메뉴 건너뛰기




Volumn 28, Issue 1, 2003, Pages 32-40

Structure, mechanism and regulation of peroxiredoxins

Author keywords

[No Author keywords available]

Indexed keywords

ABRIN; ANTIOXIDANT; CYCLOPHILIN; CYSTEINE; CYTOKINE; DIMER; DNA; ENZYME; HEME; HEPARIN; LIGAND; OLIGOMER; PEROXIDE; PEROXIREDOXIN; PRESENILIN 1; SULFENIC ACID DERIVATIVE; THIOL; UBIQUITIN;

EID: 0037222255     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(02)00003-8     Document Type: Review
Times cited : (2238)

References (56)
  • 1
    • 0028226006 scopus 로고
    • Cloning and sequencing of thiol-specific antioxidant from mammalian brain: Alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes
    • Chae H.Z., et al. Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes. Proc. Natl Acad. Sci. USA. 91:1994;7017-7021.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 7017-7021
    • Chae, H.Z.1
  • 2
    • 0028072911 scopus 로고
    • Thioredoxin-dependent peroxide reductase from yeast
    • Chae H.Z., et al. Thioredoxin-dependent peroxide reductase from yeast. J. Biol. Chem. 269:1994;27670-27678.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27670-27678
    • Chae, H.Z.1
  • 3
    • 0036249816 scopus 로고    scopus 로고
    • Peroxiredoxins
    • Hofmann B., et al. Peroxiredoxins. Biol. Chem. 383:2002;347-364.
    • (2002) Biol. Chem. , vol.383 , pp. 347-364
    • Hofmann, B.1
  • 4
    • 0024599904 scopus 로고
    • An alkyl hydroperoxide reductase from Salmonella typhimurium involved in the defense of DNA against oxidative damage. Purification and properties
    • Jacobson F.S., et al. An alkyl hydroperoxide reductase from Salmonella typhimurium involved in the defense of DNA against oxidative damage. Purification and properties. J. Biol. Chem. 264:1989;1488-1496.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1488-1496
    • Jacobson, F.S.1
  • 5
    • 0030032612 scopus 로고    scopus 로고
    • Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 1. Purification and enzymatic activities of overexpressed AhpF and AhpC proteins
    • Poole L.B., Ellis H.R. Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 1. Purification and enzymatic activities of overexpressed AhpF and AhpC proteins. Biochemistry. 35:1996;56-64.
    • (1996) Biochemistry , vol.35 , pp. 56-64
    • Poole, L.B.1    Ellis, H.R.2
  • 6
    • 0034648827 scopus 로고    scopus 로고
    • Peroxynitrite reductase activity of bacterial peroxiredoxins
    • Bryk R., et al. Peroxynitrite reductase activity of bacterial peroxiredoxins. Nature. 407:2000;211-215.
    • (2000) Nature , vol.407 , pp. 211-215
    • Bryk, R.1
  • 7
    • 0035425780 scopus 로고    scopus 로고
    • Oxidation of active center cysteine of bovine 1-Cys peroxiredoxin sulfenic acid form by peroxide and peroxynitrite
    • Peshenko I.V., Shichi H. Oxidation of active center cysteine of bovine 1-Cys peroxiredoxin sulfenic acid form by peroxide and peroxynitrite. Free Radic. Biol. Med. 31:2001;292-303.
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 292-303
    • Peshenko, I.V.1    Shichi, H.2
  • 8
    • 0000449332 scopus 로고    scopus 로고
    • Peroxiredoxins in cell signaling and HIV infection
    • C.K. et al. Sen. Academic Press
    • Jin D.-Y., Jeang K.-T. Peroxiredoxins in cell signaling and HIV infection. Sen C.K., et al. Antioxidant and Redox Regulation of Genes. 2000;381-407 Academic Press.
    • (2000) Antioxidant and Redox Regulation of Genes , pp. 381-407
    • Jin, D.-Y.1    Jeang, K.-T.2
  • 9
    • 0030805979 scopus 로고    scopus 로고
    • Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12
    • Link A.J., et al. Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 18:1997;1259-1313.
    • (1997) Electrophoresis , vol.18 , pp. 1259-1313
    • Link, A.J.1
  • 10
    • 0025996014 scopus 로고
    • + transport in erythrocyte membrane vesicles requires a cytoplasmic protein
    • + transport in erythrocyte membrane vesicles requires a cytoplasmic protein. J. Biol. Chem. 266:1991;18964-18968.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18964-18968
    • Moore, R.B.1
  • 11
    • 0001445231 scopus 로고    scopus 로고
    • Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin
    • Chae H.Z., et al. Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin. Diabetes Res. Clin. Pract. 45:1999;101-112.
    • (1999) Diabetes Res. Clin. Pract. , vol.45 , pp. 101-112
    • Chae, H.Z.1
  • 13
    • 0036287739 scopus 로고    scopus 로고
    • Advances in our understanding of peroxiredoxin, a multifunctional, mammalian redox protein
    • Fujii J., Ikeda Y. Advances in our understanding of peroxiredoxin, a multifunctional, mammalian redox protein. Redox Rep. 7:2002;123-130.
    • (2002) Redox Rep. , vol.7 , pp. 123-130
    • Fujii, J.1    Ikeda, Y.2
  • 14
    • 0034673985 scopus 로고    scopus 로고
    • Modulation of the activities of catalase-peroxidase HPI of Escherichia coli by site-directed mutagenesis
    • Hillar A., et al. Modulation of the activities of catalase-peroxidase HPI of Escherichia coli by site-directed mutagenesis. Biochemistry. 39:2000;5868-5875.
    • (2000) Biochemistry , vol.39 , pp. 5868-5875
    • Hillar, A.1
  • 15
    • 0035209075 scopus 로고    scopus 로고
    • Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli
    • Costa Seaver L., Imlay J.A. Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli. J. Bacteriol. 183:2001;7173-7181.
    • (2001) J. Bacteriol. , vol.183 , pp. 7173-7181
    • Costa Seaver, L.1    Imlay, J.A.2
  • 16
    • 0030778083 scopus 로고    scopus 로고
    • Novel application of 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole to identify cysteine sulfenic acid in the AhpC component of alkyl hydroperoxide reductase
    • Ellis H.R., Poole L.B. Novel application of 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole to identify cysteine sulfenic acid in the AhpC component of alkyl hydroperoxide reductase. Biochemistry. 36:1997;15013-15018.
    • (1997) Biochemistry , vol.36 , pp. 15013-15018
    • Ellis, H.R.1    Poole, L.B.2
  • 17
    • 0031945918 scopus 로고    scopus 로고
    • Crystal structure of a novel human peroxidase enzyme at 2.0 Å resolution
    • Choi H.-J., et al. Crystal structure of a novel human peroxidase enzyme at 2.0 Å resolution. Nat. Struct. Biol. 5:1998;400-406.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 400-406
    • Choi, H.-J.1
  • 18
    • 0030822346 scopus 로고    scopus 로고
    • Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella typhimurium
    • Ellis H.R., Poole L.B. Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella typhimurium. Biochemistry. 36:1997;13349-13356.
    • (1997) Biochemistry , vol.36 , pp. 13349-13356
    • Ellis, H.R.1    Poole, L.B.2
  • 19
    • 0033607229 scopus 로고    scopus 로고
    • Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product
    • Hirotsu S., et al. Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product. Proc. Natl Acad. Sci. USA. 96:1999;12333-12338.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 12333-12338
    • Hirotsu, S.1
  • 20
    • 0343953384 scopus 로고    scopus 로고
    • Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 Å resolution
    • Schröder E., et al. Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 Å resolution. Structure. 8:2000;605-615.
    • (2000) Structure , vol.8 , pp. 605-615
    • Schröder, E.1
  • 21
    • 0034697984 scopus 로고    scopus 로고
    • The structure of reduced tryparedoxin peroxidase reveals a decamer and insight into reactivity of 2Cys-peroxiredoxins
    • Alphey M.S., et al. The structure of reduced tryparedoxin peroxidase reveals a decamer and insight into reactivity of 2Cys-peroxiredoxins. J. Mol. Biol. 300:2000;903-916.
    • (2000) J. Mol. Biol. , vol.300 , pp. 903-916
    • Alphey, M.S.1
  • 22
    • 0037197672 scopus 로고    scopus 로고
    • Dimers to doughnuts: Redox-sensitive oligomerization of 2-cysteine peroxiredoxins
    • Wood Z.A., et al. Dimers to doughnuts: redox-sensitive oligomerization of 2-cysteine peroxiredoxins. Biochemistry. 41:2002;5493-5504.
    • (2002) Biochemistry , vol.41 , pp. 5493-5504
    • Wood, Z.A.1
  • 23
    • 0030861413 scopus 로고    scopus 로고
    • A unique cascade of oxidoreductases catalyses trypanothione-mediated peroxide metabolism in Crithidia fasciculata
    • Nogoceke E., et al. A unique cascade of oxidoreductases catalyses trypanothione-mediated peroxide metabolism in Crithidia fasciculata. Biol. Chem. 378:1997;827-836.
    • (1997) Biol. Chem. , vol.378 , pp. 827-836
    • Nogoceke, E.1
  • 24
    • 0033771859 scopus 로고    scopus 로고
    • r thioredoxin reductase
    • r thioredoxin reductase. Eur. J. Biochem. 267:2000;6126-6133.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6126-6133
    • Poole, L.B.1
  • 25
    • 0037039818 scopus 로고    scopus 로고
    • Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein
    • Bryk R., et al. Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein. Science. 295:2002;1073-1077.
    • (2002) Science , vol.295 , pp. 1073-1077
    • Bryk, R.1
  • 26
    • 0001015125 scopus 로고    scopus 로고
    • Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate
    • Seo M.S., et al. Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate. J. Biol. Chem. 275:2000;20346-20354.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20346-20354
    • Seo, M.S.1
  • 27
    • 0035943382 scopus 로고    scopus 로고
    • Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 angstrom resolution
    • Declercq J.P., et al. Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 angstrom resolution. J. Mol. Biol. 311:2001;751-759.
    • (2001) J. Mol. Biol. , vol.311 , pp. 751-759
    • Declercq, J.P.1
  • 28
    • 0033597885 scopus 로고    scopus 로고
    • Phospholipid hydroperoxides are substrates for non-selenium glutathione peroxidase
    • Fisher A.B., et al. Phospholipid hydroperoxides are substrates for non-selenium glutathione peroxidase. J. Biol. Chem. 274:1999;21326-21334.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21326-21334
    • Fisher, A.B.1
  • 29
    • 0035839494 scopus 로고    scopus 로고
    • Cyclophilin A binds to peroxiredoxins and activates its peroxidase activity
    • Lee S.P., et al. Cyclophilin A binds to peroxiredoxins and activates its peroxidase activity. J. Biol. Chem. 276:2001;29826-29832.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29826-29832
    • Lee, S.P.1
  • 30
    • 0014675209 scopus 로고
    • Some negative contrast staining features of a protein from erythrocyte ghosts
    • Harris J.R. Some negative contrast staining features of a protein from erythrocyte ghosts. J. Mol. Biol. 46:1969;329-335.
    • (1969) J. Mol. Biol. , vol.46 , pp. 329-335
    • Harris, J.R.1
  • 31
    • 0021930684 scopus 로고
    • Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium
    • Christman M.F., et al. Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium. Cell. 41:1985;753-762.
    • (1985) Cell , vol.41 , pp. 753-762
    • Christman, M.F.1
  • 32
    • 0023929362 scopus 로고
    • 2 mixed-function oxidation system
    • 2 mixed-function oxidation system. J. Biol. Chem. 263:1988;4704-4711.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4704-4711
    • Kim, K.1
  • 33
    • 0035844694 scopus 로고    scopus 로고
    • Comparison of the decameric structure of peroxiredoxin-II by transmission electron microscopy and X-ray crystallography
    • Harris J.R., et al. Comparison of the decameric structure of peroxiredoxin-II by transmission electron microscopy and X-ray crystallography. Biochim. Biophys. Acta. 1547:2001;221-234.
    • (2001) Biochim. Biophys. Acta , vol.1547 , pp. 221-234
    • Harris, J.R.1
  • 34
    • 0001084370 scopus 로고
    • Cylinder protein isolated from rat liver mitochondria
    • Kato H., et al. Cylinder protein isolated from rat liver mitochondria. Zool. Sci. 2:1985;485-490.
    • (1985) Zool. Sci. , vol.2 , pp. 485-490
    • Kato, H.1
  • 35
    • 0028260177 scopus 로고
    • Purification and characterization of a substrate protein for mitochondrial ATP-dependent protease in bovine adrenal cortex
    • Watabe S., et al. Purification and characterization of a substrate protein for mitochondrial ATP-dependent protease in bovine adrenal cortex. J. Biochem. (Tokyo). 115:1994;648-654.
    • (1994) J. Biochem. (Tokyo) , vol.115 , pp. 648-654
    • Watabe, S.1
  • 36
    • 0032473915 scopus 로고    scopus 로고
    • Porcine natural-killer-enhancing factor-B: Oligomerisation and identification as a calpain substrate in vitro
    • Schröder E., et al. Porcine natural-killer-enhancing factor-B: oligomerisation and identification as a calpain substrate in vitro. Biochim. Biophys. Acta. 1383:1998;279-291.
    • (1998) Biochim. Biophys. Acta , vol.1383 , pp. 279-291
    • Schröder, E.1
  • 37
    • 0032817414 scopus 로고    scopus 로고
    • Stimulation of peroxidase activity by decamerization related to ionic strength: AhpC protein from Amphibacillus xylanus
    • Kitano K., et al. Stimulation of peroxidase activity by decamerization related to ionic strength: AhpC protein from Amphibacillus xylanus. J. Biochem. (Tokyo). 126:1999;313-319.
    • (1999) J. Biochem. (Tokyo) , vol.126 , pp. 313-319
    • Kitano, K.1
  • 38
    • 0034730630 scopus 로고    scopus 로고
    • Cloning, over-expression and characterization of peroxiredoxin and NADH-peroxiredoxin reductase from Thermus aquaticus YT-1
    • Logan C., Mayhew S.G. Cloning, over-expression and characterization of peroxiredoxin and NADH-peroxiredoxin reductase from Thermus aquaticus YT-1. J. Biol. Chem. 275:2000;30019-30028.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30019-30028
    • Logan, C.1    Mayhew, S.G.2
  • 39
    • 0035865583 scopus 로고    scopus 로고
    • Characterization of the Mycobacterium tuberculosis H37Rv alkyl hydroperoxidase AhpC points to the importance of ionic interactions in oligomerization and activity
    • Chauhan R., Mande S.C. Characterization of the Mycobacterium tuberculosis H37Rv alkyl hydroperoxidase AhpC points to the importance of ionic interactions in oligomerization and activity. Biochem. J. 354:2001;209-215.
    • (2001) Biochem. J. , vol.354 , pp. 209-215
    • Chauhan, R.1    Mande, S.C.2
  • 40
    • 0033584454 scopus 로고    scopus 로고
    • Properties of thiol-specific anti-oxidant protein or calpromotin in solution
    • Kristensen P., et al. Properties of thiol-specific anti-oxidant protein or calpromotin in solution. Biochem. Biophys. Res. Commun. 262:1999;127-131.
    • (1999) Biochem. Biophys. Res. Commun. , vol.262 , pp. 127-131
    • Kristensen, P.1
  • 41
    • 0018761655 scopus 로고
    • Calcium-induced erythrocyte membrane changes. The role of adsorption of cytosol proteins and proteases
    • Allen D.W., Cadman S. Calcium-induced erythrocyte membrane changes. The role of adsorption of cytosol proteins and proteases. Biochim. Biophys. Acta. 551:1979;1-9.
    • (1979) Biochim. Biophys. Acta , vol.551 , pp. 1-9
    • Allen, D.W.1    Cadman, S.2
  • 42
    • 0026795940 scopus 로고
    • Calcium-activated potassium transport and high molecular weight forms of calpromotin
    • Plishker G.A., et al. Calcium-activated potassium transport and high molecular weight forms of calpromotin. J. Biol. Chem. 267:1992;21839-21843.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21839-21843
    • Plishker, G.A.1
  • 43
    • 0037065722 scopus 로고    scopus 로고
    • An NADH-dependent bacterial thioredoxin reductase-like protein, in conjunction with a glutaredoxin homologue, form a unique peroxiredoxin (AhpC) reducing system in Clostridium pasteurianum
    • Reynolds C.M., et al. An NADH-dependent bacterial thioredoxin reductase-like protein, in conjunction with a glutaredoxin homologue, form a unique peroxiredoxin (AhpC) reducing system in Clostridium pasteurianum. Biochemistry. 41:2002;1990-2001.
    • (2002) Biochemistry , vol.41 , pp. 1990-2001
    • Reynolds, C.M.1
  • 44
    • 0037082141 scopus 로고    scopus 로고
    • Tryparedoxin peroxidase of Leishmania donovani: Molecular cloning, heterologous expression, specificity and catalytic mechanism
    • Flohé L., et al. Tryparedoxin peroxidase of Leishmania donovani: molecular cloning, heterologous expression, specificity and catalytic mechanism. Arch. Biochem. Biophys. 397:2002;324-335.
    • (2002) Arch. Biochem. Biophys. , vol.397 , pp. 324-335
    • Flohé, L.1
  • 45
    • 0033200161 scopus 로고    scopus 로고
    • Activation of active-site cysteine residues in the peroxiredoxin-type tryparedoxin peroxidase of Crithidia fasciculata
    • Montemartini M., et al. Activation of active-site cysteine residues in the peroxiredoxin-type tryparedoxin peroxidase of Crithidia fasciculata. Eur. J. Biochem. 264:1999;516-524.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 516-524
    • Montemartini, M.1
  • 46
    • 0012326355 scopus 로고    scopus 로고
    • Flavin-linked redox components required for AhpC reduction in alkyl hydroperoxide reductase systems
    • S. et al. Ghisla. Agency for Scientific Publications
    • Poole L.B. Flavin-linked redox components required for AhpC reduction in alkyl hydroperoxide reductase systems. Ghisla S., et al. Flavins and Flavoproteins 1999. 1999;691-694 Agency for Scientific Publications.
    • (1999) Flavins and Flavoproteins 1999 , pp. 691-694
    • Poole, L.B.1
  • 47
    • 0035868551 scopus 로고    scopus 로고
    • Variants of peroxiredoxins expression in response to hydroperoxide stress
    • Mitsumoto A., et al. Variants of peroxiredoxins expression in response to hydroperoxide stress. Free Radic. Biol. Med. 30:2001;625-635.
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 625-635
    • Mitsumoto, A.1
  • 48
    • 0037106326 scopus 로고    scopus 로고
    • A method for detection of overoxidation of cysteine: Peroxiredoxins are oxidised in vivo at the active site cysteine during oxidative stress
    • Wagner E., et al. A method for detection of overoxidation of cysteine: peroxiredoxins are oxidised in vivo at the active site cysteine during oxidative stress. Biochem. J. 366:2002;777-785.
    • (2002) Biochem. J. , vol.366 , pp. 777-785
    • Wagner, E.1
  • 49
    • 0037082137 scopus 로고    scopus 로고
    • Regulation of thioredoxin peroxidase activity by C-terminal truncation
    • Koo K.H., et al. Regulation of thioredoxin peroxidase activity by C-terminal truncation. Arch. Biochem. Biophys. 397:2002;312-318.
    • (2002) Arch. Biochem. Biophys. , vol.397 , pp. 312-318
    • Koo, K.H.1
  • 50
    • 0033598677 scopus 로고    scopus 로고
    • Protein-sulfenic acids: Diverse roles for an unlikely player in enzyme catalysis and redox regulation
    • Claiborne A., et al. Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation. Biochemistry. 38:1999;15407-15416.
    • (1999) Biochemistry , vol.38 , pp. 15407-15416
    • Claiborne, A.1
  • 51
    • 0037205455 scopus 로고    scopus 로고
    • Proteomics analysis of cellular response to oxidative stress: Evidence for in vivo over-oxidation of peroxiredoxins at their active site
    • Rabilloud T., et al. Proteomics analysis of cellular response to oxidative stress: evidence for in vivo over-oxidation of peroxiredoxins at their active site. J. Biol. Chem. 277:2002;19396-19401.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19396-19401
    • Rabilloud, T.1
  • 52
    • 0037067763 scopus 로고    scopus 로고
    • Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation
    • Chang T.S., et al. Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation. J. Biol. Chem. 277:2002;25370-25376.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25370-25376
    • Chang, T.S.1
  • 53
    • 0034643923 scopus 로고    scopus 로고
    • Interaction of human thiol-specific antioxidant protein 1 with erythrocyte plasma membrane
    • Cha M.-K., et al. Interaction of human thiol-specific antioxidant protein 1 with erythrocyte plasma membrane. Biochemistry. 39:2000;6944-6950.
    • (2000) Biochemistry , vol.39 , pp. 6944-6950
    • Cha, M.-K.1
  • 54
    • 0036013787 scopus 로고    scopus 로고
    • Routine preparation of air-dried negatively stained and unstained specimens on holey carbon support films: A review of applications
    • Harris J.R., Scheffler D. Routine preparation of air-dried negatively stained and unstained specimens on holey carbon support films: a review of applications. Micron. 33:2002;461-480.
    • (2002) Micron , vol.33 , pp. 461-480
    • Harris, J.R.1    Scheffler, D.2
  • 55
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:1991;946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 56
    • 0032917069 scopus 로고    scopus 로고
    • Protein structural topology: Automated analysis, diagrammatic representation and database searching
    • Westhead D.R., et al. Protein structural topology: automated analysis, diagrammatic representation and database searching. Protein Sci. 8:1999;897-904.
    • (1999) Protein Sci. , vol.8 , pp. 897-904
    • Westhead, D.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.