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Volumn 9, Issue 1, 2014, Pages

Human lactate dehydrogenase A inhibitors: A molecular dynamics investigation

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME INHIBITOR; LACTATE DEHYDROGENASE; LACTATE DEHYDROGENASE A INHIBITOR; LACTATE DEHYDROGENASE ISOENZYME 5; UNCLASSIFIED DRUG;

EID: 84898407135     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0086365     Document Type: Article
Times cited : (36)

References (53)
  • 1
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: The next generation
    • Hanahan D, Weinberg RA (2011) Hallmarks of cancer: the next generation. Cell 144: 646-674.
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 2
    • 84858604270 scopus 로고    scopus 로고
    • Metabolic reprogramming: A cancer hallmark even warburg did not anticipate
    • Ward PS, Thompson CB (2012) Metabolic reprogramming: a cancer hallmark even warburg did not anticipate. Cancer Cell 21: 297-308.
    • (2012) Cancer Cell , vol.21 , pp. 297-308
    • Ward, P.S.1    Thompson, C.B.2
  • 3
    • 0001221508 scopus 로고
    • On respiratory impairment in cancer cells
    • Warburg O (1956) On respiratory impairment in cancer cells. Science 124: 269-270.
    • (1956) Science , vol.124 , pp. 269-270
    • Warburg, O.1
  • 4
    • 8144228566 scopus 로고    scopus 로고
    • Why do cancers have high aerobic glycolysis?
    • DOI 10.1038/nrc1478
    • Gatenby RA, Gillies RJ (2004) Why do cancers have high aerobic glycolysis? Nat Rev Cancer 4: 891-899. (Pubitemid 39472955)
    • (2004) Nature Reviews Cancer , vol.4 , Issue.11 , pp. 891-899
    • Gatenby, R.A.1    Gillies, R.J.2
  • 6
    • 0011858158 scopus 로고
    • Crystalline lactic dehydrogenase from heart muscle
    • Straub FB (1940) Crystalline lactic dehydrogenase from heart muscle. Biochem J 34: 483-486.
    • (1940) Biochem J , vol.34 , pp. 483-486
    • Straub, F.B.1
  • 7
    • 77950643062 scopus 로고    scopus 로고
    • Inhibitors of lactate dehydrogenase isoforms and their therapeutic potentials
    • Granchi C, Bertini S, Macchia M, Minutolo F (2010) Inhibitors of lactate dehydrogenase isoforms and their therapeutic potentials. Curr Med Chem 17: 672-697.
    • (2010) Curr Med Chem , vol.17 , pp. 672-697
    • Granchi, C.1    Bertini, S.2    Macchia, M.3    Minutolo, F.4
  • 8
    • 66449103009 scopus 로고    scopus 로고
    • LDH-A inhibition, a therapeutic strategy for treatment of hereditary leiomyomatosis and renal cell cancer
    • Xie H, Valera VA, Merino MJ, Amato AM, Signoretti S, et al. (2009) LDH-A inhibition, a therapeutic strategy for treatment of hereditary leiomyomatosis and renal cell cancer. Mol Cancer Ther 8: 626-635.
    • (2009) Mol Cancer Ther , vol.8 , pp. 626-635
    • Xie, H.1    Valera, V.A.2    Merino, M.J.3    Amato, A.M.4    Signoretti, S.5
  • 9
    • 76649126249 scopus 로고    scopus 로고
    • Inhibition of lactate dehydrogenase A induces oxidative stress and inhibits tumor progression
    • Le A, Cooper CR, Gouw AM, Dinavahi R, Maitra A, et al. (2010) Inhibition of lactate dehydrogenase A induces oxidative stress and inhibits tumor progression. Proc Natl Acad Sci U S A 107: 2037-2042.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 2037-2042
    • Le, A.1    Cooper, C.R.2    Gouw, A.M.3    Dinavahi, R.4    Maitra, A.5
  • 10
    • 0000384544 scopus 로고
    • Lactic Dehydrogenase in Human Neoplastic Tissues
    • Goldman RD, Kaplan NO, Hall TC (1964) Lactic Dehydrogenase in Human Neoplastic Tissues. Cancer Res 24: 389-399.
    • (1964) Cancer Res , vol.24 , pp. 389-399
    • Goldman, R.D.1    Kaplan, N.O.2    Hall, T.C.3
  • 11
    • 0141730410 scopus 로고    scopus 로고
    • Lactate dehydrogenase-5 (LDH-5) overexpression in non-small-cell lung cancer tissues is linked to tumour hypoxia, angiogenic factor production and poor prognosis
    • DOI 10.1038/sj.bjc.6601205
    • Koukourakis MI, Giatromanolaki A, Sivridis E, Bougioukas G, Didilis V, et al. (2003) Lactate dehydrogenase-5 (LDH-5) overexpression in non-small-cell lung cancer tissues is linked to tumour hypoxia, angiogenic factor production and poor prognosis. Br J Cancer 89: 877-885. (Pubitemid 37175811)
    • (2003) British Journal of Cancer , vol.89 , Issue.5 , pp. 877-885
    • Koukourakis, M.I.1    Giatromanolaki, A.2    Sivridis, E.3    Bougioukas, G.4    Didilis, V.5    Gatter, K.C.6    Harris, A.L.7
  • 12
    • 33749027749 scopus 로고    scopus 로고
    • Lactate dehydrogenase 5 expression in operable colorectal cancer: Strong association with survival and activated vascular endothelial growth factor pathway - A report of the tumour angiogenesis research group
    • DOI 10.1200/JCO.2006.05.9501
    • Koukourakis MI, Giatromanolaki A, Sivridis E, Gatter KC, Harris AL (2006) Lactate dehydrogenase 5 expression in operable colorectal cancer: strong association with survival and activated vascular endothelial growth factor pathway-a report of the Tumour Angiogenesis Research Group. J Clin Oncol 24: 4301-4308. (Pubitemid 46630788)
    • (2006) Journal of Clinical Oncology , vol.24 , Issue.26 , pp. 4301-4308
    • Koukourakis, M.I.1    Giatromanolaki, A.2    Sivridis, E.3    Gatter, K.C.4    Harris, A.L.5
  • 13
    • 48149091757 scopus 로고    scopus 로고
    • Lactate dehydrogenase-5 (LDH-5) expression in human gastric cancer: Association with hypoxia-inducible factor (HIF-1alpha) pathway, angiogenic factors production and poor prognosis
    • Kolev Y, Uetake H, Takagi Y, Sugihara K (2008) Lactate dehydrogenase-5 (LDH-5) expression in human gastric cancer: association with hypoxia-inducible factor (HIF-1alpha) pathway, angiogenic factors production and poor prognosis. Ann Surg Oncol 15: 2336-2344.
    • (2008) Ann Surg Oncol , vol.15 , pp. 2336-2344
    • Kolev, Y.1    Uetake, H.2    Takagi, Y.3    Sugihara, K.4
  • 14
    • 73949089935 scopus 로고    scopus 로고
    • Lactate dehydrogenase 5 expression in melanoma increases with disease progression and is associated with expression of Bcl-XL and Mcl-1, but not Bcl-2 proteins
    • Zhuang L, Scolyer RA, Murali R, McCarthy SW, Zhang XD, et al. (2010) Lactate dehydrogenase 5 expression in melanoma increases with disease progression and is associated with expression of Bcl-XL and Mcl-1, but not Bcl-2 proteins. Mod Pathol 23: 45-53.
    • (2010) Mod Pathol , vol.23 , pp. 45-53
    • Zhuang, L.1    Scolyer, R.A.2    Murali, R.3    McCarthy, S.W.4    Zhang, X.D.5
  • 15
    • 79952806402 scopus 로고    scopus 로고
    • Discovery of N-hydroxyindole-based inhibitors of human lactate dehydrogenase isoform A (LDH-A) as starvation agents against cancer cells
    • Granchi C, Roy S, Giacomelli C, Macchia M, Tuccinardi T, et al. (2011) Discovery of N-hydroxyindole-based inhibitors of human lactate dehydrogenase isoform A (LDH-A) as starvation agents against cancer cells. J Med Chem 54: 1599-1612.
    • (2011) J Med Chem , vol.54 , pp. 1599-1612
    • Granchi, C.1    Roy, S.2    Giacomelli, C.3    Macchia, M.4    Tuccinardi, T.5
  • 16
    • 0023853020 scopus 로고
    • Lactate dehydrogenase M-subunit deficiency: A new type of hereditary exertional myopathy
    • DOI 10.1016/0009-8981(88)90359-2
    • Kanno T, Sudo K, Maekawa M, Nishimura Y, Ukita M, et al. (1988) Lactate dehydrogenase M-subunit deficiency: a new type of hereditary exertional myopathy. Clin Chim Acta 173: 89-98. (Pubitemid 18077508)
    • (1988) Clinica Chimica Acta , vol.173 , Issue.1 , pp. 89-98
    • Kanno, T.1    Sudo, K.2    Maekawa, M.3    Nishimura, Y.4    Ukita, M.5    Fukutake, K.6
  • 17
    • 0035342452 scopus 로고    scopus 로고
    • Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase
    • Read JA, Winter VJ, Eszes CM, Sessions RB, Brady RL (2001) Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase. Proteins 43: 175-185.
    • (2001) Proteins , vol.43 , pp. 175-185
    • Read, J.A.1    Winter, V.J.2    Eszes, C.M.3    Sessions, R.B.4    Brady, R.L.5
  • 18
    • 84859790465 scopus 로고    scopus 로고
    • Design and synthesis of novel lactate dehydrogenase A inhibitors by fragment-based lead generation
    • Ward RA, Brassington C, Breeze AL, Caputo A, Critchlow S, et al. (2012) Design and synthesis of novel lactate dehydrogenase A inhibitors by fragment-based lead generation. J Med Chem 55: 3285-3306.
    • (2012) J Med Chem , vol.55 , pp. 3285-3306
    • Ward, R.A.1    Brassington, C.2    Breeze, A.L.3    Caputo, A.4    Critchlow, S.5
  • 19
    • 84873908263 scopus 로고    scopus 로고
    • Fragment growing and linking lead to novel nanomolar lactate dehydrogenase inhibitors
    • Kohlmann A, Zech SG, Li F, Zhou T, Squillace RM, et al. (2013) Fragment growing and linking lead to novel nanomolar lactate dehydrogenase inhibitors. J Med Chem 56: 1023-1040.
    • (2013) J Med Chem , vol.56 , pp. 1023-1040
    • Kohlmann, A.1    Zech, S.G.2    Li, F.3    Zhou, T.4    Squillace, R.M.5
  • 20
    • 84877579335 scopus 로고    scopus 로고
    • Identification of substituted 2-thio-6-oxo-1,6-dihydropyrimidines as inhibitors of human lactate dehydrogenase
    • Dragovich PS, Fauber BP, Corson LB, Ding CZ, Eigenbrot C, et al. (2013) Identification of substituted 2-thio-6-oxo-1,6-dihydropyrimidines as inhibitors of human lactate dehydrogenase. Bioorg Med Chem Lett 23: 3186-3194.
    • (2013) Bioorg Med Chem Lett , vol.23 , pp. 3186-3194
    • Dragovich, P.S.1    Fauber, B.P.2    Corson, L.B.3    Ding, C.Z.4    Eigenbrot, C.5
  • 21
    • 84884290578 scopus 로고    scopus 로고
    • Identification of 2-amino-5-aryl-pyrazines as inhibitors of human lactate dehydrogenase
    • Fauber BP, Dragovich PS, Chen J, Corson LB, Ding CZ, et al. (2013) Identification of 2-amino-5-aryl-pyrazines as inhibitors of human lactate dehydrogenase. Bioorg Med Chem Lett 23: 5533-5539.
    • (2013) Bioorg Med Chem Lett , vol.23 , pp. 5533-5539
    • Fauber, B.P.1    Dragovich, P.S.2    Chen, J.3    Corson, L.B.4    Ding, C.Z.5
  • 23
    • 23244457509 scopus 로고    scopus 로고
    • The approach to the Michaelis complex in lactate dehydrogenase: The substrate binding pathway
    • DOI 10.1529/biophysj.105.062604
    • McClendon S, Zhadin N, Callender R (2005) The approach to the Michaelis complex in lactate dehydrogenase: the substrate binding pathway. Biophys J 89: 2024-2032. (Pubitemid 41233557)
    • (2005) Biophysical Journal , vol.89 , Issue.3 , pp. 2024-2032
    • McClendon, S.1    Zhadin, N.2    Callender, R.3
  • 25
    • 77952844866 scopus 로고    scopus 로고
    • Single-molecule pulling simulations can discern active from inactive enzyme inhibitors
    • Colizzi F, Perozzo R, Scapozza L, Recanatini M, Cavalli A (2010) Single-molecule pulling simulations can discern active from inactive enzyme inhibitors. J Am Chem Soc 132: 7361-7371.
    • (2010) J Am Chem Soc , vol.132 , pp. 7361-7371
    • Colizzi, F.1    Perozzo, R.2    Scapozza, L.3    Recanatini, M.4    Cavalli, A.5
  • 26
    • 78650686774 scopus 로고    scopus 로고
    • Top leads for swine influenza A/H1N1 virus revealed by steered molecular dynamics approach
    • Mai BK, Viet MH, Li MS (2010) Top leads for swine influenza A/H1N1 virus revealed by steered molecular dynamics approach. J Chem Inf Model 50: 2236-2247.
    • (2010) J Chem Inf Model , vol.50 , pp. 2236-2247
    • Mai, B.K.1    Viet, M.H.2    Li, M.S.3
  • 27
    • 4243754128 scopus 로고    scopus 로고
    • Nonequilibrium Equality for Free Energy Differences
    • Jarzynski C (1997) Nonequilibrium Equality for Free Energy Differences. Phys Rev Lett 78: 2690-2693.
    • (1997) Phys Rev Lett , vol.78 , pp. 2690-2693
    • Jarzynski, C.1
  • 28
    • 4143087050 scopus 로고    scopus 로고
    • Calculating potentials of mean force from steered molecular dynamics simulations
    • Park S, Schulten K (2004) Calculating potentials of mean force from steered molecular dynamics simulations. J Chem Phys 120: 5946-5961.
    • (2004) J Chem Phys , vol.120 , pp. 5946-5961
    • Park, S.1    Schulten, K.2
  • 30
    • 0042885340 scopus 로고    scopus 로고
    • Free energy calculation from steered molecular dynamics simulations using Jarzynski's equality
    • Park S, Araghi F, Tajkhorshid E, Schulten K (2003) Free energy calculation from steered molecular dynamics simulations using Jarzynski's equality. J Chem Phys 119: 3559-3566.
    • (2003) J Chem Phys , vol.119 , pp. 3559-3566
    • Park, S.1    Araghi, F.2    Tajkhorshid, E.3    Schulten, K.4
  • 31
    • 0011152387 scopus 로고    scopus 로고
    • Molecular Dynamics Simulations of L-Lactate Dehydrogenase: Conformation of a Mobile Loop and Influence of the Tetrameric Protein Environment
    • Rebecca KS, Jill EG (1999) Molecular Dynamics Simulations of L-Lactate Dehydrogenase: Conformation of a Mobile Loop and Influence of the Tetrameric Protein Environment. J Mol Model 5: 153-168.
    • (1999) J Mol Model , vol.5 , pp. 153-168
    • Rebecca, K.S.1    Jill, E.G.2
  • 32
    • 77749334410 scopus 로고    scopus 로고
    • Importance of the lactate dehydrogenase quaternary structure in theoretical calculations
    • Swiderek K, Paneth P (2010) Importance of the lactate dehydrogenase quaternary structure in theoretical calculations. J Phys Chem B 114: 3393-3397.
    • (2010) J Phys Chem B , vol.114 , pp. 3393-3397
    • Swiderek, K.1    Paneth, P.2
  • 33
    • 84878939602 scopus 로고    scopus 로고
    • Toward quantitative estimates of binding affinities for protein-ligand systems involving large inhibitor compounds: A steered molecular dynamics simulation route
    • Nicolini P, Frezzato D, Gellini C, Bizzarri M, Chelli R (2013) Toward quantitative estimates of binding affinities for protein-ligand systems involving large inhibitor compounds: a steered molecular dynamics simulation route. J Comput Chem 34: 1561-1576.
    • (2013) J Comput Chem , vol.34 , pp. 1561-1576
    • Nicolini, P.1    Frezzato, D.2    Gellini, C.3    Bizzarri, M.4    Chelli, R.5
  • 34
    • 0342929614 scopus 로고
    • Nonphysical sampling distributions in Monte Carlo free-energy estimation: Umbrella sampling
    • Torrie GM, Valleau JP (1977) Nonphysical sampling distributions in Monte Carlo free-energy estimation: Umbrella sampling. J Comput Phys 23: 187-199.
    • (1977) J Comput Phys , vol.23 , pp. 187-199
    • Torrie, G.M.1    Valleau, J.P.2
  • 35
    • 84865454171 scopus 로고    scopus 로고
    • Theoretical studies of HIV-1 reverse transcriptase inhibition
    • Swiderek K, Marti S, Moliner V (2012) Theoretical studies of HIV-1 reverse transcriptase inhibition. Phys Chem Chem Phys 14: 12614-12624.
    • (2012) Phys Chem Chem Phys , vol.14 , pp. 12614-12624
    • Swiderek, K.1    Marti, S.2    Moliner, V.3
  • 37
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • Trott O, Olson AJ (2010) AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comput Chem 31: 455-461.
    • (2010) J Comput Chem , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 42
    • 79959999377 scopus 로고    scopus 로고
    • R.E.D. Server: A web service for deriving RESP and ESP charges and building force field libraries for new molecules and molecular fragments
    • Vanquelef E, Simon S, Marquant G, Garcia E, Klimerak G, et al. (2011) R.E.D. Server: a web service for deriving RESP and ESP charges and building force field libraries for new molecules and molecular fragments. Nucleic Acids Res 39: W511-517.
    • (2011) Nucleic Acids Res , vol.39
    • Vanquelef, E.1    Simon, S.2    Marquant, G.3    Garcia, E.4    Klimerak, G.5
  • 43
    • 3042524904 scopus 로고
    • A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges: The RESP model
    • Bayly CI, Cieplak P, Cornell W, Kollman PA (1993) A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges: the RESP model. The J Phys Chem 97: 10269-10280.
    • (1993) The J Phys Chem , vol.97 , pp. 10269-10280
    • Bayly, C.I.1    Cieplak, P.2    Cornell, W.3    Kollman, P.A.4
  • 44
    • 84986516411 scopus 로고
    • Application of the multimolecule and multiconformational RESP methodology to biopolymers: Charge derivation for DNA, RNA, and proteins
    • Cieplak P, Cornell WD, Bayly C, Kollman PA (1995) Application of the multimolecule and multiconformational RESP methodology to biopolymers: Charge derivation for DNA, RNA, and proteins. J Comput Chem 16: 1357-1377.
    • (1995) J Comput Chem , vol.16 , pp. 1357-1377
    • Cieplak, P.1    Cornell, W.D.2    Bayly, C.3    Kollman, P.A.4
  • 45
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
    • Hess B, Kutzner C, van der Spoel D, Lindahl E (2008) GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation. J Chem Theory Comput 4: 435-447.
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 46
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N [center-dot] log(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L (1993) Particle mesh Ewald: An N [center-dot] log(N) method for Ewald sums in large systems. J Chem Phys 98: 10089-10092.
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 48
    • 33846086933 scopus 로고    scopus 로고
    • Canonical sampling through velocity rescaling
    • Bussi G, Donadio D, Parrinello M (2007) Canonical sampling through velocity rescaling. J Chem Phys 126: 014101.
    • (2007) J Chem Phys , vol.126 , pp. 014101
    • Bussi, G.1    Donadio, D.2    Parrinello, M.3
  • 50
    • 38749123962 scopus 로고    scopus 로고
    • P-LINCS: A Parallel Linear Constraint Solver for Molecular Simulation
    • Hess B (2007) P-LINCS: A Parallel Linear Constraint Solver for Molecular Simulation. Chem Theory Comput 4: 116-122.
    • (2007) Chem Theory Comput , vol.4 , pp. 116-122
    • Hess, B.1
  • 51
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • Hoover WG (1985) Canonical dynamics: Equilibrium phase-space distributions. Phys Rev A 31: 1695-1697.
    • (1985) Phys Rev A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 52
    • 0019707626 scopus 로고
    • POLYMORPHIC TRANSITIONS IN SINGLE CRYSTALS: A NEW MOLECULAR DYNAMICS METHOD
    • DOI 10.1063/1.328693
    • Parrinello M, Rahman A (1981) Polymorphic transitions in single crystals: A new molecular dynamics method. J Appl Phys 52: 7182-7190. (Pubitemid 12456820)
    • (1981) Journal of Applied Physics , vol.52 , Issue.12 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 53
    • 0030590866 scopus 로고    scopus 로고
    • Removal of substrate inhibition in a lactate dehydrogenase from human muscle by a single residue change
    • DOI 10.1016/S0014-5793(96)01317-8, PII S0014579396013178
    • Eszes CM, Sessions RB, Clarke AR, Moreton KM, Holbrook JJ (1996) Removal of substrate inhibition in a lactate dehydrogenase from human muscle by a single residue change. FEBS Lett 399: 193-197. (Pubitemid 26426847)
    • (1996) FEBS Letters , vol.399 , Issue.3 , pp. 193-197
    • Eszes, C.M.1    Sessions, R.B.2    Clarke, A.R.3    Moreton, K.M.4    Holbrook, J.J.5


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