메뉴 건너뛰기




Volumn 83, Issue 4, 2014, Pages 440-449

High-throughput screen of natural product extracts in a yeast model of polyglutamine proteotoxicity

Author keywords

heat shock protein 70; high throughput screening; Huntington's disease; molecular chaperones

Indexed keywords

BETA GALACTOSIDASE; CHAPERONE; CYAN FLUORESCENT PROTEIN; DACTINOMYCIN; GALACTOSE; HEAT SHOCK PROTEIN 104; HEAT SHOCK PROTEIN 26; HEAT SHOCK PROTEIN 70; HUNTINGTIN; NATURAL PRODUCT; NATURAL PRODUCT EXTRACT; POLYGLUTAMINE; UNCLASSIFIED DRUG; BIOLOGICAL PRODUCT; PEPTIDE;

EID: 84899005317     PISSN: 17470277     EISSN: 17470285     Source Type: Journal    
DOI: 10.1111/cbdd.12259     Document Type: Article
Times cited : (14)

References (56)
  • 1
    • 25844487226 scopus 로고    scopus 로고
    • Diseases of unstable repeat expansion: Mechanisms and common principles
    • DOI 10.1038/nrg1691
    • Gatchel J.R., Zoghbi H.Y., (2005) Diseases of unstable repeat expansion: mechanisms and common principles. Nat Rev Genet; 6: 743-755. (Pubitemid 41400832)
    • (2005) Nature Reviews Genetics , vol.6 , Issue.10 , pp. 743-755
    • Gatchel, J.R.1    Zoghbi, H.Y.2
  • 2
    • 37849030901 scopus 로고    scopus 로고
    • Polyglutamine diseases: Emerging concepts in pathogenesis and therapy
    • Spec No. 2.
    • Shao J., Diamond M.I., (2007) Polyglutamine diseases: emerging concepts in pathogenesis and therapy. Hum Mol Genet; 16 Spec No. 2: R115-R123.
    • (2007) Hum Mol Genet , vol.16
    • Shao, J.1    Diamond, M.I.2
  • 3
    • 52049093169 scopus 로고    scopus 로고
    • Polyglutamine neurodegeneration: Protein misfolding revisited
    • Williams A.J., Paulson H.L., (2008) Polyglutamine neurodegeneration: protein misfolding revisited. Trends Neurosci; 31: 521-528.
    • (2008) Trends Neurosci , vol.31 , pp. 521-528
    • Williams, A.J.1    Paulson, H.L.2
  • 4
    • 0037062561 scopus 로고    scopus 로고
    • Amyloid-like features of polyglutamine aggregates and their assembly kinetics
    • DOI 10.1021/bi011772q
    • Chen S., Berthelier V., Hamilton J.B., O'Nuallain B., Wetzel R., (2002) Amyloid-like features of polyglutamine aggregates and their assembly kinetics. Biochemistry; 41: 7391-7399. (Pubitemid 34602457)
    • (2002) Biochemistry , vol.41 , Issue.23 , pp. 7391-7399
    • Chen, S.1    Berthelier, V.2    Hamilton, J.B.3    O'Nuallain, B.4    Wetzel, R.5
  • 6
    • 0037461730 scopus 로고    scopus 로고
    • Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders
    • DOI 10.1038/nature01301
    • Sanchez I., Mahlke C., Yuan J., (2003) Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders. Nature; 421: 373-379. (Pubitemid 36157935)
    • (2003) Nature , vol.421 , Issue.6921 , pp. 373-379
    • Sanchez, I.1    Mahlke, C.2    Yuan, J.3
  • 9
    • 38349158062 scopus 로고    scopus 로고
    • Soluble polyglutamine oligomers formed prior to inclusion body formation are cytotoxic
    • Takahashi T., Kikuchi S., Katada S., Nagai Y., Nishizawa M., Onodera O., (2008) Soluble polyglutamine oligomers formed prior to inclusion body formation are cytotoxic. Hum Mol Genet; 17: 345-356.
    • (2008) Hum Mol Genet , vol.17 , pp. 345-356
    • Takahashi, T.1    Kikuchi, S.2    Katada, S.3    Nagai, Y.4    Nishizawa, M.5    Onodera, O.6
  • 11
    • 0035897405 scopus 로고    scopus 로고
    • Identities of sequestered proteins in aggregates from cells with induced polyglutamine expression
    • DOI 10.1083/jcb.153.2.283
    • Suhr S.T., Senut M.C., Whitelegge J.P., Faull K.F., Cuizon D.B., Gage F.H., (2001) Identities of sequestered proteins in aggregates from cells with induced polyglutamine expression. J Cell Biol; 153: 283-294. (Pubitemid 34280215)
    • (2001) Journal of Cell Biology , vol.153 , Issue.2 , pp. 283-294
    • Suhr, S.T.1    Senut, M.-C.2    Whitelegge, J.P.3    Faull, K.F.4    Cuizon, D.B.5    Gage, F.H.6
  • 12
    • 48749095822 scopus 로고    scopus 로고
    • Characterization of proteins associated with polyglutamine aggregates: A novel approach towards isolation of aggregates from protein conformation disorders
    • Wang Y., Meriin A.B., Costello C.E., Sherman M.Y., (2007) Characterization of proteins associated with polyglutamine aggregates: a novel approach towards isolation of aggregates from protein conformation disorders. Prion; 1: 128-135.
    • (2007) Prion , vol.1 , pp. 128-135
    • Wang, Y.1    Meriin, A.B.2    Costello, C.E.3    Sherman, M.Y.4
  • 13
    • 0034703863 scopus 로고    scopus 로고
    • Mechanisms of chaperone suppression of polyglutamine disease: Selectivity, synergy and modulation of protein solubility in drosophila
    • Chan H.Y., Warrick J.M., Gray-Board G.L., Paulson H.L., Bonini N.M., (2000) Mechanisms of chaperone suppression of polyglutamine disease: selectivity, synergy and modulation of protein solubility in drosophila. Hum Mol Genet; 9: 2811-2820.
    • (2000) Hum Mol Genet , vol.9 , pp. 2811-2820
    • Chan, H.Y.1    Warrick, J.M.2    Gray-Board, G.L.3    Paulson, H.L.4    Bonini, N.M.5
  • 15
    • 34548608465 scopus 로고    scopus 로고
    • Modulation of polyglutamine inclusion formation by the Hsp70 chaperone machine
    • DOI 10.1016/j.yexcr.2007.07.034, PII S0014482707003527
    • Rujano M.A., Kampinga H.H., Salomons F.A., (2007) Modulation of polyglutamine inclusion formation by the hsp70 chaperone machine. Exp Cell Res; 313: 3568-3578. (Pubitemid 47404554)
    • (2007) Experimental Cell Research , vol.313 , Issue.16 , pp. 3568-3578
    • Rujano, M.A.1    Kampinga, H.H.2    Salomons, F.A.3
  • 16
    • 0034652127 scopus 로고    scopus 로고
    • Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins
    • DOI 10.1073/pnas.97.4.1589
    • Krobitsch S., Lindquist S., (2000) Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins. Proc Natl Acad Sci USA; 97: 1589-1594. (Pubitemid 30118486)
    • (2000) Proceedings of the National Academy of Sciences of the United States of America , vol.97 , Issue.4 , pp. 1589-1594
    • Krobitsch, S.1    Lindquist, S.2
  • 17
    • 0037053566 scopus 로고    scopus 로고
    • Huntingtin toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1
    • DOI 10.1083/jcb.200112104
    • Meriin A.B., Zhang X., He X., Newnam G.P., Chernoff Y.O., Sherman M.Y., (2002) Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein rnq1. J Cell Biol; 157: 997-1004. (Pubitemid 34839774)
    • (2002) Journal of Cell Biology , vol.157 , Issue.6 , pp. 997-1004
    • Meriin, A.B.1    Zhang, X.2    He, X.3    Newnam, G.P.4    Chernoff, Y.O.5    Sherman, M.Y.6
  • 18
    • 81755172428 scopus 로고    scopus 로고
    • Ordered assembly of heat shock proteins, hsp26, hsp70, hsp90, and hsp104, on expanded polyglutamine fragments revealed by chemical probes
    • Walter G.M., Smith M.C., Wisen S., Basrur V., Elenitoba-Johnson K.S., Duennwald M.L., Kumar A., Gestwicki J.E., (2011) Ordered assembly of heat shock proteins, hsp26, hsp70, hsp90, and hsp104, on expanded polyglutamine fragments revealed by chemical probes. J Biol Chem; 286: 40486-40493.
    • (2011) J Biol Chem , vol.286 , pp. 40486-40493
    • Walter, G.M.1    Smith, M.C.2    Wisen, S.3    Basrur, V.4    Elenitoba-Johnson, K.S.5    Duennwald, M.L.6    Kumar, A.7    Gestwicki, J.E.8
  • 19
    • 0034641589 scopus 로고    scopus 로고
    • Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: Their role in suppression of aggregation and cellular toxicity
    • Jana N.R., Tanaka M., Wang G., Nukina N., (2000) Polyglutamine length-dependent interaction of hsp40 and hsp70 family chaperones with truncated n-terminal huntingtin: their role in suppression of aggregation and cellular toxicity. Hum Mol Genet; 9: 2009-2018. (Pubitemid 30642666)
    • (2000) Human Molecular Genetics , vol.9 , Issue.13 , pp. 2009-2018
    • Jana, N.R.1    Tanaka, M.2    Wang, G.-H.3    Nukina, N.4
  • 21
    • 0034708793 scopus 로고    scopus 로고
    • Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract
    • DOI 10.1074/jbc.275.12.8772
    • Kobayashi Y., Kume A., Li M., Doyu M., Hata M., Ohtsuka K., Sobue G., (2000) Chaperones hsp70 and hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract. J Biol Chem; 275: 8772-8778. (Pubitemid 30180231)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.12 , pp. 8772-8778
    • Kobayashi, Y.1    Kume, A.2    Li, M.3    Doyu, M.4    Hata, M.5    Ohtsuka, K.6    Sobue, G.7
  • 23
    • 16544383250 scopus 로고    scopus 로고
    • Hsp70 and hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer
    • Wacker J.L., Zareie M.H., Fong H., Sarikaya M., Muchowski P.J., (2004) Hsp70 and hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer. Nat Struct Mol Biol; 11: 1215-1222.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 1215-1222
    • Wacker, J.L.1    Zareie, M.H.2    Fong, H.3    Sarikaya, M.4    Muchowski, P.J.5
  • 24
    • 0032727617 scopus 로고    scopus 로고
    • Suppression of polyglutamine-mediated neurodegeneration in drosophila by the molecular chaperone hsp70
    • Warrick J.M., Chan H.Y., Gray-Board G.L., Chai Y., Paulson H.L., Bonini N.M., (1999) Suppression of polyglutamine-mediated neurodegeneration in drosophila by the molecular chaperone hsp70. Nat Genet; 23: 425-428.
    • (1999) Nat Genet , vol.23 , pp. 425-428
    • Warrick, J.M.1    Chan, H.Y.2    Gray-Board, G.L.3    Chai, Y.4    Paulson, H.L.5    Bonini, N.M.6
  • 25
    • 0036566675 scopus 로고    scopus 로고
    • Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin
    • Wyttenbach A., Sauvageot O., Carmichael J., Diaz-Latoud C., Arrigo A.P., Rubinsztein D.C., (2002) Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin. Hum Mol Genet; 11: 1137-1151. (Pubitemid 34521094)
    • (2002) Human Molecular Genetics , vol.11 , Issue.9 , pp. 1137-1151
    • Wyttenbach, A.1    Sauvageot, O.2    Carmichael, J.3    Diaz-Latoud, C.4    Arrigo, A.-P.5    Rubinsztein, D.C.6
  • 26
    • 33644850056 scopus 로고    scopus 로고
    • Progressive disruption of cellular protein folding in models of polyglutamine diseases
    • DOI 10.1126/science.1124514
    • Gidalevitz T., Ben-Zvi A., Ho K.H., Brignull H.R., Morimoto R.I., (2006) Progressive disruption of cellular protein folding in models of polyglutamine diseases. Science; 311: 1471-1474. (Pubitemid 43376703)
    • (2006) Science , vol.311 , Issue.5766 , pp. 1471-1474
    • Gidalevitz, T.1    Ben-Zvi, A.2    Ho, K.H.3    Brignull, H.R.4    Morimoto, R.I.5
  • 28
    • 77949352928 scopus 로고    scopus 로고
    • Acute polyglutamine expression in inducible mouse model unravels ubiquitin/proteasome system impairment and permanent recovery attributable to aggregate formation
    • Ortega Z., Diaz-Hernandez M., Maynard C.J., Hernandez F., Dantuma N.P., Lucas J.J., (2010) Acute polyglutamine expression in inducible mouse model unravels ubiquitin/proteasome system impairment and permanent recovery attributable to aggregate formation. J Neurosci; 30: 3675-3688.
    • (2010) J Neurosci , vol.30 , pp. 3675-3688
    • Ortega, Z.1    Diaz-Hernandez, M.2    Maynard, C.J.3    Hernandez, F.4    Dantuma, N.P.5    Lucas, J.J.6
  • 29
    • 0036566266 scopus 로고    scopus 로고
    • Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy
    • Ravikumar B., Duden R., Rubinsztein D.C., (2002) Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy. Hum Mol Genet; 11: 1107-1117. (Pubitemid 34521091)
    • (2002) Human Molecular Genetics , vol.11 , Issue.9 , pp. 1107-1117
    • Ravikumar, B.1    Duden, R.2    Rubinsztein, D.C.3
  • 30
    • 14644419638 scopus 로고    scopus 로고
    • Neuronal dysfunction in a polyglutamine disease model occurs in the absence of ubiquitin-proteasome system impairment and inversely correlates with the degree of nuclear inclusion formation
    • DOI 10.1093/hmg/ddi064
    • Bowman A.B., Yoo S.Y., Dantuma N.P., Zoghbi H.Y., (2005) Neuronal dysfunction in a polyglutamine disease model occurs in the absence of ubiquitin-proteasome system impairment and inversely correlates with the degree of nuclear inclusion formation. Hum Mol Genet; 14: 679-691. (Pubitemid 40309593)
    • (2005) Human Molecular Genetics , vol.14 , Issue.5 , pp. 679-691
    • Bowman, A.B.1    Yoo, S.-Y.2    Dantuma, N.P.3    Zoghbi, H.Y.4
  • 31
    • 84855478434 scopus 로고    scopus 로고
    • A screen for enhancers of clearance identifies huntingtin as a heat shock protein 90 (hsp90) client protein
    • Baldo B., Weiss A., Parker C.N., Bibel M., Paganetti P., Kaupmann K., (2012) A screen for enhancers of clearance identifies huntingtin as a heat shock protein 90 (hsp90) client protein. J Biol Chem; 287: 1406-1414.
    • (2012) J Biol Chem , vol.287 , pp. 1406-1414
    • Baldo, B.1    Weiss, A.2    Parker, C.N.3    Bibel, M.4    Paganetti, P.5    Kaupmann, K.6
  • 34
    • 0034615932 scopus 로고    scopus 로고
    • Inhibition of polyglutamine protein aggregation and cell death by novel peptides identified by phage display screening
    • DOI 10.1074/jbc.275.14.10437
    • Nagai Y., Tucker T., Ren H., Kenan D.J., Henderson B.S., Keene J.D., Strittmatter W.J., Burke J.R., (2000) Inhibition of polyglutamine protein aggregation and cell death by novel peptides identified by phage display screening. J Biol Chem; 275: 10437-10442. (Pubitemid 30202104)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.14 , pp. 10437-10442
    • Nagai, Y.1    Tucker, T.2    Ren, H.3    Kenan, D.J.4    Henderson, B.S.5    Keene, J.D.6    Strittmatter, W.J.7    Burke, J.R.8
  • 35
    • 0242657586 scopus 로고    scopus 로고
    • A rapid cellular FRET assay of polyglutamine aggregation identifies a novel inhibitor
    • DOI 10.1016/S0896-6273(03)00697-4
    • Pollitt S.K., Pallos J., Shao J., Desai U.A., Ma A.A., Thompson L.M., Marsh J.L., Diamond M.I., (2003) A rapid cellular fret assay of polyglutamine aggregation identifies a novel inhibitor. Neuron; 40: 685-694. (Pubitemid 37431030)
    • (2003) Neuron , vol.40 , Issue.4 , pp. 685-694
    • Pollitt, S.K.1    Pallos, J.2    Shao, J.3    Desai, U.A.4    Ma, A.A.K.5    Thompson, L.M.6    Marsh, J.L.7    Diamond, M.I.8
  • 37
    • 27144503120 scopus 로고    scopus 로고
    • 17-AAG, an Hsp90 inhibitor, ameliorates polyglutamine-mediated motor neuron degeneration
    • DOI 10.1038/nm1298, PII N1298
    • Waza M., Adachi H., Katsuno M., Minamiyama M., Sang C., Tanaka F., Inukai A., Doyu M., Sobue G., (2005) 17-aag, an hsp90 inhibitor, ameliorates polyglutamine-mediated motor neuron degeneration. Nat Med; 11: 1088-1095. (Pubitemid 41486831)
    • (2005) Nature Medicine , vol.11 , Issue.10 , pp. 1088-1095
    • Waza, M.1    Adachi, H.2    Katsuno, M.3    Minamiyama, M.4    Sang, C.5    Tanaka, F.6    Inukai, A.7    Doyu, M.8    Sobue, G.9
  • 38
    • 36849044616 scopus 로고    scopus 로고
    • Celastrol inhibits polyglutamine aggregation and toxicity though induction of the heat shock response
    • DOI 10.1007/s00109-007-0251-9, Special Issue (Ed. G. Semenza): Hypoxia and Human Disease
    • Zhang Y.Q., Sarge K.D., (2007) Celastrol inhibits polyglutamine aggregation and toxicity though induction of the heat shock response. J Mol Med; 85: 1421-1428. (Pubitemid 350234097)
    • (2007) Journal of Molecular Medicine , vol.85 , Issue.12 , pp. 1421-1428
    • Zhang, Y.-Q.1    Sarge, K.D.2
  • 39
    • 34247109045 scopus 로고    scopus 로고
    • Natural products as sources of new drugs over the last 25 years
    • DOI 10.1021/np068054v
    • Newman D.J., Cragg G.M., (2007) Natural products as sources of new drugs over the last 25 years. J Nat Prod; 70: 461-477. (Pubitemid 46595760)
    • (2007) Journal of Natural Products , vol.70 , Issue.3 , pp. 461-477
    • Newman, D.J.1    Cragg, G.M.2
  • 44
    • 35648936428 scopus 로고    scopus 로고
    • Flanking Polyproline Sequences Inhibit β-Sheet Structure in Polyglutamine Segments by Inducing PPII-like Helix Structure
    • DOI 10.1016/j.jmb.2007.09.023, PII S0022283607011977
    • Darnell G., Orgel J.P., Pahl R., Meredith S.C., (2007) Flanking polyproline sequences inhibit beta-sheet structure in polyglutamine segments by inducing ppii-like helix structure. J Mol Biol; 374: 688-704. (Pubitemid 350027728)
    • (2007) Journal of Molecular Biology , vol.374 , Issue.3 , pp. 688-704
    • Darnell, G.1    Orgel, J.P.R.O.2    Pahl, R.3    Meredith, S.C.4
  • 46
    • 80054758767 scopus 로고    scopus 로고
    • Complementary cell-based high-throughput screens identify novel modulators of the unfolded protein response
    • Fribley A.M., Cruz P.G., Miller J.R., Callaghan M.U., Cai P., Narula N., Neubig R.R., et al,. (2011) Complementary cell-based high-throughput screens identify novel modulators of the unfolded protein response. J Biomol Screen; 16: 825-835.
    • (2011) J Biomol Screen , vol.16 , pp. 825-835
    • Fribley, A.M.1    Cruz, P.G.2    Miller, J.R.3    Callaghan, M.U.4    Cai, P.5    Narula, N.6    Neubig, R.R.7
  • 49
    • 0015229681 scopus 로고
    • Inhibitors of protein synthesis by ribosomes of the 80-s type
    • Battaner E., Vazquez D., (1971) Inhibitors of protein synthesis by ribosomes of the 80-s type. Biochim Biophys Acta; 254: 316-330.
    • (1971) Biochim Biophys Acta , vol.254 , pp. 316-330
    • Battaner, E.1    Vazquez, D.2
  • 50
    • 0033990336 scopus 로고    scopus 로고
    • Heat shock factors and the control of the stress response
    • Santoro M.G., (2000) Heat shock factors and the control of the stress response. Biochem Pharmacol; 59: 55-63.
    • (2000) Biochem Pharmacol , vol.59 , pp. 55-63
    • Santoro, M.G.1
  • 51
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • DOI 10.1038/nrn1587
    • Muchowski P.J., Wacker J.L., (2005) Modulation of neurodegeneration by molecular chaperones. Nat Rev Neurosci; 6: 11-22. (Pubitemid 40052135)
    • (2005) Nature Reviews Neuroscience , vol.6 , Issue.1 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 52
    • 34347258879 scopus 로고    scopus 로고
    • Small molecule inducers of heat-shock response reduce polyQ-mediated huntingtin aggregation: A possible therapeutic strategy
    • DOI 10.1159/000101849
    • Herbst M., Wanker E.E., (2007) Small molecule inducers of heat-shock response reduce polyq-mediated huntingtin aggregation. A possible therapeutic strategy. Neurodegener Dis; 4: 254-260. (Pubitemid 47000417)
    • (2007) Neurodegenerative Diseases , vol.4 , Issue.2-3 , pp. 254-260
    • Herbst, M.1    Wanker, E.E.2
  • 53
    • 1642633757 scopus 로고    scopus 로고
    • Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease
    • DOI 10.1038/nm985
    • Tanaka M., Machida Y., Niu S., Ikeda T., Jana N.R., Doi H., Kurosawa M., Nekooki M., Nukina N., (2004) Trehalose alleviates polyglutamine-mediated pathology in a mouse model of huntington disease. Nat Med; 10: 148-154. (Pubitemid 38524884)
    • (2004) Nature Medicine , vol.10 , Issue.2 , pp. 148-154
    • Tanaka, M.1    Machida, Y.2    Niu, S.3    Ikeda, T.4    Jana, N.R.5    Doi, H.6    Kurosawa, M.7    Nekooki, M.8    Nukina, N.9
  • 54
    • 75749136948 scopus 로고    scopus 로고
    • Modulation of heat shock transcription factor 1 as a therapeutic target for small molecule intervention in neurodegenerative disease
    • Neef D.W., Turski M.L., Thiele D.J., (2010) Modulation of heat shock transcription factor 1 as a therapeutic target for small molecule intervention in neurodegenerative disease. PLoS Biol; 8: e1000291.
    • (2010) PLoS Biol , vol.8
    • Neef, D.W.1    Turski, M.L.2    Thiele, D.J.3
  • 56
    • 77950887221 scopus 로고    scopus 로고
    • Flavonol activation defines an unanticipated ligand-binding site in the kinase-rnase domain of ire1
    • Wiseman R.L., Zhang Y., Lee K.P., Harding H.P., Haynes C.M., Price J., Sicheri F., Ron D., (2010) Flavonol activation defines an unanticipated ligand-binding site in the kinase-rnase domain of ire1. Mol Cell; 38: 291-304.
    • (2010) Mol Cell , vol.38 , pp. 291-304
    • Wiseman, R.L.1    Zhang, Y.2    Lee, K.P.3    Harding, H.P.4    Haynes, C.M.5    Price, J.6    Sicheri, F.7    Ron, D.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.