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Volumn 4, Issue 10, 2009, Pages

Human Sirt-1: Molecular Modeling and Structure-Function Relationships of an Unordered Protein

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE REGULATOR OF SIRT1 PROTEIN, HUMAN; NUCLEAR PROTEIN; SIRT1 PROTEIN, HUMAN; SIRTUIN; SIRTUIN 1; TRANSCRIPTION FACTOR;

EID: 77957655795     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0007350     Document Type: Article
Times cited : (65)

References (60)
  • 2
    • 35349011726 scopus 로고    scopus 로고
    • Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity
    • Kim EJ, Kho JH, Kang MR, Um SJ, (2007) Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity. Mol Cell 28: 277-90.
    • (2007) Mol Cell , vol.28 , pp. 277-290
    • Kim, E.J.1    Kho, J.H.2    Kang, M.R.3    Um, S.J.4
  • 4
    • 34547875773 scopus 로고    scopus 로고
    • Sirtuins: critical regulators at the crossroads between cancer and aging
    • Saunders LR, Verdin E, (2007) Sirtuins: critical regulators at the crossroads between cancer and aging. Oncogene 26: 5489-5504.
    • (2007) Oncogene , vol.26 , pp. 5489-5504
    • Saunders, L.R.1    Verdin, E.2
  • 5
    • 0035913903 scopus 로고    scopus 로고
    • hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase
    • Vaziri H, Dessain SK, Ng Eaton E, Imai SI, Frye RA, et al.(2001) hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase. Cell 107: 149-159.
    • (2001) Cell , vol.107 , pp. 149-159
    • Vaziri, H.1    Dessain, S.K.2    Ng Eaton, E.3    Imai, S.I.4    Frye, R.A.5
  • 6
    • 16344384026 scopus 로고    scopus 로고
    • Suppression of FOXO1 activity by FHL2 through SIRT1-mediated deacetylation
    • Yang Y, Hou H, Haller EM, Nicosia SV, Bai W, (2005) Suppression of FOXO1 activity by FHL2 through SIRT1-mediated deacetylation. EMBO J 24: 1021-1032.
    • (2005) EMBO J , vol.24 , pp. 1021-1032
    • Yang, Y.1    Hou, H.2    Haller, E.M.3    Nicosia, S.V.4    Bai, W.5
  • 7
    • 14544282413 scopus 로고    scopus 로고
    • Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1
    • Rodgers JT, Lerin C, Haas W, Gygi SP, Spiegelman BM, et al.(2005) Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1. Nature 434: 113-118.
    • (2005) Nature , vol.434 , pp. 113-118
    • Rodgers, J.T.1    Lerin, C.2    Haas, W.3    Gygi, S.P.4    Spiegelman, B.M.5
  • 8
    • 35549008884 scopus 로고    scopus 로고
    • SIRT1 promotes endothelium-dependent vascular relaxation by activating endothelial nitric oxide synthase
    • Mattagajasingh I, Kim CS, Naqvi A, Yamamori T, Hoffman TA, et al.(2007) SIRT1 promotes endothelium-dependent vascular relaxation by activating endothelial nitric oxide synthase. Proc Natl Acad Sci USA 104: 14855-14860.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 14855-14860
    • Mattagajasingh, I.1    Kim, C.S.2    Naqvi, A.3    Yamamori, T.4    Hoffman, T.A.5
  • 9
    • 3042681042 scopus 로고    scopus 로고
    • Sirt1 promotes fat mobilization in white adipocytes by repressing PPARgamma
    • Picard F, Kurtev M, Chung N, Topark-Ngarm A, Senawong T, et al.(2004) Sirt1 promotes fat mobilization in white adipocytes by repressing PPARgamma. Nature 429: 771-776.
    • (2004) Nature , vol.429 , pp. 771-776
    • Picard, F.1    Kurtev, M.2    Chung, N.3    Topark-Ngarm, A.4    Senawong, T.5
  • 10
    • 42649146208 scopus 로고    scopus 로고
    • SIRT1, an antiinflammatory and antiaging protein, is decreased in lungs of patients with chronic obstructive pulmonary disease
    • Rajendrasozhan S, Yang SR, Kinnula VL, Rahman I, (2008) SIRT1, an antiinflammatory and antiaging protein, is decreased in lungs of patients with chronic obstructive pulmonary disease. Am J Respir Crit Care Med 177: 861-870.
    • (2008) Am J Respir Crit Care Med , vol.177 , pp. 861-870
    • Rajendrasozhan, S.1    Yang, S.R.2    Kinnula, V.L.3    Rahman, I.4
  • 11
    • 36248935670 scopus 로고    scopus 로고
    • Sirt1 interacts with transducin-like enhancer of split-1 to inhibit nuclear factor kappaB-mediated transcription
    • Ghosh HS, Spencer JV, Ng B, McBurney MW, Robbins PD, (2007) Sirt1 interacts with transducin-like enhancer of split-1 to inhibit nuclear factor kappaB-mediated transcription. Biochem J 408: 105-111.
    • (2007) Biochem J , vol.408 , pp. 105-111
    • Ghosh, H.S.1    Spencer, J.V.2    Ng, B.3    McBurney, M.W.4    Robbins, P.D.5
  • 12
    • 0033214237 scopus 로고    scopus 로고
    • The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
    • Kaeberlein M, McVey M, Guarente L, (1999) The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms. Genes Dev 13: 2570-80.
    • (1999) Genes Dev , vol.13 , pp. 2570-2580
    • Kaeberlein, M.1    McVey, M.2    Guarente, L.3
  • 13
    • 33746245679 scopus 로고    scopus 로고
    • C. elegans 14-3-3 proteins regulate life span and interact with SIR-2.1 and DAF-16/FOXO
    • Wang Y, Oh SW, Deplancke B, Luo J, Walhout AJ, et al.(2006) C. elegans 14-3-3 proteins regulate life span and interact with SIR-2.1 and DAF-16/FOXO. Mech Ageing Dev 127: 741-747.
    • (2006) Mech Ageing Dev , vol.127 , pp. 741-747
    • Wang, Y.1    Oh, S.W.2    Deplancke, B.3    Luo, J.4    Walhout, A.J.5
  • 14
    • 3943071801 scopus 로고    scopus 로고
    • Sirtuin activators mimic caloric restriction and delay ageing in metazoans
    • Wood JG, Rogina B, Lavu S, Howitz K, Helfand SL, et al.(2004) Sirtuin activators mimic caloric restriction and delay ageing in metazoans. Nature 430: 686-689.
    • (2004) Nature , vol.430 , pp. 686-689
    • Wood, J.G.1    Rogina, B.2    Lavu, S.3    Howitz, K.4    Helfand, S.L.5
  • 15
  • 16
    • 34547914840 scopus 로고    scopus 로고
    • Sirtuins: the 'magnificent seven', function, metabolism and longevity
    • Dali-Youcef N, Lagouge M, Froelich S, Koehl C, Schoonjans K, et al.(2007) Sirtuins: the 'magnificent seven', function, metabolism and longevity. Ann Med 39: 335-345.
    • (2007) Ann Med , vol.39 , pp. 335-345
    • Dali-Youcef, N.1    Lagouge, M.2    Froelich, S.3    Koehl, C.4    Schoonjans, K.5
  • 17
    • 33751113602 scopus 로고    scopus 로고
    • Mammalian sirtuins-emerging roles in physiology, aging, and calorie restriction
    • Haigis MC, Guarente LP, (2006) Mammalian sirtuins-emerging roles in physiology, aging, and calorie restriction. Genes Dev 20: 2913-2921.
    • (2006) Genes Dev , vol.20 , pp. 2913-2921
    • Haigis, M.C.1    Guarente, L.P.2
  • 18
    • 34848817393 scopus 로고    scopus 로고
    • Diabetes Spectrum
    • Hollander P, (2007) Diabetes Spectrum 20: 159.
    • (2007) , vol.20 , pp. 159
    • Hollander, P.1
  • 19
    • 36749087548 scopus 로고    scopus 로고
    • Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes
    • Milne JC, Lambert PD, Schenk S, Carney DP, Smith JJ, et al.(2007) Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes. Nature 450: 712-6.
    • (2007) Nature , vol.450 , pp. 712-716
    • Milne, J.C.1    Lambert, P.D.2    Schenk, S.3    Carney, D.P.4    Smith, J.J.5
  • 20
    • 63149150180 scopus 로고    scopus 로고
    • Discovery of oxazolo4,5-b.pyridines and related heterocyclic analogs as novel SIRT1 activators
    • Bemis JE, Vu CB, Xie R, Nunes JJ, Ng PY, et al.(2009) Discovery of oxazolo4,5-b.pyridines and related heterocyclic analogs as novel SIRT1 activators. Bioorg Med Chem Lett 19: 2350-3.
    • (2009) Bioorg Med Chem Lett , vol.19 , pp. 2350-2353
    • Bemis, J.E.1    Vu, C.B.2    Xie, R.3    Nunes, J.J.4    Ng, P.Y.5
  • 21
    • 2942534101 scopus 로고    scopus 로고
    • Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone/protein deacetylases
    • Zhao K, Harshaw R, Chai X, Marmorstein R, (2004) Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone/protein deacetylases. Proc Natl Acad Sci USA 101: 8563.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 8563
    • Zhao, K.1    Harshaw, R.2    Chai, X.3    Marmorstein, R.4
  • 22
    • 0037072885 scopus 로고    scopus 로고
    • Structural basis for the NAD-dependent deacetylase mechanism of Sir2
    • Chang JH, Kim HC, Hwang KY, Lee JW, Jackson SP, et al.(2002) Structural basis for the NAD-dependent deacetylase mechanism of Sir2. J Biol Chem 277: 34489-34498.
    • (2002) J Biol Chem , vol.277 , pp. 34489-34498
    • Chang, J.H.1    Kim, H.C.2    Hwang, K.Y.3    Lee, J.W.4    Jackson, S.P.5
  • 24
    • 0035917536 scopus 로고    scopus 로고
    • Crystal structure of a SIR2 homolog-NAD complex
    • Min J, Landry J, Sternglanz R, Xu RM, (2001) Crystal structure of a SIR2 homolog-NAD complex. Cell 105: 269.
    • (2001) Cell , vol.105 , pp. 269
    • Min, J.1    Landry, J.2    Sternglanz, R.3    Xu, R.M.4
  • 25
    • 15244355745 scopus 로고    scopus 로고
    • Mechanism of sirtuin inhibition by nicotinamide: altering the NAD(+) cosubstrate specificity of a Sir2 enzyme
    • Avalos JL, Bever KM, Wolberger C, (2005) Mechanism of sirtuin inhibition by nicotinamide: altering the NAD(+) cosubstrate specificity of a Sir2 enzyme. Mol Cell 17: 855.
    • (2005) Mol Cell , vol.17 , pp. 855
    • Avalos, J.L.1    Bever, K.M.2    Wolberger, C.3
  • 26
    • 1542298916 scopus 로고    scopus 로고
    • Structure and Substrate Binding Properties of cobB, a Sir2 Homolog Protein Deacetylase from Escherichia coli
    • Zhao K, Chai X, Marmorstein R, (2004) Structure and Substrate Binding Properties of cobB, a Sir2 Homolog Protein Deacetylase from Escherichia coli. Journal of Molecular Biology 337: 731.
    • (2004) Journal of Molecular Biology , vol.337 , pp. 731
    • Zhao, K.1    Chai, X.2    Marmorstein, R.3
  • 27
    • 33947203766 scopus 로고    scopus 로고
    • Evaluation of the structural quality of modeled proteins by using globularity criteria
    • Costantini S, Facchiano AM, Colonna G, (2007) Evaluation of the structural quality of modeled proteins by using globularity criteria. BMC Structural Biology 7: 9.
    • (2007) BMC Structural Biology , vol.7 , pp. 9
    • Costantini, S.1    Facchiano, A.M.2    Colonna, G.3
  • 30
    • 0034663597 scopus 로고    scopus 로고
    • Application of enhanced multiple sequence alignment profiles to improve protein secondary structure prediction
    • Cuff JA, Barton GJ, (2000) Application of enhanced multiple sequence alignment profiles to improve protein secondary structure prediction. Proteins: Structure, Function and Genetics 40: 502-511.
    • (2000) Proteins: Structure, Function and Genetics , vol.40 , pp. 502-511
    • Cuff, J.A.1    Barton, G.J.2
  • 31
    • 58849136179 scopus 로고    scopus 로고
    • Prediction of the protein structural class by specific peptide frequencies
    • Costantini S, Facchiano AM, (2009) Prediction of the protein structural class by specific peptide frequencies. Biochimie 91: 226-9.
    • (2009) Biochimie , vol.91 , pp. 226-229
    • Costantini, S.1    Facchiano, A.M.2
  • 32
    • 36749031065 scopus 로고    scopus 로고
    • ClusPro: performance in CAPRI rounds 6-11 and the new server
    • Comeau SR, Kozakov D, Brenke R, Shen Y, Beglov D, et al.(2007) ClusPro: performance in CAPRI rounds 6-11 and the new server. Proteins 69: 781-5.
    • (2007) Proteins , vol.69 , pp. 781-785
    • Comeau, S.R.1    Kozakov, D.2    Brenke, R.3    Shen, Y.4    Beglov, D.5
  • 33
    • 2642524483 scopus 로고    scopus 로고
    • A physical reference state unifies the structure-derived potential of mean force for protein folding and binding
    • Liu S, Zhang C, Zhou H, Zhou Y, (2004) A physical reference state unifies the structure-derived potential of mean force for protein folding and binding. Proteins 56: 93-101.
    • (2004) Proteins , vol.56 , pp. 93-101
    • Liu, S.1    Zhang, C.2    Zhou, H.3    Zhou, Y.4
  • 34
    • 33744956371 scopus 로고    scopus 로고
    • Use of substrate analogs and mutagenesis to study substrate binding and catalysis in the Sir2 family of NAD-dependent protein deacetylases
    • Khan AN, Lewis PN, (2006) Use of substrate analogs and mutagenesis to study substrate binding and catalysis in the Sir2 family of NAD-dependent protein deacetylases. J Biol Chem 281: 11702-11.
    • (2006) J Biol Chem , vol.281 , pp. 11702-11711
    • Khan, A.N.1    Lewis, P.N.2
  • 35
    • 0141719702 scopus 로고    scopus 로고
    • Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan
    • Howitz KT, Bitterman KJ, Cohen HY, Lamming DW, Lavu S, et al.(2003) Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan. Nature 425: 191-196.
    • (2003) Nature , vol.425 , pp. 191-196
    • Howitz, K.T.1    Bitterman, K.J.2    Cohen, H.Y.3    Lamming, D.W.4    Lavu, S.5
  • 36
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, Jones DT, (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. Journal of Molecular Biology 337: 635-645.
    • (2004) Journal of Molecular Biology , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 37
    • 36749081458 scopus 로고    scopus 로고
    • Assessment of disorder predictions in CASP7
    • Bordoli L, Kiefer F, Schwede T, (2007) Assessment of disorder predictions in CASP7. Proteins 69S: 129-136.
    • (2007) Proteins , vol.69 S , pp. 129-136
    • Bordoli, L.1    Kiefer, F.2    Schwede, T.3
  • 38
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson HJ, Wright PE, (2005) Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6: 197-208.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 40
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa P, (2002) Intrinsically unstructured proteins. Trends Biochem Sci 27: 527-533.
    • (2002) Trends Biochem Sci , vol.27 , pp. 527-533
    • Tompa, P.1
  • 41
    • 33847768609 scopus 로고    scopus 로고
    • Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions
    • Xie H, Vucetic S, Iakoucheva LM, Oldfield CJ, Dunker AK, et al.(2007) Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions. J Proteome Res 6: 1882-1898.
    • (2007) J Proteome Res , vol.6 , pp. 1882-1898
    • Xie, H.1    Vucetic, S.2    Iakoucheva, L.M.3    Oldfield, C.J.4    Dunker, A.K.5
  • 42
    • 34250365395 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of the NAD+-dependent histone deacetylase SIRT1
    • Tanno M, Sakamoto J, Miura T, Shimamoto K, Horio Y, (2007) Nucleocytoplasmic shuttling of the NAD+-dependent histone deacetylase SIRT1. J Biol Chem 282: 6823-32.
    • (2007) J Biol Chem , vol.282 , pp. 6823-6832
    • Tanno, M.1    Sakamoto, J.2    Miura, T.3    Shimamoto, K.4    Horio, Y.5
  • 43
    • 53649100104 scopus 로고    scopus 로고
    • JNK2-dependent regulation of SIRT1 protein stability
    • Ford J, Ahmed S, Allison S, Jiang M, Milner J, (2008) JNK2-dependent regulation of SIRT1 protein stability Cell Cycle 19: 3091-3097.
    • (2008) Cell Cycle , vol.19 , pp. 3091-3097
    • Ford, J.1    Ahmed, S.2    Allison, S.3    Jiang, M.4    Milner, J.5
  • 44
    • 4344590155 scopus 로고    scopus 로고
    • Small molecules that regulate lifespan: evidence for xenohormesis
    • Lamming DW, Wood JG, Sinclair DA, (2004) Small molecules that regulate lifespan: evidence for xenohormesis. Mol Microbiol 53: 1003-9.
    • (2004) Mol Microbiol , vol.53 , pp. 1003-1009
    • Lamming, D.W.1    Wood, J.G.2    Sinclair, D.A.3
  • 46
    • 33947304756 scopus 로고    scopus 로고
    • Substrate competition as a source of ultrasensitivity in the inactivation of Wee1
    • Kim SY, Ferrell JE, (2007) Substrate competition as a source of ultrasensitivity in the inactivation of Wee1. Cell 128: 1133.
    • (2007) Cell , vol.128 , pp. 1133
    • Kim, S.Y.1    Ferrell, J.E.2
  • 47
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson T, (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.3
  • 48
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL, (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234: 779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 49
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM, (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 26: 283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 50
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C, (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 2: 2577-2637.
    • (1983) Biopolymers , vol.2 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 51
    • 34248164010 scopus 로고    scopus 로고
    • Crystal structures of an ATP-dependent hexokinase with broad substrate specificity from the hyperthermophilic archaeon Sulfolobus tokodaii
    • Nishimasu H, Fushinobu S, Shoun H, Wakagi T, (2007) Crystal structures of an ATP-dependent hexokinase with broad substrate specificity from the hyperthermophilic archaeon Sulfolobus tokodaii. J Biol Chem 282: 9923-9931.
    • (2007) J Biol Chem , vol.282 , pp. 9923-9931
    • Nishimasu, H.1    Fushinobu, S.2    Shoun, H.3    Wakagi, T.4
  • 52
    • 34548136236 scopus 로고    scopus 로고
    • An evaluation of automated homology modelling methods at low target-template sequence similarity
    • Dalton JAR, Jackson RM, (2007) An evaluation of automated homology modelling methods at low target-template sequence similarity. Bioinformatics 23: 1901-1908.
    • (2007) Bioinformatics , vol.23 , pp. 1901-1908
    • Dalton, J.A.R.1    Jackson, R.M.2
  • 54
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • Shi J, Blundell TL, Mizuguchi K, (2001) FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J Mol Biol 310: 243-257.
    • (2001) J Mol Biol , vol.310 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 55
    • 0242362161 scopus 로고    scopus 로고
    • Combining local-structure, fold-recognition, and new fold methods for protein structure prediction
    • Karplus K, Karchin R, Draper J, Casper J, Mandel-Gutfreund Y, et al.(2003) Combining local-structure, fold-recognition, and new fold methods for protein structure prediction. Proteins 6: 491-6.
    • (2003) Proteins , vol.6 , pp. 491-496
    • Karplus, K.1    Karchin, R.2    Draper, J.3    Casper, J.4    Mandel-Gutfreund, Y.5
  • 56
    • 0037188507 scopus 로고    scopus 로고
    • Evaluating conformational free energies: the colony energy and its application to the problem of loop prediction
    • Xiang Z, Soto CS, Honig B, (2002) Evaluating conformational free energies: the colony energy and its application to the problem of loop prediction. PNAS 99: 7432-7437.
    • (2002) PNAS , vol.99 , pp. 7432-7437
    • Xiang, Z.1    Soto, C.S.2    Honig, B.3
  • 58
    • 34248570351 scopus 로고    scopus 로고
    • Simulation of conformational changes occurring when a protein interacts with its receptor
    • Costantini S, Colonna G, Facchiano AM, (2007) Simulation of conformational changes occurring when a protein interacts with its receptor. Computational Biology and Chemistry 31: 196-206.
    • (2007) Computational Biology and Chemistry , vol.31 , pp. 196-206
    • Costantini, S.1    Colonna, G.2    Facchiano, A.M.3
  • 59
    • 56149094423 scopus 로고    scopus 로고
    • Molecular modelling of co-receptor CD8aa and its complex with MHC class I and T-cell receptor in sea bream (Sparus aurata)
    • Costantini S, Buonocore F, Facchiano AM, (2008) Molecular modelling of co-receptor CD8aa and its complex with MHC class I and T-cell receptor in sea bream (Sparus aurata). Fish Shellfish Immunology 25: 782-90.
    • (2008) Fish Shellfish Immunology , vol.25 , pp. 782-790
    • Costantini, S.1    Buonocore, F.2    Facchiano, A.M.3
  • 60
    • 0030028728 scopus 로고    scopus 로고
    • Principals of protein-protein interactions derived from structural studies
    • Jones S, Thornton JM, (1996) Principals of protein-protein interactions derived from structural studies. PNAS 93: 13-20.
    • (1996) PNAS , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2


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