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Volumn 6, Issue 4, 2011, Pages

Critical factors governing the difference in antizyme-binding affinities between human ornithine decarboxylase and antizyme inhibitor

Author keywords

[No Author keywords available]

Indexed keywords

ANTIZYME; ANTIZYME INHIBITOR; HETERODIMER; MUTANT PROTEIN; ORNITHINE DECARBOXYLASE; REGULATOR PROTEIN; UNCLASSIFIED DRUG; ENZYME INHIBITOR; PROTEIN; SOLVENT;

EID: 79955721220     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0019253     Document Type: Article
Times cited : (18)

References (56)
  • 1
    • 33744951504 scopus 로고    scopus 로고
    • Regulation of ornithine decarboxylase
    • Pegg AE, (2006) Regulation of ornithine decarboxylase. J Biol Chem 281: 14529-14532.
    • (2006) J Biol Chem , vol.281 , pp. 14529-14532
    • Pegg, A.E.1
  • 2
    • 0020215250 scopus 로고
    • Polyamine metabolism and function
    • Pegg AE, McCann PP, (1982) Polyamine metabolism and function. Am J Physiol 243: C212-221.
    • (1982) Am J Physiol , vol.243
    • Pegg, A.E.1    McCann, P.P.2
  • 3
    • 0034809529 scopus 로고    scopus 로고
    • The ornithine decarboxylase gene is essential for cell survival during early murine development
    • Pendeville H, Carpino N, Marine JC, Takahashi Y, Muller M, et al. (2001) The ornithine decarboxylase gene is essential for cell survival during early murine development. Mol Cell Biol 21: 6549-6558.
    • (2001) Mol Cell Biol , vol.21 , pp. 6549-6558
    • Pendeville, H.1    Carpino, N.2    Marine, J.C.3    Takahashi, Y.4    Muller, M.5
  • 4
    • 11244337377 scopus 로고    scopus 로고
    • Polyamines regulate their synthesis by inducing expression and blocking degradation of ODC antizyme
    • Palanimurugan R, Scheel H, Hofmann K, Dohmen RJ, (2004) Polyamines regulate their synthesis by inducing expression and blocking degradation of ODC antizyme. EMBO J 23: 4857-4867.
    • (2004) EMBO J , vol.23 , pp. 4857-4867
    • Palanimurugan, R.1    Scheel, H.2    Hofmann, K.3    Dohmen, R.J.4
  • 6
    • 0035099627 scopus 로고    scopus 로고
    • Polyamines in cell growth and cell death: Molecular mechanisms and therapeutic applications
    • Thomas T, Thomas TJ, (2001) Polyamines in cell growth and cell death: Molecular mechanisms and therapeutic applications. Cell Mol Life Sci 58: 244-258.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 244-258
    • Thomas, T.1    Thomas, T.J.2
  • 7
    • 0026683752 scopus 로고
    • Ornithine decarboxylase activity is critical for cell transformation
    • Auvinen M, Paasinen A, Andersson LC, Holtta E, (1992) Ornithine decarboxylase activity is critical for cell transformation. Nature 360: 355-358.
    • (1992) Nature , vol.360 , pp. 355-358
    • Auvinen, M.1    Paasinen, A.2    Andersson, L.C.3    Holtta, E.4
  • 8
    • 0031001040 scopus 로고    scopus 로고
    • Ornithine decarboxylase overexpression leads to increased epithelial tumor invasiveness
    • Smith MK, Goral MA, Wright JH, Matrisian LM, Morris RJ, et al. (1997) Ornithine decarboxylase overexpression leads to increased epithelial tumor invasiveness. Cancer Res 57: 2104-2108.
    • (1997) Cancer Res , vol.57 , pp. 2104-2108
    • Smith, M.K.1    Goral, M.A.2    Wright, J.H.3    Matrisian, L.M.4    Morris, R.J.5
  • 9
    • 0030741841 scopus 로고    scopus 로고
    • Ornithine decarboxylase overexpression is a sufficient condition for tumor promotion in mouse skin
    • O'Brien TG, Megosh LC, Gilliard G, Soler AP, (1997) Ornithine decarboxylase overexpression is a sufficient condition for tumor promotion in mouse skin. Cancer Res 57: 2630-2637.
    • (1997) Cancer Res , vol.57 , pp. 2630-2637
    • O'Brien, T.G.1    Megosh, L.C.2    Gilliard, G.3    Soler, A.P.4
  • 10
    • 21244479016 scopus 로고    scopus 로고
    • Ornithine decarboxylase prevents tumor necrosis factor alpha-induced apoptosis by decreasing intracellular reactive oxygen species
    • Liu GY, Hung YC, Hsu PC, Liao YF, Chang WH, et al. (2005) Ornithine decarboxylase prevents tumor necrosis factor alpha-induced apoptosis by decreasing intracellular reactive oxygen species. Apoptosis 10: 569-581.
    • (2005) Apoptosis , vol.10 , pp. 569-581
    • Liu, G.Y.1    Hung, Y.C.2    Hsu, P.C.3    Liao, Y.F.4    Chang, W.H.5
  • 11
    • 23944520426 scopus 로고    scopus 로고
    • Ornithine decarboxylase prevents methotrexate-induced apoptosis by reducing intracellular reactive oxygen species production
    • Huang CC, Hsu PC, Hung YC, Liao YF, Liu CC, et al. (2005) Ornithine decarboxylase prevents methotrexate-induced apoptosis by reducing intracellular reactive oxygen species production. Apoptosis 10: 895-907.
    • (2005) Apoptosis , vol.10 , pp. 895-907
    • Huang, C.C.1    Hsu, P.C.2    Hung, Y.C.3    Liao, Y.F.4    Liu, C.C.5
  • 12
    • 33646389797 scopus 로고    scopus 로고
    • Increasing ornithine decarboxylase activity is another way of prolactin preventing methotrexate-induced apoptosis: CROSSTALK BETWEEN ODC AND BCL-2
    • Hsu PC, Hour TC, Liao YF, Hung YC, Liu CC, et al. (2006) Increasing ornithine decarboxylase activity is another way of prolactin preventing methotrexate-induced apoptosis: CROSSTALK BETWEEN ODC AND BCL-2. Apoptosis 11: 389-399.
    • (2006) Apoptosis , vol.11 , pp. 389-399
    • Hsu, P.C.1    Hour, T.C.2    Liao, Y.F.3    Hung, Y.C.4    Liu, C.C.5
  • 13
    • 0022322163 scopus 로고
    • Molecular mechanism for the regulation of hepatic ornithine decarboxylase
    • Hayashi S, Kameji T, Fujita K, Murakami Y, Kanamoto R, et al. (1985) Molecular mechanism for the regulation of hepatic ornithine decarboxylase. Adv Enzyme Regul 23: 311-329.
    • (1985) Adv Enzyme Regul , vol.23 , pp. 311-329
    • Hayashi, S.1    Kameji, T.2    Fujita, K.3    Murakami, Y.4    Kanamoto, R.5
  • 14
    • 0033625355 scopus 로고    scopus 로고
    • Interleukin-1beta induces elevation of spermidine/spermine N1-acetyltransferase activity and an increase in the amount of putrescine in synovial adherent cells from patients with rheumatoid arthritis
    • Furumitsu Y, Yukioka K, Yukioka M, Ochi T, Morishima Y, et al. (2000) Interleukin-1beta induces elevation of spermidine/spermine N1-acetyltransferase activity and an increase in the amount of putrescine in synovial adherent cells from patients with rheumatoid arthritis. J Rheumatol 27: 1352-1357.
    • (2000) J Rheumatol , vol.27 , pp. 1352-1357
    • Furumitsu, Y.1    Yukioka, K.2    Yukioka, M.3    Ochi, T.4    Morishima, Y.5
  • 15
    • 0242432597 scopus 로고    scopus 로고
    • Increased expression of ornithine decarboxylase in distal tubules of early diabetic rat kidneys: are polyamines paracrine hypertrophic factors?
    • Deng A, Munger KA, Valdivielso JM, Satriano J, Lortie M, et al. (2003) Increased expression of ornithine decarboxylase in distal tubules of early diabetic rat kidneys: are polyamines paracrine hypertrophic factors? Diabetes 52: 1235-1239.
    • (2003) Diabetes , vol.52 , pp. 1235-1239
    • Deng, A.1    Munger, K.A.2    Valdivielso, J.M.3    Satriano, J.4    Lortie, M.5
  • 16
    • 0342980390 scopus 로고    scopus 로고
    • Central role for ornithine decarboxylase in beta-adrenoceptor mediated hypertrophy
    • Schluter KD, Frischkopf K, Flesch M, Rosenkranz S, Taimor G, et al. (2000) Central role for ornithine decarboxylase in beta-adrenoceptor mediated hypertrophy. Cardiovasc Res 45: 410-417.
    • (2000) Cardiovasc Res , vol.45 , pp. 410-417
    • Schluter, K.D.1    Frischkopf, K.2    Flesch, M.3    Rosenkranz, S.4    Taimor, G.5
  • 17
    • 0031812234 scopus 로고    scopus 로고
    • Ornithine decarboxylase in human brain: influence of aging, regional distribution, and Alzheimer's disease
    • Morrison LD, Cao XC, Kish SJ, (1998) Ornithine decarboxylase in human brain: influence of aging, regional distribution, and Alzheimer's disease. J Neurochem 71: 288-294.
    • (1998) J Neurochem , vol.71 , pp. 288-294
    • Morrison, L.D.1    Cao, X.C.2    Kish, S.J.3
  • 18
    • 0030834335 scopus 로고    scopus 로고
    • Human ornithine decarboxylase-overproducing NIH3T3 cells induce rapidly growing, highly vascularized tumors in nude mice
    • Auvinen M, Laine A, Paasinen-Sohns A, Kangas A, Kangas L, et al. (1997) Human ornithine decarboxylase-overproducing NIH3T3 cells induce rapidly growing, highly vascularized tumors in nude mice. Cancer Res 57: 3016-3025.
    • (1997) Cancer Res , vol.57 , pp. 3016-3025
    • Auvinen, M.1    Laine, A.2    Paasinen-Sohns, A.3    Kangas, A.4    Kangas, L.5
  • 19
    • 0028016495 scopus 로고
    • Ornithine decarboxylase is a mediator of c-Myc-induced apoptosis
    • Packham G, Cleveland JL, (1994) Ornithine decarboxylase is a mediator of c-Myc-induced apoptosis. Mol Cell Biol 14: 5741-5747.
    • (1994) Mol Cell Biol , vol.14 , pp. 5741-5747
    • Packham, G.1    Cleveland, J.L.2
  • 20
    • 4944242891 scopus 로고    scopus 로고
    • Polyamines and cancer: old molecules, new understanding
    • Gerner EW, Meyskens FL Jr, (2004) Polyamines and cancer: old molecules, new understanding. Nat Rev Cancer 4: 781-792.
    • (2004) Nat Rev Cancer , vol.4 , pp. 781-792
    • Gerner, E.W.1    Meyskens Jr., F.L.2
  • 21
    • 0031733015 scopus 로고    scopus 로고
    • Polyamine metabolism as target for cancer chemoprevention (Review)
    • Seiler N, Atanassov CL, Raul F, (1998) Polyamine metabolism as target for cancer chemoprevention (Review). Int J Oncol 13: 993-1006.
    • (1998) Int J Oncol , vol.13 , pp. 993-1006
    • Seiler, N.1    Atanassov, C.L.2    Raul, F.3
  • 22
    • 0030052923 scopus 로고    scopus 로고
    • Ornithine decarboxylase antizyme: A novel type of regulatory protein
    • Hayashi S, Murakami Y, Matsufuji S, (1996) Ornithine decarboxylase antizyme: A novel type of regulatory protein. Trends Biochem Sci 21: 27-30.
    • (1996) Trends Biochem Sci , vol.21 , pp. 27-30
    • Hayashi, S.1    Murakami, Y.2    Matsufuji, S.3
  • 23
    • 0026667106 scopus 로고
    • Regulated degradation of ornithine decarboxylase requires interaction with the polyamine-inducible protein antizyme
    • Li X, Coffino P, (1992) Regulated degradation of ornithine decarboxylase requires interaction with the polyamine-inducible protein antizyme. Mol Cell Biol 12: 3556-3562.
    • (1992) Mol Cell Biol , vol.12 , pp. 3556-3562
    • Li, X.1    Coffino, P.2
  • 24
    • 0035291218 scopus 로고    scopus 로고
    • Regulation of cellular polyamines by antizyme
    • Coffino P, (2001) Regulation of cellular polyamines by antizyme. Nat Rev Mol Cell Biol 2: 188-194.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 188-194
    • Coffino, P.1
  • 25
    • 0026714435 scopus 로고
    • Ornithine decarboxylase is degradaded by the 26S proteasome without ubiquitination
    • Murakami Y, Matsufuji S, Kameji T, Hayashi S, Igarashi K, et al. (1992) Ornithine decarboxylase is degradaded by the 26S proteasome without ubiquitination. Nature 360: 597-600.
    • (1992) Nature , vol.360 , pp. 597-600
    • Murakami, Y.1    Matsufuji, S.2    Kameji, T.3    Hayashi, S.4    Igarashi, K.5
  • 26
    • 0002222618 scopus 로고    scopus 로고
    • Degradation of ornithine decarboxylase,
    • In: Peters JM, Harris JR, Finley D, editors, Plenum Press, New York
    • Coffino P, (1998) Degradation of ornithine decarboxylase, In: Peters JM, Harris JR, Finley D, editors. Ubiquitin and the Biology of the Cell pp. 411-427 Plenum Press, New York.
    • (1998) Ubiquitin and the Biology of the Cell , pp. 411-427
    • Coffino, P.1
  • 27
    • 0035067587 scopus 로고    scopus 로고
    • Antizyme, a mediator of ubiquitin-independent proteasomal degradation
    • Coffino P, (2001) Antizyme, a mediator of ubiquitin-independent proteasomal degradation. Biochimie 83: 319-323.
    • (2001) Biochimie , vol.83 , pp. 319-323
    • Coffino, P.1
  • 28
    • 27644538375 scopus 로고    scopus 로고
    • The antizyme family: polyamines and beyond
    • Mangold U, (2005) The antizyme family: polyamines and beyond. IUBMB Life 57: 671-676.
    • (2005) IUBMB Life , vol.57 , pp. 671-676
    • Mangold, U.1
  • 29
    • 70350389829 scopus 로고    scopus 로고
    • Critical factors determining dimerization of human antizyme inhibitor
    • Su KL, Liao YF, Hung HC, Liu GY, (2009) Critical factors determining dimerization of human antizyme inhibitor. J Biol Chem 284: 26768-26777.
    • (2009) J Biol Chem , vol.284 , pp. 26768-26777
    • Su, K.L.1    Liao, Y.F.2    Hung, H.C.3    Liu, G.Y.4
  • 30
    • 0345701307 scopus 로고    scopus 로고
    • Determinants of proteasome recognition of ornithine decarboxylase, a ubiquitin independent substrate
    • Zhang M, Pickart CM, Coffino P, (2003) Determinants of proteasome recognition of ornithine decarboxylase, a ubiquitin independent substrate. EMBO J 22: 1488-1496.
    • (2003) EMBO J , vol.22 , pp. 1488-1496
    • Zhang, M.1    Pickart, C.M.2    Coffino, P.3
  • 31
    • 2442645033 scopus 로고    scopus 로고
    • Proteasomes begin ornithine decarboxylase digestion at the C-terminus
    • Zhang M, MacDonald AI, Hoyt MA, Coffino P, (2004) Proteasomes begin ornithine decarboxylase digestion at the C-terminus. J Biol Chem 279: 20959-20965.
    • (2004) J Biol Chem , vol.279 , pp. 20959-20965
    • Zhang, M.1    MacDonald, A.I.2    Hoyt, M.A.3    Coffino, P.4
  • 32
    • 0028831608 scopus 로고
    • Autoregulatory frameshifting in decoding mammalian ornithine decarboxylase antizyme
    • Matsufuji S, Matsufuji T, Miyazaki Y, Murakami Y, Atkins JF, et al. (1995) Autoregulatory frameshifting in decoding mammalian ornithine decarboxylase antizyme. Cell 80: 51-60.
    • (1995) Cell , vol.80 , pp. 51-60
    • Matsufuji, S.1    Matsufuji, T.2    Miyazaki, Y.3    Murakami, Y.4    Atkins, J.F.5
  • 33
    • 0034177792 scopus 로고    scopus 로고
    • Properties of a polyamine transporter regulated by antizyme
    • Sakata K, Kashiwagi K, Igarashi K, (2000) Properties of a polyamine transporter regulated by antizyme. Biochem J 347: 297-303.
    • (2000) Biochem J , vol.347 , pp. 297-303
    • Sakata, K.1    Kashiwagi, K.2    Igarashi, K.3
  • 34
    • 33749050639 scopus 로고    scopus 로고
    • Antizyme inhibitor: mysterious modulator of cell proliferation
    • Mangold U, (2006) Antizyme inhibitor: mysterious modulator of cell proliferation. Cell Mol Life Sci 63: 2095-2101.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 2095-2101
    • Mangold, U.1
  • 35
    • 0030020026 scopus 로고    scopus 로고
    • Cloning of antizyme inhibitor, a highly homologous protein to ornithine decarboxylase
    • Murakami Y, Ichiba T, Matsufuji S, Hayashi S, (1996) Cloning of antizyme inhibitor, a highly homologous protein to ornithine decarboxylase. J Biol Chem 271: 3340-3342.
    • (1996) J Biol Chem , vol.271 , pp. 3340-3342
    • Murakami, Y.1    Ichiba, T.2    Matsufuji, S.3    Hayashi, S.4
  • 36
    • 0034654021 scopus 로고    scopus 로고
    • Antizyme inhibitor is rapidly induced in growth-stimulated mouse fibroblasts and releases ornithine decarboxylase from antizyme suppression
    • Nilsson J, Grahn B, Heby O, (2000) Antizyme inhibitor is rapidly induced in growth-stimulated mouse fibroblasts and releases ornithine decarboxylase from antizyme suppression. Biochem J 346: 699-704.
    • (2000) Biochem J , vol.346 , pp. 699-704
    • Nilsson, J.1    Grahn, B.2    Heby, O.3
  • 37
    • 67650815445 scopus 로고    scopus 로고
    • Antizyme and antizyme inhibitor, a regulatory tango
    • Kahana C, (2009) Antizyme and antizyme inhibitor, a regulatory tango. Cell Mol Life Sci 66: 2479-2488.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 2479-2488
    • Kahana, C.1
  • 38
    • 11144222575 scopus 로고    scopus 로고
    • Degradation of antizyme inhibitor, an ornithine decarboxylase homologous protein, is ubiquitin-dependent and is inhibited by antizyme
    • Bercovich Z, Kahana C, (2004) Degradation of antizyme inhibitor, an ornithine decarboxylase homologous protein, is ubiquitin-dependent and is inhibited by antizyme. J Biol Chem 279: 54097-54102.
    • (2004) J Biol Chem , vol.279 , pp. 54097-54102
    • Bercovich, Z.1    Kahana, C.2
  • 39
    • 12744273396 scopus 로고    scopus 로고
    • Regulation of all members of the antizyme family by antizyme inhibitor
    • Mangold U, Leberer E, (2005) Regulation of all members of the antizyme family by antizyme inhibitor. Biochem J 385: 21-28.
    • (2005) Biochem J , vol.385 , pp. 21-28
    • Mangold, U.1    Leberer, E.2
  • 40
    • 33747830765 scopus 로고    scopus 로고
    • Overexpression of antizyme-inhibitor in NIH3T3 fibroblasts provides growth advantage through neutralization of antizyme functions
    • Keren-Paz A, Bercovich Z, Porat Z, Erez O, Brener O, et al. (2006) Overexpression of antizyme-inhibitor in NIH3T3 fibroblasts provides growth advantage through neutralization of antizyme functions. Oncogene 25: 5163-5172.
    • (2006) Oncogene , vol.25 , pp. 5163-5172
    • Keren-Paz, A.1    Bercovich, Z.2    Porat, Z.3    Erez, O.4    Brener, O.5
  • 41
    • 33746102203 scopus 로고    scopus 로고
    • Regulation of cell proliferation by the antizyme inhibitor: evidence for an antizyme independent mechanism
    • Kim SW, Mangold U, Waghorne C, Mobascher A, Shantz LM, et al. (2006) Regulation of cell proliferation by the antizyme inhibitor: evidence for an antizyme independent mechanism. J Cell Sci 119: 2583-2591.
    • (2006) J Cell Sci , vol.119 , pp. 2583-2591
    • Kim, S.W.1    Mangold, U.2    Waghorne, C.3    Mobascher, A.4    Shantz, L.M.5
  • 42
    • 12844280568 scopus 로고    scopus 로고
    • Stable siRNA-mediated silencing of antizyme inhibitor: regulation of ornithine decarboxylase activity
    • Choi KS, Suh YH, Kim WH, Lee TH, Jung MH, (2005) Stable siRNA-mediated silencing of antizyme inhibitor: regulation of ornithine decarboxylase activity. Res Commun 328: 206-212.
    • (2005) Res Commun , vol.328 , pp. 206-212
    • Choi, K.S.1    Suh, Y.H.2    Kim, W.H.3    Lee, T.H.4    Jung, M.H.5
  • 43
    • 0033135202 scopus 로고    scopus 로고
    • Structure of mammalian ornithine decarboxylase at 1.6 A resolution: stereochemical implications of PLP-dependent amino acid decarboxylases
    • Kern AD, Oliveira MA, Coffino P, Hackert ML, (1999) Structure of mammalian ornithine decarboxylase at 1.6 A resolution: stereochemical implications of PLP-dependent amino acid decarboxylases. Structure 7: 567-581.
    • (1999) Structure , vol.7 , pp. 567-581
    • Kern, A.D.1    Oliveira, M.A.2    Coffino, P.3    Hackert, M.L.4
  • 44
    • 0034614359 scopus 로고    scopus 로고
    • Crystal structure of human ornithine decarboxylase at 2.1 Å resolution: structural insights to antizyme binding
    • Almrud JJ, Oliveira MA, Kern AD, Grishin NV, Phillips MA, et al. (2000) Crystal structure of human ornithine decarboxylase at 2.1 Å resolution: structural insights to antizyme binding. J Mol Biol 295: 7-16.
    • (2000) J Mol Biol , vol.295 , pp. 7-16
    • Almrud, J.J.1    Oliveira, M.A.2    Kern, A.D.3    Grishin, N.V.4    Phillips, M.A.5
  • 45
    • 0022234410 scopus 로고
    • Equilibrium between active and inactive forms of rat liver ornithine decarboxylase mediated by L-ornithine and salts
    • Solano F, Penafiel R, Solano ME, Lozano JA, (1985) Equilibrium between active and inactive forms of rat liver ornithine decarboxylase mediated by L-ornithine and salts. FEBS Lett 190: 324-328.
    • (1985) FEBS Lett , vol.190 , pp. 324-328
    • Solano, F.1    Penafiel, R.2    Solano, M.E.3    Lozano, J.A.4
  • 46
    • 5444225208 scopus 로고    scopus 로고
    • Multiple active site conformations revealed by distant site mutation in ornithine decarboxylase
    • Jackson LK, Baldwin J, Akella R, Goldsmith EJ, Phillips MA, (2004) Multiple active site conformations revealed by distant site mutation in ornithine decarboxylase. Biochemistry 43: 12990-12999.
    • (2004) Biochemistry , vol.43 , pp. 12990-12999
    • Jackson, L.K.1    Baldwin, J.2    Akella, R.3    Goldsmith, E.J.4    Phillips, M.A.5
  • 47
    • 0038159264 scopus 로고    scopus 로고
    • X-ray structure determination of Trypanosoma brucei ornithine decarboxylase bound to D-ornithine and to G418: insights into substrate binding and ODC conformational flexibility
    • Jackson LK, Goldsmith EJ, Phillips MA, (2003) X-ray structure determination of Trypanosoma brucei ornithine decarboxylase bound to D-ornithine and to G418: insights into substrate binding and ODC conformational flexibility. J Biol Chem 278: 22037-22043.
    • (2003) J Biol Chem , vol.278 , pp. 22037-22043
    • Jackson, L.K.1    Goldsmith, E.J.2    Phillips, M.A.3
  • 48
    • 43049116507 scopus 로고    scopus 로고
    • Crystallographic and biochemical studies revealing the structural basis for antizyme inhibitor function
    • Albeck S, Dym O, Unger T, Snapir Z, Bercovich Z, et al. (2008) Crystallographic and biochemical studies revealing the structural basis for antizyme inhibitor function. Protein Sci 17: 793-802.
    • (2008) Protein Sci , vol.17 , pp. 793-802
    • Albeck, S.1    Dym, O.2    Unger, T.3    Snapir, Z.4    Bercovich, Z.5
  • 49
    • 67449096722 scopus 로고    scopus 로고
    • Docking of antizyme to ornithine decarboxylase and antizyme inhibitor using experimental mutant and double-mutant cycle data
    • Cohavi O, Tobi D, Schreiber G, (2009) Docking of antizyme to ornithine decarboxylase and antizyme inhibitor using experimental mutant and double-mutant cycle data. J Mol Biol 390: 503-515.
    • (2009) J Mol Biol , vol.390 , pp. 503-515
    • Cohavi, O.1    Tobi, D.2    Schreiber, G.3
  • 50
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K, (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 51
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM, (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 52
    • 0036154258 scopus 로고    scopus 로고
    • Size distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems
    • Schuck P, Perugini MA, Gonzales NR, Howlett GJ, Schubert D, (2002) Size distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems. Biophys J 82: 1096-1111.
    • (2002) Biophys J , vol.82 , pp. 1096-1111
    • Schuck, P.1    Perugini, M.A.2    Gonzales, N.R.3    Howlett, G.J.4    Schubert, D.5
  • 53
    • 0042855798 scopus 로고    scopus 로고
    • On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation
    • Schuck P, (2003) On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation. Anal Biochem 320: 104-124.
    • (2003) Anal Biochem , vol.320 , pp. 104-124
    • Schuck, P.1
  • 54
    • 57549085173 scopus 로고    scopus 로고
    • Characterizing protein-protein interactions by sedimentation velocity analytical ultracentrifugation
    • Unit 18 15
    • Brown PH, Balbo A, Schuck P, (2008) Characterizing protein-protein interactions by sedimentation velocity analytical ultracentrifugation. Curr Protoc Immunol Chapter 18: Unit 18 15.
    • (2008) Curr Protoc Immunol Chapter , vol.18
    • Brown, P.H.1    Balbo, A.2    Schuck, P.3
  • 55
    • 23244445215 scopus 로고    scopus 로고
    • Sedimentation velocity analysis of heterogeneous protein-protein interactions: sedimentation coefficient distributions c(s) and asymptotic boundary profiles from Gilbert-Jenkins theory
    • Dam J, Schuck P, (2005) Sedimentation velocity analysis of heterogeneous protein-protein interactions: sedimentation coefficient distributions c(s) and asymptotic boundary profiles from Gilbert-Jenkins theory. Biophys J 89: 651-666.
    • (2005) Biophys J , vol.89 , pp. 651-666
    • Dam, J.1    Schuck, P.2
  • 56
    • 0003443949 scopus 로고
    • Analytical Ultracentrifugation in Biochemistry and Polymer Science
    • The Royal Society of Chemistry, Cambridge, UK
    • Laue TM, Shah BD, Ridgeway TM, Pelleter SL, (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science, The Royal Society of Chemistry, Cambridge, UK.
    • (1992)
    • Laue, T.M.1    Shah, B.D.2    Ridgeway, T.M.3    Pelleter, S.L.4


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