메뉴 건너뛰기




Volumn 52, Issue 20, 2013, Pages 3523-3531

Crystal structure of glucokinase regulatory protein

Author keywords

[No Author keywords available]

Indexed keywords

ATOMIC LEVELS; BLOOD GLUCOSE; CYTOSOLS; DOMAIN INTERFACES; GLUCOKINASE; H-D EXCHANGE; REGULATORY PROTEIN;

EID: 84878216569     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi4000782     Document Type: Article
Times cited : (35)

References (27)
  • 1
    • 79959798614 scopus 로고    scopus 로고
    • Glucokinase activators for diabetes therapy: May 2010 status report
    • Matschinsky, F. M. 2011, Glucokinase activators for diabetes therapy: May 2010 status report Diabetes Care 34 (Suppl. 2) S236-S243
    • (2011) Diabetes Care , vol.34 , Issue.SUPPL. 2
    • Matschinsky, F.M.1
  • 2
    • 14644394924 scopus 로고    scopus 로고
    • Glucokinase and glucose homeostasis: Proven concepts and new ideas
    • Zelent, D. 2005, Glucokinase and glucose homeostasis: Proven concepts and new ideas Biochem. Soc. Trans. 33, 306-310
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 306-310
    • Zelent, D.1
  • 3
    • 80955139676 scopus 로고    scopus 로고
    • The active conformation of human glucokinase is not altered by allosteric activators
    • Petit, P. 2011, The active conformation of human glucokinase is not altered by allosteric activators Acta Crystallogr. D67, 929-935
    • (2011) Acta Crystallogr. , vol.67 , pp. 929-935
    • Petit, P.1
  • 4
    • 1542791635 scopus 로고    scopus 로고
    • Structural basis for allosteric regulation of the monomeric allosteric enzyme human glucokinase
    • Kamata, K., Mitsuya, M., Nishimura, T., Eiki, J., and Nagata, Y. (2004) Structural basis for allosteric regulation of the monomeric allosteric enzyme human glucokinase Structure 12, 429-438
    • (2004) Structure , vol.12 , pp. 429-438
    • Kamata, K.1    Mitsuya, M.2    Nishimura, T.3    Eiki, J.4    Nagata, Y.5
  • 5
    • 0025285220 scopus 로고
    • Demonstration of a slow conformational change in liver glucokinase by fluorescence spectroscopy
    • Lin, S. X. and Neet, K. E. (1990) Demonstration of a slow conformational change in liver glucokinase by fluorescence spectroscopy J. Biol. Chem. 265, 9670-9675
    • (1990) J. Biol. Chem. , vol.265 , pp. 9670-9675
    • Lin, S.X.1    Neet, K.E.2
  • 6
    • 67349139275 scopus 로고    scopus 로고
    • Assessing the potential of glucokinase activators in diabetes therapy
    • Matschinsky, F. M. (2009) Assessing the potential of glucokinase activators in diabetes therapy Nat. Rev. Drug Discovery 8, 399-416
    • (2009) Nat. Rev. Drug Discovery , vol.8 , pp. 399-416
    • Matschinsky, F.M.1
  • 7
    • 0024543929 scopus 로고
    • A protein from rat liver confers to glucokinase the property of being antagonistically regulated by fructose 6-phosphate and fructose 1-phosphate
    • Van Schaftingen, E. (1989) A protein from rat liver confers to glucokinase the property of being antagonistically regulated by fructose 6-phosphate and fructose 1-phosphate Eur. J. Biochem. 179, 179-184
    • (1989) Eur. J. Biochem. , vol.179 , pp. 179-184
    • Van Schaftingen, E.1
  • 8
    • 0037041034 scopus 로고    scopus 로고
    • Identification of fructose 6-phosphate- and fructose 1-phosphate-binding residues in the regulatory protein of glucokinase
    • Veiga-da-Cunha, M. and Van Schaftingen, E. (2002) Identification of fructose 6-phosphate- and fructose 1-phosphate-binding residues in the regulatory protein of glucokinase J. Biol. Chem. 277, 8466-8473
    • (2002) J. Biol. Chem. , vol.277 , pp. 8466-8473
    • Veiga-Da-Cunha, M.1    Van Schaftingen, E.2
  • 9
    • 0034931419 scopus 로고    scopus 로고
    • Regulation of hepatic glucose metabolism by translocation of glucokinase between the nucleus and the cytoplasm in hepatocytes
    • Toyoda, Y., Tsuchida, A., Iwami, E., Shironoguchi, H., and Miwa, I. (2001) Regulation of hepatic glucose metabolism by translocation of glucokinase between the nucleus and the cytoplasm in hepatocytes Horm. Metab. Res. 33, 329-336
    • (2001) Horm. Metab. Res. , vol.33 , pp. 329-336
    • Toyoda, Y.1    Tsuchida, A.2    Iwami, E.3    Shironoguchi, H.4    Miwa, I.5
  • 11
    • 0031859694 scopus 로고    scopus 로고
    • Small amounts of fructose markedly augment net hepatic glucose uptake in the conscious dog
    • Shiota, M., Galassetti, P., Monohan, M., Neal, D. W., and Cherrington, A. D. (1998) Small amounts of fructose markedly augment net hepatic glucose uptake in the conscious dog Diabetes 47, 867-873
    • (1998) Diabetes , vol.47 , pp. 867-873
    • Shiota, M.1    Galassetti, P.2    Monohan, M.3    Neal, D.W.4    Cherrington, A.D.5
  • 12
    • 53649083280 scopus 로고    scopus 로고
    • Activation and translocation of glucokinase in rat primary hepatocytes monitored by high content image analysis
    • Wolff, M., Kauschke, S. G., Schmidt, S., and Heilker, R. (2008) Activation and translocation of glucokinase in rat primary hepatocytes monitored by high content image analysis J. Biomol. Screening 13, 837-846
    • (2008) J. Biomol. Screening , vol.13 , pp. 837-846
    • Wolff, M.1    Kauschke, S.G.2    Schmidt, S.3    Heilker, R.4
  • 13
    • 0029918678 scopus 로고    scopus 로고
    • Amino acid conservation in animal glucokinases. Identification of residues implicated in the interaction with the regulatory protein
    • Veiga-da-Cunha, M., Courtois, S., Michel, A., Gosselain, E., and Van Schaftingen, E. (1996) Amino acid conservation in animal glucokinases. Identification of residues implicated in the interaction with the regulatory protein J. Biol. Chem. 271, 6292-6297
    • (1996) J. Biol. Chem. , vol.271 , pp. 6292-6297
    • Veiga-Da-Cunha, M.1    Courtois, S.2    Michel, A.3    Gosselain, E.4    Van Schaftingen, E.5
  • 14
    • 57649133952 scopus 로고    scopus 로고
    • Biophysical characterization of the interaction between hepatic glucokinase and its regulatory protein: Impact of physiological and pharmacological effectors
    • Anderka, O. 2008, Biophysical characterization of the interaction between hepatic glucokinase and its regulatory protein: Impact of physiological and pharmacological effectors J. Biol. Chem. 283, 31333-31340
    • (2008) J. Biol. Chem. , vol.283 , pp. 31333-31340
    • Anderka, O.1
  • 15
    • 1642326708 scopus 로고    scopus 로고
    • Differences in regulatory properties between human and rat glucokinase regulatory protein
    • Brocklehurst, K. J., Davies, R. A., and Agius, L. (2004) Differences in regulatory properties between human and rat glucokinase regulatory protein Biochem. J. 378, 693-697
    • (2004) Biochem. J. , vol.378 , pp. 693-697
    • Brocklehurst, K.J.1    Davies, R.A.2    Agius, L.3
  • 16
    • 0345803934 scopus 로고    scopus 로고
    • Mapping temperature-induced conformational changes in the Escherichia coli heat shock transcription factor sigma 32 by amide hydrogen exchange
    • Rist, W., Jorgensen, T. J., Roepstorff, P., Bukau, B., and Mayer, M. P. (2003) Mapping temperature-induced conformational changes in the Escherichia coli heat shock transcription factor sigma 32 by amide hydrogen exchange J. Biol. Chem. 278, 51415-51421
    • (2003) J. Biol. Chem. , vol.278 , pp. 51415-51421
    • Rist, W.1    Jorgensen, T.J.2    Roepstorff, P.3    Bukau, B.4    Mayer, M.P.5
  • 18
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • Soding, J., Biegert, A., and Lupas, A. N. (2005) The HHpred interactive server for protein homology detection and structure prediction Nucleic Acids Res. 33, W244-W248
    • (2005) Nucleic Acids Res. , vol.33
    • Soding, J.1    Biegert, A.2    Lupas, A.N.3
  • 19
    • 77950793231 scopus 로고    scopus 로고
    • Experimental phasing with SHELXC/D/E: Combining chain tracing with density modification
    • Sheldrick, G. M. (2010) Experimental phasing with SHELXC/D/E: Combining chain tracing with density modification Acta Crystallogr. D66, 479-485
    • (2010) Acta Crystallogr. , vol.66 , pp. 479-485
    • Sheldrick, G.M.1
  • 20
    • 0347383760 scopus 로고    scopus 로고
    • ARP/wARP and automatic interpretation of protein electron density maps
    • Morris, R. J., Perrakis, A., and Lamzin, V. S. (2003) ARP/wARP and automatic interpretation of protein electron density maps Methods Enzymol. 374, 229-244
    • (2003) Methods Enzymol. , vol.374 , pp. 229-244
    • Morris, R.J.1    Perrakis, A.2    Lamzin, V.S.3
  • 21
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. and Cowtan, K. (2004) Coot: Model-building tools for molecular graphics Acta Crystallogr. D60, 2126-2132
    • (2004) Acta Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 22
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • Davis, I. W. 2007, MolProbity: All-atom contacts and structure validation for proteins and nucleic acids Nucleic Acids Res. 35, W375-W383
    • (2007) Nucleic Acids Res. , vol.35
    • Davis, I.W.1
  • 23
    • 0032932006 scopus 로고    scopus 로고
    • The SIS domain: A phosphosugar-binding domain
    • Bateman, A. (1999) The SIS domain: A phosphosugar-binding domain Trends Biochem. Sci. 24, 94-95
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 94-95
    • Bateman, A.1
  • 24
    • 1842555070 scopus 로고    scopus 로고
    • Rational protein crystallization by mutational surface engineering
    • Derewenda, Z. S. (2004) Rational protein crystallization by mutational surface engineering Structure 12, 529-535
    • (2004) Structure , vol.12 , pp. 529-535
    • Derewenda, Z.S.1
  • 25
    • 0032529009 scopus 로고    scopus 로고
    • Involvement of the C terminus in intramolecular nitrogen channeling in glucosamine 6-phosphate synthase: Evidence from a 1.6 Å crystal structure of the isomerase domain
    • Teplyakov, A., Obmolova, G., Badet-Denisot, M. A., Badet, B., and Polikarpov, I. (1998) Involvement of the C terminus in intramolecular nitrogen channeling in glucosamine 6-phosphate synthase: Evidence from a 1.6 Å crystal structure of the isomerase domain Structure 6, 1047-1055
    • (1998) Structure , vol.6 , pp. 1047-1055
    • Teplyakov, A.1    Obmolova, G.2    Badet-Denisot, M.A.3    Badet, B.4    Polikarpov, I.5
  • 26
    • 70350124065 scopus 로고    scopus 로고
    • Evolution of vertebrate glucokinase regulatory protein from a bacterial N-acetylmuramate 6-phosphate etherase
    • Veiga-da-Cunha, M., Sokolova, T., Opperdoes, F., and Van Schaftingen, E. (2009) Evolution of vertebrate glucokinase regulatory protein from a bacterial N-acetylmuramate 6-phosphate etherase Biochem. J. 423, 323-332
    • (2009) Biochem. J. , vol.423 , pp. 323-332
    • Veiga-Da-Cunha, M.1    Sokolova, T.2    Opperdoes, F.3    Van Schaftingen, E.4
  • 27
    • 33845536286 scopus 로고    scopus 로고
    • Glucokinase regulatory network in pancreatic β-cells and liver
    • Baltrusch, S. and Tiedge, M. (2006) Glucokinase regulatory network in pancreatic β-cells and liver Diabetes 55, S55-S64
    • (2006) Diabetes , vol.55
    • Baltrusch, S.1    Tiedge, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.