메뉴 건너뛰기




Volumn 111, Issue 2, 2014, Pages 839-844

Erratum: Structural insights into gene repression by the orphan nuclear receptor SHP (Proceedings of the National Academy of Sciences of the United States of America (2014) 111 (839-844) DOI: 10.1073/pnas.1322827111);Structural insights into gene repression by the orphan nuclear receptor SHP

Author keywords

[No Author keywords available]

Indexed keywords

E1A LIKE INHIBITOR OF DIFFERENTIATION 1; ORPHAN NUCLEAR RECEPTOR; PROTEIN; SMALL HETERODIMER PARTNER; UNCLASSIFIED DRUG;

EID: 84892621275     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1402462111     Document Type: Erratum
Times cited : (22)

References (54)
  • 1
    • 0012473279 scopus 로고
    • The nuclear receptor superfamily: The second decade
    • Mangelsdorf DJ, et al. (1995) The nuclear receptor superfamily: The second decade. Cell 83(6):835-839.
    • (1995) Cell , vol.83 , Issue.6 , pp. 835-839
    • Mangelsdorf, D.J.1
  • 2
    • 3242888465 scopus 로고    scopus 로고
    • Gene silencing by nuclear orphan receptors
    • Zhang Y, Dufau ML (2004) Gene silencing by nuclear orphan receptors. Vitam Horm 68:1-48.
    • (2004) Vitam Horm , vol.68 , pp. 1-48
    • Zhang, Y.1    Dufau, M.L.2
  • 3
    • 13944276441 scopus 로고    scopus 로고
    • Crystallographic identification and functional characterization of phospholipids as ligands for the orphan nuclear receptor steroidogenic factor-1
    • Li Y, et al. (2005) Crystallographic identification and functional characterization of phospholipids as ligands for the orphan nuclear receptor steroidogenic factor-1. Mol Cell 17(4):491-502.
    • (2005) Mol Cell , vol.17 , Issue.4 , pp. 491-502
    • Li, Y.1
  • 4
    • 13544263313 scopus 로고    scopus 로고
    • Structural analyses reveal phosphatidyl inositols as ligands for the NR5 orphan receptors SF-1 and LRH-1
    • Krylova IN, et al. (2005) Structural analyses reveal phosphatidyl inositols as ligands for the NR5 orphan receptors SF-1 and LRH-1. Cell 120(3):343-355.
    • (2005) Cell , vol.120 , Issue.3 , pp. 343-355
    • Krylova, I.N.1
  • 5
    • 0033681001 scopus 로고    scopus 로고
    • Asymmetry in the PPARgamma/RXRalpha crystal structure reveals the molecular basis of heterodimerization among nuclear receptors
    • Gampe RT, Jr., et al. (2000) Asymmetry in the PPARgamma/RXRalpha crystal structure reveals the molecular basis of heterodimerization among nuclear receptors. Mol Cell 5(3):545-555.
    • (2000) Mol Cell , vol.5 , Issue.3 , pp. 545-555
    • Gampe, R.T.1
  • 6
    • 77954844606 scopus 로고    scopus 로고
    • Structural basis for hydroxycholesterols as natural ligands of orphan nuclear receptor RORgamma
    • Jin L, et al. (2010) Structural basis for hydroxycholesterols as natural ligands of orphan nuclear receptor RORgamma. Mol Endocrinol 24(5):923-929.
    • (2010) Mol Endocrinol , vol.24 , Issue.5 , pp. 923-929
    • Jin, L.1
  • 7
    • 71749101440 scopus 로고    scopus 로고
    • Multiple binding modes between HNF4alpha and the LXXLL motifs of PGC-1alpha lead to full activation
    • Rha GB, Wu G, Shoelson SE, Chi YI (2009) Multiple binding modes between HNF4alpha and the LXXLL motifs of PGC-1alpha lead to full activation. J Biol Chem 284(50): 35165-35176.
    • (2009) J Biol Chem , vol.284 , Issue.50 , pp. 35165-35176
    • Rha, G.B.1    Wu, G.2    Shoelson, S.E.3    Chi, Y.I.4
  • 8
    • 84863143896 scopus 로고    scopus 로고
    • Structural conservation of ligand binding reveals a bile acid-like signaling pathway in nematodes
    • Zhi X, et al. (2012) Structural conservation of ligand binding reveals a bile acid-like signaling pathway in nematodes. J Biol Chem 287(7):4894-4903.
    • (2012) J Biol Chem , vol.287 , Issue.7 , pp. 4894-4903
    • Zhi, X.1
  • 9
    • 0038646966 scopus 로고    scopus 로고
    • Activation of nuclear receptors: A perspective from structural genomics
    • Li Y, Lambert MH, Xu HE (2003) Activation of nuclear receptors: A perspective from structural genomics. Structure 11(7):741-746.
    • (2003) Structure , vol.11 , Issue.7 , pp. 741-746
    • Li, Y.1    Lambert, M.H.2    Xu, H.E.3
  • 10
    • 18244393501 scopus 로고    scopus 로고
    • Structural basis for antagonist-mediated recruitment of nuclear co-repressors by PPARalpha
    • Xu HE, et al. (2002) Structural basis for antagonist-mediated recruitment of nuclear co-repressors by PPARalpha. Nature 415(6873):813-817.
    • (2002) Nature , vol.415 , Issue.6873 , pp. 813-817
    • Xu, H.E.1
  • 11
    • 27844509037 scopus 로고    scopus 로고
    • Transcriptional corepression by SHP: Molecular mechanisms and physiological consequences
    • B?vner A, Sanyal S, Gustafsson JA, Treuter E (2005) Transcriptional corepression by SHP: Molecular mechanisms and physiological consequences. Trends Endocrinol Metab 16(10):478-488.
    • (2005) Trends Endocrinol Metab , vol.16 , Issue.10 , pp. 478-488
    • Bvner, A.1    Sanyal, S.2    Gustafsson, J.A.3    Treuter, E.4
  • 12
    • 0030001371 scopus 로고    scopus 로고
    • An orphan nuclear hormone receptor that lacks a DNA binding domain and heterodimerizes with other receptors
    • Seol W, Choi HS, Moore DD (1996) An orphan nuclear hormone receptor that lacks a DNA binding domain and heterodimerizes with other receptors. Science 272(5266): 1336-1339.
    • (1996) Science , vol.272 , Issue.5266 , pp. 1336-1339
    • Seol, W.1    Choi, H.S.2    Moore, D.D.3
  • 13
    • 0033637121 scopus 로고    scopus 로고
    • A regulatory cascade of the nuclear receptors FXR, SHP-1, and LRH-1 represses bile acid biosynthesis
    • Goodwin B, et al. (2000) A regulatory cascade of the nuclear receptors FXR, SHP-1, and LRH-1 represses bile acid biosynthesis. Mol Cell 6(3):517-526.
    • (2000) Mol Cell , vol.6 , Issue.3 , pp. 517-526
    • Goodwin, B.1
  • 14
    • 0033636789 scopus 로고    scopus 로고
    • Molecular basis for feedback regulation of bile acid synthesis by nuclear receptors
    • Lu TT, et al. (2000) Molecular basis for feedback regulation of bile acid synthesis by nuclear receptors. Mol Cell 6(3):507-515.
    • (2000) Mol Cell , vol.6 , Issue.3 , pp. 507-515
    • Lu, T.T.1
  • 15
    • 84870334072 scopus 로고    scopus 로고
    • Nuclear receptors HNF4α and LRH-1 cooperate in regulating Cyp7a1 in vivo
    • Kir S, Zhang Y, Gerard RD, Kliewer SA, Mangelsdorf DJ (2012) Nuclear receptors HNF4α and LRH-1 cooperate in regulating Cyp7a1 in vivo. J Biol Chem 287(49): 41334-41341.
    • (2012) J Biol Chem , vol.287 , Issue.49 , pp. 41334-41341
    • Kir, S.1    Zhang, Y.2    Gerard, R.D.3    Kliewer, S.A.4    Mangelsdorf, D.J.5
  • 16
    • 0037169541 scopus 로고    scopus 로고
    • Dual mechanisms for repression of the monomeric orphan receptor liver receptor homologous protein-1 by the orphan small heterodimer partner
    • Lee YK, Moore DD (2002) Dual mechanisms for repression of the monomeric orphan receptor liver receptor homologous protein-1 by the orphan small heterodimer partner. J Biol Chem 277(4):2463-2467.
    • (2002) J Biol Chem , vol.277 , Issue.4 , pp. 2463-2467
    • Lee, Y.K.1    Moore, D.D.2
  • 17
    • 0030712244 scopus 로고    scopus 로고
    • Novel receptor interaction and repression domains in the orphan receptor SHP
    • Seol W, Chung M, Moore DD (1997) Novel receptor interaction and repression domains in the orphan receptor SHP. Mol Cell Biol 17(12):7126-7131.
    • (1997) Mol Cell Biol , vol.17 , Issue.12 , pp. 7126-7131
    • Seol, W.1    Chung, M.2    Moore, D.D.3
  • 18
    • 22144487356 scopus 로고    scopus 로고
    • Structural and biochemical basis for selective repression of the orphan nuclear receptor liver receptor homolog 1 by small heterodimer partner
    • Li Y, et al. (2005) Structural and biochemical basis for selective repression of the orphan nuclear receptor liver receptor homolog 1 by small heterodimer partner. Proc Natl Acad Sci USA 102(27):9505-9510.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.27 , pp. 9505-9510
    • Li, Y.1
  • 19
    • 58949091760 scopus 로고    scopus 로고
    • SMILE, a new orphan nuclear receptor SHP-interacting protein, regulates SHP-repressed estrogen receptor transactivation
    • Xie YB, et al. (2008) SMILE, a new orphan nuclear receptor SHP-interacting protein, regulates SHP-repressed estrogen receptor transactivation. Biochem J 416(3):463-473.
    • (2008) Biochem J , vol.416 , Issue.3 , pp. 463-473
    • Xie, Y.B.1
  • 20
    • 35648935499 scopus 로고    scopus 로고
    • Involvement of corepressor complex subunit GPS2 in transcriptional pathways governing human bile acid biosynthesis
    • Sanyal S, et al. (2007) Involvement of corepressor complex subunit GPS2 in transcriptional pathways governing human bile acid biosynthesis. Proc Natl Acad Sci USA 104(40):15665-15670.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.40 , pp. 15665-15670
    • Sanyal, S.1
  • 21
    • 11344263349 scopus 로고    scopus 로고
    • Functional role of G9a-induced histone methylation in small heterodimer partner-mediated transcriptional repression
    • Boulias K, Talianidis I (2004) Functional role of G9a-induced histone methylation in small heterodimer partner-mediated transcriptional repression. Nucleic Acids Res 32(20):6096-6103.
    • (2004) Nucleic Acids Res , vol.32 , Issue.20 , pp. 6096-6103
    • Boulias, K.1    Talianidis, I.2
  • 22
    • 33846910174 scopus 로고    scopus 로고
    • Coordinated recruitment of histone methyltransferase G9a and other chromatin-modifying enzymes in SHP-mediated regulation of hepatic bile acid metabolism
    • Fang S, et al. (2007) Coordinated recruitment of histone methyltransferase G9a and other chromatin-modifying enzymes in SHP-mediated regulation of hepatic bile acid metabolism. Mol Cell Biol 27(4):1407-1424.
    • (2007) Mol Cell Biol , vol.27 , Issue.4 , pp. 1407-1424
    • Fang, S.1
  • 23
    • 4344601668 scopus 로고    scopus 로고
    • Role of an mSin3A-Swi/Snf chromatin remodeling complex in the feedback repression of bile acid biosynthesis by SHP
    • Kemper JK, Kim H, Miao J, Bhalla S, Bae Y (2004) Role of an mSin3A-Swi/Snf chromatin remodeling complex in the feedback repression of bile acid biosynthesis by SHP. Mol Cell Biol 24(17):7707-7719.
    • (2004) Mol Cell Biol , vol.24 , Issue.17 , pp. 7707-7719
    • Kemper, J.K.1    Kim, H.2    Miao, J.3    Bhalla, S.4    Bae, Y.5
  • 24
    • 0035984883 scopus 로고    scopus 로고
    • A transcriptional inhibitor targeted by the atypical orphan nuclear receptor SHP
    • B?vner A, Johansson L, Toresson G, Gustafsson JA, Treuter E (2002) A transcriptional inhibitor targeted by the atypical orphan nuclear receptor SHP. EMBO Rep 3(5): 478-484.
    • (2002) EMBO Rep , vol.3 , Issue.5 , pp. 478-484
    • Bvner, A.1    Johansson, L.2    Toresson, G.3    Gustafsson, J.A.4    Treuter, E.5
  • 25
    • 77955573162 scopus 로고    scopus 로고
    • Transcriptional corepressor SHP recruits SIRT1 histone deacetylase to inhibit LRH-1 transactivation
    • Chanda D, Xie YB, Choi HS (2010) Transcriptional corepressor SHP recruits SIRT1 histone deacetylase to inhibit LRH-1 transactivation. Nucleic Acids Res 38(14):4607-4619.
    • (2010) Nucleic Acids Res , vol.38 , Issue.14 , pp. 4607-4619
    • Chanda, D.1    Xie, Y.B.2    Choi, H.S.3
  • 26
    • 0034458872 scopus 로고    scopus 로고
    • Cells degrade a novel inhibitor of differentiation with E1A-like properties upon exiting the cell cycle
    • Miyake S, et al. (2000) Cells degrade a novel inhibitor of differentiation with E1A-like properties upon exiting the cell cycle. Mol Cell Biol 20(23):8889-8902.
    • (2000) Mol Cell Biol , vol.20 , Issue.23 , pp. 8889-8902
    • Miyake, S.1
  • 27
    • 0034460363 scopus 로고    scopus 로고
    • A novel Rb- and p300- binding protein inhibits transactivation by MyoD
    • MacLellan WR, Xiao G, Abdellatif M, Schneider MD (2000) A novel Rb- and p300- binding protein inhibits transactivation by MyoD. Mol Cell Biol 20(23):8903-8915.
    • (2000) Mol Cell Biol , vol.20 , Issue.23 , pp. 8903-8915
    • Maclellan, W.R.1    Xiao, G.2    Abdellatif, M.3    Schneider, M.D.4
  • 28
    • 77955302379 scopus 로고    scopus 로고
    • Novel polymorphisms of nuclear receptor SHP associated with functional and structural changes
    • Zhou T, et al. (2010) Novel polymorphisms of nuclear receptor SHP associated with functional and structural changes. J Biol Chem 285(32):24871-24881.
    • (2010) J Biol Chem , vol.285 , Issue.32 , pp. 24871-24881
    • Zhou, T.1
  • 29
    • 33644617967 scopus 로고    scopus 로고
    • Unveiling hidden features of orphan nuclear receptors: The case of the small heterodimer partner (SHP)
    • Macchiarulo A, Rizzo G, Costantino G, Fiorucci S, Pellicciari R (2006) Unveiling hidden features of orphan nuclear receptors: The case of the small heterodimer partner (SHP). J Mol Graph Model 24(5):362-372.
    • (2006) J Mol Graph Model , vol.24 , Issue.5 , pp. 362-372
    • Macchiarulo, A.1    Rizzo, G.2    Costantino, G.3    Fiorucci, S.4    Pellicciari, R.5
  • 30
    • 2342447392 scopus 로고    scopus 로고
    • Differential role of the loop region between helices H6 and H7 within the orphan nuclear receptors small heterodimer partner and DAX-1
    • Park YY, et al. (2004) Differential role of the loop region between helices H6 and H7 within the orphan nuclear receptors small heterodimer partner and DAX-1. Mol Endocrinol 18(5):1082-1095.
    • (2004) Mol Endocrinol , vol.18 , Issue.5 , pp. 1082-1095
    • Park, Y.Y.1
  • 31
    • 0036086509 scopus 로고    scopus 로고
    • Loss of nuclear receptor SHP impairs but does not eliminate negative feedback regulation of bile acid synthesis
    • Kerr TA, et al. (2002) Loss of nuclear receptor SHP impairs but does not eliminate negative feedback regulation of bile acid synthesis. Dev Cell 2(6):713-720.
    • (2002) Dev Cell , vol.2 , Issue.6 , pp. 713-720
    • Kerr, T.A.1
  • 32
    • 18444377348 scopus 로고    scopus 로고
    • Redundant pathways for negative feedback regulation of bile acid production
    • Wang L, et al. (2002) Redundant pathways for negative feedback regulation of bile acid production. Dev Cell 2(6):721-731.
    • (2002) Dev Cell , vol.2 , Issue.6 , pp. 721-731
    • Wang, L.1
  • 33
    • 27844546989 scopus 로고    scopus 로고
    • Fibroblast growth factor 15 functions as an enterohepatic signal to regulate bile acid homeostasis
    • Inagaki T, et al. (2005) Fibroblast growth factor 15 functions as an enterohepatic signal to regulate bile acid homeostasis. Cell Metab 2(4):217-225.
    • (2005) Cell Metab , vol.2 , Issue.4 , pp. 217-225
    • Inagaki, T.1
  • 34
    • 33846409855 scopus 로고    scopus 로고
    • Adamantyl-substituted retinoid-related molecules bind small heterodimer partner and modulate the Sin3A repressor
    • Farhana L, et al. (2007) Adamantyl-substituted retinoid-related molecules bind small heterodimer partner and modulate the Sin3A repressor. Cancer Res 67(1):318-325.
    • (2007) Cancer Res , vol.67 , Issue.1 , pp. 318-325
    • Farhana, L.1
  • 35
    • 79959850300 scopus 로고    scopus 로고
    • Ligand-dependent regulation of the activity of the orphan nuclear receptor, small heterodimer partner (SHP), in the repression of bile acid biosynthetic CYP7A1 and CYP8B1 genes
    • Miao J, et al. (2011) Ligand-dependent regulation of the activity of the orphan nuclear receptor, small heterodimer partner (SHP), in the repression of bile acid biosynthetic CYP7A1 and CYP8B1 genes. Mol Endocrinol 25(7):1159-1169.
    • (2011) Mol Endocrinol , vol.25 , Issue.7 , pp. 1159-1169
    • Miao, J.1
  • 36
    • 34250173035 scopus 로고    scopus 로고
    • An adamantyl-substituted retinoid-derived molecule that inhibits cancer cell growth and angiogenesis by inducing apoptosis and binds to small heterodimer partner nuclear receptor: Effects of modifying its carboxylate group on apoptosis, proliferation, and protein-tyrosine phosphatase activity
    • Dawson MI, et al. (2007) An adamantyl-substituted retinoid-derived molecule that inhibits cancer cell growth and angiogenesis by inducing apoptosis and binds to small heterodimer partner nuclear receptor: Effects of modifying its carboxylate group on apoptosis, proliferation, and protein-tyrosine phosphatase activity. J Med Chem 50(11):2622-2639.
    • (2007) J Med Chem , vol.50 , Issue.11 , pp. 2622-2639
    • Dawson, M.I.1
  • 37
    • 42449160533 scopus 로고    scopus 로고
    • Molecular recognition of parathyroid hormone by its G protein-coupled receptor
    • Pioszak AA, Xu HE (2008) Molecular recognition of parathyroid hormone by its G protein-coupled receptor. Proc Natl Acad Sci USA 105(13):5034-5039.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.13 , pp. 5034-5039
    • Pioszak, A.A.1    Xu, H.E.2
  • 38
    • 84884185072 scopus 로고    scopus 로고
    • The crystal structure of the orphan nuclear receptor NR2E3/PNR ligand binding domain reveals a dimeric auto-repressed conformation
    • Tan MH, et al. (2013) The crystal structure of the orphan nuclear receptor NR2E3/PNR ligand binding domain reveals a dimeric auto-repressed conformation. PLoS ONE 8(9): e74359.
    • (2013) PLoS ONE , vol.8 , Issue.9
    • Tan, M.H.1
  • 39
    • 57449090890 scopus 로고    scopus 로고
    • The structure of corepressor Dax-1 bound to its target nuclear receptor LRH-1
    • Sablin EP, et al. (2008) The structure of corepressor Dax-1 bound to its target nuclear receptor LRH-1. Proc Natl Acad Sci USA 105(47):18390-18395.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.47 , pp. 18390-18395
    • Sablin, E.P.1
  • 40
    • 54749139305 scopus 로고    scopus 로고
    • Identification of COUP-TFII orphan nuclear receptor as a retinoic acid-activated receptor
    • Kruse SW, et al. (2008) Identification of COUP-TFII orphan nuclear receptor as a retinoic acid-activated receptor. PLoS Biol 6(9):e227.
    • (2008) PLoS Biol , vol.6 , Issue.9
    • Kruse, S.W.1
  • 41
    • 78951492767 scopus 로고    scopus 로고
    • The orphan nuclear receptor TR4 is a vitamin A-activated nuclear receptor
    • Zhou XE, et al. (2011) The orphan nuclear receptor TR4 is a vitamin A-activated nuclear receptor. J Biol Chem 286(4):2877-2885.
    • (2011) J Biol Chem , vol.286 , Issue.4 , pp. 2877-2885
    • Zhou, X.E.1
  • 42
    • 33646545699 scopus 로고    scopus 로고
    • Nuclear receptor TLX prevents retinal dystrophy and recruits the corepressor atrophin1
    • Zhang CL, Zou Y, Yu RT, Gage FH, Evans RM (2006) Nuclear receptor TLX prevents retinal dystrophy and recruits the corepressor atrophin1. Genes Dev 20(10): 1308-1320.
    • (2006) Genes Dev , vol.20 , Issue.10 , pp. 1308-1320
    • Zhang, C.L.1    Zou, Y.2    Yu, R.T.3    Gage, F.H.4    Evans, R.M.5
  • 43
    • 33846941161 scopus 로고    scopus 로고
    • A cell cycle-dependent co-repressor mediates photoreceptor cell-specific nuclear receptor function
    • Takezawa S, et al. (2007) A cell cycle-dependent co-repressor mediates photoreceptor cell-specific nuclear receptor function. EMBO J 26(3):764-774.
    • (2007) EMBO J , vol.26 , Issue.3 , pp. 764-774
    • Takezawa, S.1
  • 44
    • 33644771241 scopus 로고    scopus 로고
    • Histone deacetylase-associating Atrophin proteins are nuclear receptor corepressors
    • Wang L, Rajan H, Pitman JL, McKeown M, Tsai CC (2006) Histone deacetylase-associating Atrophin proteins are nuclear receptor corepressors. Genes Dev 20(5):525-530.
    • (2006) Genes Dev , vol.20 , Issue.5 , pp. 525-530
    • Wang, L.1    Rajan, H.2    Pitman, J.L.3    McKeown, M.4    Tsai, C.C.5
  • 45
    • 0034677882 scopus 로고    scopus 로고
    • Interaction of the corepressor Alien with DAX-1 is abrogated by mutations of DAX-1 involved in adrenal hypoplasia congenita
    • Altincicek B, et al. (2000) Interaction of the corepressor Alien with DAX-1 is abrogated by mutations of DAX-1 involved in adrenal hypoplasia congenita. J Biol Chem 275(11): 7662-7667.
    • (2000) J Biol Chem , vol.275 , Issue.11 , pp. 7662-7667
    • Altincicek, B.1
  • 46
    • 0033637850 scopus 로고    scopus 로고
    • Dynamic stabilization of nuclear receptor ligand binding domains by hormone or corepressor binding
    • Pissios P, Tzameli I, Kushner P, Moore DD (2000) Dynamic stabilization of nuclear receptor ligand binding domains by hormone or corepressor binding. Mol Cell 6(2): 245-253.
    • (2000) Mol Cell , vol.6 , Issue.2 , pp. 245-253
    • Pissios, P.1    Tzameli, I.2    Kushner, P.3    Moore, D.D.4
  • 47
    • 0033855471 scopus 로고    scopus 로고
    • Structural basis for autorepression of retinoid X receptor by tetramer formation and the AF-2 helix
    • Gampe RT, Jr., et al. (2000) Structural basis for autorepression of retinoid X receptor by tetramer formation and the AF-2 helix. Genes Dev 14(17):2229-2241.
    • (2000) Genes Dev , vol.14 , Issue.17 , pp. 2229-2241
    • Gampe, R.T.1
  • 48
    • 0029012163 scopus 로고
    • Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha
    • Bourguet W, Ruff M, Chambon P, Gronemeyer H, Moras D (1995) Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha. Nature 375(6530):377-382.
    • (1995) Nature , vol.375 , Issue.6530 , pp. 377-382
    • Bourguet, W.1    Ruff, M.2    Chambon, P.3    Gronemeyer, H.4    Moras, D.5
  • 49
    • 71449125748 scopus 로고    scopus 로고
    • A gate-latch-lock mechanism for hormone signalling by abscisic acid receptors
    • Melcher K, et al. (2009) A gate-latch-lock mechanism for hormone signalling by abscisic acid receptors. Nature 462(7273):602-608.
    • (2009) Nature , vol.462 , Issue.7273 , pp. 602-608
    • Melcher, K.1
  • 50
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47(Pt 2):110-119.
    • (1991) Acta Crystallogr A , vol.47 , Issue.2 PART , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 51
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60(Pt 12 Pt 1):2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , Issue.PART 12 AND PART 1 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 52
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger AT, et al. (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr D Biol Crystallogr 54(Pt 5): 905-921.
    • (1998) Acta Crystallogr D Biol Crystallogr , vol.54 , Issue.PART 5 , pp. 905-921
    • Brünger, A.T.1
  • 54
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Ashkenazy H, Erez E, Martz E, Pupko T, Ben-Tal N (2010) ConSurf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res 38(Web Server issue):W529-W533.
    • (2010) Nucleic Acids Res , vol.38 , Issue.WEB SERVER ISSUE
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.