메뉴 건너뛰기




Volumn 371, Issue 1, 2007, Pages 93-111

Enzymatic and Structural Characterisation of Amphinase, a Novel Cytotoxic Ribonuclease from Rana pipiens Oocytes

Author keywords

Amphinase; cytotoxic RNase; enzyme efficiency; substrate specificity; X ray crystallography

Indexed keywords

ADENINE; AMINO ACID; AMPHINASE; CYSTEINE; CYTOSINE; GLYCAN; GUANINE; RANPIRNASE; RECOMBINANT ENZYME; RIBONUCLEASE; RIBONUCLEASE A; RIBONUCLEASE INHIBITOR; RNA; SINGLE STRANDED RNA; UNCLASSIFIED DRUG; URACIL;

EID: 34447094846     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.04.071     Document Type: Article
Times cited : (27)

References (79)
  • 2
    • 0001987910 scopus 로고    scopus 로고
    • Evolution of vertebrate ribonucleases: ribonuclease A superfamily
    • D'Alessio G., and Riordan J.F. (Eds), Academic Press, New York
    • Beintema J.J., Breukelman H.J., Carsana A., and Furia A. Evolution of vertebrate ribonucleases: ribonuclease A superfamily. In: D'Alessio G., and Riordan J.F. (Eds). Ribonucleases: Structures and Functions (1997), Academic Press, New York 245-269
    • (1997) Ribonucleases: Structures and Functions , pp. 245-269
    • Beintema, J.J.1    Breukelman, H.J.2    Carsana, A.3    Furia, A.4
  • 4
    • 8444222667 scopus 로고    scopus 로고
    • Human ribonuclease A superfamily members, eosinophil-derived neurotoxin and pancreatic ribonuclease, induce dendritic cell maturation and activation
    • Yang D., Chen Q., Rosenberg H.F., Rybak S.M., Newton D.L., Wang Z.Y., et al. Human ribonuclease A superfamily members, eosinophil-derived neurotoxin and pancreatic ribonuclease, induce dendritic cell maturation and activation. J. Immunol. 173 (2004) 6134-6142
    • (2004) J. Immunol. , vol.173 , pp. 6134-6142
    • Yang, D.1    Chen, Q.2    Rosenberg, H.F.3    Rybak, S.M.4    Newton, D.L.5    Wang, Z.Y.6
  • 5
    • 0003017687 scopus 로고    scopus 로고
    • Antitumour RNases
    • D'Alessio G., and Riodan J.F. (Eds), Academic Press, New York
    • Youle R.J., and D'Alessio G. Antitumour RNases. In: D'Alessio G., and Riodan J.F. (Eds). Ribonucleases: Structures and Functions (1997), Academic Press, New York 491-514
    • (1997) Ribonucleases: Structures and Functions , pp. 491-514
    • Youle, R.J.1    D'Alessio, G.2
  • 6
    • 0035018435 scopus 로고    scopus 로고
    • Cancer chemotherapy-ribonucleases to the rescue
    • Leland P.A., and Raines R.T. Cancer chemotherapy-ribonucleases to the rescue. Chem. Biol. 8 (2001) 405-413
    • (2001) Chem. Biol. , vol.8 , pp. 405-413
    • Leland, P.A.1    Raines, R.T.2
  • 7
    • 0041696477 scopus 로고    scopus 로고
    • Cytotoxic ribonucleases and RNA interference (RNAi)
    • Ardelt B., Ardelt W., and Darzynkiewicz Z. Cytotoxic ribonucleases and RNA interference (RNAi). Cell Cycle 2 (2003) 22-24
    • (2003) Cell Cycle , vol.2 , pp. 22-24
    • Ardelt, B.1    Ardelt, W.2    Darzynkiewicz, Z.3
  • 8
    • 27644542234 scopus 로고    scopus 로고
    • On the track of antitumour ribonucleases
    • Benito A., Ribó M., and Vilanova M. On the track of antitumour ribonucleases. Mol. Biosyst. 1 (2005) 294-302
    • (2005) Mol. Biosyst. , vol.1 , pp. 294-302
    • Benito, A.1    Ribó, M.2    Vilanova, M.3
  • 9
    • 0025960523 scopus 로고
    • Amino acid sequence of an anti-tumor protein from Rana pipiens oocytes and early embryos. Homology to pancreatic ribonucleases
    • Ardelt W., Mikulski S.M., and Shogen K. Amino acid sequence of an anti-tumor protein from Rana pipiens oocytes and early embryos. Homology to pancreatic ribonucleases. J. Biol. Chem. 266 (1991) 245-251
    • (1991) J. Biol. Chem. , vol.266 , pp. 245-251
    • Ardelt, W.1    Mikulski, S.M.2    Shogen, K.3
  • 11
    • 33344475705 scopus 로고    scopus 로고
    • Ribonucleases as a novel pro-apoptotic anticancer strategy: review of the preclinical and clinical data for Ranpirnase
    • Costanzi J., Sidransky D., Navon A., and Goldsweig H. Ribonucleases as a novel pro-apoptotic anticancer strategy: review of the preclinical and clinical data for Ranpirnase. Cancer Invest. 23 (2005) 643-650
    • (2005) Cancer Invest. , vol.23 , pp. 643-650
    • Costanzi, J.1    Sidransky, D.2    Navon, A.3    Goldsweig, H.4
  • 12
    • 33645761337 scopus 로고    scopus 로고
    • Ranpirnase-an antitumour ribonuclease: its potential role in malignant mesothelioma
    • Pavlakis N., and Vogelzang N.J. Ranpirnase-an antitumour ribonuclease: its potential role in malignant mesothelioma. Expert Opin. Biol. Ther. 6 (2006) 391-399
    • (2006) Expert Opin. Biol. Ther. , vol.6 , pp. 391-399
    • Pavlakis, N.1    Vogelzang, N.J.2
  • 13
    • 0000512084 scopus 로고
    • Enzymatic characterization of Onconase, a novel ribonuclease with anti-tumor activity
    • Ardelt W., Lee H.-S., Randolph G., Viera A., Mikulski S.M., and Shogen K. Enzymatic characterization of Onconase, a novel ribonuclease with anti-tumor activity. Protein Sci. 3 (1994) 137
    • (1994) Protein Sci. , vol.3 , pp. 137
    • Ardelt, W.1    Lee, H.-S.2    Randolph, G.3    Viera, A.4    Mikulski, S.M.5    Shogen, K.6
  • 14
    • 0028266432 scopus 로고
    • Refined 1.7 Å X-ray crystallographic structure of P-30 protein, an amphibian ribonuclease with anti-tumor activity
    • Mosimann S.C., Ardelt W., and James M.N.G. Refined 1.7 Å X-ray crystallographic structure of P-30 protein, an amphibian ribonuclease with anti-tumor activity. J. Mol. Biol. 236 (1994) 1141-1153
    • (1994) J. Mol. Biol. , vol.236 , pp. 1141-1153
    • Mosimann, S.C.1    Ardelt, W.2    James, M.N.G.3
  • 15
    • 0141483327 scopus 로고    scopus 로고
    • Contribution of active-site residues to the function of onconase, a ribonuclease with antitumoral activity
    • Lee J.E., and Raines R.T. Contribution of active-site residues to the function of onconase, a ribonuclease with antitumoral activity. Biochemistry 42 (2003) 11443-11450
    • (2003) Biochemistry , vol.42 , pp. 11443-11450
    • Lee, J.E.1    Raines, R.T.2
  • 16
    • 0037407561 scopus 로고    scopus 로고
    • ONCONASE® and its therapeutic potential
    • Saxena S.K., Shogen K., and Ardelt W. ONCONASE® and its therapeutic potential. Lab. Med. 34 (2003) 380-387
    • (2003) Lab. Med. , vol.34 , pp. 380-387
    • Saxena, S.K.1    Shogen, K.2    Ardelt, W.3
  • 17
    • 0032513148 scopus 로고    scopus 로고
    • The Rana catesbeiana rcr gene encoding a cytotoxic ribonuclease. Tissue distribution, cloning, purification, cytotoxicity, and active residues for RNase activity
    • Huang H.-C., Wang S.-C., Leu Y.-J., Lu S.-C., and Liao Y.-D. The Rana catesbeiana rcr gene encoding a cytotoxic ribonuclease. Tissue distribution, cloning, purification, cytotoxicity, and active residues for RNase activity. J. Biol. Chem. 273 (1998) 6395-6401
    • (1998) J. Biol. Chem. , vol.273 , pp. 6395-6401
    • Huang, H.-C.1    Wang, S.-C.2    Leu, Y.-J.3    Lu, S.-C.4    Liao, Y.-D.5
  • 18
    • 0034326938 scopus 로고    scopus 로고
    • Purification and cloning of cytotoxic ribonucleases from Rana catesbeiana (bullfrog)
    • Liao Y.-D., Huang H.-C., Leu Y.-J., Wei C.-W., Tang P.-C., and Wang S.-C. Purification and cloning of cytotoxic ribonucleases from Rana catesbeiana (bullfrog). Nucl. Acids Res. 28 (2000) 4097-4104
    • (2000) Nucl. Acids Res. , vol.28 , pp. 4097-4104
    • Liao, Y.-D.1    Huang, H.-C.2    Leu, Y.-J.3    Wei, C.-W.4    Tang, P.-C.5    Wang, S.-C.6
  • 19
    • 0037470067 scopus 로고    scopus 로고
    • Residues involved in the catalysis, base specificity, and cytotoxicity of ribonuclease from Rana catesbeiana based upon mutagenesis and X-ray crystallography
    • Leu Y.-J., Chern S.-S., Wang S.-C., Hsiao Y.-Y., Amiraslanov I., Liaw Y.-C., and Liao Y.-D. Residues involved in the catalysis, base specificity, and cytotoxicity of ribonuclease from Rana catesbeiana based upon mutagenesis and X-ray crystallography. J. Biol. Chem. 278 (2003) 7300-7309
    • (2003) J. Biol. Chem. , vol.278 , pp. 7300-7309
    • Leu, Y.-J.1    Chern, S.-S.2    Wang, S.-C.3    Hsiao, Y.-Y.4    Amiraslanov, I.5    Liaw, Y.-C.6    Liao, Y.-D.7
  • 20
    • 34447095870 scopus 로고    scopus 로고
    • Tsai, C.-J., Liu, J.-H., Liao, Y.-D., Chen, L.-Y., Cheng, P.-T. & Sun, Y.-J. (2003). Retro and novel binding modes in cytotoxic ribonucleases from Rana catesbeiana of two crystal structures complexed with 2′,5′-CpG and d(ApCpGpA). Protein Data Bank (unpublished).
  • 21
    • 0842345350 scopus 로고
    • The origin of specificity in binding: a detailed example in a protein-nucleic acid interaction
    • Schmitt F.O. (Ed), Rockefeller University Press, New York
    • Richards F.M., Wyckoff H.W., and Allewell N. The origin of specificity in binding: a detailed example in a protein-nucleic acid interaction. In: Schmitt F.O. (Ed). The Neurosciences: Second Study Program (1970), Rockefeller University Press, New York 901-912
    • (1970) The Neurosciences: Second Study Program , pp. 901-912
    • Richards, F.M.1    Wyckoff, H.W.2    Allewell, N.3
  • 26
    • 33646095781 scopus 로고    scopus 로고
    • Tandemization endows bovine pancreatic ribonuclease with cytotoxic activity
    • Leich F., Köditz J., Ulbrich-Hofman R., and Arnold U. Tandemization endows bovine pancreatic ribonuclease with cytotoxic activity. J. Mol. Biol. 358 (2006) 1305-1313
    • (2006) J. Mol. Biol. , vol.358 , pp. 1305-1313
    • Leich, F.1    Köditz, J.2    Ulbrich-Hofman, R.3    Arnold, U.4
  • 27
    • 0024291642 scopus 로고
    • Structure of phosphate-free ribonuclease A refined at 1.26 Å
    • Wlodawer A., Svensson L.A., Sjölin L., and Gilliland G.L. Structure of phosphate-free ribonuclease A refined at 1.26 Å. Biochemistry 27 (1988) 2705-2717
    • (1988) Biochemistry , vol.27 , pp. 2705-2717
    • Wlodawer, A.1    Svensson, L.A.2    Sjölin, L.3    Gilliland, G.L.4
  • 28
    • 0000403579 scopus 로고
    • The active site and mechanism of action of bovine pancreatic ribonuclease
    • Findlay D., Herries D.G., Mathias A.P., Rabin B.R., and Ross C.A. The active site and mechanism of action of bovine pancreatic ribonuclease. Nature 190 (1961) 781-784
    • (1961) Nature , vol.190 , pp. 781-784
    • Findlay, D.1    Herries, D.G.2    Mathias, A.P.3    Rabin, B.R.4    Ross, C.A.5
  • 29
    • 0027949817 scopus 로고
    • Value of general acid-base catalysis to ribonuclease A
    • Thompson J.E., and Raines R.T. Value of general acid-base catalysis to ribonuclease A. J. Am. Chem. Soc. 116 (1994) 5467-5468
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 5467-5468
    • Thompson, J.E.1    Raines, R.T.2
  • 30
    • 0001709899 scopus 로고
    • Ribonuclease-A: least-squares refinement of the structure at 1.45 Å resolution
    • Borkakoti N., Moss D.M., and Palmer R.A. Ribonuclease-A: least-squares refinement of the structure at 1.45 Å resolution. Acta Crystallog. sect. B 38 (1982) 2210-2217
    • (1982) Acta Crystallog. sect. B , vol.38 , pp. 2210-2217
    • Borkakoti, N.1    Moss, D.M.2    Palmer, R.A.3
  • 31
    • 0032560446 scopus 로고    scopus 로고
    • His···Asp catalytic dyad of ribonuclease A: structure and function of the wild-type, D121N, and D121A enzymes
    • Schultz L.W., Quirk D.J., and Raines R.T. His···Asp catalytic dyad of ribonuclease A: structure and function of the wild-type, D121N, and D121A enzymes. Biochemistry 38 (1998) 8886-8898
    • (1998) Biochemistry , vol.38 , pp. 8886-8898
    • Schultz, L.W.1    Quirk, D.J.2    Raines, R.T.3
  • 32
    • 0028983940 scopus 로고
    • Ribonuclease A: revealing structure-function relationships with semisynthesis
    • Messmore J.M., Fuchs D.N., and Raines R.T. Ribonuclease A: revealing structure-function relationships with semisynthesis. J. Am. Chem. Soc. 117 (1995) 8057-8060
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 8057-8060
    • Messmore, J.M.1    Fuchs, D.N.2    Raines, R.T.3
  • 34
    • 0034684274 scopus 로고    scopus 로고
    • Pentavalent organo-vanadates as transition state analogues for phosphoryl transfer reactions
    • Messmore J.M., and Raines R.T. Pentavalent organo-vanadates as transition state analogues for phosphoryl transfer reactions. J. Am. Chem. Soc. 122 (2000) 9911-9916
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 9911-9916
    • Messmore, J.M.1    Raines, R.T.2
  • 35
    • 0028564999 scopus 로고
    • The structures of RNase A complexed with 3′-CMP and d(CpA): active site conformation and conserved water molecules
    • Zegers I., Maes D., Dao-Thi M.-H., Poortmans F., Palmer R., and Wyns L. The structures of RNase A complexed with 3′-CMP and d(CpA): active site conformation and conserved water molecules. Protein Sci. 3 (1994) 2322-2339
    • (1994) Protein Sci. , vol.3 , pp. 2322-2339
    • Zegers, I.1    Maes, D.2    Dao-Thi, M.-H.3    Poortmans, F.4    Palmer, R.5    Wyns, L.6
  • 37
    • 0030037085 scopus 로고    scopus 로고
    • Contribution of a tyrosine side chain to ribonuclease A catalysis and stability
    • Eberhardt E.S., Wittmayer P.K., Templer B.M., and Raines R.T. Contribution of a tyrosine side chain to ribonuclease A catalysis and stability. Protein Sci. 5 (1996) 1697-1703
    • (1996) Protein Sci. , vol.5 , pp. 1697-1703
    • Eberhardt, E.S.1    Wittmayer, P.K.2    Templer, B.M.3    Raines, R.T.4
  • 38
    • 0029032586 scopus 로고
    • Engineering ribonuclease A: production, purification and characterization of wild-type enzyme and mutants at Gln11
    • del Cardayré S.B., Ribó M., Yokel E.M., Quirk D.J., Rutter W.J., and Raines R.T. Engineering ribonuclease A: production, purification and characterization of wild-type enzyme and mutants at Gln11. Protein Eng. 8 (1995) 261-273
    • (1995) Protein Eng. , vol.8 , pp. 261-273
    • del Cardayré, S.B.1    Ribó, M.2    Yokel, E.M.3    Quirk, D.J.4    Rutter, W.J.5    Raines, R.T.6
  • 39
    • 24044506284 scopus 로고    scopus 로고
    • The importance of dynamic effects on the enzyme activity. X-ray structure and molecular dynamics of Onconase mutants
    • Merlino A., Mazzarella L., Carannante A., Di Fiore A., Di Donato A., Notomista E., and Sica F. The importance of dynamic effects on the enzyme activity. X-ray structure and molecular dynamics of Onconase mutants. J. Biol. Chem. 280 (2005) 17953-17960
    • (2005) J. Biol. Chem. , vol.280 , pp. 17953-17960
    • Merlino, A.1    Mazzarella, L.2    Carannante, A.3    Di Fiore, A.4    Di Donato, A.5    Notomista, E.6    Sica, F.7
  • 40
    • 0033593472 scopus 로고    scopus 로고
    • Refined crystal structures of native human angiogenin and two active site variants: implications for the unique functional properties of an enzyme involved in neovascularisation during tumour growth
    • Leonidas D.D., Shapiro R., Allen S.C., Subbarao G.V., Veluraja K., and Acharya K.R. Refined crystal structures of native human angiogenin and two active site variants: implications for the unique functional properties of an enzyme involved in neovascularisation during tumour growth. J. Mol. Biol. 285 (1999) 1209-1233
    • (1999) J. Mol. Biol. , vol.285 , pp. 1209-1233
    • Leonidas, D.D.1    Shapiro, R.2    Allen, S.C.3    Subbarao, G.V.4    Veluraja, K.5    Acharya, K.R.6
  • 41
    • 0022836621 scopus 로고
    • Evolutionary role of posttranslational modifications of proteins, as illustrated by the glycosylation characteristics of the digestive enzyme pancreatic ribonuclease
    • Beintema J.J. Evolutionary role of posttranslational modifications of proteins, as illustrated by the glycosylation characteristics of the digestive enzyme pancreatic ribonuclease. J. Mol. Evol. 24 (1986) 118-120
    • (1986) J. Mol. Evol. , vol.24 , pp. 118-120
    • Beintema, J.J.1
  • 43
    • 0030816760 scopus 로고    scopus 로고
    • An angiogenic protein from bovine serum and milk. Purification and primary structure of angiogenin-2
    • Strydom D.J., Bond M.D., and Vallee B.L. An angiogenic protein from bovine serum and milk. Purification and primary structure of angiogenin-2. Eur. J. Biochem. 247 (1997) 535-544
    • (1997) Eur. J. Biochem. , vol.247 , pp. 535-544
    • Strydom, D.J.1    Bond, M.D.2    Vallee, B.L.3
  • 44
    • 0023665255 scopus 로고
    • The crystal structure of ribonuclease B at 2.5-Å resolution
    • Williams R.L., Greene S.M., and McPherson A. The crystal structure of ribonuclease B at 2.5-Å resolution. J. Biol. Chem. 262 (1987) 16020-16031
    • (1987) J. Biol. Chem. , vol.262 , pp. 16020-16031
    • Williams, R.L.1    Greene, S.M.2    McPherson, A.3
  • 46
    • 1342281681 scopus 로고    scopus 로고
    • Glycosylation of onconase increases its conformational stability and toxicity for cancer cells
    • Kim B.-M., Kim H., Raines R.T., and Lee Y. Glycosylation of onconase increases its conformational stability and toxicity for cancer cells. Biochem. Biophys. Res. Commun. 315 (2004) 976-983
    • (2004) Biochem. Biophys. Res. Commun. , vol.315 , pp. 976-983
    • Kim, B.-M.1    Kim, H.2    Raines, R.T.3    Lee, Y.4
  • 47
    • 0027043131 scopus 로고
    • Revisiting the action of bovine ribonuclease A and pancreatic-type ribonucleases on double-stranded RNA
    • Libonati M., and Sorrentino S. Revisiting the action of bovine ribonuclease A and pancreatic-type ribonucleases on double-stranded RNA. Mol. Cell. Biochem. 117 (1992) 139-151
    • (1992) Mol. Cell. Biochem. , vol.117 , pp. 139-151
    • Libonati, M.1    Sorrentino, S.2
  • 48
    • 0342373028 scopus 로고
    • The isolation of ribounclease B, a glycoprotein, from bovine pancreatic juice
    • Plummer Jr. T.H., and Hirs C.H. The isolation of ribounclease B, a glycoprotein, from bovine pancreatic juice. J. Biol. Chem. 238 (1963) 1396-1401
    • (1963) J. Biol. Chem. , vol.238 , pp. 1396-1401
    • Plummer Jr., T.H.1    Hirs, C.H.2
  • 49
    • 0021981875 scopus 로고
    • Human seminal ribonuclease. A tool to check the role of basic charges and glycosylation of a ribonuclease in the action of the enzyme on double-stranded RNA
    • Sorrentino S., Lavitrano M., De Prisco R., and Libonati M. Human seminal ribonuclease. A tool to check the role of basic charges and glycosylation of a ribonuclease in the action of the enzyme on double-stranded RNA. Biochim. Biophys. Acta 827 (1985) 135-139
    • (1985) Biochim. Biophys. Acta , vol.827 , pp. 135-139
    • Sorrentino, S.1    Lavitrano, M.2    De Prisco, R.3    Libonati, M.4
  • 50
    • 0032528298 scopus 로고    scopus 로고
    • Eosinophil cationic protein/RNase 3 is another RNase A-family ribonuclease with direct antiviral activity
    • Domachowske J.B., Dyer K.D., Adams A.G., Leto T.L., and Rosenberg H.F. Eosinophil cationic protein/RNase 3 is another RNase A-family ribonuclease with direct antiviral activity. Nucl. Acids Res. 26 (1998) 3358-3363
    • (1998) Nucl. Acids Res. , vol.26 , pp. 3358-3363
    • Domachowske, J.B.1    Dyer, K.D.2    Adams, A.G.3    Leto, T.L.4    Rosenberg, H.F.5
  • 51
    • 0000597698 scopus 로고
    • Compositional protein analysis using 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate, a novel derivatization reagent
    • Angeletti R.H. (Ed), Academic Press, San Diego, CA
    • Cohen S.A., De Antonis K., and Michaud D.P. Compositional protein analysis using 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate, a novel derivatization reagent. In: Angeletti R.H. (Ed). Techniques in Protein Chemistry IV (1993), Academic Press, San Diego, CA 289-298
    • (1993) Techniques in Protein Chemistry IV , pp. 289-298
    • Cohen, S.A.1    De Antonis, K.2    Michaud, D.P.3
  • 52
    • 0015783856 scopus 로고
    • Determination of the amino acid sequence of porcine trypsin by sequenator analysis
    • Hermodson M.A., Ericsson L.H., Neurath H., and Walsh K.A. Determination of the amino acid sequence of porcine trypsin by sequenator analysis. Biochemistry 12 (1973) 3146-3153
    • (1973) Biochemistry , vol.12 , pp. 3146-3153
    • Hermodson, M.A.1    Ericsson, L.H.2    Neurath, H.3    Walsh, K.A.4
  • 53
    • 0002510219 scopus 로고
    • Fragmentation of polypeptides by chemical methods
    • Darbre A. (Ed), John Wiley and Sons, Chichester, New York
    • Fontana A., and Gross E. Fragmentation of polypeptides by chemical methods. In: Darbre A. (Ed). Practical Protein Chemistry-a Handbook (1986), John Wiley and Sons, Chichester, New York 67-120
    • (1986) Practical Protein Chemistry-a Handbook , pp. 67-120
    • Fontana, A.1    Gross, E.2
  • 54
    • 0014325267 scopus 로고
    • Reversible blocking of amino groups with citraconic anhydride
    • Dixon H.B.F., and Perham R.N. Reversible blocking of amino groups with citraconic anhydride. Biochem. J. 109 (1968) 312-314
    • (1968) Biochem. J. , vol.109 , pp. 312-314
    • Dixon, H.B.F.1    Perham, R.N.2
  • 56
    • 34447099203 scopus 로고
    • Sambrook J., Fritch E.F., and Maniatis T. (Eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • In: Sambrook J., Fritch E.F., and Maniatis T. (Eds). Molecular Cloning: a Laboratory Manual. 2nd edit (1989), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (1989) Molecular Cloning: a Laboratory Manual. 2nd edit
  • 57
    • 0027050499 scopus 로고
    • Cis proline mutants of ribonuclease A. I. Thermal stability
    • Schultz D.A., and Baldwin R.L. Cis proline mutants of ribonuclease A. I. Thermal stability. Protein Sci. 1 (1992) 910-916
    • (1992) Protein Sci. , vol.1 , pp. 910-916
    • Schultz, D.A.1    Baldwin, R.L.2
  • 58
    • 0025840179 scopus 로고
    • Cytotoxic potential of ribonuclease and ribonuclease hybrid proteins
    • Rybak S.M., Saxena S.K., Ackerman E.J., and Youle R.J. Cytotoxic potential of ribonuclease and ribonuclease hybrid proteins. J. Biol. Chem. 266 (1991) 21202-21207
    • (1991) J. Biol. Chem. , vol.266 , pp. 21202-21207
    • Rybak, S.M.1    Saxena, S.K.2    Ackerman, E.J.3    Youle, R.J.4
  • 59
    • 0038756863 scopus 로고    scopus 로고
    • Potent inhibition of ribonuclease A by oligo(vinylsulfonic acid)
    • Smith B.D., Soellner M.B., and Raines R.T. Potent inhibition of ribonuclease A by oligo(vinylsulfonic acid). J. Biol. Chem. 278 (2003) 20934-20938
    • (2003) J. Biol. Chem. , vol.278 , pp. 20934-20938
    • Smith, B.D.1    Soellner, M.B.2    Raines, R.T.3
  • 60
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace C.N., Vajdos F., Fee L., Grimsley G., and Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4 (1995) 2411-2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 61
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays
    • Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods 65 (1983) 55-63
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 62
    • 0001036525 scopus 로고
    • Alkylation and identification of the histidine residues at the active site of ribonuclease
    • Crestfield A.M., Stein W.H., and Moore S. Alkylation and identification of the histidine residues at the active site of ribonuclease. J. Biol. Chem. 238 (1963) 2413-2420
    • (1963) J. Biol. Chem. , vol.238 , pp. 2413-2420
    • Crestfield, A.M.1    Stein, W.H.2    Moore, S.3
  • 63
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 65
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Bailey S. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D 50 (1994) 760-763
    • (1994) Acta Crystallog. sect. D , vol.50 , pp. 760-763
    • Bailey, S.1
  • 66
    • 0000952473 scopus 로고
    • On the treatment of negative intensity observations
    • French S., and Wilson K. On the treatment of negative intensity observations. Acta Crystallog. sect. A 34 (1978) 517-525
    • (1978) Acta Crystallog. sect. A , vol.34 , pp. 517-525
    • French, S.1    Wilson, K.2
  • 67
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33 (1968) 491-497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 68
    • 84920325457 scopus 로고
    • AMoRe: an automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A 50 (1994) 157-163
    • (1994) Acta Crystallog. sect. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 70
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.-Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A 47 (1991) 110-119
    • (1991) Acta Crystallog. sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 71
    • 0026597444 scopus 로고
    • Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger A.T. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355 (1992) 472-475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 72
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld R., and Kornfeld S. Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 54 (1985) 631-664
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 73
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A., and Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallog. 30 (1997) 1022-1025
    • (1997) J. Appl. Crystallog. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 74
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum likelihood method. Acta Crystallog. sect. D 53 (1997) 240-255
    • (1997) Acta Crystallog. sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 75
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallog. sect. D 60 (2004) 2126-2132
    • (2004) Acta Crystallog. sect. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 76
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26 (1993) 283-291
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 77
    • 0031718310 scopus 로고    scopus 로고
    • Homology modeling, model and software evaluation: three related resources
    • Rodriguez R., Chinea G., Lopez N., Pons T., and Vriend G. Homology modeling, model and software evaluation: three related resources. Bioinformatics 14 (1998) 523-528
    • (1998) Bioinformatics , vol.14 , pp. 523-528
    • Rodriguez, R.1    Chinea, G.2    Lopez, N.3    Pons, T.4    Vriend, G.5
  • 79
    • 0015866154 scopus 로고
    • Environment and exposure to solvent of protein atoms. Lysozyme and insulin
    • Shrake A., and Rupley J.A. Environment and exposure to solvent of protein atoms. Lysozyme and insulin. J. Mol. Biol. 79 (1973) 351-371
    • (1973) J. Mol. Biol. , vol.79 , pp. 351-371
    • Shrake, A.1    Rupley, J.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.