메뉴 건너뛰기




Volumn 18, Issue 1, 2014, Pages 23-29

Allostery and compartmentalization: Old but not forgotten

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL COENZYME A; ADENOSINE TRIPHOSPHATE; CHEMOKINE RECEPTOR CCR5; DNA BINDING PROTEIN; EFAVIRENZ; G PROTEIN COUPLED RECEPTOR; MARAVIROC; PHOSPHOGLYCERATE DEHYDROGENASE; TUBERCULOSTATIC AGENT;

EID: 84896753299     PISSN: 13695274     EISSN: 18790364     Source Type: Journal    
DOI: 10.1016/j.mib.2014.01.007     Document Type: Review
Times cited : (4)

References (57)
  • 1
    • 73649152457 scopus 로고
    • Allosteric proteins and cellular control systems
    • Monod J., Changeux J.P., Jacob F. Allosteric proteins and cellular control systems. J Mol Biol 1963, 6:306-329.
    • (1963) J Mol Biol , vol.6 , pp. 306-329
    • Monod, J.1    Changeux, J.P.2    Jacob, F.3
  • 3
    • 84861219631 scopus 로고    scopus 로고
    • Allostery and the Monod-Wyman-Changeux model after 50 years
    • Changeux J.P. Allostery and the Monod-Wyman-Changeux model after 50 years. Annu Rev Biophys 2012, 41:103-133.
    • (2012) Annu Rev Biophys , vol.41 , pp. 103-133
    • Changeux, J.P.1
  • 6
    • 61849182514 scopus 로고    scopus 로고
    • Taming tuberculosis: a challenge for science and society
    • Nathan C. Taming tuberculosis: a challenge for science and society. Cell Host Microbe 2009, 5:220-224.
    • (2009) Cell Host Microbe , vol.5 , pp. 220-224
    • Nathan, C.1
  • 8
    • 77952356637 scopus 로고    scopus 로고
    • Tuberculosis: what we don't know can, and does, hurt us
    • Russell D.G., Barry C.E., Flynn J.L. Tuberculosis: what we don't know can, and does, hurt us. Science 2010, 328:852-856.
    • (2010) Science , vol.328 , pp. 852-856
    • Russell, D.G.1    Barry, C.E.2    Flynn, J.L.3
  • 9
    • 84876275408 scopus 로고    scopus 로고
    • The underappreciated role of allostery in the cellular network
    • Nussinov R., Tsai C.J., Ma B. The underappreciated role of allostery in the cellular network. Annu Rev Biophys 2013, 42:169-189.
    • (2013) Annu Rev Biophys , vol.42 , pp. 169-189
    • Nussinov, R.1    Tsai, C.J.2    Ma, B.3
  • 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 2005, 1:15-25.
    • (2005) Cell Metab , vol.1 , pp. 15-25
    • Kahn, B.B.1    Alquier, T.2    Carling, D.3    Hardie, D.G.4
  • 12
    • 84884629488 scopus 로고    scopus 로고
    • How does hemoglobin generate such diverse functionality of physiological relevance?
    • Yonetani T., Kanaori K. How does hemoglobin generate such diverse functionality of physiological relevance?. Biochim Biophys Acta 2013, 1834:1873-1884.
    • (2013) Biochim Biophys Acta , vol.1834 , pp. 1873-1884
    • Yonetani, T.1    Kanaori, K.2
  • 13
    • 84876266689 scopus 로고    scopus 로고
    • Allostery in disease and in drug discovery
    • Nussinov R., Tsai C.J. Allostery in disease and in drug discovery. Cell 2013, 153:293-305.
    • (2013) Cell , vol.153 , pp. 293-305
    • Nussinov, R.1    Tsai, C.J.2
  • 14
    • 0032441604 scopus 로고    scopus 로고
    • Efavirenz
    • discussion 1065-1066
    • Adkins J.C., Noble S. Efavirenz. Drugs 1998, 56:1055-1064. discussion 1065-1066.
    • (1998) Drugs , vol.56 , pp. 1055-1064
    • Adkins, J.C.1    Noble, S.2
  • 15
    • 78650147139 scopus 로고    scopus 로고
    • Allostery at G protein-coupled receptor homo- and heteromers: uncharted pharmacological landscapes
    • Smith N.J., Milligan G. Allostery at G protein-coupled receptor homo- and heteromers: uncharted pharmacological landscapes. Pharmacol Rev 2010, 62:701-725.
    • (2010) Pharmacol Rev , vol.62 , pp. 701-725
    • Smith, N.J.1    Milligan, G.2
  • 16
    • 79953213637 scopus 로고    scopus 로고
    • 'Molecular switches' on mGluR allosteric ligands that modulate modes of pharmacology
    • Wood M.R., Hopkins C.R., Brogan J.T., Conn P.J., Lindsley C.W. 'Molecular switches' on mGluR allosteric ligands that modulate modes of pharmacology. Biochemistry 2011, 50:2403-2410.
    • (2011) Biochemistry , vol.50 , pp. 2403-2410
    • Wood, M.R.1    Hopkins, C.R.2    Brogan, J.T.3    Conn, P.J.4    Lindsley, C.W.5
  • 17
    • 11144250804 scopus 로고    scopus 로고
    • Tuberculosis - metabolism and respiration in the absence of growth
    • Boshoff H.I., Barry C.E. Tuberculosis - metabolism and respiration in the absence of growth. Nat Rev Microbiol 2005, 3:70-80.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 70-80
    • Boshoff, H.I.1    Barry, C.E.2
  • 18
  • 19
    • 0029976980 scopus 로고    scopus 로고
    • An in vitro model for sequential study of shiftdown of Mycobacterium tuberculosis through two stages of nonreplicating persistence
    • Wayne L.G., Hayes L.G. An in vitro model for sequential study of shiftdown of Mycobacterium tuberculosis through two stages of nonreplicating persistence. Infect Immun 1996, 64:2062-2069.
    • (1996) Infect Immun , vol.64 , pp. 2062-2069
    • Wayne, L.G.1    Hayes, L.G.2
  • 20
    • 50149113470 scopus 로고    scopus 로고
    • The protonmotive force is required for maintaining ATP homeostasis and viability of hypoxic, nonreplicating Mycobacterium tuberculosis
    • Rao S.P., Alonso S., Rand L., Dick T., Pethe K. The protonmotive force is required for maintaining ATP homeostasis and viability of hypoxic, nonreplicating Mycobacterium tuberculosis. Proc Natl Acad Sci U S A 2008, 105:11945-11950.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 11945-11950
    • Rao, S.P.1    Alonso, S.2    Rand, L.3    Dick, T.4    Pethe, K.5
  • 22
    • 84857881099 scopus 로고    scopus 로고
    • Contrasting catalytic and allosteric mechanisms for phosphoglycerate dehydrogenases
    • Grant G.A. Contrasting catalytic and allosteric mechanisms for phosphoglycerate dehydrogenases. Arch Biochem Biophys 2012, 519:175-185.
    • (2012) Arch Biochem Biophys , vol.519 , pp. 175-185
    • Grant, G.A.1
  • 23
    • 66649133096 scopus 로고    scopus 로고
    • Role of the anion-binding site in catalysis and regulation of Mycobacterium tuberculosis d-3-phosphoglycerate dehydrogenase
    • Burton R.L., Chen S., Xu X.L., Grant G.A. Role of the anion-binding site in catalysis and regulation of Mycobacterium tuberculosis d-3-phosphoglycerate dehydrogenase. Biochemistry 2009, 48:4808-4815.
    • (2009) Biochemistry , vol.48 , pp. 4808-4815
    • Burton, R.L.1    Chen, S.2    Xu, X.L.3    Grant, G.A.4
  • 24
    • 35748973899 scopus 로고    scopus 로고
    • A novel mechanism for substrate inhibition in Mycobacterium tuberculosis d-3-phosphoglycerate dehydrogenase
    • Burton R.L., Chen S., Xu X.L., Grant G.A. A novel mechanism for substrate inhibition in Mycobacterium tuberculosis d-3-phosphoglycerate dehydrogenase. J Biol Chem 2007, 282:31517-31524.
    • (2007) J Biol Chem , vol.282 , pp. 31517-31524
    • Burton, R.L.1    Chen, S.2    Xu, X.L.3    Grant, G.A.4
  • 25
    • 0025581736 scopus 로고
    • The shikimate pathway-a metabolic tree with many branches
    • Bentley R. The shikimate pathway-a metabolic tree with many branches. Crit Rev Biochem Mol Biol 1990, 25:307-384.
    • (1990) Crit Rev Biochem Mol Biol , vol.25 , pp. 307-384
    • Bentley, R.1
  • 26
    • 0017103437 scopus 로고
    • Constitutive and repressivle enzymes of the common pathway of aromatic biosynthesis in Escherichia coli K-12: regulation of enzyme synthesis at different growth rates
    • Tribe D.E., Camakaris H., Pittard J. Constitutive and repressivle enzymes of the common pathway of aromatic biosynthesis in Escherichia coli K-12: regulation of enzyme synthesis at different growth rates. J Bacteriol 1976, 127:1085-1097.
    • (1976) J Bacteriol , vol.127 , pp. 1085-1097
    • Tribe, D.E.1    Camakaris, H.2    Pittard, J.3
  • 27
    • 0015503828 scopus 로고
    • The separation of three allosterically inhibitable 3-deoxy-d-arabino-heptulosonate 7-phosphate synthases from extracts of Neurospora crassa and the purification of the tyrosine inhibitable isoenzyme
    • Hoffmann P.J., Doy C.H., Catcheside D.E. The separation of three allosterically inhibitable 3-deoxy-d-arabino-heptulosonate 7-phosphate synthases from extracts of Neurospora crassa and the purification of the tyrosine inhibitable isoenzyme. Biochim Biophys Acta 1972, 268:550-561.
    • (1972) Biochim Biophys Acta , vol.268 , pp. 550-561
    • Hoffmann, P.J.1    Doy, C.H.2    Catcheside, D.E.3
  • 29
    • 84876409727 scopus 로고    scopus 로고
    • Three sites and you are out: ternary synergistic allostery controls aromatic amino acid biosynthesis in Mycobacterium tuberculosis
    • Blackmore N.J., Reichau S., Jiao W., Hutton R.D., Baker E.N., Jameson G.B., Parker E.J. Three sites and you are out: ternary synergistic allostery controls aromatic amino acid biosynthesis in Mycobacterium tuberculosis. J Mol Biol 2013, 425:1582-1592.
    • (2013) J Mol Biol , vol.425 , pp. 1582-1592
    • Blackmore, N.J.1    Reichau, S.2    Jiao, W.3    Hutton, R.D.4    Baker, E.N.5    Jameson, G.B.6    Parker, E.J.7
  • 30
    • 77957276754 scopus 로고    scopus 로고
    • Synergistic allostery, a sophisticated regulatory network for the control of aromatic amino acid biosynthesis in Mycobacterium tuberculosis
    • Webby C.J., Jiao W., Hutton R.D., Blackmore N.J., Baker H.M., Baker E.N., Jameson G.B., Parker E.J. Synergistic allostery, a sophisticated regulatory network for the control of aromatic amino acid biosynthesis in Mycobacterium tuberculosis. J Biol Chem 2010, 285:30567-30576.
    • (2010) J Biol Chem , vol.285 , pp. 30567-30576
    • Webby, C.J.1    Jiao, W.2    Hutton, R.D.3    Blackmore, N.J.4    Baker, H.M.5    Baker, E.N.6    Jameson, G.B.7    Parker, E.J.8
  • 31
    • 77950961726 scopus 로고    scopus 로고
    • Activity-based metabolomic profiling of enzymatic function: identification of Rv1248c as a mycobacterial 2-hydroxy-3-oxoadipate synthase
    • de Carvalho L.P., Zhao H., Dickinson C.E., Arango N.M., Lima C.D., Fischer S.M., Ouerfelli O., Nathan C., Rhee K.Y. Activity-based metabolomic profiling of enzymatic function: identification of Rv1248c as a mycobacterial 2-hydroxy-3-oxoadipate synthase. Chem Biol 2010, 17:323-332.
    • (2010) Chem Biol , vol.17 , pp. 323-332
    • de Carvalho, L.P.1    Zhao, H.2    Dickinson, C.E.3    Arango, N.M.4    Lima, C.D.5    Fischer, S.M.6    Ouerfelli, O.7    Nathan, C.8    Rhee, K.Y.9
  • 32
    • 80052174382 scopus 로고    scopus 로고
    • Functional plasticity and allosteric regulation of alpha-ketoglutarate decarboxylase in central mycobacterial metabolism
    • Wagner T., Bellinzoni M., Wehenkel A., O'Hare H.M., Alzari P.M. Functional plasticity and allosteric regulation of alpha-ketoglutarate decarboxylase in central mycobacterial metabolism. Chem Biol 2011, 18:1011-1020.
    • (2011) Chem Biol , vol.18 , pp. 1011-1020
    • Wagner, T.1    Bellinzoni, M.2    Wehenkel, A.3    O'Hare, H.M.4    Alzari, P.M.5
  • 33
    • 84881234530 scopus 로고    scopus 로고
    • Influence of allosteric regulators on individual steps in the reaction catalyzed by Mycobacterium tuberculosis 2-hydroxy-3-oxoadipate synthase
    • Balakrishnan A., Jordan F., Nathan C.F. Influence of allosteric regulators on individual steps in the reaction catalyzed by Mycobacterium tuberculosis 2-hydroxy-3-oxoadipate synthase. J Biol Chem 2013, 288:21688-21702.
    • (2013) J Biol Chem , vol.288 , pp. 21688-21702
    • Balakrishnan, A.1    Jordan, F.2    Nathan, C.F.3
  • 35
    • 20744445530 scopus 로고    scopus 로고
    • Proteomic identification of M. tuberculosis protein kinase substrates: PknB recruits GarA, a FHA domain-containing protein, through activation loop-mediated interactions
    • Villarino A., Duran R., Wehenkel A., Fernandez P., England P., Brodin P., Cole S.T., Zimny-Arndt U., Jungblut P.R., Cervenansky C., et al. Proteomic identification of M. tuberculosis protein kinase substrates: PknB recruits GarA, a FHA domain-containing protein, through activation loop-mediated interactions. J Mol Biol 2005, 350:953-963.
    • (2005) J Mol Biol , vol.350 , pp. 953-963
    • Villarino, A.1    Duran, R.2    Wehenkel, A.3    Fernandez, P.4    England, P.5    Brodin, P.6    Cole, S.T.7    Zimny-Arndt, U.8    Jungblut, P.R.9    Cervenansky, C.10
  • 36
    • 0022555851 scopus 로고
    • Bacterial periplasmic transport systems: structure, mechanism, and evolution
    • Ames G.F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu Rev Biochem 1986, 55:397-425.
    • (1986) Annu Rev Biochem , vol.55 , pp. 397-425
    • Ames, G.F.1
  • 37
    • 84889604825 scopus 로고    scopus 로고
    • Biogenesis of a bacterial organelle: the carboxysome assembly pathway
    • Cameron J.C., Wilson S.C., Bernstein S.L., Kerfeld C.A. Biogenesis of a bacterial organelle: the carboxysome assembly pathway. Cell 2013, 155:1131-1140.
    • (2013) Cell , vol.155 , pp. 1131-1140
    • Cameron, J.C.1    Wilson, S.C.2    Bernstein, S.L.3    Kerfeld, C.A.4
  • 38
    • 0033991699 scopus 로고    scopus 로고
    • Macromolecular compartmentation and channeling
    • Ovadi J., Srere P.A. Macromolecular compartmentation and channeling. Int Rev Cytol 2000, 192:255-280.
    • (2000) Int Rev Cytol , vol.192 , pp. 255-280
    • Ovadi, J.1    Srere, P.A.2
  • 39
    • 0032491445 scopus 로고    scopus 로고
    • Interaction between citrate synthase and malate dehydrogenase. Substrate channeling of oxaloacetate
    • Morgunov I., Srere P.A. Interaction between citrate synthase and malate dehydrogenase. Substrate channeling of oxaloacetate. J Biol Chem 1998, 273:29540-29544.
    • (1998) J Biol Chem , vol.273 , pp. 29540-29544
    • Morgunov, I.1    Srere, P.A.2
  • 40
    • 0025359442 scopus 로고
    • Enzyme-enzyme interactions and their metabolic role
    • Srere P.A., Ovadi J. Enzyme-enzyme interactions and their metabolic role. FEBS Lett 1990, 268:360-364.
    • (1990) FEBS Lett , vol.268 , pp. 360-364
    • Srere, P.A.1    Ovadi, J.2
  • 41
    • 0025778722 scopus 로고
    • Channeling: the pathway that cannot be beaten
    • Srere P.A. Channeling: the pathway that cannot be beaten. J Theor Biol 1991, 152:23.
    • (1991) J Theor Biol , vol.152 , pp. 23
    • Srere, P.A.1
  • 44
    • 40849118255 scopus 로고    scopus 로고
    • Bacterial growth and cell division: a mycobacterial perspective
    • table of contents
    • Hett E.C., Rubin E.J. Bacterial growth and cell division: a mycobacterial perspective. Microbiol Mol Biol Rev 2008, 72:126-156. table of contents.
    • (2008) Microbiol Mol Biol Rev , vol.72 , pp. 126-156
    • Hett, E.C.1    Rubin, E.J.2
  • 46
    • 33745505203 scopus 로고    scopus 로고
    • Foundations of antibiotic resistance in bacterial physiology: the mycobacterial paradigm
    • Nguyen L., Thompson C.J. Foundations of antibiotic resistance in bacterial physiology: the mycobacterial paradigm. Trends Microbiol 2006, 14:304-312.
    • (2006) Trends Microbiol , vol.14 , pp. 304-312
    • Nguyen, L.1    Thompson, C.J.2
  • 48
    • 33646937005 scopus 로고    scopus 로고
    • Interaction between polyketide synthase and transporter suggests coupled synthesis and export of virulence lipid in M. tuberculosis
    • Jain M., Cox J.S. Interaction between polyketide synthase and transporter suggests coupled synthesis and export of virulence lipid in M. tuberculosis. PLoS Pathog 2005, 1:e2.
    • (2005) PLoS Pathog , vol.1
    • Jain, M.1    Cox, J.S.2
  • 49
    • 0031813213 scopus 로고    scopus 로고
    • Identification and characterization of a 29-kilodalton protein from Mycobacterium tuberculosis culture filtrate recognized by mouse memory effector cells
    • Rosenkrands I., Rasmussen P.B., Carnio M., Jacobsen S., Theisen M., Andersen P. Identification and characterization of a 29-kilodalton protein from Mycobacterium tuberculosis culture filtrate recognized by mouse memory effector cells. Infect Immun 1998, 66:2728-2735.
    • (1998) Infect Immun , vol.66 , pp. 2728-2735
    • Rosenkrands, I.1    Rasmussen, P.B.2    Carnio, M.3    Jacobsen, S.4    Theisen, M.5    Andersen, P.6
  • 51
    • 74849140487 scopus 로고    scopus 로고
    • Structure and mechanisms of a protein-based organelle in Escherichia coli
    • Tanaka S., Sawaya M.R., Yeates T.O. Structure and mechanisms of a protein-based organelle in Escherichia coli. Science 2010, 327:81-84.
    • (2010) Science , vol.327 , pp. 81-84
    • Tanaka, S.1    Sawaya, M.R.2    Yeates, T.O.3
  • 53
    • 84883333320 scopus 로고    scopus 로고
    • The bacterial carbon-fixing organelle is formed by shell envelopment of preassembled cargo
    • Chen A.H., Robinson-Mosher A., Savage D.F., Silver P.A., Polka J.K. The bacterial carbon-fixing organelle is formed by shell envelopment of preassembled cargo. PLoS ONE 2013, 8:e76127.
    • (2013) PLoS ONE , vol.8
    • Chen, A.H.1    Robinson-Mosher, A.2    Savage, D.F.3    Silver, P.A.4    Polka, J.K.5
  • 55
    • 78049411009 scopus 로고    scopus 로고
    • Metabolomics of Mycobacterium tuberculosis reveals compartmentalized co-catabolism of carbon substrates
    • de Carvalho L.P., Fischer S.M., Marrero J., Nathan C., Ehrt S., Rhee K.Y. Metabolomics of Mycobacterium tuberculosis reveals compartmentalized co-catabolism of carbon substrates. Chem Biol 2010, 17:1122-1131.
    • (2010) Chem Biol , vol.17 , pp. 1122-1131
    • de Carvalho, L.P.1    Fischer, S.M.2    Marrero, J.3    Nathan, C.4    Ehrt, S.5    Rhee, K.Y.6
  • 57
    • 84856814983 scopus 로고    scopus 로고
    • Revealing the allosterome: systematic identification of metabolite-protein interactions
    • Orsak T., Smith T.L., Eckert D., Lindsley J.E., Borges C.R., Rutter J. Revealing the allosterome: systematic identification of metabolite-protein interactions. Biochemistry 2012, 51:225-232.
    • (2012) Biochemistry , vol.51 , pp. 225-232
    • Orsak, T.1    Smith, T.L.2    Eckert, D.3    Lindsley, J.E.4    Borges, C.R.5    Rutter, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.