메뉴 건너뛰기




Volumn 5, Issue 10, 2016, Pages 903-917

TNP [N2-(m-Trifluorobenzyl), N6-(p-nitrobenzyl)purine] ameliorates diet induced obesity and insulin resistance via inhibition of the IP6K1 pathway

Author keywords

Akt; Diabetes; Energy expenditure; Inositol pyrophosphate; IP6K; Obesity

Indexed keywords

CYTOCHROME P450 1A2; CYTOCHROME P450 2C9; CYTOCHROME P450 2D6; CYTOCHROME P450 3A4; GLUCOSE; INOSITOL HEXAKISPHOSPHATE KINASE 1; INOSITOL PYROPHOSPHATE; N6 (4 NITROBENZYL) N2 [3 (TRIFLUOROMETHYL)BENZYL] 9H PURINE 2,6 DIAMINE; PHOSPHORIC ACID DERIVATIVE; PHOSPHOTRANSFERASE; PHOSPHOTRANSFERASE INHIBITOR; PROTEIN KINASE B; UNCLASSIFIED DRUG;

EID: 84992170437     PISSN: None     EISSN: 22128778     Source Type: Journal    
DOI: 10.1016/j.molmet.2016.08.008     Document Type: Article
Times cited : (48)

References (96)
  • 6
    • 34547463821 scopus 로고    scopus 로고
    • Do we need new drugs for the treatment of type 2 diabetes mellitus?
    • [6] Vervoort, G., T.C., Do we need new drugs for the treatment of type 2 diabetes mellitus?. Netherlands Journal of Medicine 65 (2007), 157–159.
    • (2007) Netherlands Journal of Medicine , vol.65 , pp. 157-159
    • Vervoort, G.1    T.C.2
  • 7
    • 84891919414 scopus 로고    scopus 로고
    • Long-term drug treatment for obesity: a systematic and clinical review
    • [7] Yanovski, S.Z., Y.J., Long-term drug treatment for obesity: a systematic and clinical review. JAMA 311 (2014), 74–86.
    • (2014) JAMA , vol.311 , pp. 74-86
    • Yanovski, S.Z.1    Y.J.2
  • 8
    • 79961165599 scopus 로고    scopus 로고
    • Current and future drug targets in weight management
    • [8] Witkamp, R.F., Current and future drug targets in weight management. Pharmaceutical Research 28 (2011), 1792–1818.
    • (2011) Pharmaceutical Research , vol.28 , pp. 1792-1818
    • Witkamp, R.F.1
  • 11
    • 27944474772 scopus 로고    scopus 로고
    • Serine kinases as new drug targets for the treatment of type 2 diabetes. Current medicinal chemistry-immunology
    • [11] Rondinone, C., Serine kinases as new drug targets for the treatment of type 2 diabetes. Current medicinal chemistry-immunology. Endocrine & Metabolic Agents 5 (2005), 529–536.
    • (2005) Endocrine & Metabolic Agents , vol.5 , pp. 529-536
    • Rondinone, C.1
  • 12
    • 77953169046 scopus 로고    scopus 로고
    • Cellular bioenergetics as a target for obesity therapy
    • [12] Tseng, Y.H., C.A., Kahn, C.R., Cellular bioenergetics as a target for obesity therapy. Nature Reviews Drug Discovery 9 (2010), 465–482.
    • (2010) Nature Reviews Drug Discovery , vol.9 , pp. 465-482
    • Tseng, Y.H.1    C.A.2    Kahn, C.R.3
  • 13
    • 77954941113 scopus 로고    scopus 로고
    • Anti-diabetic drugs inhibit obesity-linked phosphorylation of PPARgamma by Cdk5
    • [13] Choi, J.H., B.A., Estall, J.L., Kajimura, S., Boström, P., Laznik, D., et al. Anti-diabetic drugs inhibit obesity-linked phosphorylation of PPARgamma by Cdk5. Nature 466 (2010), 451–456.
    • (2010) Nature , vol.466 , pp. 451-456
    • Choi, J.H.1    B.A.2    Estall, J.L.3    Kajimura, S.4    Boström, P.5    Laznik, D.6
  • 14
    • 2942560866 scopus 로고    scopus 로고
    • Inhibition of insulin secretion as a new drug target in the treatment of metabolic disorders
    • [14] Hansen, J.B., A.P., Bodvarsdottir, T.B., Wahl, P., Inhibition of insulin secretion as a new drug target in the treatment of metabolic disorders. Current Medicinal Chemistry 11 (2004), 1595–1615.
    • (2004) Current Medicinal Chemistry , vol.11 , pp. 1595-1615
    • Hansen, J.B.1    A.P.2    Bodvarsdottir, T.B.3    Wahl, P.4
  • 16
    • 2442710044 scopus 로고    scopus 로고
    • Genetic vulnerability to diet-induced obesity in the C57BL/6J mouse: physiological and molecular characteristics
    • [16] Collins, S., M.T., Surwit, R.S., Robidoux, J., Genetic vulnerability to diet-induced obesity in the C57BL/6J mouse: physiological and molecular characteristics. Physiology & Behavior 81 (2004), 243–248.
    • (2004) Physiology & Behavior , vol.81 , pp. 243-248
    • Collins, S.1    M.T.2    Surwit, R.S.3    Robidoux, J.4
  • 17
    • 34248393099 scopus 로고    scopus 로고
    • High-fat diets: modeling the metabolic disorders of human obesity in rodents
    • [17] Buettner, R., S.J., Bollheimer, L.C., High-fat diets: modeling the metabolic disorders of human obesity in rodents. Obesity (Silver Spring) 15 (2007), 798–808.
    • (2007) Obesity (Silver Spring) , vol.15 , pp. 798-808
    • Buettner, R.1    S.J.2    Bollheimer, L.C.3
  • 18
    • 84872515516 scopus 로고    scopus 로고
    • Kinase drug discovery–what's next in the field?
    • [18] Cohen, P., A.D., Kinase drug discovery–what's next in the field?. ACS Chemical Biology 8 (2013), 96–104.
    • (2013) ACS Chemical Biology , vol.8 , pp. 96-104
    • Cohen, P.1    A.D.2
  • 19
    • 80052293419 scopus 로고    scopus 로고
    • Inositol pyrophosphates as mammalian cell signals
    • [19] Chakraborty, A., K.S., Snyder, S.H., Inositol pyrophosphates as mammalian cell signals. Science Signalling, 4, 2011, re1.
    • (2011) Science Signalling , vol.4 , pp. re1
    • Chakraborty, A.1    K.S.2    Snyder, S.H.3
  • 20
    • 84878393302 scopus 로고    scopus 로고
    • Inositol pyrophosphates: between signalling and metabolism
    • [20] Wilson, M.S., L.T., Saiardi, A., Inositol pyrophosphates: between signalling and metabolism. Biochemical Journal 452 (2013), 369–379.
    • (2013) Biochemical Journal , vol.452 , pp. 369-379
    • Wilson, M.S.1    L.T.2    Saiardi, A.3
  • 21
    • 84940960231 scopus 로고    scopus 로고
    • The emerging roles of inositol pyrophosphates in eukaryotic cell physiology
    • [21] Thota, S.G., B.R., The emerging roles of inositol pyrophosphates in eukaryotic cell physiology. Journal of Biosciences 40 (2015), 593–605.
    • (2015) Journal of Biosciences , vol.40 , pp. 593-605
    • Thota, S.G.1    B.R.2
  • 22
    • 84958042064 scopus 로고    scopus 로고
    • Towards pharmacological intervention in inositol pyrophosphate signalling
    • [22] Shears, S., Towards pharmacological intervention in inositol pyrophosphate signalling. Biochemical Society Transactions 44 (2016), 191–196.
    • (2016) Biochemical Society Transactions , vol.44 , pp. 191-196
    • Shears, S.1
  • 24
    • 0033581832 scopus 로고    scopus 로고
    • Synthesis of diphosphoinositol pentakisphosphate by a newly identified family of higher inositol polyphosphate kinases
    • [24] Saiardi, A., E.-B.H., Snowman, A.M., Tempst, P., Snyder, S.H., Synthesis of diphosphoinositol pentakisphosphate by a newly identified family of higher inositol polyphosphate kinases. Current Biology 9 (1999), 1323–1326.
    • (1999) Current Biology , vol.9 , pp. 1323-1326
    • Saiardi, A.1    E.-B.H.2    Snowman, A.M.3    Tempst, P.4    Snyder, S.H.5
  • 25
    • 0035914367 scopus 로고    scopus 로고
    • Identification and characterization of a novel inositol hexakisphosphate kinase
    • [25] Saiardi, A., N.E., Luo, H.R., Snowman, A.M., Snyder, S.H., Identification and characterization of a novel inositol hexakisphosphate kinase. Journal of Biological Chemistry 276 (2001), 39179–39185.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 39179-39185
    • Saiardi, A.1    N.E.2    Luo, H.R.3    Snowman, A.M.4    Snyder, S.H.5
  • 26
    • 84904651228 scopus 로고    scopus 로고
    • Discovery of InsP6-kinases as InsP6-dephosphorylating enzymes provides a new mechanism of cytosolic InsP6 degradation driven by the cellular ATP/ADP ratio
    • [26] Wundenberg, T., G.N., Lin, H., Mayr, G.W., Discovery of InsP6-kinases as InsP6-dephosphorylating enzymes provides a new mechanism of cytosolic InsP6 degradation driven by the cellular ATP/ADP ratio. Biochemical Journal 462 (2014), 173–184.
    • (2014) Biochemical Journal , vol.462 , pp. 173-184
    • Wundenberg, T.1    G.N.2    Lin, H.3    Mayr, G.W.4
  • 27
    • 85009515808 scopus 로고    scopus 로고
    • Inositol hexakisphosphate kinase 1 (IP6K1) activity is required for cytoplasmic dynein-driven transport
    • p. pii: BCJ20160610
    • [27] Chanduri, M., R.A., Malla, A.B., Wu, M., Fiedler, D., Mallik, R., et al. Inositol hexakisphosphate kinase 1 (IP6K1) activity is required for cytoplasmic dynein-driven transport. Biochemical Journal, 2016 p. pii: BCJ20160610.
    • (2016) Biochemical Journal
    • Chanduri, M.1    R.A.2    Malla, A.B.3    Wu, M.4    Fiedler, D.5    Mallik, R.6
  • 28
    • 84886805114 scopus 로고    scopus 로고
    • Inositol hexakisphosphate kinase 1 maintains hemostasis in mice by regulating platelet polyphosphate levels
    • [28] Ghosh, S., S.D., Suman, K., Lakshmi, B.J., Manorama, R., Kumar, S., et al. Inositol hexakisphosphate kinase 1 maintains hemostasis in mice by regulating platelet polyphosphate levels. Blood 122 (2013), 1478–1486.
    • (2013) Blood , vol.122 , pp. 1478-1486
    • Ghosh, S.1    S.D.2    Suman, K.3    Lakshmi, B.J.4    Manorama, R.5    Kumar, S.6
  • 30
    • 84894581100 scopus 로고    scopus 로고
    • Inositol hexakisphosphate kinase-1 regulates behavioral responses via GSK3 signaling pathways
    • [30] Chakraborty, A., L.C., Xu, J., Snyder, S.H., Beaulieu, J.M., Inositol hexakisphosphate kinase-1 regulates behavioral responses via GSK3 signaling pathways. Molecular Psychiatry 19 (2014), 284–293.
    • (2014) Molecular Psychiatry , vol.19 , pp. 284-293
    • Chakraborty, A.1    L.C.2    Xu, J.3    Snyder, S.H.4    Beaulieu, J.M.5
  • 31
    • 17944372902 scopus 로고    scopus 로고
    • GRAB: a physiologic guanine nucleotide exchange factor for Rab3A, which interacts with inositol hexakisphosphate kinase
    • [31] Luo, H.R., S.A., Nagata, E., Ye, K., Yu, H., Jung, T.S., et al. GRAB: a physiologic guanine nucleotide exchange factor for Rab3A, which interacts with inositol hexakisphosphate kinase. Neuron 31 (2001), 439–451.
    • (2001) Neuron , vol.31 , pp. 439-451
    • Luo, H.R.1    S.A.2    Nagata, E.3    Ye, K.4    Yu, H.5    Jung, T.S.6
  • 32
    • 78649961357 scopus 로고    scopus 로고
    • Inositol pyrophosphates inhibit Akt signaling, regulate insulin sensitivity and weight gain
    • [32] Chakraborty, A., K.M., Bello, N.T., Maxwell, M., Potter, J.J., Juluri, K.R., et al. Inositol pyrophosphates inhibit Akt signaling, regulate insulin sensitivity and weight gain. Cell 143 (2010), 897–910.
    • (2010) Cell , vol.143 , pp. 897-910
    • Chakraborty, A.1    K.M.2    Bello, N.T.3    Maxwell, M.4    Potter, J.J.5    Juluri, K.R.6
  • 33
    • 36448947507 scopus 로고    scopus 로고
    • Requirement of inositol pyrophosphates for full exocytotic capacity in pancreatic beta cells
    • [33] Illies, C., G.J., Fiume, R., Leibiger, B., Yu, J., Juhl, K., et al. Requirement of inositol pyrophosphates for full exocytotic capacity in pancreatic beta cells. Science 318 (2007), 1299–1302.
    • (2007) Science , vol.318 , pp. 1299-1302
    • Illies, C.1    G.J.2    Fiume, R.3    Leibiger, B.4    Yu, J.5    Juhl, K.6
  • 34
    • 81055137383 scopus 로고    scopus 로고
    • Influence of inositol pyrophosphates on cellular energy dynamics
    • [34] Szijgyarto, Z., G.A., Azevedo, C., Saiardi, A., Influence of inositol pyrophosphates on cellular energy dynamics. Science 334 (2011), 802–805.
    • (2011) Science , vol.334 , pp. 802-805
    • Szijgyarto, Z.1    G.A.2    Azevedo, C.3    Saiardi, A.4
  • 35
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB signaling: navigating downstream
    • [35] Manning, B.D., C.L., AKT/PKB signaling: navigating downstream. Cell 129 (2007), 1261–1274.
    • (2007) Cell , vol.129 , pp. 1261-1274
    • Manning, B.D.1    C.L.2
  • 36
    • 0030824358 scopus 로고    scopus 로고
    • A role for the serine/threonine kinase, Akt, in insulin-stimulated glucose uptake
    • [36] Summers, S.A., B.M., A role for the serine/threonine kinase, Akt, in insulin-stimulated glucose uptake. Biochemical Society Transactions 25 (1997), 981–988.
    • (1997) Biochemical Society Transactions , vol.25 , pp. 981-988
    • Summers, S.A.1    B.M.2
  • 37
    • 84894829780 scopus 로고    scopus 로고
    • Akt/PKB activation and insulin signaling: a novel insulin signaling pathway in the treatment of type 2 diabetes
    • [37] Mackenzie, R.W., E.B., Akt/PKB activation and insulin signaling: a novel insulin signaling pathway in the treatment of type 2 diabetes. Diabetes, Metabolic Syndrome and Obesity: Targets and Therapy 13 (2014), 55–64.
    • (2014) Diabetes, Metabolic Syndrome and Obesity: Targets and Therapy , vol.13 , pp. 55-64
    • Mackenzie, R.W.1    E.B.2
  • 38
    • 0035368548 scopus 로고    scopus 로고
    • Insulin resistance and a diabetes mellitus-like syndrome in mice lacking the protein kinase Akt2 (PKB beta)
    • [38] Cho, H., M.J., Kim, J.K., Thorvaldsen, J.L., Chu, Q., Crenshaw, E.B. 3rd, et al. Insulin resistance and a diabetes mellitus-like syndrome in mice lacking the protein kinase Akt2 (PKB beta). Science 292 (2001), 1728–1731.
    • (2001) Science , vol.292 , pp. 1728-1731
    • Cho, H.1    M.J.2    Kim, J.K.3    Thorvaldsen, J.L.4    Chu, Q.5    Crenshaw, E.B.6
  • 39
    • 38649091396 scopus 로고    scopus 로고
    • Fast/Glycolytic muscle fiber growth reduces fat mass and improves metabolic parameters in obese mice
    • [39] Izumiya, Y., H.T., Morris, C., Sato, K., Zeng, L., Viereck, J., et al. Fast/Glycolytic muscle fiber growth reduces fat mass and improves metabolic parameters in obese mice. Cell Metabolism 7 (2008), 159–172.
    • (2008) Cell Metabolism , vol.7 , pp. 159-172
    • Izumiya, Y.1    H.T.2    Morris, C.3    Sato, K.4    Zeng, L.5    Viereck, J.6
  • 40
    • 84938747174 scopus 로고    scopus 로고
    • Adiponectin enhances cold-induced browning of subcutaneous adipose tissue via promoting M2 macrophage proliferation
    • [40] Hui, X., G.P., Zhang, J., Nie, T., Pan, Y., Wu, D., et al. Adiponectin enhances cold-induced browning of subcutaneous adipose tissue via promoting M2 macrophage proliferation. Cell Metabolism 22 (2015), 279–290.
    • (2015) Cell Metabolism , vol.22 , pp. 279-290
    • Hui, X.1    G.P.2    Zhang, J.3    Nie, T.4    Pan, Y.5    Wu, D.6
  • 41
    • 20044389885 scopus 로고    scopus 로고
    • Insulin-stimulated phosphorylation of the Akt substrate AS160 is impaired in skeletal muscle of type 2 diabetic subjects
    • [41] Karlsson, H.K., Z.J., Kane, S., Krook, A., Lienhard, G.E., Wallberg-Henriksson, H., Insulin-stimulated phosphorylation of the Akt substrate AS160 is impaired in skeletal muscle of type 2 diabetic subjects. Diabetes 54 (2005), 1692–1697.
    • (2005) Diabetes , vol.54 , pp. 1692-1697
    • Karlsson, H.K.1    Z.J.2    Kane, S.3    Krook, A.4    Lienhard, G.E.5    Wallberg-Henriksson, H.6
  • 42
    • 0031852665 scopus 로고    scopus 로고
    • Insulin-stimulated Akt kinase activity is reduced in skeletal muscle from NIDDM subjects
    • [42] Krook, A., R.R., Jiang, X.J., Zierath, J.R., Wallberg-Henriksson, H., Insulin-stimulated Akt kinase activity is reduced in skeletal muscle from NIDDM subjects. Diabetes 47 (1998), 1281–1286.
    • (1998) Diabetes , vol.47 , pp. 1281-1286
    • Krook, A.1    R.R.2    Jiang, X.J.3    Zierath, J.R.4    Wallberg-Henriksson, H.5
  • 43
    • 79953317808 scopus 로고    scopus 로고
    • Obesity-induced overexpression of miRNA-143 inhibits insulin-stimulated AKT activation and impairs glucose metabolism
    • [43] Jordan, S.D., K.M., Willmes, D.M., Redemann, N., Wunderlich, F.T., Brönneke, H.S., et al. Obesity-induced overexpression of miRNA-143 inhibits insulin-stimulated AKT activation and impairs glucose metabolism. Nature Cell Biology 13 (2011), 434–446.
    • (2011) Nature Cell Biology , vol.13 , pp. 434-446
    • Jordan, S.D.1    K.M.2    Willmes, D.M.3    Redemann, N.4    Wunderlich, F.T.5    Brönneke, H.S.6
  • 44
    • 27144450970 scopus 로고    scopus 로고
    • Insulin-sensitive protein kinases (atypical protein kinase C and protein kinase B/Akt): actions and defects in obesity and type II diabetes
    • [44] Farese, R.V., S.M., Standaert, M.L., Insulin-sensitive protein kinases (atypical protein kinase C and protein kinase B/Akt): actions and defects in obesity and type II diabetes. Experimental Biology and Medicine (Maywood) 230 (2005), 593–605.
    • (2005) Experimental Biology and Medicine (Maywood) , vol.230 , pp. 593-605
    • Farese, R.V.1    S.M.2    Standaert, M.L.3
  • 45
    • 80052026626 scopus 로고    scopus 로고
    • Inositol hexakisphosphate kinase 1 regulates neutrophil function in innate immunity by inhibiting phosphatidylinositol-(3,4,5)-trisphosphate signaling
    • [45] Prasad, A., J.Y., Chakraborty, A., Li, Y., Jain, S.K., Zhong, J., et al. Inositol hexakisphosphate kinase 1 regulates neutrophil function in innate immunity by inhibiting phosphatidylinositol-(3,4,5)-trisphosphate signaling. Nature Immunology 12 (2011), 752–760.
    • (2011) Nature Immunology , vol.12 , pp. 752-760
    • Prasad, A.1    J.Y.2    Chakraborty, A.3    Li, Y.4    Jain, S.K.5    Zhong, J.6
  • 46
    • 84877350576 scopus 로고    scopus 로고
    • Cigarette smoke (CS) and nicotine delay neutrophil spontaneous death via suppressing production of diphosphoinositol pentakisphosphate
    • [46] Xu, Y., L.H., Bajrami, B., Kwak, H., Cao, S., Liu, P., et al. Cigarette smoke (CS) and nicotine delay neutrophil spontaneous death via suppressing production of diphosphoinositol pentakisphosphate. Proceedings of the National Academy of Sciences of the United States of America 110 (2013), 7726–7731.
    • (2013) Proceedings of the National Academy of Sciences of the United States of America , vol.110 , pp. 7726-7731
    • Xu, Y.1    L.H.2    Bajrami, B.3    Kwak, H.4    Cao, S.5    Liu, P.6
  • 47
    • 0141540848 scopus 로고    scopus 로고
    • Inositol pyrophosphates mediate chemotaxis in Dictyostelium via pleckstrin homology domain-PtdIns(3,4,5)P3 interactions
    • [47] Luo, H.R., H.Y., Chen, J.C., Saiardi, A., Iijima, M., Ye, K., et al. Inositol pyrophosphates mediate chemotaxis in Dictyostelium via pleckstrin homology domain-PtdIns(3,4,5)P3 interactions. Cell 114 (2003), 559–572.
    • (2003) Cell , vol.114 , pp. 559-572
    • Luo, H.R.1    H.Y.2    Chen, J.C.3    Saiardi, A.4    Iijima, M.5    Ye, K.6
  • 48
    • 84874408677 scopus 로고    scopus 로고
    • Synthesis and characterization of non-hydrolysable diphosphoinositol polyphosphate second messengers
    • [48] Wu, M., D.B., Trevisan, A.J., Fiedler, D., Synthesis and characterization of non-hydrolysable diphosphoinositol polyphosphate second messengers. Chemical Science 4 (2013), 405–410.
    • (2013) Chemical Science , vol.4 , pp. 405-410
    • Wu, M.1    D.B.2    Trevisan, A.J.3    Fiedler, D.4
  • 49
    • 84957068217 scopus 로고    scopus 로고
    • Cellular delivery and photochemical release of a caged inositol-pyrophosphate induces PH-domain translocation in cellulo
    • [49] Pavlovic, I., T.D., Vargas, J.R., McKinlay, C.J., Hauke, S., Anstaett, P., et al. Cellular delivery and photochemical release of a caged inositol-pyrophosphate induces PH-domain translocation in cellulo. Nature Communications, 7, 2016, 10622.
    • (2016) Nature Communications , vol.7 , pp. 10622
    • Pavlovic, I.1    T.D.2    Vargas, J.R.3    McKinlay, C.J.4    Hauke, S.5    Anstaett, P.6
  • 50
    • 84892727198 scopus 로고    scopus 로고
    • What we talk about when we talk about fat
    • [50] Rosen, E.D., S.B., What we talk about when we talk about fat. Cell 156 (2014), 20–44.
    • (2014) Cell , vol.156 , pp. 20-44
    • Rosen, E.D.1    S.B.2
  • 51
    • 84887431711 scopus 로고    scopus 로고
    • Brown and beige fat: development, function and therapeutic potential
    • [51] Harms, M., S.P., Brown and beige fat: development, function and therapeutic potential. Nature Medicine 19 (2013), 1252–1263.
    • (2013) Nature Medicine , vol.19 , pp. 1252-1263
    • Harms, M.1    S.P.2
  • 53
    • 12244284906 scopus 로고    scopus 로고
    • Purine-based inhibitors of inositol-1,4,5-trisphosphate-3-kinase
    • [53] Chang, Y.T., C.G., Bae, Y.S., Burdett, M., Moon, H.S., Lee, J.W., et al. Purine-based inhibitors of inositol-1,4,5-trisphosphate-3-kinase. ChemBioChem 3 (2002), 897–901.
    • (2002) ChemBioChem , vol.3 , pp. 897-901
    • Chang, Y.T.1    C.G.2    Bae, Y.S.3    Burdett, M.4    Moon, H.S.5    Lee, J.W.6
  • 54
    • 67449093365 scopus 로고    scopus 로고
    • Characterization of a selective inhibitor of inositol hexakisphosphate kinases: use in defining biological roles and metabolic relationships of inositol pyrophosphates
    • [54] Padmanabhan, U., D.D., Fridy, P.C., York, J.D., Downes, C.P., Characterization of a selective inhibitor of inositol hexakisphosphate kinases: use in defining biological roles and metabolic relationships of inositol pyrophosphates. Journal of Biological Chemistry 284 (2009), 10571–10582.
    • (2009) Journal of Biological Chemistry , vol.284 , pp. 10571-10582
    • Padmanabhan, U.1    D.D.2    Fridy, P.C.3    York, J.D.4    Downes, C.P.5
  • 55
    • 83655198346 scopus 로고    scopus 로고
    • Structural basis for an inositol pyrophosphate kinase surmounting phosphate crowding
    • [55] Wang, H., F.J., Hall, T.M., Shears, S.B., Structural basis for an inositol pyrophosphate kinase surmounting phosphate crowding. Nature Chemical Biology 8 (2011), 111–116.
    • (2011) Nature Chemical Biology , vol.8 , pp. 111-116
    • Wang, H.1    F.J.2    Hall, T.M.3    Shears, S.B.4
  • 56
    • 84929966581 scopus 로고    scopus 로고
    • (OSM) protects against cardiac ischaemia/reperfusion injury in diabetic mice by regulating apoptosis, mitochondrial biogenesis and insulin sensitivity
    • [56] Sun, D., L.S., Wu, H., Zhang, M., Zhang, X., Wei, L., et al. (OSM) protects against cardiac ischaemia/reperfusion injury in diabetic mice by regulating apoptosis, mitochondrial biogenesis and insulin sensitivity. Journal of Cellular and Molecular Medicine 19 (2015), 1296–1307.
    • (2015) Journal of Cellular and Molecular Medicine , vol.19 , pp. 1296-1307
    • Sun, D.1    L.S.2    Wu, H.3    Zhang, M.4    Zhang, X.5    Wei, L.6
  • 57
    • 84899413885 scopus 로고    scopus 로고
    • Inositol pyrophosphates mediate the effects of aging on bone marrow mesenchymal stem cells by inhibiting Akt signaling
    • [57] Zhang, Z., Z.C., Liu, B., Liang, D., Qin, X., Li, X., et al. Inositol pyrophosphates mediate the effects of aging on bone marrow mesenchymal stem cells by inhibiting Akt signaling. Journal of Stem Cell Research & Therapy, 5, 2014, 33.
    • (2014) Journal of Stem Cell Research & Therapy , vol.5 , pp. 33
    • Zhang, Z.1    Z.C.2    Liu, B.3    Liang, D.4    Qin, X.5    Li, X.6
  • 59
    • 40649083560 scopus 로고    scopus 로고
    • Gene deletion of inositol hexakisphosphate kinase 1 reveals inositol pyrophosphate regulation of insulin secretion, growth, and spermiogenesis
    • [59] Bhandari, R., J.K., Resnick, A.C., Snyder, S.H., Gene deletion of inositol hexakisphosphate kinase 1 reveals inositol pyrophosphate regulation of insulin secretion, growth, and spermiogenesis. Proceedings of the National Academy of Sciences of the United States of America 105 (2008), 2349–2353.
    • (2008) Proceedings of the National Academy of Sciences of the United States of America , vol.105 , pp. 2349-2353
    • Bhandari, R.1    J.K.2    Resnick, A.C.3    Snyder, S.H.4
  • 61
    • 65949094795 scopus 로고    scopus 로고
    • Inositol pyrophosphates and their unique metabolic complexity: analysis by gel electrophoresis
    • [61] Losito, O., S.Z., Resnick, A.C., Saiardi, A., Inositol pyrophosphates and their unique metabolic complexity: analysis by gel electrophoresis. PLoS One, 4, 2009, e5580.
    • (2009) PLoS One , vol.4 , pp. e5580
    • Losito, O.1    S.Z.2    Resnick, A.C.3    Saiardi, A.4
  • 63
    • 84874215124 scopus 로고    scopus 로고
    • Midbrain-derived neurotrophins support survival of immature striatal projection neurons
    • [63] Baydyuk, M., X.Y., Tessarollo, L., Xu, B., Midbrain-derived neurotrophins support survival of immature striatal projection neurons. Journal of Neuroscience 33 (2013), 3363–3369.
    • (2013) Journal of Neuroscience , vol.33 , pp. 3363-3369
    • Baydyuk, M.1    X.Y.2    Tessarollo, L.3    Xu, B.4
  • 64
    • 0024342953 scopus 로고
    • Optimizing sampling designs for volume measurements of components of human brain using a stereological method
    • [64] Regeur, L., P.B., Optimizing sampling designs for volume measurements of components of human brain using a stereological method. Journal of Microscopy 155 (1989), 113–121.
    • (1989) Journal of Microscopy , vol.155 , pp. 113-121
    • Regeur, L.1    P.B.2
  • 65
    • 0030857878 scopus 로고    scopus 로고
    • Low-density lipoprotein receptor knockout mice exhibit exaggerated microvascular responses to inflammatory stimuli
    • [65] Henninger, D.D., G.M., Granger, D.N., Low-density lipoprotein receptor knockout mice exhibit exaggerated microvascular responses to inflammatory stimuli. Circulation Research 81 (1997), 274–281.
    • (1997) Circulation Research , vol.81 , pp. 274-281
    • Henninger, D.D.1    G.M.2    Granger, D.N.3
  • 66
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
    • [66] Sarbassov, D.D., G.D., Ali, S.M., Sabatini, D.M., Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 307 (2005), 1098–1101.
    • (2005) Science , vol.307 , pp. 1098-1101
    • Sarbassov, D.D.1    G.D.2    Ali, S.M.3    Sabatini, D.M.4
  • 67
    • 0031127305 scopus 로고    scopus 로고
    • Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Balpha
    • [67] Alessi, D.R., J.S., Downes, C.P., Holmes, A.B., Gaffney, P.R., Reese, C.B., et al. Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Balpha. Current Biology 7 (1997), 261–269.
    • (1997) Current Biology , vol.7 , pp. 261-269
    • Alessi, D.R.1    J.S.2    Downes, C.P.3    Holmes, A.B.4    Gaffney, P.R.5    Reese, C.B.6
  • 68
    • 0031264289 scopus 로고    scopus 로고
    • A role for brown adipose tissue in diet-induced thermogenesis
    • [68] Rothwell, N.J., S.M., A role for brown adipose tissue in diet-induced thermogenesis. Obesity Research 5 (1997), 650–656.
    • (1997) Obesity Research , vol.5 , pp. 650-656
    • Rothwell, N.J.1    S.M.2
  • 69
    • 58149529580 scopus 로고    scopus 로고
    • UCP1: its involvement and utility in obesity
    • [69] Kozak, L.P., A.-K.R, UCP1: its involvement and utility in obesity. International Journal of Obesity (Lond) 32:Suppl. 7 (2008), S32–S38.
    • (2008) International Journal of Obesity (Lond) , vol.32 , pp. S32-S38
    • Kozak, L.P.1    A.-K.R2
  • 70
    • 84992198589 scopus 로고    scopus 로고
    • Brown adipose tissue as an anti-obesity tissue in humans
    • [70] Chechi, K., N.J., Richard, D., Brown adipose tissue as an anti-obesity tissue in humans. Obesity Review, 2013.
    • (2013) Obesity Review
    • Chechi, K.1    N.J.2    Richard, D.3
  • 71
    • 0037008157 scopus 로고    scopus 로고
    • betaAR signaling required for diet-induced thermogenesis and obesity resistance
    • [71] Bachman, E.S., D.H., Zhang, C.Y., Cinti, S., Bianco, A.C., Kobilka, B.K., et al. betaAR signaling required for diet-induced thermogenesis and obesity resistance. Science 297 (2002), 843–845.
    • (2002) Science , vol.297 , pp. 843-845
    • Bachman, E.S.1    D.H.2    Zhang, C.Y.3    Cinti, S.4    Bianco, A.C.5    Kobilka, B.K.6
  • 72
    • 84901821975 scopus 로고    scopus 로고
    • FGF21-based pharmacotherapy–potential utility for metabolic disorders
    • [72] Gimeno, R.E., M.D., FGF21-based pharmacotherapy–potential utility for metabolic disorders. Trends in Endocrinology and Metabolism 25 (2014), 303–311.
    • (2014) Trends in Endocrinology and Metabolism , vol.25 , pp. 303-311
    • Gimeno, R.E.1    M.D.2
  • 74
    • 84899472730 scopus 로고    scopus 로고
    • A heart-adipose tissue connection in the regulation of energy metabolism
    • [74] Collins, S., A heart-adipose tissue connection in the regulation of energy metabolism. Nature Reviews Endocrinology 10 (2014), 157–163.
    • (2014) Nature Reviews Endocrinology , vol.10 , pp. 157-163
    • Collins, S.1
  • 75
    • 78649706279 scopus 로고    scopus 로고
    • The effect of plasma protein binding on in vivo efficacy: misconceptions in drug discovery
    • [75] Smith, D.A., D.L., Kerns, E.H., The effect of plasma protein binding on in vivo efficacy: misconceptions in drug discovery. Nature Reviews Drug Discovery 9 (2010), 929–939.
    • (2010) Nature Reviews Drug Discovery , vol.9 , pp. 929-939
    • Smith, D.A.1    D.L.2    Kerns, E.H.3
  • 76
    • 84905740317 scopus 로고    scopus 로고
    • Inhibition of Notch signaling promotes browning of white adipose tissue and ameliorates obesity
    • [76] Bi, P., S.T., Liu, W., Yue, F., Yang, X., Liang, X.R., et al. Inhibition of Notch signaling promotes browning of white adipose tissue and ameliorates obesity. Nature Medicine, 2014.
    • (2014) Nature Medicine
    • Bi, P.1    S.T.2    Liu, W.3    Yue, F.4    Yang, X.5    Liang, X.R.6
  • 77
    • 84862776702 scopus 로고    scopus 로고
    • A PGC1-α-dependent myokine that drives brown-fat-like development of white fat and thermogenesis
    • [77] Boström, P., W.J., Jedrychowski, M.P., Korde, A., Ye, L., Lo, J.C., et al. A PGC1-α-dependent myokine that drives brown-fat-like development of white fat and thermogenesis. Nature 481 (2012), 463–468.
    • (2012) Nature , vol.481 , pp. 463-468
    • Boström, P.1    W.J.2    Jedrychowski, M.P.3    Korde, A.4    Ye, L.5    Lo, J.C.6
  • 78
    • 33747627853 scopus 로고    scopus 로고
    • Pharmacological targeting of adipocytes/fat metabolism for treatment of obesity and diabetes
    • [78] Pilch, P.F., B.N., Pharmacological targeting of adipocytes/fat metabolism for treatment of obesity and diabetes. Molecular Pharmacology 70 (2006), 779–785.
    • (2006) Molecular Pharmacology , vol.70 , pp. 779-785
    • Pilch, P.F.1    B.N.2
  • 81
    • 84876269773 scopus 로고    scopus 로고
    • Adaptive thermogenesis with weight loss in humans
    • [81] Müller, M.J., B.-W.A., Adaptive thermogenesis with weight loss in humans. Obesity (Silver Spring) 21 (2013), 218–228.
    • (2013) Obesity (Silver Spring) , vol.21 , pp. 218-228
    • Müller, M.J.1    B.-W.A.2
  • 84
    • 84898022580 scopus 로고    scopus 로고
    • Inositol pyrophosphates mediate the DNA-PK/ATM-p53 cell death pathway by regulating CK2 phosphorylation of Tti1/Tel2
    • [84] Rao, F., C.J., Xu, J., Xu, R., Vandiver, M.S., Tyagi, R., et al. Inositol pyrophosphates mediate the DNA-PK/ATM-p53 cell death pathway by regulating CK2 phosphorylation of Tti1/Tel2. Molecular Cell 54 (2014), 119–132.
    • (2014) Molecular Cell , vol.54 , pp. 119-132
    • Rao, F.1    C.J.2    Xu, J.3    Xu, R.4    Vandiver, M.S.5    Tyagi, R.6
  • 85
    • 84904728412 scopus 로고    scopus 로고
    • PI3K/Akt is involved in brown adipogenesis mediated by growth differentiation factor-5 in association with activation of the Smad pathway
    • [85] Hinoi, E., I.T., Fujita, H., Watanabe, T., Odaka, Y., Ozaki, K., et al. PI3K/Akt is involved in brown adipogenesis mediated by growth differentiation factor-5 in association with activation of the Smad pathway. Biochemical and Biophysical Research 450 (2014), 255–260.
    • (2014) Biochemical and Biophysical Research , vol.450 , pp. 255-260
    • Hinoi, E.1    I.T.2    Fujita, H.3    Watanabe, T.4    Odaka, Y.5    Ozaki, K.6
  • 86
    • 0038532266 scopus 로고    scopus 로고
    • Insulin-induced up-regulated uncoupling protein-1 expression is mediated by insulin receptor substrate 1 through the phosphatidylinositol 3-kinase/Akt signaling pathway in fetal brown adipocytes
    • [86] Valverde, A.M., A.M., Mur, C., Navarro, P., Pons, S., Cassard-Doulcier, A.M., et al. Insulin-induced up-regulated uncoupling protein-1 expression is mediated by insulin receptor substrate 1 through the phosphatidylinositol 3-kinase/Akt signaling pathway in fetal brown adipocytes. Journal of Biological Chemistry 278 (2003), 10221–10231.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 10221-10231
    • Valverde, A.M.1    A.M.2    Mur, C.3    Navarro, P.4    Pons, S.5    Cassard-Doulcier, A.M.6
  • 87
    • 84942819409 scopus 로고    scopus 로고
    • MicroRNA-455 regulates brown adipogenesis via a novel HIF1an-AMPK-PGC1α signaling network
    • [87] Zhang, H., G.M., Townsend, K.L., Huang, T.L., An, D., Yan, X., et al. MicroRNA-455 regulates brown adipogenesis via a novel HIF1an-AMPK-PGC1α signaling network. EMBO Reports 16 (2015), 1378–1393.
    • (2015) EMBO Reports , vol.16 , pp. 1378-1393
    • Zhang, H.1    G.M.2    Townsend, K.L.3    Huang, T.L.4    An, D.5    Yan, X.6
  • 89
    • 84951806052 scopus 로고    scopus 로고
    • Phosphoproteomics identifies CK2 as a negative regulator of beige adipocyte thermogenesis and energy expenditure
    • [89] Shinoda, K., O.K., Hasegawa, Y., Chang, H.Y., Ogura, M., Sato, A., et al. Phosphoproteomics identifies CK2 as a negative regulator of beige adipocyte thermogenesis and energy expenditure. Cell Metabolism 22 (2015), 997–1008.
    • (2015) Cell Metabolism , vol.22 , pp. 997-1008
    • Shinoda, K.1    O.K.2    Hasegawa, Y.3    Chang, H.Y.4    Ogura, M.5    Sato, A.6
  • 90
    • 64549127790 scopus 로고    scopus 로고
    • PGC-1alpha, SIRT1 and AMPK, an energy sensing network that controls energy expenditure
    • [90] Cantó, C., A.J., PGC-1alpha, SIRT1 and AMPK, an energy sensing network that controls energy expenditure. Current Opinion in Lipidology 20 (2009), 98–105.
    • (2009) Current Opinion in Lipidology , vol.20 , pp. 98-105
    • Cantó, C.1    A.J.2
  • 91
    • 83455163789 scopus 로고    scopus 로고
    • The blood-testis barrier and its implications for male contraception
    • [91] Cheng, C.Y., M.D., The blood-testis barrier and its implications for male contraception. Pharmacological Reviews 64 (2012), 16–64.
    • (2012) Pharmacological Reviews , vol.64 , pp. 16-64
    • Cheng, C.Y.1    M.D.2
  • 92
    • 84938819393 scopus 로고    scopus 로고
    • Inositol hexakisphosphate Kinase-3 regulates the morphology and synapse formation of cerebellar purkinje cells via spectrin/adducin
    • [92] Fu, C., X.J., Li, R.J., Crawford, J.A., Khan, A.B., Ma, T.M., et al. Inositol hexakisphosphate Kinase-3 regulates the morphology and synapse formation of cerebellar purkinje cells via spectrin/adducin. Journal of Neuroscience 35 (2015), 11056–11067.
    • (2015) Journal of Neuroscience , vol.35 , pp. 11056-11067
    • Fu, C.1    X.J.2    Li, R.J.3    Crawford, J.A.4    Khan, A.B.5    Ma, T.M.6
  • 93
    • 77952626956 scopus 로고    scopus 로고
    • Zinc release from thapsigargin/IP3-sensitive stores in cultured cortical neurons
    • [93] Stork, C.J., L.Y., Zinc release from thapsigargin/IP3-sensitive stores in cultured cortical neurons. Journal of Molecular Signaling, 5, 2010, 5.
    • (2010) Journal of Molecular Signaling , vol.5 , pp. 5
    • Stork, C.J.1    L.Y.2
  • 94
    • 84857498763 scopus 로고    scopus 로고
    • IP3 3-kinase opposes NGF driven neurite outgrowth
    • [94] Eva, R., B.-C.D., Patel, K., Cullen, P.J., Banting, G., IP3 3-kinase opposes NGF driven neurite outgrowth. PLoS One, 7, 2012, e32386.
    • (2012) PLoS One , vol.7 , pp. e32386
    • Eva, R.1    B.-C.D.2    Patel, K.3    Cullen, P.J.4    Banting, G.5
  • 95
    • 84958046831 scopus 로고    scopus 로고
    • Modulation of epidermal growth factor stimulated ERK phosphorylation and cell motility by inositol trisphosphate kinase
    • [95] Sekar, M.C., S.K., Leloup, L., Wells, A., Modulation of epidermal growth factor stimulated ERK phosphorylation and cell motility by inositol trisphosphate kinase. Journal of Pharmaceutical Sciences and Pharmacology 1 (2014), 160–164.
    • (2014) Journal of Pharmaceutical Sciences and Pharmacology , vol.1 , pp. 160-164
    • Sekar, M.C.1    S.K.2    Leloup, L.3    Wells, A.4
  • 96
    • 3843133857 scopus 로고    scopus 로고
    • The IHPK1 gene is disrupted at the 3p21.31 breakpoint of t(3;9) in a family with type 2 diabetes mellitus
    • [96] Kamimura, J., W.K., Kadowaki, H., Watanabe, Y., Miyake, K., Harada, N., et al. The IHPK1 gene is disrupted at the 3p21.31 breakpoint of t(3;9) in a family with type 2 diabetes mellitus. Journal of Human Genetics 49 (2004), 360–365.
    • (2004) Journal of Human Genetics , vol.49 , pp. 360-365
    • Kamimura, J.1    W.K.2    Kadowaki, H.3    Watanabe, Y.4    Miyake, K.5    Harada, N.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.