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Volumn 8, Issue 2, 1999, Pages 430-434

Variants of ribonuclease inhibitor that resist oxidation

Author keywords

Angiogenin; cis peptide bond; Cysteine; Cystine; Disulfide bond; Leucine rich repeat; Protein stability; Ribonuclease A

Indexed keywords

ALANINE; CYSTEINE; CYSTINE; CYTOSKELETON PROTEIN; PANCREATIC RIBONUCLEASE; RIBONUCLEASE; RIBONUCLEASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 0033042937     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.2.430     Document Type: Article
Times cited : (36)

References (34)
  • 1
    • 0019881267 scopus 로고
    • Activation of latent ribonuclease in the fat-body of fleshfly (Sarcophaga peregrina) larvae on pupation
    • Aoki Y, Natori S. 1981. Activation of latent ribonuclease in the fat-body of fleshfly (Sarcophaga peregrina) larvae on pupation. J Biochem (Tokyo) 196:699-703.
    • (1981) J Biochem (Tokyo) , vol.196 , pp. 699-703
    • Aoki, Y.1    Natori, S.2
  • 2
    • 77956940788 scopus 로고
    • Pancreatic ribonuclease
    • Blackburn P, Moore S. 1982. Pancreatic ribonuclease. Enzymes XV:317-433.
    • (1982) Enzymes , vol.15 , pp. 317-433
    • Blackburn, P.1    Moore, S.2
  • 3
    • 0028382370 scopus 로고
    • The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues
    • Blake CCF, Ghosh M, Harlos K, Avezoux A, Anthony C. 1994. The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues. Nat Struct Biol 1:102-105; 557.
    • (1994) Nat Struct Biol , vol.1 , pp. 102-105
    • Blake, C.C.F.1    Ghosh, M.2    Harlos, K.3    Avezoux, A.4    Anthony, C.5
  • 4
    • 0029768918 scopus 로고    scopus 로고
    • Oxidation of sulfhydryl groups of ribonuclease inhibitor in epithelial cells is sufficient for its intracellular degradation
    • Blázuez M, Fominaya JM, Hofsteenge J. 1996. Oxidation of sulfhydryl groups of ribonuclease inhibitor in epithelial cells is sufficient for its intracellular degradation. J Biol Chem 271:18638-18642.
    • (1996) J Biol Chem , vol.271 , pp. 18638-18642
    • Blázuez, M.1    Fominaya, J.M.2    Hofsteenge, J.3
  • 5
    • 0001582892 scopus 로고
    • Structure of a cis-peptide unit: Molecular conformation of the cyclic disulphide L-cysteinyl-L-cysteine
    • Capasso S, Mattia C, Mazzarella L. 1977. Structure of a cis-peptide unit: Molecular conformation of the cyclic disulphide L-cysteinyl-L-cysteine. Acta Crystallogr B33:2080-2083.
    • (1977) Acta Crystallogr , vol.B33 , pp. 2080-2083
    • Capasso, S.1    Mattia, C.2    Mazzarella, L.3
  • 6
    • 0029032586 scopus 로고
    • Engineering ribonuclease A: Production, purification, and characterization of wild-type enzyme and mutants at Gln11
    • delCardayré SB, Ribó M, Yokel EM, Quirk DJ, Rutter WJ, Raines RT. 1995. Engineering ribonuclease A: Production, purification, and characterization of wild-type enzyme and mutants at Gln11. Protein Eng 8:261-273.
    • (1995) Protein Eng , vol.8 , pp. 261-273
    • DelCardayré, S.B.1    Ribó, M.2    Yokel, E.M.3    Quirk, D.J.4    Rutter, W.J.5    Raines, R.T.6
  • 8
    • 0023707101 scopus 로고
    • Theoretical treatment of tight-binding inhibition of an enzyme. Ribonuclease inhibitor as a special case
    • Fominaya J, García-Segura JM, Ferreras M, Gavilanes JG. 1988. Theoretical treatment of tight-binding inhibition of an enzyme. Ribonuclease inhibitor as a special case. Biochem J 253:517-522.
    • (1988) Biochem J , vol.253 , pp. 517-522
    • Fominaya, J.1    García-Segura, J.M.2    Ferreras, M.3    Gavilanes, J.G.4
  • 9
    • 0026470181 scopus 로고
    • Inactivation of ribonuclease inhibitor by thiol-disulfide exchange
    • Fominaya JM, Hofsteenge J. 1992. Inactivation of ribonuclease inhibitor by thiol-disulfide exchange. J Biol Chem 267:24655-24660.
    • (1992) J Biol Chem , vol.267 , pp. 24655-24660
    • Fominaya, J.M.1    Hofsteenge, J.2
  • 10
    • 25344444823 scopus 로고
    • Solution conformations of the cyclic Cys=Cys disulfide structural motif
    • Hodges RS, Smith JAs, eds. (ESCOM, 1994). Norwell, MA: Kluwer Academic
    • García-Echeverría C, Rich DH. 1994. Solution conformations of the cyclic Cys=Cys disulfide structural motif. In Hodges RS, Smith JAs, eds. Proceedings of the thirteenth American peptide symposium (ESCOM, 1994). Norwell, MA: Kluwer Academic. pp 782-784.
    • (1994) Proceedings of the Thirteenth American Peptide Symposium , pp. 782-784
    • García-Echeverría, C.1    Rich, D.H.2
  • 11
    • 0032079381 scopus 로고    scopus 로고
    • Structure determination of the three-disulfide bond isomers of alpha-conotoxin GI: A model tor the role of disulfide bonds in structural stability
    • Gehrmann J, Alewood PF, Craik DJ. 1998. Structure determination of the three-disulfide bond isomers of alpha-conotoxin GI: A model tor the role of disulfide bonds in structural stability. J Mol Biol 278:401-415.
    • (1998) J Mol Biol , vol.278 , pp. 401-415
    • Gehrmann, J.1    Alewood, P.F.2    Craik, D.J.3
  • 12
    • 0002130286 scopus 로고    scopus 로고
    • Ribonuclease inhibitor
    • D'Alessio G, Riordan JF, eds. New York: Academic Press
    • Hofsteenge J. 1997. Ribonuclease inhibitor. In: D'Alessio G, Riordan JF, eds. Ribonucleases: Structures and functions. New York: Academic Press. pp 621-658.
    • (1997) Ribonucleases: Structures and Functions , pp. 621-658
    • Hofsteenge, J.1
  • 13
    • 0027718173 scopus 로고
    • Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats
    • Kobe B, Deisenhofer J. 1993. Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats. Nature 366:751-756.
    • (1993) Nature , vol.366 , pp. 751-756
    • Kobe, B.1    Deisenhofer, J.2
  • 14
    • 0028080261 scopus 로고
    • The leucine-rich repeat: A versatile binding motif
    • Kobe B, Deisenhofer J. 1994. The leucine-rich repeat: A versatile binding motif. Trends Biochem Sci 19:415-421.
    • (1994) Trends Biochem Sci , vol.19 , pp. 415-421
    • Kobe, B.1    Deisenhofer, J.2
  • 15
    • 0028911034 scopus 로고
    • A structural basis of the interactions between leucine-rich repeats and protein ligands
    • Kobe B, Deisenhofer J. 1995. A structural basis of the interactions between leucine-rich repeats and protein ligands. Nature 374:183-186.
    • (1995) Nature , vol.374 , pp. 183-186
    • Kobe, B.1    Deisenhofer, J.2
  • 16
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel TA, Roberts JD, Zakour RA. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol 154:367-382.
    • (1987) Methods Enzymol , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 18
    • 0024496381 scopus 로고
    • Tight-binding inhibition of angiogenin and ribonuclease A by placental ribonuclease inhibitor
    • Lee FS, Shapiro R, Vallee BL. 1989. Tight-binding inhibition of angiogenin and ribonuclease A by placental ribonuclease inhibitor. Biochemistry 28:225-230.
    • (1989) Biochemistry , vol.28 , pp. 225-230
    • Lee, F.S.1    Shapiro, R.2    Vallee, B.L.3
  • 19
    • 0027350918 scopus 로고
    • Structure and action of mammalian ribonuclease (angiogenin) inhibitor
    • Lee FS, Vallee BL. 1993. Structure and action of mammalian ribonuclease (angiogenin) inhibitor. Prog Nucl Acid Res Mol Biol 44:1-30.
    • (1993) Prog Nucl Acid Res Mol Biol , vol.44 , pp. 1-30
    • Lee, F.S.1    Vallee, B.L.2
  • 21
    • 0001250970 scopus 로고
    • Cyclo-L-cystine acetic acid
    • Mez H-C. 1993. Cyclo-L-cystine acetic acid. Cryst Struct Commun 3:657-660.
    • (1993) Cryst Struct Commun , vol.3 , pp. 657-660
    • Mez, H.-C.1
  • 23
    • 0030864496 scopus 로고    scopus 로고
    • Molecular recognition of human angiogenin by placental ribonuclease inhibitor - An X-ray crystallographic study at 2.0 Å resolution
    • Papageorgiou AC, Shapiro R, Acharya KR. 1997. Molecular recognition of human angiogenin by placental ribonuclease inhibitor - An X-ray crystallographic study at 2.0 Å resolution. EMBO J 16:5162-5177.
    • (1997) EMBO J , vol.16 , pp. 5162-5177
    • Papageorgiou, A.C.1    Shapiro, R.2    Acharya, K.R.3
  • 24
    • 0027757087 scopus 로고
    • A ribonuclease inhibitor expresses anti-angiogenic properties and leads to reduced tumor growth in mice
    • Polakowski IJ, Lewis MK, Muthukkaruppan V, Erdman B, Kubai L, Auerbach R. 1993. A ribonuclease inhibitor expresses anti-angiogenic properties and leads to reduced tumor growth in mice. Am J Pathol 143:507-517.
    • (1993) Am J Pathol , vol.143 , pp. 507-517
    • Polakowski, I.J.1    Lewis, M.K.2    Muthukkaruppan, V.3    Erdman, B.4    Kubai, L.5    Auerbach, R.6
  • 25
    • 0030912818 scopus 로고    scopus 로고
    • Nature's transitory covalent bond
    • Raines RT. 1997. Nature's transitory covalent bond. Nat Struct Biol 4:424-427.
    • (1997) Nat Struct Biol , vol.4 , pp. 424-427
    • Raines, R.T.1
  • 26
    • 0001005285 scopus 로고    scopus 로고
    • Ribonuclease A
    • Raines RT. 1998. Ribonuclease A. Chem Rev 98:1045-1065.
    • (1998) Chem Rev , vol.98 , pp. 1045-1065
    • Raines, R.T.1
  • 28
    • 0000238273 scopus 로고
    • Human placental ribonuclease inhibitor abolishes both angiogenic and ribonucleolytic activities of angiogenin
    • Shapiro R, Vallee BL. 1987. Human placental ribonuclease inhibitor abolishes both angiogenic and ribonucleolytic activities of angiogenin. Proc Natl Acad Sci USA 84:2238-2241.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 2238-2241
    • Shapiro, R.1    Vallee, B.L.2
  • 29
    • 0025979460 scopus 로고
    • A molecular constraint that generates a cis peptide bond
    • Sukumaran DK, Prorok M, Lawrence DS. 1991. A molecular constraint that generates a cis peptide bond. J Am Chem Soc 113:706-707.
    • (1991) J Am Chem Soc , vol.113 , pp. 706-707
    • Sukumaran, D.K.1    Prorok, M.2    Lawrence, D.S.3
  • 31
    • 0001273194 scopus 로고
    • Heats of hydrogenation. IV. Hydrogenation of some cis- and trans-cycloölefines
    • Turner RB, Meador WR. 1957. Heats of hydrogenation. IV. Hydrogenation of some cis- and trans-cycloölefines. J Am Chem Soc 79:4133-4136.
    • (1957) J Am Chem Soc , vol.79 , pp. 4133-4136
    • Turner, R.B.1    Meador, W.R.2
  • 32
    • 0025006582 scopus 로고
    • Protein chemical and kinetic characterization of recombinant porcine ribonuclease inhibitor expressed in saccharomyces cerevisiae
    • Vicentini AM, Kieffer B, Mathies R, Meyhack B, Hemmings BA, Stone SR, Hofsteenge J. 1990. Protein chemical and kinetic characterization of recombinant porcine ribonuclease inhibitor expressed in Saccharomyces cerevisiae. Biochemistry 29:8827-8834.
    • (1990) Biochemistry , vol.29 , pp. 8827-8834
    • Vicentini, A.M.1    Kieffer, B.2    Mathies, R.3    Meyhack, B.4    Hemmings, B.A.5    Stone, S.R.6    Hofsteenge, J.7
  • 34
    • 0024428106 scopus 로고
    • Dependence of formation of small disulfide loops in two-cysteine peptides on the number and types of intervening amino acids
    • Zhang R, Snyder GH. 1989. Dependence of formation of small disulfide loops in two-cysteine peptides on the number and types of intervening amino acids. J Biol Chem 264:18472-18479.
    • (1989) J Biol Chem , vol.264 , pp. 18472-18479
    • Zhang, R.1    Snyder, G.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.