메뉴 건너뛰기




Volumn 9, Issue 7, 2014, Pages

Rational modification of estrogen receptor by combination of computational and experimental analysis

Author keywords

[No Author keywords available]

Indexed keywords

4 NONYLPHENOL; 4 TERT OCTYLPHENOL; 4,4' ISOPROPYLIDENEDIPHENOL; AMINO ACID; ENDOCRINE DISRUPTOR; ESTROGEN RECEPTOR; ETHINYLESTRADIOL; TAMOXIFEN; PROTEIN BINDING;

EID: 84905046391     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0102658     Document Type: Article
Times cited : (9)

References (61)
  • 1
    • 0024545638 scopus 로고
    • Gene regulation by steroid hormones
    • Beato M (1989) Gene regulation by steroid hormones. Cell 56: 335-344.
    • (1989) Cell , vol.56 , pp. 335-344
    • Beato, M.1
  • 2
    • 0034466972 scopus 로고    scopus 로고
    • Estrogen receptor alpha and estrogen receptor beta: Regulation by selective estrogen receptor modulators and importance in breast cancer
    • DOI 10.1186/bcr78
    • Katzenellenbogen BS, Katzenellenbogen JA (2000) Estrogen receptor transcription and transactivation. Estrogen receptor alpha and estrogen receptor beta: regulation by selective estrogen receptor modulators and importance in breast cancer. Breast Cancer Research 2: 335-344. (Pubitemid 32223616)
    • (2000) Breast Cancer Research , vol.2 , Issue.5 , pp. 335-344
    • Katzenellenbogen, B.S.1    Katzenellenbogen, J.A.2
  • 3
    • 0035050785 scopus 로고    scopus 로고
    • Role of estrogen receptor beta in estrogen action
    • DOI 10.1146/annurev.physiol.63.1.165
    • Pettersson K, Gustafsson JA (2001) Role of estrogen receptor beta in estrogen action. Annual Review of Physiology 63: 165-192. (Pubitemid 32318327)
    • (2001) Annual Review of Physiology , vol.63 , pp. 165-192
    • Pettersson, K.1    Gustafsson, J.-A.2
  • 4
    • 78751633381 scopus 로고    scopus 로고
    • The varied roles of nuclear receptors during vertebrate embryonic development
    • Chung AC, Cooney AJ (2003) The varied roles of nuclear receptors during vertebrate embryonic development. Nuclear Receptor Signaling 1: 1-7.
    • (2003) Nuclear Receptor Signaling , vol.1 , pp. 1-7
    • Chung, A.C.1    Cooney, A.J.2
  • 5
    • 66649085200 scopus 로고    scopus 로고
    • Increased exposure to estrogens disturbs maturation, steroidogenesis, and cholesterol homeostasis via estrogen receptor a in adult mouse Leydig cells
    • Strauss L, Kallio J, Desai N, Pakarinen P, Miettinen T, et al. (2009) Increased exposure to estrogens disturbs maturation, steroidogenesis, and cholesterol homeostasis via estrogen receptor a in adult mouse Leydig cells. Endocrinology 150: 2865-2872.
    • (2009) Endocrinology , vol.150 , pp. 2865-2872
    • Strauss, L.1    Kallio, J.2    Desai, N.3    Pakarinen, P.4    Miettinen, T.5
  • 6
    • 84857779333 scopus 로고    scopus 로고
    • Autoantibodies to estrogen receptor a interfere with T lymphocyte homeostasis and are associated with disease activity in systemic lupus erythematosus
    • Colasanti T, Maselli A, Conti F, Sanchez M, Alessandri C, et al. (2012) Autoantibodies to estrogen receptor a interfere with T lymphocyte homeostasis and are associated with disease activity in systemic lupus erythematosus. Arthritis and Rheumatism 64: 778-787.
    • (2012) Arthritis and Rheumatism , vol.64 , pp. 778-787
    • Colasanti, T.1    Maselli, A.2    Conti, F.3    Sanchez, M.4    Alessandri, C.5
  • 7
    • 80053630034 scopus 로고    scopus 로고
    • Myeloid-specific estrogen receptor a deficiency impairs metabolic homeostasis and accelerates atherosclerotic lesion development
    • Ribas V, Drew BG, Le JA, Soleymani T, Daraei P, et al. (2011) Myeloid-specific estrogen receptor a deficiency impairs metabolic homeostasis and accelerates atherosclerotic lesion development. PNAS 108: 16457-16462.
    • (2011) PNAS , vol.108 , pp. 16457-16462
    • Ribas, V.1    Drew, B.G.2    Le, J.A.3    Soleymani, T.4    Daraei, P.5
  • 8
    • 0030593681 scopus 로고    scopus 로고
    • ERbeta: Identification and characterization of a novel human estrogen receptor
    • DOI 10.1016/0014-5793(96)00782-X
    • Mosselman S, Polman J, Dijkema R (1996) ER beta: identification and characterization of a novel human estrogen receptor. FEBS Letters 392: 49-53. (Pubitemid 26268330)
    • (1996) FEBS Letters , vol.392 , Issue.1 , pp. 49-53
    • Mosselman, S.1    Polman, J.2    Dijkema, R.3
  • 9
    • 52049106638 scopus 로고    scopus 로고
    • Extra-nuclear Signaling of Estrogen Receptors
    • Fu X, Simoncini T (2008) Extra-nuclear Signaling of Estrogen Receptors. IUBMB Life 60: 502-510.
    • (2008) IUBMB Life , vol.60 , pp. 502-510
    • Fu, X.1    Simoncini, T.2
  • 10
    • 34548076290 scopus 로고    scopus 로고
    • Membrane-associated estrogen receptor signaling pathways in human cancers
    • DOI 10.1158/1078-0432.CCR-07-1373
    • Pietras RJ, Márquez-Garbán DC (2007) Membrane-associated estrogen receptor signaling pathways in human cancers. Clinical Cancer Research 13: 4672-4676. (Pubitemid 47294772)
    • (2007) Clinical Cancer Research , vol.13 , Issue.16 , pp. 4672-4676
    • Pietras, R.J.1    Marquez-Garban, D.C.2
  • 11
    • 0033054115 scopus 로고    scopus 로고
    • The structure of the nuclear hormone receptors
    • DOI 10.1016/S0039-128X(99)00014-8, PII S0039128X99000148
    • Kumar R, Thompson EB (1999) The structure of the nuclear hormone receptors. Steroids 64: 310-319. (Pubitemid 29284331)
    • (1999) Steroids , vol.64 , Issue.5 , pp. 310-319
    • Kumar, R.1    Thompson, E.B.2
  • 14
    • 0028862855 scopus 로고
    • Analysis of the structural core of the human estrogen receptor ligand binding domain by selective proteolysis/mass spectrometric analysis
    • Seielstad DA, Carlson KE, Kushner PJ, Greene GL, Katzenellenbogen JA (1995) Analysis of the structural core of the human estrogen receptor ligand binding domain by selective proteolysis/mass spectrometric analysis. Biochemistry 34: 12605-12615.
    • (1995) Biochemistry , vol.34 , pp. 12605-12615
    • Seielstad, D.A.1    Carlson, K.E.2    Kushner, P.J.3    Greene, G.L.4    Katzenellenbogen, J.A.5
  • 15
    • 0034468021 scopus 로고    scopus 로고
    • Structure-function relationships in DNA- and ligand-binding domains of estrogen receptors
    • DOI 10.1186/bcr80
    • Ruff M, Gangloff M, Wurtz JM, Moras D (2000) Estrogen receptor transcription and transactivation: structure-function relationship in DNA- and ligand-binding domains of estrogen receptors. Breast Cancer Research 2: 353-359. (Pubitemid 32223618)
    • (2000) Breast Cancer Research , vol.2 , Issue.5 , pp. 353-359
    • Ruff, M.1    Gangloff, M.2    Wurtz, J.M.3    Moras, D.4
  • 17
    • 0033976103 scopus 로고    scopus 로고
    • Differential binding affinities of PCBs, HO-PCBs, and aroclors with recombinant human, rainbow trout (Onchorhynkiss mykiss), and green anole (Anolis carolinensis) estrogen receptors, using a semi-high throughput competitive binding assay
    • Matthews J, Zacharewski TR (2000) Differential binding affinities PCBs, HOPCBs and Aroclors with recombinant human, rainbow trout (Onchorhynkiss mykiss) and reptilian (Anolis carolinensis) estrogen receptors using a semi-high throughput competitive binding assay. Toxicological Sciences 53: 326-339. (Pubitemid 30100150)
    • (2000) Toxicological Sciences , vol.53 , Issue.2 , pp. 326-339
    • Matthews, J.1    Zacharewski, T.2
  • 18
    • 0034668703 scopus 로고    scopus 로고
    • Differential estrogen receptor binding of estrogenic substances: A species comparison
    • DOI 10.1016/S0960-0760(00)00126-6, PII S0960076000001266
    • Matthews J, Celius T, Halgren R, Zacharewski T (2000) Differential estrogen receptor binding of estrogenic substances: a species comparison. Journal of Steroid Biochemistry & Molecular Biology 74: 223-234. (Pubitemid 32121658)
    • (2000) Journal of Steroid Biochemistry and Molecular Biology , vol.74 , Issue.4 , pp. 223-234
    • Matthews, J.1    Celius, T.2    Halgren, R.3    Zacharewski, T.4
  • 19
    • 0028921939 scopus 로고
    • Rainbow trout estrogen receptor presents an equal specificity but a differential sensitivity for estrogens than human estrogen receptor
    • Le Drean Y, Kern L, Pakdel F, Valotaire Y (1995) Rainbow trout estrogen receptor presents an equal specificity but a differential sensitivity for estrogens than human estrogen receptor. Molecular and Cellular Endocrinology 109 27-35.
    • (1995) Molecular and Cellular Endocrinology , vol.109 , pp. 27-35
    • Le Drean, Y.1    Kern, L.2    Pakdel, F.3    Valotaire, Y.4
  • 20
    • 0032576482 scopus 로고    scopus 로고
    • Xenoendocrine disrupters - environmental impacts
    • Sumpter JP (1998) Xenoendocrine disrupters - environmental impacts. Toxicology Letters 102-103: 337-342.
    • (1998) Toxicology Letters , vol.102-103 , pp. 337-342
    • Sumpter, J.P.1
  • 22
    • 0036367569 scopus 로고    scopus 로고
    • Potential effects of certain persistent organic pollutants and endocrine disrupting chemicals on the health of children
    • Damstra T (2002) Potential effects of certain persistent organic pollutants and endocrine disrupting chemicals on the health of children. Journal of Toxicology and Clinical Toxicology 40: 457-465.
    • (2002) Journal of Toxicology and Clinical Toxicology , vol.40 , pp. 457-465
    • Damstra, T.1
  • 23
    • 0346728622 scopus 로고    scopus 로고
    • Similarities and differences in uterine gene expression patterns caused by treatment with physiological and non-physiological estrogens
    • DOI 10.1677/jme.0.0310487
    • Watanabe H, Suzuki A, Kobayashi M, Lubahn DB, Handa H, et al. (2003) Similarities and differences in uterine gene expression patterns caused by treatment with physiological and non-physiological estrogens. Journal of Molecular Endocrinology 31: 487-497. (Pubitemid 38054519)
    • (2003) Journal of Molecular Endocrinology , vol.31 , Issue.3 , pp. 487-497
    • Watanabe, H.1    Suzuki, A.2    Kobayashi, M.3    Lubahn, D.B.4    Handa, H.5    Iguchi, T.6
  • 24
    • 0036072321 scopus 로고    scopus 로고
    • Clues from wildlife to create an assay for thyroid system disruption
    • Colborn T (2002) Clues from wildlife to create an assay for thyroid system disruption. Environmental Health Perspectives 110: 363-367.
    • (2002) Environmental Health Perspectives , vol.110 , pp. 363-367
    • Colborn, T.1
  • 25
    • 0031844641 scopus 로고    scopus 로고
    • Endocrine disruption in wildlife: A critical review of the evidence
    • Tyler CR, Jobling S, Sumpter JP (1998) Endocrine disruption in wildlife: a critical review of the evidence. Critical Review of Toxicology 28: 319-361. (Pubitemid 28389719)
    • (1998) Critical Reviews in Toxicology , vol.28 , Issue.4 , pp. 319-361
    • Tyler, C.R.1    Jobling, S.2    Sumpter, J.P.3
  • 27
    • 0035878961 scopus 로고    scopus 로고
    • Evidence for endocrine disruption in perch (Perca fluviatilis) and roach (Rutilus rutilus) in a remote Swedish lake in the vicinity of a public refuse dump
    • DOI 10.1006/taap.2001.9194
    • Noaksson E, Tjärnlund U, Bosveld AT, Balk L (2001) Evidence for endocrine disruption in perch (Perca fluviatilis) and roach (Rutilus rutilus) in a remote swedish lake in the vicinity of a public refuse dump. Toxicology and Applied Pharmacology 174: 160-176. (Pubitemid 32675519)
    • (2001) Toxicology and Applied Pharmacology , vol.174 , Issue.2 , pp. 160-176
    • Noaksson, E.1    Tjarnlund, U.2    Bosveld, A.T.C.3    Balk, L.4
  • 28
    • 77957722517 scopus 로고    scopus 로고
    • Endocrine modulation, inhibition of ovarian development and hepatic alterations in rainbow trout exposed to polluted river water
    • Viganò L, Benfenati E, Bottero S, Cevasco A, Monteverde M, et al. (2010) Endocrine modulation, inhibition of ovarian development and hepatic alterations in rainbow trout exposed to polluted river water. Environmental Pollution 158: 3675-3683.
    • (2010) Environmental Pollution , vol.158 , pp. 3675-3683
    • Viganò, L.1    Benfenati, E.2    Bottero, S.3    Cevasco, A.4    Monteverde, M.5
  • 30
    • 0032813357 scopus 로고    scopus 로고
    • The extent of oestrogenic contamination in the UK estuarine and marine environments - Further surveys of flounder
    • DOI 10.1016/S0048-9697(99)00175-8, PII S0048969799001758
    • Allen Y, Matthiessen P, Scott AP, Haworth S, Feist S, et al. (1999) The extent of oestrogenic contamination in the UK estuarine and marine environments - further surveys of flounder. The Science of the Total Environment 233: 5-20. (Pubitemid 29389752)
    • (1999) Science of the Total Environment , vol.233 , Issue.1-3 , pp. 5-20
    • Allen, Y.1    Matthiessen, P.2    Scott, A.P.3    Haworth, S.4    Feist, S.5    Thain, J.E.6
  • 31
    • 0033627291 scopus 로고    scopus 로고
    • Elevated serum vitellogenin levels and gonadal abnormalities in wild male flounder (Pleuronectes yokohamae) from Tokyo Bay, Japan
    • DOI 10.1016/S0141-1136(99)00047-1, PII S0141113699000471
    • Hashimoto S, Bessho H, Hara A, Nakamura M, Iguchi TF, K. (2000) Elevated serum vitellogenin levels and gonadal abnormalities in wild male flounder (Pleuronectes yokohamae) from Tokyo Bay, Japan. Mar Environ Res 49: 37-53. (Pubitemid 29512345)
    • (2000) Marine Environmental Research , vol.49 , Issue.1 , pp. 37-53
    • Hashimoto, S.1    Bessho, H.2    Hara, A.3    Nakamura, M.4    Iguchi, T.5    Fujita, K.6
  • 32
    • 48949094847 scopus 로고    scopus 로고
    • Chemical and biological analysis of endocrine-disrupting hormones and estrogenic activity in an advanced sewage treatment plant
    • Muller M, Rabenoelina F, Balaguer P, Patureau D, Lemenach K, et al. (2008) Chemical and biological analysis of endocrine-disrupting hormones and estrogenic activity in an advanced sewage treatment plant. Environmental Toxicology and Chemistry 27: 1649-1658.
    • (2008) Environmental Toxicology and Chemistry , vol.27 , pp. 1649-1658
    • Muller, M.1    Rabenoelina, F.2    Balaguer, P.3    Patureau, D.4    Lemenach, K.5
  • 33
    • 83655169773 scopus 로고    scopus 로고
    • Biological effects and bioaccumulation of steroidal and phenolic endocrine disrupting chemicals in high-back crucian carp exposed to wastewater treatment plant effluents
    • Liu J, Wang R, Huang B, Lin C, Zhou J, et al. (2012) Biological effects and bioaccumulation of steroidal and phenolic endocrine disrupting chemicals in high-back crucian carp exposed to wastewater treatment plant effluents. Environmental Pollution 162: 325-331.
    • (2012) Environmental Pollution , vol.162 , pp. 325-331
    • Liu, J.1    Wang, R.2    Huang, B.3    Lin, C.4    Zhou, J.5
  • 34
    • 0032446607 scopus 로고    scopus 로고
    • The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen
    • DOI 10.1016/S0092-8674(00)81717-1
    • Shiau AK, Barstad D, Loria PM, Cheng L, Kushner PJ, et al. (1998) The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell 95: 927-937. (Pubitemid 29019045)
    • (1998) Cell , vol.95 , Issue.7 , pp. 927-937
    • Shiau, A.K.1    Barstad, D.2    Loria, P.M.3    Cheng, L.4    Kushner, P.J.5    Agard, D.A.6    Greene, G.L.7
  • 38
    • 0037156439 scopus 로고    scopus 로고
    • Prediction of the bioaccumulation factors and body burden of natural and synthetic estrogens in aquatic organisms in the river systems
    • DOI 10.1016/S0048-9697(01)01036-1, PII S0048969701010361
    • Lai KM, Scrimshaw MD, Lester JN (2002) Prediction of the bioaccumulation factors and body burden of natural and synthetic estrogens in aquatic organisms in the river systems. The Science of the Total Environonment 289: 159-168. (Pubitemid 34311792)
    • (2002) Science of the Total Environment , vol.289 , Issue.1-3 , pp. 159-168
    • Lai, K.M.1    Scrimshaw, M.D.2    Lester, J.N.3
  • 39
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases
    • Whitmore A, Wallace BA (2008) Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers 89: 392-400.
    • (2008) Biopolymers , vol.89 , pp. 392-400
    • Whitmore, A.1    Wallace, B.A.2
  • 40
    • 0035810957 scopus 로고    scopus 로고
    • Increase in the stability and helical content of estrogen receptor alpha in the presence of the estrogen response element: Analysis by circular dichroism spectroscopy
    • DOI 10.1021/bi002846l
    • Greenfield NJ, Vijayanathan V, Thomas TJ, Gallo MA, Thomas T (2001) Increase in the stability and helical content of estrogen receptor in the presence of the estrogen response element: analysis by circular dichroism spectroscopy. Biochemistry 40: 6646-6652. (Pubitemid 32552788)
    • (2001) Biochemistry , vol.40 , Issue.22 , pp. 6646-6652
    • Greenfield, N.1    Vijayanathan, V.2    Thomas, T.J.3    Gallo, M.A.4    Thomas, T.5
  • 41
    • 27644540697 scopus 로고    scopus 로고
    • Conformational dynamics of estrogen receptors alpha and beta as revealed by intrinsic tryptophan fluorescence and circular dichroism
    • DOI 10.1677/jme.1.01830
    • Nair SK, Thomas TJ, Greenfield NJ, Chen A, He H, et al. (2005) Conformational dynamics of estrogen receptors and as revealed by intrinsic tryptophan fluorescence and circular dichroism. Journal of Molecular Endocrinology 35: 211-223. (Pubitemid 41568117)
    • (2005) Journal of Molecular Endocrinology , vol.35 , Issue.2 , pp. 211-223
    • Nair, S.K.1    Thomas, T.J.2    Greenfield, N.J.3    Chen, A.4    He, H.5    Thomas, T.6
  • 43
    • 84889587777 scopus 로고    scopus 로고
    • In vitro tests aiding ecological risk assessment of ciprofloxacin, tamoxifen and cyclophosphamide in range of concentrations released in hospital wastewater and surface water
    • Mater N, Geret F, Castillo L, Faucet-Marquisa V, Albasia C, et al. (2014) In vitro tests aiding ecological risk assessment of ciprofloxacin, tamoxifen and cyclophosphamide in range of concentrations released in hospital wastewater and surface water. Environment International 63: 191-200.
    • (2014) Environment International , vol.63 , pp. 191-200
    • Mater, N.1    Geret, F.2    Castillo, L.3    Faucet-Marquisa, V.4    Albasia, C.5
  • 44
    • 84867718095 scopus 로고    scopus 로고
    • Association of endocrine-disrupting chemicals with total organic carbon in riverine water and suspended particulate matter from the Pearl River, China
    • Gong J, Ran Y, Chen D, Yang Y, Zeng EY (2012) Association of endocrine-disrupting chemicals with total organic carbon in riverine water and suspended particulate matter from the Pearl River, China. Environmental Toxicology and Chemistry 31: 2456-2464.
    • (2012) Environmental Toxicology and Chemistry , vol.31 , pp. 2456-2464
    • Gong, J.1    Ran, Y.2    Chen, D.3    Yang, Y.4    Zeng, E.Y.5
  • 45
    • 0034069492 scopus 로고    scopus 로고
    • Estrogenic activity of octylphenol, nonylphenol, bisphenol A and methoxychlor in rats
    • Laws SC, Carey SA, Ferrell JM, Bodman GJ, Cooper RL (2000) Estrogenic activity of octylphenol, nonylphenol, bisphenol A and methoxychlor in rats. Toxicological Sciences 54: 154-167. (Pubitemid 30152466)
    • (2000) Toxicological Sciences , vol.54 , Issue.1 , pp. 154-167
    • Laws, S.C.1    Carey, S.A.2    Ferrell, J.M.3    Bodman, G.J.4    Cooper, R.L.5
  • 47
    • 84890044388 scopus 로고    scopus 로고
    • Receptor-based high-throughput screening and identification of estrogens in dietary supplements using bioaffinity liquid-chromatography ion mobility mass spectrometry
    • Aqai P, Gomez Blesa N, Major H, Pedotti M, Varani L, et al. (2013) Receptor-based high-throughput screening and identification of estrogens in dietary supplements using bioaffinity liquid-chromatography ion mobility mass spectrometry. Analytical and Bioanalytical Chemistry 405: 9427-9436.
    • (2013) Analytical and Bioanalytical Chemistry , vol.405 , pp. 9427-9436
    • Aqai, P.1    Gomez Blesa, N.2    Major, H.3    Pedotti, M.4    Varani, L.5
  • 50
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang Y (2008) I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 9: 1-8.
    • (2008) BMC Bioinformatics , vol.9 , pp. 1-8
    • Zhang, Y.1
  • 51
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: A unified platform for automated protein structure and function prediction
    • Roy A, Kucukural A, Zhang Y (2010) I-TASSER: a unified platform for automated protein structure and function prediction. Nature Protocols 5: 725-738.
    • (2010) Nature Protocols , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 56
    • 40549111613 scopus 로고    scopus 로고
    • FACTS: Fast analytical continuum treatment of solvation
    • DOI 10.1002/jcc.20832
    • Haberthur U, Caflisch A (2008) FACTS: fast analytical continuum treatment of solvation. Journal of Computational Chemistry 29: 701-715. (Pubitemid 351364845)
    • (2008) Journal of Computational Chemistry , vol.29 , Issue.5 , pp. 701-715
    • Haberthur, U.1    Caflisch, A.2
  • 58
    • 0026279733 scopus 로고
    • Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system
    • Studier FW (1991) Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system. Journal of molecular Biology 219: 37-44.
    • (1991) Journal of Molecular Biology , vol.219 , pp. 37-44
    • Studier, F.W.1
  • 59
    • 0026879345 scopus 로고
    • Overproduction of full-length and truncated human estrogen receptors in Escherichia coli
    • Ahrens H, Schuh TJ, Rainish BL, Furlow JD, Gorski J, et al. (1992) Overproduction of full-length and truncated human estrogen receptors in Escherichia coli. Receptor 2: 77-92.
    • (1992) Receptor , vol.2 , pp. 77-92
    • Ahrens, H.1    Schuh, T.J.2    Rainish, B.L.3    Furlow, J.D.4    Gorski, J.5
  • 60
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • DOI 10.1006/abio.2000.4880
    • Sreerama N, Woody RW (2000) Estimation of protein secondary structure from CD spectra: Comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set. Analitical Biochemistry 287: 252-260. (Pubitemid 32006234)
    • (2000) Analytical Biochemistry , vol.287 , Issue.2 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 61
    • 34548819311 scopus 로고    scopus 로고
    • Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions
    • Greenfield NJ (2006) Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions. Nature Protocols 1: 2527-2535.
    • (2006) Nature Protocols , vol.1 , pp. 2527-2535
    • Greenfield, N.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.