메뉴 건너뛰기




Volumn 520, Issue 7547, 2015, Pages 312-316

Crystal structures of the human adiponectin receptors

(24)  Tanabe, Hiroaki a,b   Fujii, Yoshifumi a   Okada Iwabu, Miki b,c   Iwabu, Masato b,c,d   Nakamura, Yoshihiro a   Hosaka, Toshiaki a   Motoyama, Kanna a   Ikeda, Mariko a   Wakiyama, Motoaki a   Terada, Takaho a   Ohsawa, Noboru a   Hato, Masakatsu a   Ogasawara, Satoshi e   Hino, Tomoya d,e   Murata, Takeshi a,d,e,f   Iwata, So a,d,e,g,h,i   Hirata, Kunio i   Kawano, Yoshiaki i   Yamamoto, Masaki i   Kimura Someya, Tomomi a   more..

a RIKEN   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ADIPONECTIN; ADIPONECTIN RECEPTOR 1; ADIPONECTIN RECEPTOR 2; G PROTEIN COUPLED RECEPTOR; HISTIDINE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; UNCOUPLING PROTEIN 2; ZINC ION; ADIPONECTIN RECEPTOR; ADIPOR1 PROTEIN, HUMAN; ADIPOR2 PROTEIN, HUMAN; ZINC;

EID: 84928409629     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature14301     Document Type: Article
Times cited : (170)

References (58)
  • 1
    • 0028787490 scopus 로고
    • A novel serum protein similar to C1q, produced exclusively in adipocytes
    • Scherer, P. E., Williams, S., Fogliano, M., Baldini, G. & Lodish, H. F. A novel serum protein similar to C1q, produced exclusively in adipocytes. J. Biol. Chem. 270, 26746-26749 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 26746-26749
    • Scherer, P.E.1    Williams, S.2    Fogliano, M.3    Baldini, G.4    Lodish, H.F.5
  • 2
    • 17544382289 scopus 로고    scopus 로고
    • AdipoQ is a novel adipose-specific gene dysregulated in obesity
    • Hu, E., Liang, P. & Spiegelman, B. M. AdipoQ is a novel adipose-specific gene dysregulated in obesity. J. Biol. Chem. 271, 10697-10703 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 10697-10703
    • Hu, E.1    Liang, P.2    Spiegelman, B.M.3
  • 3
    • 0029980285 scopus 로고    scopus 로고
    • cDNA cloning and expression of a novel adipose specific collagen-like factor, apM1 (AdiPose Most abundant Gene transcript 1)
    • Maeda, K. et al. cDNA cloning and expression of a novel adipose specific collagen-like factor, apM1 (AdiPose Most abundant Gene transcript 1). Biochem. Biophys. Res. Commun. 221, 286-289 (1996).
    • (1996) Biochem. Biophys. Res. Commun. , vol.221 , pp. 286-289
    • Maeda, K.1
  • 4
    • 0029836585 scopus 로고    scopus 로고
    • Isolation and characterization of GBP28, a novel gelatin-binding protein purified from human plasma
    • Nakano, Y., Tobe, T., Choi-Miura, N. H., Mazda, T. & Tomita, M. Isolation and characterization of GBP28, a novel gelatin-binding protein purified from human plasma. J. Biochem. 120, 803-812 (1996).
    • (1996) J. Biochem. , vol.120 , pp. 803-812
    • Nakano, Y.1    Tobe, T.2    Choi-Miura, N.H.3    Mazda, T.4    Tomita, M.5
  • 5
    • 0034096988 scopus 로고    scopus 로고
    • Plasma concentrations of a novel, adipose-specific protein, adiponectin, in type 2 diabetic patients
    • Hotta, K. et al. Plasma concentrations of a novel, adipose-specific protein, adiponectin, in type 2 diabetic patients. Arterioscler. Thromb. Vasc. Biol. 20, 1595-1599 (2000).
    • (2000) Arterioscler. Thromb. Vasc. Biol. , vol.20 , pp. 1595-1599
    • Hotta, K.1
  • 6
    • 17944365228 scopus 로고    scopus 로고
    • The fat-derived hormone adiponectin reverses insulin resistance associated with both lipoatrophy and obesity
    • Yamauchi, T. et al. The fat-derived hormone adiponectin reverses insulin resistance associated with both lipoatrophy and obesity. Nature Med. 7, 941-946 (2001).
    • (2001) Nature Med. , vol.7 , pp. 941-946
    • Yamauchi, T.1
  • 7
    • 0034881391 scopus 로고    scopus 로고
    • The adipocyte-secreted protein Acrp30 enhances hepatic insulin action
    • Berg, A. H., Combs, T. P., Du, X., Brownlee, M. & Scherer, P. E. The adipocyte-secreted protein Acrp30 enhances hepatic insulin action. Nature Med. 7, 947-953 (2001).
    • (2001) Nature Med. , vol.7 , pp. 947-953
    • Berg, A.H.1    Combs, T.P.2    Du, X.3    Brownlee, M.4    Scherer, P.E.5
  • 8
    • 0035852760 scopus 로고    scopus 로고
    • Proteolytic cleavage product of 30-kDa adipocyte complement-related protein increases fatty acid oxidation in muscle and causes weight loss in mice
    • Fruebis, J. et al. Proteolytic cleavage product of 30-kDa adipocyte complement-related protein increases fatty acid oxidation in muscle and causes weight loss in mice. Proc. Natl Acad. Sci. USA 98, 2005-2010 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 2005-2010
    • Fruebis, J.1
  • 9
    • 0036851817 scopus 로고    scopus 로고
    • Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase
    • Yamauchi, T. et al. Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase. Nature Med. 8, 1288-1295 (2002).
    • (2002) Nature Med. , vol.8 , pp. 1288-1295
    • Yamauchi, T.1
  • 10
    • 0037059013 scopus 로고    scopus 로고
    • Enhanced muscle fat oxidation and glucose transport by ACRP30 globular domain: Acetyl-CoA carboxylase inhibition and AMP-activated protein kinase activation
    • Tomas, E. et al. Enhanced muscle fat oxidation and glucose transport by ACRP30 globular domain: acetyl-CoA carboxylase inhibition and AMP-activated protein kinase activation. Proc. Natl Acad. Sci. USA 99, 16309-16313 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 16309-16313
    • Tomas, E.1
  • 11
    • 20844451123 scopus 로고    scopus 로고
    • AMP-activated protein kinase: Ancient energy gauge provides clues to modern understanding of metabolism
    • Kahn, B. B., Alquier, T., Carling, D. & Hardie, D. G. AMP-activated protein kinase: ancient energy gauge provides clues to modern understanding of metabolism. Cell Metab. 1, 15-25 (2005).
    • (2005) Cell Metab. , vol.1 , pp. 15-25
    • Kahn, B.B.1    Alquier, T.2    Carling, D.3    Hardie, D.G.4
  • 12
    • 0034713444 scopus 로고    scopus 로고
    • Roles of PPARs in health and disease
    • Kersten, S., Desvergne, B. & Wahli, W. Roles of PPARs in health and disease. Nature 405, 421-424 (2000).
    • (2000) Nature , vol.405 , pp. 421-424
    • Kersten, S.1    Desvergne, B.2    Wahli, W.3
  • 13
    • 0037462684 scopus 로고    scopus 로고
    • Globular adiponectin protected ob/ob mice from diabetes and ApoE-deficient mice from atherosclerosis
    • Yamauchi, T. et al. Globular adiponectin protected ob/ob mice from diabetes and ApoE-deficient mice from atherosclerosis. J. Biol. Chem. 278, 2461-2468 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 2461-2468
    • Yamauchi, T.1
  • 14
    • 0037494960 scopus 로고    scopus 로고
    • Cloning of adiponectin receptors that mediate antidiabetic metabolic effects
    • Yamauchi, T. et al. Cloning of adiponectin receptors that mediate antidiabetic metabolic effects. Nature 423, 762-769 (2003).
    • (2003) Nature , vol.423 , pp. 762-769
    • Yamauchi, T.1
  • 15
    • 0030938936 scopus 로고    scopus 로고
    • G-protein-coupled receptors: Molecular mechanisms involved in receptor activation and selectivity of G-protein recognition
    • Wess, J. G-protein-coupled receptors: molecular mechanisms involved in receptor activation and selectivity of G-protein recognition. FASEB J. 11, 346-354 (1997).
    • (1997) FASEB J. , vol.11 , pp. 346-354
    • Wess, J.1
  • 16
    • 33847733103 scopus 로고    scopus 로고
    • Targeted disruption of AdipoR1 and AdipoR2 causes abrogation of adiponectin binding and metabolic actions
    • Yamauchi, T. et al. Targeted disruption of AdipoR1 and AdipoR2 causes abrogation of adiponectin binding and metabolic actions. Nature Med. 13, 332-339 (2007).
    • (2007) Nature Med. , vol.13 , pp. 332-339
    • Yamauchi, T.1
  • 17
    • 84888639952 scopus 로고    scopus 로고
    • A small-molecule AdipoR agonist for type 2 diabetes and short life in obesity
    • Okada-Iwabu, M. et al. A small-molecule AdipoR agonist for type 2 diabetes and short life in obesity. Nature 503, 493-499 (2013).
    • (2013) Nature , vol.503 , pp. 493-499
    • Okada-Iwabu, M.1
  • 18
    • 1842782781 scopus 로고    scopus 로고
    • Metalloregulation of yeast membrane steroid receptor homologs
    • Lyons, T. J. et al. Metalloregulation of yeast membrane steroid receptor homologs. Proc. Natl Acad. Sci. USA 101, 5506-5511 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 5506-5511
    • Lyons, T.J.1
  • 19
    • 36248970132 scopus 로고    scopus 로고
    • Crystal structure of the human β2 adrenergic G-protein-coupled receptor
    • Rasmussen, S. G. et al. Crystal structure of the human β2 adrenergic G-protein-coupled receptor. Nature 450, 383-387 (2007).
    • (2007) Nature , vol.450 , pp. 383-387
    • Rasmussen, S.G.1
  • 20
    • 36448995359 scopus 로고    scopus 로고
    • High-resolution crystal structure of an engineered human β2-adrenergic G protein-coupled receptor
    • Cherezov, V. et al. High-resolution crystal structure of an engineered human β2-adrenergic G protein-coupled receptor. Science 318, 1258-1265 (2007).
    • (2007) Science , vol.318 , pp. 1258-1265
    • Cherezov, V.1
  • 21
    • 36448978229 scopus 로고    scopus 로고
    • GPCR engineering yields high-resolution structural insights into β2-adrenergic receptor function
    • Rosenbaum, D. M. et al. GPCR engineering yields high-resolution structural insights into β2-adrenergic receptor function. Science 318, 1266-1273 (2007).
    • (2007) Science , vol.318 , pp. 1266-1273
    • Rosenbaum, D.M.1
  • 22
    • 78651411166 scopus 로고    scopus 로고
    • Structure of a nanobody-stabilized active state of the β2 adrenoceptor
    • Rasmussen, S. G. et al. Structure of a nanobody-stabilized active state of the β2 adrenoceptor. Nature 469, 175-180 (2011).
    • (2011) Nature , vol.469 , pp. 175-180
    • Rasmussen, S.G.1
  • 23
    • 78651399683 scopus 로고    scopus 로고
    • Structure and function of an irreversible agonist-β2 adrenoceptor complex
    • Rosenbaum, D. M. et al. Structure and function of an irreversible agonist-β2 adrenoceptor complex. Nature 469, 236-240 (2011).
    • (2011) Nature , vol.469 , pp. 236-240
    • Rosenbaum, D.M.1
  • 24
    • 84873685831 scopus 로고    scopus 로고
    • Molecular signatures of G-protein-coupled receptors
    • Venkatakrishnan, A. J. et al. Molecular signatures of G-protein-coupled receptors. Nature 494, 185-194 (2013).
    • (2013) Nature , vol.494 , pp. 185-194
    • Venkatakrishnan, A.J.1
  • 25
    • 80051658642 scopus 로고    scopus 로고
    • Crystal structure of the β2 adrenergic receptor-Gs protein complex
    • Rasmussen, S. G. et al. Crystal structure of the β2 adrenergic receptor-Gs protein complex. Nature 477, 549-555 (2011).
    • (2011) Nature , vol.477 , pp. 549-555
    • Rasmussen, S.G.1
  • 26
    • 79960070651 scopus 로고    scopus 로고
    • Structure of the human histamine H1 receptor complex with doxepin
    • Shimamura, T. et al. Structure of the human histamine H1 receptor complex with doxepin. Nature 475, 65-70 (2011).
    • (2011) Nature , vol.475 , pp. 65-70
    • Shimamura, T.1
  • 27
    • 82555187387 scopus 로고    scopus 로고
    • Crystal structure-based virtual screening for fragment-like ligands of the human histamine H1 receptor
    • de Graaf, C. et al. Crystal structure-based virtual screening for fragment-like ligands of the human histamine H1 receptor. J. Med. Chem. 54, 8195-8206 (2011).
    • (2011) J. Med. Chem. , vol.54 , pp. 8195-8206
    • De Graaf, C.1
  • 28
    • 84923136394 scopus 로고    scopus 로고
    • Expression, purification, crystallization, and preliminary X-ray crystallographic studies of the human adiponectin receptors, AdipoR1 and AdipoR2
    • Tanabe, H. et al. Expression, purification, crystallization, and preliminary X-ray crystallographic studies of the human adiponectin receptors, AdipoR1 and AdipoR2. J. Struct. Funct. Genomics 16, 11-23 (2015).
    • (2015) J. Struct. Funct. Genomics , vol.16 , pp. 11-23
    • Tanabe, H.1
  • 29
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservationmapping in 3D
    • Holm, L. & Rosenstrom, P. Dali server: conservationmapping in 3D. Nucleic Acids Res. 38, W545-W549 (2010).
    • (2010) Nucleic Acids Res. , vol.38 , pp. W545-W549
    • Holm, L.1    Rosenstrom, P.2
  • 30
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A G protein-coupled receptor
    • Palczewski, K. et al. Crystal structure of rhodopsin: a G protein-coupled receptor. Science 289, 739-745 (2000).
    • (2000) Science , vol.289 , pp. 739-745
    • Palczewski, K.1
  • 31
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases
    • Pebay-Peyroula, E., Rummel, G., Rosenbusch, J. P. & Landau, E. M. X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases. Science 277, 1676-1681 (1997).
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 32
    • 84881193006 scopus 로고    scopus 로고
    • Structure of the human glucagon class B G-protein-coupled receptor
    • Siu, F. Y. et al. Structure of the human glucagon class B G-protein-coupled receptor. Nature 499, 444-449 (2013).
    • (2013) Nature , vol.499 , pp. 444-449
    • Siu, F.Y.1
  • 33
    • 84897580006 scopus 로고    scopus 로고
    • Structure of a class C GPCR metabotropic glutamate receptor 1 bound to an allosteric modulator
    • Wu, H. et al. Structure of a class C GPCR metabotropic glutamate receptor 1 bound to an allosteric modulator. Science 344, 58-64 (2014).
    • (2014) Science , vol.344 , pp. 58-64
    • Wu, H.1
  • 34
    • 36849037428 scopus 로고    scopus 로고
    • Structure of a site-2 protease family intramembrane metalloprotease
    • Feng, L. et al. Structure of a site-2 protease family intramembrane metalloprotease. Science 318, 1608-1612 (2007).
    • (2007) Science , vol.318 , pp. 1608-1612
    • Feng, L.1
  • 35
    • 0026736225 scopus 로고
    • Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases
    • Bode, W., Gomis-Ruth, F. X., Huber, R., Zwilling, R. & Stocker, W. Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases. Nature 358, 164-167 (1992).
    • (1992) Nature , vol.358 , pp. 164-167
    • Bode, W.1    Gomis-Ruth, F.X.2    Huber, R.3    Zwilling, R.4    Stocker, W.5
  • 36
    • 0024218271 scopus 로고
    • Refined structure of human carbonic anhydrase II at 2.0 Å resolution
    • Eriksson, A. E., Jones, T. A. & Liljas, A. Refined structure of human carbonic anhydrase II at 2.0 Å resolution. Proteins 4, 274-282 (1988).
    • (1988) Proteins , vol.4 , pp. 274-282
    • Eriksson, A.E.1    Jones, T.A.2    Liljas, A.3
  • 37
    • 33744972277 scopus 로고    scopus 로고
    • APPL1 binds to adiponectin receptors and mediates adiponectin signalling and function
    • Mao, X. et al. APPL1 binds to adiponectin receptors and mediates adiponectin signalling and function. Nature Cell Biol. 8, 516-523 (2006).
    • (2006) Nature Cell Biol. , vol.8 , pp. 516-523
    • Mao, X.1
  • 38
    • 85027940060 scopus 로고    scopus 로고
    • A new manual dispensing system for in meso membrane protein crystallization with using a stepping motor-based dispenser
    • Hato, M., Hosaka, T., Tanabe, H., Kitsunai, T. & Yokoyama, S. A new manual dispensing system for in meso membrane protein crystallization with using a stepping motor-based dispenser. J. Struct. Funct. Genomics 15, 165-171 (2014).
    • (2014) J. Struct. Funct. Genomics , vol.15 , pp. 165-171
    • Hato, M.1    Hosaka, T.2    Tanabe, H.3    Kitsunai, T.4    Yokoyama, S.5
  • 39
    • 84876256823 scopus 로고    scopus 로고
    • Achievement of protein micro-crystallography at SPring-8 beamline BL32XU
    • Hirata, K. et al. Achievement of protein micro-crystallography at SPring-8 beamline BL32XU. J. Phys. Conf. Ser. 425, 012002 (2013).
    • (2013) J. Phys. Conf. Ser. , vol.425 , pp. 012002
    • Hirata, K.1
  • 40
    • 84863549892 scopus 로고    scopus 로고
    • Tumor volume and lymphovascular space invasion as a prognostic factor in early invasive adenocarcinoma of the cervix
    • Murakami, I. et al. Tumor volume and lymphovascular space invasion as a prognostic factor in early invasive adenocarcinoma of the cervix. J. Gynecol. Oncol. 23, 153-158 (2012).
    • (2012) J. Gynecol. Oncol. , vol.23 , pp. 153-158
    • Murakami, I.1
  • 41
    • 20644437994 scopus 로고    scopus 로고
    • Beamline Scheduling Software: Administration software for automatic operation of the RIKEN structural genomics beamlines at SPring-8
    • Ueno, G., Kanda, H., Kumasaka, T. & Yamamoto, M. Beamline Scheduling Software: administration software for automatic operation of the RIKEN structural genomics beamlines at SPring-8. J. Synchrotron Radiat. 12, 380-384 (2005).
    • (2005) J. Synchrotron Radiat. , vol.12 , pp. 380-384
    • Ueno, G.1    Kanda, H.2    Kumasaka, T.3    Yamamoto, M.4
  • 42
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 44
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 45
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger, T. C. Maximum-likelihood density modification. Acta Crystallogr. D 56, 965-972 (2000).
    • (2000) Acta Crystallogr. D , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
  • 46
    • 0037242985 scopus 로고    scopus 로고
    • Automated side-chain model building and sequence assignment by template matching
    • Terwilliger, T. C. Automated side-chain model building and sequence assignment by template matching. Acta Crystallogr. D 59, 45-49 (2003).
    • (2003) Acta Crystallogr. D , vol.59 , pp. 45-49
    • Terwilliger, T.C.1
  • 48
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 49
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D 66, 12-21 (2010).
    • (2010) Acta Crystallogr. D , vol.66 , pp. 12-21
    • Chen, V.B.1
  • 51
    • 77951872309 scopus 로고    scopus 로고
    • Adioponectin and AdipoR1 regulate PGC-1α and mitochondria by Ca2+ and AMPK/SIRT1
    • Iwabu, M. et al. Adioponectin and AdipoR1 regulate PGC-1α and mitochondria by Ca2+ and AMPK/SIRT1. Nature 464, 1313-1319 (2010).
    • (2010) Nature , vol.464 , pp. 1313-1319
    • Iwabu, M.1
  • 52
    • 0037122766 scopus 로고    scopus 로고
    • Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase
    • Minokoshi, Y. et al. Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase. Nature 415, 339-343 (2002).
    • (2002) Nature , vol.415 , pp. 339-343
    • Minokoshi, Y.1
  • 53
    • 0037119375 scopus 로고    scopus 로고
    • Oligomerization state-dependent activation of NF-κB signaling pathway by adipocyte complement-related protein of 30 kDa (Acrp30)
    • Tsao, T. S., Murrey, H. E., Hug, C., Lee, D. H. & Lodish, H. F. Oligomerization state-dependent activation of NF-κB signaling pathway by adipocyte complement-related protein of 30 kDa (Acrp30). J. Biol. Chem. 277, 29359-29362 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 29359-29362
    • Tsao, T.S.1    Murrey, H.E.2    Hug, C.3    Lee, D.H.4    Lodish, H.F.5
  • 54
    • 0030592623 scopus 로고    scopus 로고
    • The α1 and α2 isoforms of the AMP-activated protein kinase have similar activities in rat liver but exhibit differences in substrate specificity in vitro
    • Woods, A., Salt, I., Scott, J., Hardie, D. G. & Carling, D. The α1 and α2 isoforms of the AMP-activated protein kinase have similar activities in rat liver but exhibit differences in substrate specificity in vitro. FEBS Lett. 397, 347-351 (1996).
    • (1996) FEBS Lett. , vol.397 , pp. 347-351
    • Woods, A.1    Salt, I.2    Scott, J.3    Hardie, D.G.4    Carling, D.5
  • 55
    • 0034070567 scopus 로고    scopus 로고
    • Metabolic stress and altered glucose transport. Activation of AMP-activated protein kinase as a unifying couplingmechanism
    • Hayashi, T. et al. Metabolic stress and altered glucose transport. Activation of AMP-activated protein kinase as a unifying couplingmechanism. Diabetes 49, 527-531 (2000).
    • (2000) Diabetes , vol.49 , pp. 527-531
    • Hayashi, T.1
  • 56
    • 84857254248 scopus 로고    scopus 로고
    • Crystal structure of a lipid G protein-coupled receptor
    • Hanson, M. A. et al. Crystal structure of a lipid G protein-coupled receptor. Science 335, 851-855 (2012).
    • (2012) Science , vol.335 , pp. 851-855
    • Hanson, M.A.1
  • 57
    • 79959564813 scopus 로고    scopus 로고
    • Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation
    • Lebon, G. et al. Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation. Nature 474, 521-525 (2011).
    • (2011) Nature , vol.474 , pp. 521-525
    • Lebon, G.1
  • 58
    • 8844250818 scopus 로고    scopus 로고
    • Anabaena sensory rhodopsin: A photochromic color sensor at 2.0 Å
    • Vogeley, L. et al. Anabaena sensory rhodopsin: a photochromic color sensor at 2.0 Å. Science 306, 1390-1393 (2004).
    • (2004) Science , vol.306 , pp. 1390-1393
    • Vogeley, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.