridge ML, Kelly LE. 1990. Sequence analysis, and chromosomal localization of a gene encoding a cystatin-like protein from Drosophila melanogaster. FEBS Lett 274:141-145.
    • (1990) FEBS Lett , vol.274 , pp. 141-145
    • Delbridge, M.L.1    Kelly, L.E.2
  • 22
    • 0029666256 scopus 로고    scopus 로고
    • Fetuin/ alpha-2-HS glycoprotein is a transforming growth factor-beta type II receptor mimic and cytokine antagonist
    • Demetriou M, Binkert C, Sukhu B, Tenenbaum HC, Dennis JW. 1996. Fetuin/ alpha-2-HS glycoprotein is a transforming growth factor-beta type II receptor mimic and cytokine antagonist. J Biol Chem 271:12755-12761.
    • (1996) J Biol Chem , vol.271 , pp. 12755-12761
    • Demetriou, M.1    Binkert, C.2    Sukhu, B.3    Tenenbaum, H.C.4    Dennis, J.W.5
  • 23
    • 0027416960 scopus 로고
    • Structure of rat genes encoding androgen-regulated cystatin-related proteins (CRPs): A new member of the cystatin superfamily
    • Devos A, de Clercq N, Vercaeren I, Heyns W, Rombauts W, Peeters B. 1993. Structure of rat genes encoding androgen-regulated cystatin-related proteins (CRPs): A new member of the cystatin superfamily. Gene 125:159-167.
    • (1993) Gene , vol.125 , pp. 159-167
    • Devos, A.1    De Clercq, N.2    Vercaeren, I.3    Heyns, W.4    Rombauts, W.5    Peeters, B.6
  • 25
    • 0026817136 scopus 로고
    • Reconstructing history with amino acid sequences
    • Doolittle RF. 1992. Reconstructing history with amino acid sequences. Protein Sci 1:191-200.
    • (1992) Protein Sci , vol.1 , pp. 191-200
    • Doolittle, R.F.1
  • 26
    • 0004046531 scopus 로고
    • Molecular Biology Intelligence Unit, R.G. Landes Company, Texas, International. Austin: Springer-Verlag
    • Dziegielewska KM, Brown WM. 1995. Fetuin. Molecular Biology Intelligence Unit, R.G. Landes Company, Texas, International. Austin: Springer-Verlag.
    • (1995) Fetuin
    • Dziegielewska, K.M.1    Brown, W.M.2
  • 29
    • 0019838616 scopus 로고
    • Intragenic amplification and divergence in the mouse a-fetoprotein gene
    • Eiferman FA, Young PR, Scott RW, Tilghman SM. 1981. Intragenic amplification and divergence in the mouse a-fetoprotein gene. Nature 294:713-718.
    • (1981) Nature , vol.294 , pp. 713-718
    • Eiferman, F.A.1    Young, P.R.2    Scott, R.W.3    Tilghman, S.M.4
  • 31
    • 0023656053 scopus 로고
    • A cystatin-like cysteine proteinase inhibitor from venom of the African puff adder (Bitis arietans)
    • Evans HJ, Barrett AJ. 1987. A cystatin-like cysteine proteinase inhibitor from venom of the African puff adder (Bitis arietans). Biochem J 246:795-797.
    • (1987) Biochem J , vol.246 , pp. 795-797
    • Evans, H.J.1    Barrett, A.J.2
  • 33
    • 0025772329 scopus 로고
    • The human kininogen gene (KNG) mapped to chromosome 3q26-qter by analysis of somatic cell hybrids using the polymerase chain reaction
    • Fong D, Smith DI, Hsieh WT. 1991. The human kininogen gene (KNG) mapped to chromosome 3q26-qter by analysis of somatic cell hybrids using the polymerase chain reaction. Hum Genet 87:189-192.
    • (1991) Hum Genet , vol.87 , pp. 189-192
    • Fong, D.1    Smith, D.I.2    Hsieh, W.T.3
  • 35
    • 0014268847 scopus 로고
    • Physical evidence for transferrins as single polypeptide chains
    • Greene FC, Feeney RE. 1968. Physical evidence for transferrins as single polypeptide chains. Biochemistry 7:1366-1371.
    • (1968) Biochemistry , vol.7 , pp. 1366-1371
    • Greene, F.C.1    Feeney, R.E.2
  • 36
    • 0021141631 scopus 로고
    • The disulphide bridges of human cystatin C (g-trace) and chicken cystatin
    • Grubb A, Löfberg H, Barrett AJ. 1984. The disulphide bridges of human cystatin C (g-trace) and chicken cystatin. FEBS Lett 170:370-374.
    • (1984) FEBS Lett , vol.170 , pp. 370-374
    • Grubb, A.1    Löfberg, H.2    Barrett, A.J.3
  • 37
    • 0016813430 scopus 로고
    • Purification and heterogeneity of human kininogen. Use of DEAE-chromatography, molecular sieving and antibody specific immunosorbents
    • Hamberg U, Elg P, Nissinen E, Stelwagen P. 1975. Purification and heterogeneity of human kininogen. Use of DEAE-chromatography, molecular sieving and antibody specific immunosorbents. Int J Peptide Protein Res 7:261-280.
    • (1975) Int J Peptide Protein Res , vol.7 , pp. 261-280
    • Hamberg, U.1    Elg, P.2    Nissinen, E.3    Stelwagen, P.4
  • 38
    • 0028123712 scopus 로고
    • Evidence for the absence of intron H of the histidine-rich glycoprotein (HRG) gene: Genetic mapping and in situ localization of HRG to chromosome 3q28-q29
    • Hennis BC, Frants RR, Bakker E, Vossen RH, van der Poort EW, Blonden LA, Cox S, Khan PM, Spurr NK, Kluft C. 1994. Evidence for the absence of intron H of the histidine-rich glycoprotein (HRG) gene: Genetic mapping and in situ localization of HRG to chromosome 3q28-q29. Genomics 19:195-197.
    • (1994) Genomics , vol.19 , pp. 195-197
    • Hennis, B.C.1    Frants, R.R.2    Bakker, E.3    Vossen, R.H.4    Van Der Poort, E.W.5    Blonden, L.A.6    Cox, S.7    Khan, P.M.8    Spurr, N.K.9    Kluft, C.10
  • 40
    • 0025970993 scopus 로고
    • Mapping of the gene for human cysteine proteinase inhibitor stefin A, STF1, to chromosome 3cen-q21
    • Hsieh WT, Fong D, Sloane BF, Golembieski W, Smith DI. 1991. Mapping of the gene for human cysteine proteinase inhibitor stefin A, STF1, to chromosome 3cen-q21. Genomics 9:207-209.
    • (1991) Genomics , vol.9 , pp. 207-209
    • Hsieh, W.T.1    Fong, D.2    Sloane, B.F.3    Golembieski, W.4    Smith, D.I.5
  • 41
    • 0028939368 scopus 로고
    • Structural organization, expression and chromosomal mapping of the mouse cystatin-C-encoding gene (Cst3)
    • Huh C, Nagle JW, Kozak CA, Abrahamson M, Karlsson S. 1995. Structural organization, expression and chromosomal mapping of the mouse cystatin-C-encoding gene (Cst3). Gene 152:221-226.
    • (1995) Gene , vol.152 , pp. 221-226
    • Huh, C.1    Nagle, J.W.2    Kozak, C.A.3    Abrahamson, M.4    Karlsson, S.5
  • 42
    • 0030019236 scopus 로고    scopus 로고
    • Transgenic rice established to express corn cystatin exhibits strong inhibitory activity against insect gut proteinases
    • Irie K, Hosoyama H, Takeuchi T, Iwabuchi K, Watanabe H, Abe M, Abe K, Arai S. 1996. Transgenic rice established to express corn cystatin exhibits strong inhibitory activity against insect gut proteinases. Plant Mol Biol 30:149-157.
    • (1996) Plant Mol Biol , vol.30 , pp. 149-157
    • Irie, K.1    Hosoyama, H.2    Takeuchi, T.3    Iwabuchi, K.4    Watanabe, H.5    Abe, M.6    Abe, K.7    Arai, S.8
  • 43
    • 0029965177 scopus 로고    scopus 로고
    • Walking, cloning, and mapping with YACs in 3q27: Localization of five ESTs including three members of the cystatin gene family and identification of CpG islands
    • James LA, Ogilvie DJ, Yamakawa Y, Stirling CJ, Anand R. 1996. Walking, cloning, and mapping with YACs in 3q27: Localization of five ESTs including three members of the cystatin gene family and identification of CpG islands. Genomics 32:425-430.
    • (1996) Genomics , vol.32 , pp. 425-430
    • James, L.A.1    Ogilvie, D.J.2    Yamakawa, Y.3    Stirling, C.J.4    Anand, R.5
  • 45
    • 0027956047 scopus 로고
    • Immunological significance of invariant chain from the aspect of its structural homology with the cystatin family
    • Katunuma H, Kakegawa H, Matsunaga Y, Saibara T. 1994. Immunological significance of invariant chain from the aspect of its structural homology with the cystatin family. FEBS Lett 39:265-269.
    • (1994) FEBS Lett , vol.39 , pp. 265-269
    • Katunuma, H.1    Kakegawa, H.2    Matsunaga, Y.3    Saibara, T.4
  • 46
    • 0022445020 scopus 로고
    • Completion of the primary structure of human high-molecular-mass kininogen. The amino acid sequence of the entire heavy chain and evidence for its evolution by gene triplication
    • Kellermann J, Lottspeich F, Henschen A, Müller-Esterl W. 1986. Completion of the primary structure of human high-molecular-mass kininogen. The amino acid sequence of the entire heavy chain and evidence for its evolution by gene triplication. Eur J Biochem 154:471-478.
    • (1986) Eur J Biochem , vol.154 , pp. 471-478
    • Kellermann, J.1    Lottspeich, F.2    Henschen, A.3    Müller-Esterl, W.4
  • 48
    • 0024414068 scopus 로고
    • The arrangement of disulfide loops in human α-HS glyco-protein. Similarity to the disulfide bridge structures of cystatins and kininogens
    • Kellermann J, Haupt H, Auerswald E-A, Müller-Esterl W. 1989. The arrangement of disulfide loops in human α-HS glyco-protein. Similarity to the disulfide bridge structures of cystatins and kininogens. J Biol Chem 264:14121-14128.
    • (1989) J Biol Chem , vol.264 , pp. 14121-14128
    • Kellermann, J.1    Haupt, H.2    Auerswald, E.-A.3    Müller-Esterl, W.4
  • 50
    • 0020518332 scopus 로고
    • A single gene for bovine high molecular weight and low molecular weight kininogens
    • Kitamura N, Takagaki Y, Furuto S, Tanaka T, Nawa H, Nakanishi S. 1983. A single gene for bovine high molecular weight and low molecular weight kininogens. Nature 305:545-549.
    • (1983) Nature , vol.305 , pp. 545-549
    • Kitamura, N.1    Takagaki, Y.2    Furuto, S.3    Tanaka, T.4    Nawa, H.5    Nakanishi, S.6
  • 51
    • 0023737498 scopus 로고
    • Human histidine-rich glycoprotein gene: Evidence for evolutionary relatedness to cystatin supergene family
    • Koide T. 1988. Human histidine-rich glycoprotein gene: Evidence for evolutionary relatedness to cystatin supergene family. Thromb Res Suppl VIII:91-97.
    • (1988) Thromb Res Suppl , vol.8 , pp. 91-97
    • Koide, T.1
  • 52
    • 0022462086 scopus 로고
    • Amino acid sequence of human histidine-rich glycoprotein derived from the nucleotide sequence of its cDNA
    • Koide T, Foster D, Yoshitake S, Davie EW. 1986. Amino acid sequence of human histidine-rich glycoprotein derived from the nucleotide sequence of its cDNA. Biochemistry 25:2220-2225.
    • (1986) Biochemistry , vol.25 , pp. 2220-2225
    • Koide, T.1    Foster, D.2    Yoshitake, S.3    Davie, E.W.4
  • 53
    • 0025965712 scopus 로고
    • Gene organization of oryzacystatin-II, a new cystatin superfamily member of plant origin, is closely related to that of oryzacystatin-I but different from those of the animal cystatins
    • Kondo H, Abe K, Emori Y, Arai S. 1991. Gene organization of oryzacystatin-II, a new cystatin superfamily member of plant origin, is closely related to that of oryzacystatin-I but different from those of the animal cystatins. FEBS Lett 278:87-90.
    • (1991) FEBS Lett , vol.278 , pp. 87-90
    • Kondo, H.1    Abe, K.2    Emori, Y.3    Arai, S.4
  • 54
    • 0024424222 scopus 로고
    • Cloning and sequence analysis of the genomic DNA fragment encoding oryzacystatin
    • Kondo H, Emori Y, Abe K, Suzuki K, Arai S. 1989. Cloning and sequence analysis of the genomic DNA fragment encoding oryzacystatin. Gene 81:259-265.
    • (1989) Gene , vol.81 , pp. 259-265
    • Kondo, H.1    Emori, Y.2    Abe, K.3    Suzuki, K.4    Arai, S.5
  • 55
    • 0025160575 scopus 로고
    • Two distinct cystatin species in rice seeds with different specificities against cysteine proteinases. Molecular cloning, expression, and biochemical studies on oryzacystatin-II
    • Kondo H, Abe K, Nishimura I, Watanabe H, Emori Y, Arai S. 1990. Two distinct cystatin species in rice seeds with different specificities against cysteine proteinases. Molecular cloning, expression, and biochemical studies on oryzacystatin-II. J Biol Chem 265:15832-15837.
    • (1990) J Biol Chem , vol.265 , pp. 15832-15837
    • Kondo, H.1    Abe, K.2    Nishimura, I.3    Watanabe, H.4    Emori, Y.5    Arai, S.6
  • 56
    • 1842279017 scopus 로고
    • 2-HS-glyco-protein: The A and B chains with a connecting sequence are encoded by a single mRNA transcript
    • 2-HS-glyco-protein: The A and B chains with a connecting sequence are encoded by a single mRNA transcript. Proc Natl Acad Sci USA 54:4403-4407.
    • (1987) Proc Natl Acad Sci USA , vol.54 , pp. 4403-4407
    • Lee, C.-C.1    Bowman, B.H.2    Yang, F.3
  • 57
    • 0027256327 scopus 로고
    • Histidine-rich glycoprotein: An abundant plasma protein in search of a function
    • Leung L. 1993. Histidine-rich glycoprotein: An abundant plasma protein in search of a function. J Lab Clin Med 121:630-631.
    • (1993) J Lab Clin Med , vol.121 , pp. 630-631
    • Leung, L.1
  • 58
    • 0028947279 scopus 로고
    • Temporary inhibition of papain by hairpin loop mutants of chicken cystatin. Distorted binding of the lopps results in cleavage of the Gly(9)-Ala10 bond
    • Machleidt W, Nagler DK, Assfalg-Machleidt I, Stubbs MT, Fritz H, Auerswald EA. 1995. Temporary inhibition of papain by hairpin loop mutants of chicken cystatin. Distorted binding of the lopps results in cleavage of the Gly(9)-Ala10 bond. FEBS Lett 361:185-190.
    • (1995) FEBS Lett , vol.361 , pp. 185-190
    • Machleidt, W.1    Nagler, D.K.2    Assfalg-Machleidt, I.3    Stubbs, M.T.4    Fritz, H.5    Auerswald, E.A.6
  • 60
    • 0021710575 scopus 로고
    • A mono-sited transferrin from a representative deuterostome: The ascidian Pyura stolonifera (subphylum Urochordata)
    • Martin AW, Huebers E, Huebers H, Webb J, Finch CA. 1984. A mono-sited transferrin from a representative deuterostome: The ascidian Pyura stolonifera (subphylum Urochordata). Blood 64:1047-1052.
    • (1984) Blood , vol.64 , pp. 1047-1052
    • Martin, A.W.1    Huebers, E.2    Huebers, H.3    Webb, J.4    Finch, C.A.5
  • 61
    • 0028077339 scopus 로고
    • Structural characterization of human stefin a in solution and implications for binding to cysteine proteinases
    • Martin JR, Jerala R, Kroon-Zitko L, Zerovnik E, Turk V, Waltho JP. 1994. Structural characterization of human stefin A in solution and implications for binding to cysteine proteinases. Eur J Biochem 225:1181-1194.
    • (1994) Eur J Biochem , vol.225 , pp. 1181-1194
    • Martin, J.R.1    Jerala, R.2    Kroon-Zitko, L.3    Zerovnik, E.4    Turk, V.5    Waltho, J.P.6
  • 64
    • 0026687497 scopus 로고
    • Purification of bovine histidine rich glycoprotein
    • Muldbjerg M, Schousboe I, Halkier T. 1992. Purification of bovine histidine rich glycoprotein. Thromb Res 65:815-819.
    • (1992) Thromb Res , vol.65 , pp. 815-819
    • Muldbjerg, M.1    Schousboe, I.2    Halkier, T.3
  • 65
    • 0022350512 scopus 로고
    • Genealogy of mammalian cysteine proteinase inhibitors. Common evolutionary origin of stefins, cystatins and kininogens
    • Müller-Esterl W, Fritz H, Kellermann J, Lottspeich F, Machleidt W, Turk V. 1985. Genealogy of mammalian cysteine proteinase inhibitors. Common evolutionary origin of stefins, cystatins and kininogens. FEBS Lett 191:221-226.
    • (1985) FEBS Lett , vol.191 , pp. 221-226
    • Müller-Esterl, W.1    Fritz, H.2    Kellermann, J.3    Lottspeich, F.4    Machleidt, W.5    Turk, V.6
  • 66
    • 0027162768 scopus 로고
    • Sweet-tasting protein monellin is related to the cystatin family of thiol proteinase inhibitors
    • Murzin AG. 1993. Sweet-tasting protein monellin is related to the cystatin family of thiol proteinase inhibitors. J Mol Biol 230:689-694.
    • (1993) J Mol Biol , vol.230 , pp. 689-694
    • Murzin, A.G.1
  • 67
    • 0020677388 scopus 로고
    • Primary structures of bovine liver low molecular weight kininogen precursors and their two mRNAs
    • Nawa H, Kitamura N, Hirose T, Asai M, Inayama S, Nakanishi S. 1983. Primary structures of bovine liver low molecular weight kininogen precursors and their two mRNAs. Proc Natl Acad Sci USA 80:90-94.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 90-94
    • Nawa, H.1    Kitamura, N.2    Hirose, T.3    Asai, M.4    Inayama, S.5    Nakanishi, S.6
  • 68
    • 0024349862 scopus 로고
    • Studies on the reactive site of the cystatin superfamily using recombinant cystatin A mutants. Evidence that the QVVAG region is not essential for cysteine proteinase inhibitory activities
    • Nikawa T, Towatari T, Ike Y, Katunuma N. 1989. Studies on the reactive site of the cystatin superfamily using recombinant cystatin A mutants. Evidence that the QVVAG region is not essential for cysteine proteinase inhibitory activities. FEBS Lett 255:309-314.
    • (1989) FEBS Lett , vol.255 , pp. 309-314
    • Nikawa, T.1    Towatari, T.2    Ike, Y.3    Katunuma, N.4
  • 69
    • 0023660834 scopus 로고
    • Crystal structure of the intensely sweet protein monellin
    • Ogata C, Harada M, Tomlinson G, Shin WC, Kim SH. 1987. Crystal structure of the intensely sweet protein monellin. Nature 328:139-142.
    • (1987) Nature , vol.328 , pp. 139-142
    • Ogata, C.1    Harada, M.2    Tomlinson, G.3    Shin, W.C.4    Kim, S.H.5
  • 70
    • 0021676017 scopus 로고
    • Isolation of a human cDNA for a-thiol proteinase inhibitor and its identity with low molecular weight kininogen
    • Ohkubo I, Kurachi K, Takasawa T, Shiokawa H, Sasaki M. 1984. Isolation of a human cDNA for a-thiol proteinase inhibitor and its identity with low molecular weight kininogen. Biochemistry 23:5691-5697.
    • (1984) Biochemistry , vol.23 , pp. 5691-5697
    • Ohkubo, I.1    Kurachi, K.2    Takasawa, T.3    Shiokawa, H.4    Sasaki, M.5
  • 72
    • 0006615873 scopus 로고
    • Structural model of human ceruloplasmin based on internal triplication, hydrophilic/hydrophobic character, and secondary structure of domains
    • Ortel TL, Takahashi N, Putnam FW. 1984. Structural model of human ceruloplasmin based on internal triplication, hydrophilic/hydrophobic character, and secondary structure of domains. Proc Natl Acad Sci USA 81:4761-4765.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 4761-4765
    • Ortel, T.L.1    Takahashi, N.2    Putnam, F.W.3
  • 73
    • 0023223411 scopus 로고
    • Four Ia invariant chain forms derive from a single gene by alternative splicing and alternative initiation of transcription/translation
    • O'Sullivan DM, Noonan D, Quaranta V. 1987. Four Ia invariant chain forms derive from a single gene by alternative splicing and alternative initiation of transcription/translation. J Exp Med 166:444-460.
    • (1987) J Exp Med , vol.166 , pp. 444-460
    • O'Sullivan, D.M.1    Noonan, D.2    Quaranta, V.3
  • 74
    • 0017803863 scopus 로고
    • Testosterone regulates the synthesis of major proteins in rat ventral prostate
    • Parker MG, Scrace GT, Mainwaring WIA. 1978. Testosterone regulates the synthesis of major proteins in rat ventral prostate. Biochem J 170:115-121.
    • (1978) Biochem J , vol.170 , pp. 115-121
    • Parker, M.G.1    Scrace, G.T.2    Mainwaring, W.I.A.3
  • 75
    • 84946989447 scopus 로고
    • Fetuin, a new globulin isolated from serum
    • Pedersen KO. 1994. Fetuin, a new globulin isolated from serum. Nature 154:575.
    • (1994) Nature , vol.154 , pp. 575
    • Pedersen, K.O.1
  • 78
    • 0025022426 scopus 로고
    • Evolution of proteins of the cystatin superfamily
    • Rawlings ND, Barrett AJ. 1990. Evolution of proteins of the cystatin superfamily. J Mol Evol 30:60-11.
    • (1990) J Mol Evol , vol.30 , pp. 60-111
    • Rawlings, N.D.1    Barrett, A.J.2
  • 79
    • 0023656183 scopus 로고
    • Amino acid sequence of a cystatin from venom of the African puff adder (Bitis arietans)
    • Ritonja A, Evans HJ, Machleidt W, Barrett AJ. 1987. Amino acid sequence of a cystatin from venom of the African puff adder (Bitis arietans). Biochem J 246:799-802.
    • (1987) Biochem J , vol.246 , pp. 799-802
    • Ritonja, A.1    Evans, H.J.2    Machleidt, W.3    Barrett, A.J.4
  • 80
    • 0028938024 scopus 로고
    • Three members of the human cystatin gene superfamily, AHSG, HRG, and KNG, map within one megabase of genomic DNA at 3q27
    • Rizzu P, Baldini A. 1995. Three members of the human cystatin gene superfamily, AHSG, HRG, and KNG, map within one megabase of genomic DNA at 3q27. Cytogenet Cell Genet 70:26-28.
    • (1995) Cytogenet Cell Genet , vol.70 , pp. 26-28
    • Rizzu, P.1    Baldini, A.2
  • 81
    • 0025109431 scopus 로고
    • Inhibition of cysteine proteinases by a protein inhibitor from potato
    • Rowan AD, Brzin J, Buttle DJ, Barret AJ. 1990. Inhibition of cysteine proteinases by a protein inhibitor from potato. FEBS Lett 269:328-330.
    • (1990) FEBS Lett , vol.269 , pp. 328-330
    • Rowan, A.D.1    Brzin, J.2    Buttle, D.J.3    Barret, A.J.4
  • 83
    • 0022555509 scopus 로고
    • Human low-Mr kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases
    • Salvesen G, Parkes C, Abrahamson M, Grubb A, Barrett AJ. 1986. Human low-Mr kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases. Biochem J 234:429-434.
    • (1986) Biochem J , vol.234 , pp. 429-434
    • Salvesen, G.1    Parkes, C.2    Abrahamson, M.3    Grubb, A.4    Barrett, A.J.5
  • 84
    • 0028038951 scopus 로고
    • MHC class II antigen processing: Biology of invariant chain
    • Sant AJ, Miller J. 1994. MHC class II antigen processing: Biology of invariant chain. Curr Opin Immunol 6:57-63.
    • (1994) Curr Opin Immunol , vol.6 , pp. 57-63
    • Sant, A.J.1    Miller, J.2
  • 85
    • 0027171758 scopus 로고
    • Determination of the disulphide bridge arrangement of bovine histidine-rich glycoprotein
    • Sorensen CB, Krogh-Pedersen H, Petersen TE. 1993. Determination of the disulphide bridge arrangement of bovine histidine-rich glycoprotein. FEBS Lett 325:285-290.
    • (1993) FEBS Lett , vol.325 , pp. 285-290
    • Sorensen, C.B.1    Krogh-Pedersen, H.2    Petersen, T.E.3
  • 86
    • 0023054136 scopus 로고
    • Alternative splicing and alternative initiation of transplantation explain the four forms of Ia antigen-associated invariant chain
    • Strubin M, Berte C, Mach B. 1986. Alternative splicing and alternative initiation of transplantation explain the four forms of Ia antigen-associated invariant chain. EMBO J 5:3483-3488.
    • (1986) EMBO J , vol.5 , pp. 3483-3488
    • Strubin, M.1    Berte, C.2    Mach, B.3
  • 87
    • 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 MT, Laber B, Bode W, Huber R, Jerala R, Lenarcic B, Turk V. 1990. 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 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
  • 89
    • 0022002505 scopus 로고
    • A new function of kininogens as thiol-proteinase inhibitors: Inhibition of papain and cathepsins B, H and L by bovine, rat and human plasma kininogens
    • Sueyoshi T, Enjyoji K-I, Shimada T, Kato H, Iwanaga S, Bando Y, Kominami E, Katunuma N. 1985. A new function of kininogens as thiol-proteinase inhibitors: Inhibition of papain and cathepsins B, H and L by bovine, rat and human plasma kininogens. FEBS Lett 182:193-195.
    • (1985) FEBS Lett , vol.182 , pp. 193-195
    • Sueyoshi, T.1    Enjyoji, K.-I.2    Shimada, T.3    Kato, H.4    Iwanaga, S.5    Bando, Y.6    Kominami, E.7    Katunuma, N.8
  • 90
    • 0022432076 scopus 로고
    • Purification and characterization of an inhibitor of the cysteine protease from the hemolymph of Sarcophaga peregrina larvae
    • Suzuki T, Natori S. 1985. Purification and characterization of an inhibitor of the cysteine protease from the hemolymph of Sarcophaga peregrina larvae. J Biol Chem 260:5115-5120.
    • (1985) J Biol Chem , vol.260 , pp. 5115-5120
    • Suzuki, T.1    Natori, S.2
  • 91
    • 0028895217 scopus 로고
    • Solution structure of a human cystatin A variant, cystatin A2-98 M65L, by NMR spectroscopy. A possible role of the interactions between N- and C-termini to maintain the inhibitory active form of cystatin A
    • Tate S, Ushioda T, Utsunomiya-Tate N, Shibuya K, Ohyama Y, Nakano Y, Kaji H, Inagaki F, Samejima T, Kainosho M. 1995. Solution structure of a human cystatin A variant, cystatin A2-98 M65L, by NMR spectroscopy. A possible role of the interactions between N-and C-termini to maintain the inhibitory active form of cystatin A. Biochemistry 34:14637-14648.
    • (1995) Biochemistry , vol.34 , pp. 14637-14648
    • Tate, S.1    Ushioda, T.2    Utsunomiya-Tate, N.3    Shibuya, K.4    Ohyama, Y.5    Nakano, Y.6    Kaji, H.7    Inagaki, F.8    Samejima, T.9    Kainosho, M.10
  • 92
    • 0027967160 scopus 로고
    • The human type 2 cystatin gene family consists of eight to nine members, with at least seven genes clustered at a single locus on human chromosome 20
    • Thiesse M, Millar SJ, Dickinson DP. 1994. The human type 2 cystatin gene family consists of eight to nine members, with at least seven genes clustered at a single locus on human chromosome 20. DNA Cell Biol 13:97-116.
    • (1994) DNA Cell Biol , vol.13 , pp. 97-116
    • Thiesse, M.1    Millar, S.J.2    Dickinson, D.P.3
  • 94
    • 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
  • 95
    • 0027691245 scopus 로고
    • Characterization of a genomic sequence coding for potato multicystatin, an eight-domain cysteine proteinase inhibitor
    • Waldron C, Wegrich LM, Merlo PA, Walsh TA. 1993. Characterization of a genomic sequence coding for potato multicystatin, an eight-domain cysteine proteinase inhibitor. Plant Mol Biol 23:801-812.
    • (1993) Plant Mol Biol , vol.23 , pp. 801-812
    • Waldron, C.1    Wegrich, L.M.2    Merlo, P.A.3    Walsh, T.A.4
  • 96
    • 0027740380 scopus 로고
    • Proteolysis of the 85-kilodalton crystalline cysteine proteinase inhibitor from potato releases functional cystatin domains
    • Walsh TA, Strickland JA. 1993. Proteolysis of the 85-kilodalton crystalline cysteine proteinase inhibitor from potato releases functional cystatin domains. Plant Physiol 103:1227-1234.
    • (1993) Plant Physiol , vol.103 , pp. 1227-1234
    • Walsh, T.A.1    Strickland, J.A.2
  • 97
    • 0025219724 scopus 로고
    • Tissue-specific expression and androgen regulation of different genes encoding rat prostatic 22-kilodalton glycoproteins homologous to human and rat cystatin
    • Winderickx J, Hemschoote K, De Clercq N, Van Dijck P, Peeters B, Rombauts W, Verhoeven G, Heyns W. 1990. Tissue-specific expression and androgen regulation of different genes encoding rat prostatic 22-kilodalton glycoproteins homologous to human and rat cystatin. Mol Endocrinol 4:657-667.
    • (1990) Mol Endocrinol , vol.4 , pp. 657-667
    • Winderickx, J.1    Hemschoote, K.2    De Clercq, N.3    Van Dijck, P.4    Peeters, B.5    Rombauts, W.6    Verhoeven, G.7    Heyns, W.8
  • 99
    • 0026457935 scopus 로고
    • Primary structure of the antihemorrhagic factor in serum of the Japanese Habu: A snake venom metalloproteinase inhibitor with a double-headed cystatin domain
    • Yamakawa Y, Omori-Satoh T. 1992. Primary structure of the antihemorrhagic factor in serum of the Japanese Habu: A snake venom metalloproteinase inhibitor with a double-headed cystatin domain. J Biochem 112:583-589.
    • (1992) J Biochem , vol.112 , pp. 583-589
    • Yamakawa, Y.1    Omori-Satoh, T.2
  • 100
    • 0027249330 scopus 로고
    • Isolation and characterization of mouse countertrypsin, a new trypsin inhibitor belonging to the mammalian fetuin family
    • Yamamoto K, Sinohara H. 1993. Isolation and characterization of mouse countertrypsin, a new trypsin inhibitor belonging to the mammalian fetuin family. J Biol Chem 268:17750-17753.
    • (1993) J Biol Chem , vol.268 , pp. 17750-17753
    • Yamamoto, K.1    Sinohara, H.2


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