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Volumn 1838, Issue 6, 2014, Pages 1594-1618

Plasma membranes as heat stress sensors: From lipid-controlled molecular switches to therapeutic applications

(22)  Vigh, László a,a   Török, Zsolt a   Crul, Tim a   Maresca, Bruno b   Schütz, Gerhard J c   Viana, Felix d   Dindia, Laura e   Piotto, Stefano b   Brameshuber, Mario c   Balogh, Gábor a   Péter, Mária a   Porta, Amalia b   Trapani, Alfonso b   Gombos, Imre a   Glatz, Attila a   Gungor, Burcin a   Peksel, Begüm a   Csoboz, Bálint a   Horváth, Ibolya a   Vijayan, Mathilakath M e,f   more..


Author keywords

Cell to cell heterogeneity; Heat shock response; Lipid raft; Lipidomics; Membrane lipid therapy; Stress hormone; TRP channel

Indexed keywords

BENZYL ALCOHOL; CHAPERONE; GLUCOCORTICOID; HEAT SHOCK PROTEIN 70; HEAT SHOCK TRANSCRIPTION FACTOR 1; HEME OXYGENASE 1; HYDROXAMIC ACID; LIPID; STRESS HORMONE; TEPRENONE; THIOCTIC ACID; TRANSIENT RECEPTOR POTENTIAL CHANNEL;

EID: 84899420778     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2013.12.015     Document Type: Review
Times cited : (104)

References (349)
  • 1
    • 15544377794 scopus 로고    scopus 로고
    • Molecular and evolutionary basis of the cellular stress response
    • D. Kultz Molecular and evolutionary basis of the cellular stress response Annu. Rev. Physiol. 67 2005 225
    • (2005) Annu. Rev. Physiol. , vol.67 , pp. 225
    • Kultz, D.1
  • 4
    • 34547190663 scopus 로고    scopus 로고
    • Can the stress protein response be controlled by 'membrane-lipid therapy'?
    • L. Vigh, I. Horvath, B. Maresca, and J.L. Harwood Can the stress protein response be controlled by 'membrane-lipid therapy'? Trends Biochem. Sci. 32 2007 357
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 357
    • Vigh, L.1    Horvath, I.2    Maresca, B.3    Harwood, J.L.4
  • 5
    • 0031786750 scopus 로고    scopus 로고
    • Does the membrane's physical state control the expression of heat shock and other genes?
    • L. Vigh, B. Maresca, and J.L. Harwood Does the membrane's physical state control the expression of heat shock and other genes? Trends Biochem. Sci. 23 1998 369
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 369
    • Vigh, L.1    Maresca, B.2    Harwood, J.L.3
  • 7
    • 84877580262 scopus 로고    scopus 로고
    • Structure and dynamics of molecular networks: A novel paradigm of drug discovery: A comprehensive review
    • P. Csermely, T. Korcsmaros, H.J. Kiss, G. London, and R. Nussinov Structure and dynamics of molecular networks: a novel paradigm of drug discovery: a comprehensive review Pharmacol. Ther. 138 2013 333
    • (2013) Pharmacol. Ther. , vol.138 , pp. 333
    • Csermely, P.1    Korcsmaros, T.2    Kiss, H.J.3    London, G.4    Nussinov, R.5
  • 10
    • 0030398406 scopus 로고    scopus 로고
    • Local stoichiometries determined by counting individual molecules
    • T. Schmidt, G.J. Schutz, H.J. Gruber, and H. Schindler Local stoichiometries determined by counting individual molecules Anal. Chem. 68 1996 4397
    • (1996) Anal. Chem. , vol.68 , pp. 4397
    • Schmidt, T.1    Schutz, G.J.2    Gruber, H.J.3    Schindler, H.4
  • 12
    • 84856458463 scopus 로고    scopus 로고
    • Detection and quantification of biomolecular association in living cells using single-molecule microscopy, Methods in enzymology
    • M. Brameshuber and G.J. Schutz, Detection and quantification of biomolecular association in living cells using single-molecule microscopy, methods in enzymology, vol 505: imaging and spectroscopic analysis of living cells 505 (2012) 159.
    • (2012) Imaging and Spectroscopic Analysis of Living Cells 505 , vol.505 , pp. 159
    • Brameshuber, M.1    Schutz, G.J.2
  • 14
    • 0037947831 scopus 로고    scopus 로고
    • Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors
    • L.J. Foster, C.L. de Hoog, and M. Mann Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors Proc. Natl. Acad. Sci. U. S. A. 100 2003 5813
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 5813
    • Foster, L.J.1    De Hoog, C.L.2    Mann, M.3
  • 15
    • 0035433580 scopus 로고    scopus 로고
    • Mass spectrometric characterization of proteins extracted from Jurkat T cell detergent-resistant membrane domains
    • P.D. von Haller, S. Donohoe, D.R. Goodlett, R. Aebersold, and J.D. Watts Mass spectrometric characterization of proteins extracted from Jurkat T cell detergent-resistant membrane domains Proteomics 1 2001 1010
    • (2001) Proteomics , vol.1 , pp. 1010
    • Von Haller, P.D.1    Donohoe, S.2    Goodlett, D.R.3    Aebersold, R.4    Watts, J.D.5
  • 16
    • 0026352248 scopus 로고
    • GPI-anchored cell-surface molecules complexed to protein tyrosine kinases
    • I. Stefanova, V. Horejsi, I.J. Ansotegui, W. Knapp, and H. Stockinger GPI-anchored cell-surface molecules complexed to protein tyrosine kinases Science 254 1991 1016
    • (1991) Science , vol.254 , pp. 1016
    • Stefanova, I.1    Horejsi, V.2    Ansotegui, I.J.3    Knapp, W.4    Stockinger, H.5
  • 17
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell-surface
    • D.A. Brown, and J.K. Rose Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell-surface Cell 68 1992 533
    • (1992) Cell , vol.68 , pp. 533
    • Brown, D.A.1    Rose, J.K.2
  • 18
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • K. Simons, and E. Ikonen Functional rafts in cell membranes Nature 387 1997 569
    • (1997) Nature , vol.387 , pp. 569
    • Simons, K.1    Ikonen, E.2
  • 19
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • D.A. Zacharias, J.D. Violin, A.C. Newton, and R.Y. Tsien Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells Science 296 2002 913
    • (2002) Science , vol.296 , pp. 913
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 21
    • 78651247184 scopus 로고    scopus 로고
    • Near-critical fluctuations and cytoskeleton-assisted phase separation lead to subdiffusion in cell membranes
    • J. Ehrig, E.P. Petrov, and P. Schwille Near-critical fluctuations and cytoskeleton-assisted phase separation lead to subdiffusion in cell membranes Biophys. J. 100 2011 80
    • (2011) Biophys. J. , vol.100 , pp. 80
    • Ehrig, J.1    Petrov, E.P.2    Schwille, P.3
  • 23
    • 79959655729 scopus 로고    scopus 로고
    • Minimal model of plasma membrane heterogeneity requires coupling cortical actin to criticality
    • B.B. Machta, S. Papanikolaou, J.P. Sethna, and S.L. Veatch Minimal model of plasma membrane heterogeneity requires coupling cortical actin to criticality Biophys. J. 100 2011 1668
    • (2011) Biophys. J. , vol.100 , pp. 1668
    • Machta, B.B.1    Papanikolaou, S.2    Sethna, J.P.3    Veatch, S.L.4
  • 24
    • 84861991991 scopus 로고    scopus 로고
    • Active remodeling of cortical actin regulates spatiotemporal organization of cell surface molecules
    • K. Gowrishankar, S. Ghosh, S. Saha, R.C. Mayor, and M. Rao Active remodeling of cortical actin regulates spatiotemporal organization of cell surface molecules Cell 149 2012 1353
    • (2012) Cell , vol.149 , pp. 1353
    • Gowrishankar, K.1    Ghosh, S.2    Saha, S.3    Mayor, R.C.4    Rao, M.5
  • 26
    • 0028808338 scopus 로고
    • Diffusion influenced binary reactive processes in membranes involving identical particles: A Monte Carlo study
    • S. Bergling Diffusion influenced binary reactive processes in membranes involving identical particles: a Monte Carlo study Biophys. Chem. 56 1995 227
    • (1995) Biophys. Chem. , vol.56 , pp. 227
    • Bergling, S.1
  • 28
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • G.I. Bell Models for the specific adhesion of cells to cells Science 200 1978 618
    • (1978) Science , vol.200 , pp. 618
    • Bell, G.I.1
  • 30
    • 33744797629 scopus 로고    scopus 로고
    • Coexisting domains in the plasma membranes of live cells characterized by spin-label ESR spectroscopy
    • M.J. Swamy, L. Ciani, M. Ge, A.K. Smith, D. Holowka, B. Baird, and J.H. Freed Coexisting domains in the plasma membranes of live cells characterized by spin-label ESR spectroscopy Biophys. J. 90 2006 4452
    • (2006) Biophys. J. , vol.90 , pp. 4452
    • Swamy, M.J.1    Ciani, L.2    Ge, M.3    Smith, A.K.4    Holowka, D.5    Baird, B.6    Freed, J.H.7
  • 31
    • 84871789466 scopus 로고    scopus 로고
    • Sub-resolution lipid domains exist in the plasma membrane and regulate protein diffusion and distribution
    • D.M. Owen, D.J. Williamson, A. Magenau, and K. Gaus Sub-resolution lipid domains exist in the plasma membrane and regulate protein diffusion and distribution Nat. Commun. 3 2012 1256
    • (2012) Nat. Commun. , vol.3 , pp. 1256
    • Owen, D.M.1    Williamson, D.J.2    Magenau, A.3    Gaus, K.4
  • 32
    • 84876490935 scopus 로고    scopus 로고
    • Colocalization of the ganglioside G(M1) and cholesterol detected by secondary ion mass spectrometry
    • M.M. Lozano, Z. Liu, E. Sunnick, A. Janshoff, K. Kumar, and S.G. Boxer Colocalization of the ganglioside G(M1) and cholesterol detected by secondary ion mass spectrometry J. Am. Chem. Soc. 135 2013 5620
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 5620
    • Lozano, M.M.1    Liu, Z.2    Sunnick, E.3    Janshoff, A.4    Kumar, K.5    Boxer, S.G.6
  • 34
    • 33644875032 scopus 로고    scopus 로고
    • The TRP superfamily of cation channels
    • C. Montell The TRP superfamily of cation channels Sci. STKE 2005 2005 re3
    • (2005) Sci. STKE , vol.2005 , pp. 3
    • Montell, C.1
  • 36
    • 0347504835 scopus 로고    scopus 로고
    • TRP channels as cellular sensors
    • D.E. Clapham TRP channels as cellular sensors Nature 426 2003 517
    • (2003) Nature , vol.426 , pp. 517
    • Clapham, D.E.1
  • 38
    • 7444240741 scopus 로고    scopus 로고
    • Clues to understanding cold sensation: Thermodynamics and electrophysiological analysis of the cold receptor TRPM8
    • S. Brauchi, P. Orio, and R. Latorre Clues to understanding cold sensation: thermodynamics and electrophysiological analysis of the cold receptor TRPM8 Proc. Natl. Acad. Sci. U. S. A. 101 2004 15494
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 15494
    • Brauchi, S.1    Orio, P.2    Latorre, R.3
  • 39
    • 4043077669 scopus 로고    scopus 로고
    • The principle of temperature-dependent gating in cold- and heat-sensitive TRP channels
    • T. Voets, G. Droogmans, U. Wissenbach, A. Janssens, V. Flockerzi, and B. Nilius The principle of temperature-dependent gating in cold- and heat-sensitive TRP channels Nature 430 2004 748
    • (2004) Nature , vol.430 , pp. 748
    • Voets, T.1    Droogmans, G.2    Wissenbach, U.3    Janssens, A.4    Flockerzi, V.5    Nilius, B.6
  • 43
    • 33846149200 scopus 로고    scopus 로고
    • Transient receptor potential ion channels as participants in thermosensation and thermoregulation
    • M.J. Caterina Transient receptor potential ion channels as participants in thermosensation and thermoregulation Am. J. Physiol. Regul. Integr. Comp. Physiol. 292 2007 R64 R76
    • (2007) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.292
    • Caterina, M.J.1
  • 44
    • 0037033077 scopus 로고    scopus 로고
    • Heat-evoked activation of TRPV4 channels in a HEK293 cell expression system and in native mouse aorta endothelial cells
    • H. Watanabe, J. Vriens, S.H. Suh, C.D. Benham, G. Droogmans, and B. Nilius Heat-evoked activation of TRPV4 channels in a HEK293 cell expression system and in native mouse aorta endothelial cells J. Biol. Chem. 277 2002 47044
    • (2002) J. Biol. Chem. , vol.277 , pp. 47044
    • Watanabe, H.1    Vriens, J.2    Suh, S.H.3    Benham, C.D.4    Droogmans, G.5    Nilius, B.6
  • 46
    • 84874229704 scopus 로고    scopus 로고
    • TRPV1 channels are intrinsically heat sensitive and negatively regulated by phosphoinositide lipids
    • E. Cao, J.F. Cordero-Morales, B. Liu, F. Qin, and D. Julius TRPV1 channels are intrinsically heat sensitive and negatively regulated by phosphoinositide lipids Neuron 77 2013 667
    • (2013) Neuron , vol.77 , pp. 667
    • Cao, E.1    Cordero-Morales, J.F.2    Liu, B.3    Qin, F.4    Julius, D.5
  • 47
    • 33646899582 scopus 로고    scopus 로고
    • A hot-sensing cold receptor: C-terminal domain determines thermosensation in transient receptor potential channels
    • S. Brauchi, G. Orta, M. Salazar, E. Rosenmann, and R. Latorre A hot-sensing cold receptor: C-terminal domain determines thermosensation in transient receptor potential channels J. Neurosci. 26 2006 4835
    • (2006) J. Neurosci. , vol.26 , pp. 4835
    • Brauchi, S.1    Orta, G.2    Salazar, M.3    Rosenmann, E.4    Latorre, R.5
  • 48
    • 83755207202 scopus 로고    scopus 로고
    • A thermodynamic framework for understanding temperature sensing by transient receptor potential (TRP) channels
    • D.E. Clapham, and C. Miller A thermodynamic framework for understanding temperature sensing by transient receptor potential (TRP) channels Proc. Natl. Acad. Sci. U. S. A. 108 2011 19492
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 19492
    • Clapham, D.E.1    Miller, C.2
  • 49
    • 17844373771 scopus 로고    scopus 로고
    • PI(4,5)P2 regulates the activation and desensitization of TRPM8 channels through the TRP domain
    • T. Rohacs, C.M. Lopes, I. Michailidis, and D.E. Logothetis PI(4,5)P2 regulates the activation and desensitization of TRPM8 channels through the TRP domain Nat. Neurosci. 8 2005 626
    • (2005) Nat. Neurosci. , vol.8 , pp. 626
    • Rohacs, T.1    Lopes, C.M.2    Michailidis, I.3    Logothetis, D.E.4
  • 50
    • 34248149453 scopus 로고    scopus 로고
    • Bidirectional shifts of TRPM8 channel gating by temperature and chemical agents modulate the cold sensitivity of mammalian thermoreceptors
    • A. Malkia, R. Madrid, V. Meseguer, E. de la Pena, M. Valero, C. Belmonte, and F. Viana Bidirectional shifts of TRPM8 channel gating by temperature and chemical agents modulate the cold sensitivity of mammalian thermoreceptors J. Physiol. 581 2007 155
    • (2007) J. Physiol. , vol.581 , pp. 155
    • Malkia, A.1    Madrid, R.2    Meseguer, V.3    De La Pena, E.4    Valero, M.5    Belmonte, C.6    Viana, F.7
  • 51
    • 42949125051 scopus 로고    scopus 로고
    • Pirt, a phosphoinositide-binding protein, functions as a regulatory subunit of TRPV1
    • A.Y. Kim, Z. Tang, Q. Liu, K.N. Patel, D. Maag, Y. Geng, and X. Dong Pirt, a phosphoinositide-binding protein, functions as a regulatory subunit of TRPV1 Cell 133 2008 475
    • (2008) Cell , vol.133 , pp. 475
    • Kim, A.Y.1    Tang, Z.2    Liu, Q.3    Patel, K.N.4    Maag, D.5    Geng, Y.6    Dong, X.7
  • 53
    • 33845991187 scopus 로고    scopus 로고
    • The cold and menthol receptor TRPM8 contains a functionally important double cysteine motif
    • I. Dragoni, E. Guida, and P. McIntyre The cold and menthol receptor TRPM8 contains a functionally important double cysteine motif J. Biol. Chem. 281 2006 37353
    • (2006) J. Biol. Chem. , vol.281 , pp. 37353
    • Dragoni, I.1    Guida, E.2    McIntyre, P.3
  • 54
    • 84861534004 scopus 로고    scopus 로고
    • N-glycosylation of TRPM8 ion channels modulates temperature sensitivity of cold thermoreceptor neurons
    • M. Pertusa, R. Madrid, C. Morenilla-Palao, C. Belmonte, and F. Viana N-glycosylation of TRPM8 ion channels modulates temperature sensitivity of cold thermoreceptor neurons J. Biol. Chem. 287 2012 18218
    • (2012) J. Biol. Chem. , vol.287 , pp. 18218
    • Pertusa, M.1    Madrid, R.2    Morenilla-Palao, C.3    Belmonte, C.4    Viana, F.5
  • 57
    • 78449231767 scopus 로고    scopus 로고
    • Endogenous lipid-derived ligands for sensory TRP ion channels and their pain modulation
    • S. Bang, S. Yoo, U. Oh, and S.W. Hwang Endogenous lipid-derived ligands for sensory TRP ion channels and their pain modulation Arch. Pharm. Res. 33 2010 1509
    • (2010) Arch. Pharm. Res. , vol.33 , pp. 1509
    • Bang, S.1    Yoo, S.2    Oh, U.3    Hwang, S.W.4
  • 58
    • 34548658196 scopus 로고    scopus 로고
    • Regulation of transient receptor potential (TRP) channels by phosphoinositides
    • T. Rohacs, and B. Nilius Regulation of transient receptor potential (TRP) channels by phosphoinositides Pflugers Arch. 455 2007 157
    • (2007) Pflugers Arch. , vol.455 , pp. 157
    • Rohacs, T.1    Nilius, B.2
  • 59
    • 77956799526 scopus 로고    scopus 로고
    • Gating of transient receptor potential melastatin 8 (TRPM8) channels activated by cold and chemical agonists in planar lipid bilayers
    • E. Zakharian, C. Cao, and T. Rohacs Gating of transient receptor potential melastatin 8 (TRPM8) channels activated by cold and chemical agonists in planar lipid bilayers J. Neurosci. 30 2010 12526
    • (2010) J. Neurosci. , vol.30 , pp. 12526
    • Zakharian, E.1    Cao, C.2    Rohacs, T.3
  • 60
    • 0035808040 scopus 로고    scopus 로고
    • The complex and intriguing lives of PIP2 with ion channels and transporters
    • D.W. Hilgemann, S. Feng, and C. Nasuhoglu The complex and intriguing lives of PIP2 with ion channels and transporters Sci. STKE 2001 2001 re19
    • (2001) Sci. STKE , vol.2001 , pp. 19
    • Hilgemann, D.W.1    Feng, S.2    Nasuhoglu, C.3
  • 61
    • 48249116482 scopus 로고    scopus 로고
    • PIP2 is a necessary cofactor for ion channel function: How and why?
    • B.C. Suh, and B. Hille PIP2 is a necessary cofactor for ion channel function: how and why? Annu. Rev. Biophys. 37 2008 175
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 175
    • Suh, B.C.1    Hille, B.2
  • 62
    • 84874230625 scopus 로고    scopus 로고
    • Phosphoinositide sensitivity of ion channels, a functional perspective
    • N. Gamper, and T. Rohacs Phosphoinositide sensitivity of ion channels, a functional perspective Subcell. Biochem. 59 2012 289
    • (2012) Subcell. Biochem. , vol.59 , pp. 289
    • Gamper, N.1    Rohacs, T.2
  • 63
    • 14044261739 scopus 로고    scopus 로고
    • Functional control of cold- and menthol-sensitive TRPM8 ion channels by phosphatidylinositol 4,5-bisphosphate
    • B. Liu, and F. Qin Functional control of cold- and menthol-sensitive TRPM8 ion channels by phosphatidylinositol 4,5-bisphosphate J. Neurosci. 25 2005 1674
    • (2005) J. Neurosci. , vol.25 , pp. 1674
    • Liu, B.1    Qin, F.2
  • 65
    • 59449084852 scopus 로고    scopus 로고
    • Activity of the neuronal cold sensor TRPM8 is regulated by phospholipase C via the phospholipid phosphoinositol 4,5-bisphosphate
    • R.L. Daniels, Y. Takashima, and D.D. McKemy Activity of the neuronal cold sensor TRPM8 is regulated by phospholipase C via the phospholipid phosphoinositol 4,5-bisphosphate J. Biol. Chem. 284 2009 1570
    • (2009) J. Biol. Chem. , vol.284 , pp. 1570
    • Daniels, R.L.1    Takashima, Y.2    McKemy, D.D.3
  • 67
    • 0037799198 scopus 로고    scopus 로고
    • A modular PIP2 binding site as a determinant of capsaicin receptor sensitivity
    • E.D. Prescott, and D. Julius A modular PIP2 binding site as a determinant of capsaicin receptor sensitivity Science 300 2003 1284
    • (2003) Science , vol.300 , pp. 1284
    • Prescott, E.D.1    Julius, D.2
  • 68
    • 54449099889 scopus 로고    scopus 로고
    • Determinants of molecular specificity in phosphoinositide regulation. Phosphatidylinositol (4,5)-bisphosphate (PI(4,5)P2) is the endogenous lipid regulating TRPV1
    • R.M. Klein, C.A. Ufret-Vincenty, L. Hua, and S.E. Gordon Determinants of molecular specificity in phosphoinositide regulation. Phosphatidylinositol (4,5)-bisphosphate (PI(4,5)P2) is the endogenous lipid regulating TRPV1 J. Biol. Chem. 283 2008 26208
    • (2008) J. Biol. Chem. , vol.283 , pp. 26208
    • Klein, R.M.1    Ufret-Vincenty, C.A.2    Hua, L.3    Gordon, S.E.4
  • 71
    • 33947515995 scopus 로고    scopus 로고
    • Modulation of the cold-activated channel TRPM8 by lysophospholipids and polyunsaturated fatty acids
    • D.A. Andersson, M. Nash, and S. Bevan Modulation of the cold-activated channel TRPM8 by lysophospholipids and polyunsaturated fatty acids J. Neurosci. 27 2007 3347
    • (2007) J. Neurosci. , vol.27 , pp. 3347
    • Andersson, D.A.1    Nash, M.2    Bevan, S.3
  • 75
    • 23044515008 scopus 로고    scopus 로고
    • Lipids as regulators of the activity of transient receptor potential type V1 (TRPV1) channels
    • L. De Petrocellis, and V. Di Marzo Lipids as regulators of the activity of transient receptor potential type V1 (TRPV1) channels Life Sci. 77 2005 1651
    • (2005) Life Sci. , vol.77 , pp. 1651
    • De Petrocellis, L.1    Di Marzo, V.2
  • 77
    • 77953527601 scopus 로고    scopus 로고
    • Farnesyl pyrophosphate is a novel pain-producing molecule via specific activation of TRPV3
    • S. Bang, S. Yoo, T.J. Yang, H. Cho, and S.W. Hwang Farnesyl pyrophosphate is a novel pain-producing molecule via specific activation of TRPV3 J. Biol. Chem. 285 2010 19362
    • (2010) J. Biol. Chem. , vol.285 , pp. 19362
    • Bang, S.1    Yoo, S.2    Yang, T.J.3    Cho, H.4    Hwang, S.W.5
  • 78
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • D. Lingwood, and K. Simons Lipid rafts as a membrane-organizing principle Science 327 2010 46
    • (2010) Science , vol.327 , pp. 46
    • Lingwood, D.1    Simons, K.2
  • 79
    • 0346655136 scopus 로고    scopus 로고
    • Targeting of ion channels to membrane microdomains: Localization of KV channels to lipid rafts
    • J.R. Martens, K. O'Connell, and M. Tamkun Targeting of ion channels to membrane microdomains: localization of KV channels to lipid rafts Trends Pharmacol. Sci. 25 2004 16
    • (2004) Trends Pharmacol. Sci. , vol.25 , pp. 16
    • Martens, J.R.1    O'Connell, K.2    Tamkun, M.3
  • 80
    • 0942277046 scopus 로고    scopus 로고
    • A role for hTRPC1 and lipid raft domains in store-mediated calcium entry in human platelets
    • S.L. Brownlow, A.G. Harper, M.T. Harper, and S.O. Sage A role for hTRPC1 and lipid raft domains in store-mediated calcium entry in human platelets Cell Calcium 35 2004 107
    • (2004) Cell Calcium , vol.35 , pp. 107
    • Brownlow, S.L.1    Harper, A.G.2    Harper, M.T.3    Sage, S.O.4
  • 84
    • 84874537340 scopus 로고    scopus 로고
    • The membrane-associated transient receptor potential vanilloid channel is the central heat shock receptor controlling the cellular heat shock response in epithelial cells
    • Z. Bromberg, P. Goloubinoff, Y. Saidi, and Y.G. Weiss The membrane-associated transient receptor potential vanilloid channel is the central heat shock receptor controlling the cellular heat shock response in epithelial cells PLoS One 8 2013 e57149
    • (2013) PLoS One , vol.8 , pp. 57149
    • Bromberg, Z.1    Goloubinoff, P.2    Saidi, Y.3    Weiss, Y.G.4
  • 85
    • 0034454682 scopus 로고    scopus 로고
    • How do glucocorticoids influence stress responses? Integrating permissive, suppressive, stimulatory, and preparative actions
    • R.M. Sapolsky, L.M. Romero, and A.U. Munck How do glucocorticoids influence stress responses? Integrating permissive, suppressive, stimulatory, and preparative actions Endocr. Rev. 21 2000 55
    • (2000) Endocr. Rev. , vol.21 , pp. 55
    • Sapolsky, R.M.1    Romero, L.M.2    Munck, A.U.3
  • 86
    • 0033509296 scopus 로고    scopus 로고
    • Cortisol in teleosts: Dynamics, mechanisms of action, and metabolic regulation
    • T.P. Mommsen, M.M. Vijayan, and T.W. Moon Cortisol in teleosts: dynamics, mechanisms of action, and metabolic regulation Rev. Fish Biol. Fish. 9 1999 211
    • (1999) Rev. Fish Biol. Fish. , vol.9 , pp. 211
    • Mommsen, T.P.1    Vijayan, M.M.2    Moon, T.W.3
  • 87
    • 0034617126 scopus 로고    scopus 로고
    • Steroid hormone-induced effects on membrane fluidity and their potential roles in non-genomic mechanisms
    • K.P. Whiting, C.J. Restall, and P.F. Brain Steroid hormone-induced effects on membrane fluidity and their potential roles in non-genomic mechanisms Life Sci. 67 2000 743
    • (2000) Life Sci. , vol.67 , pp. 743
    • Whiting, K.P.1    Restall, C.J.2    Brain, P.F.3
  • 88
    • 0033668897 scopus 로고    scopus 로고
    • Nongenomic membrane actions of glucocorticoids in vertebrates
    • R.J. Borski Nongenomic membrane actions of glucocorticoids in vertebrates Trends Endocrinol. Metab. 11 2000 427
    • (2000) Trends Endocrinol. Metab. , vol.11 , pp. 427
    • Borski, R.J.1
  • 89
    • 23744452040 scopus 로고    scopus 로고
    • Ectothermy and endothermy: Evolutionary perspectives of thermoprotection by HSPs
    • A. Shabtay, and Z. Arad Ectothermy and endothermy: evolutionary perspectives of thermoprotection by HSPs J. Exp. Biol. 208 2005 2773
    • (2005) J. Exp. Biol. , vol.208 , pp. 2773
    • Shabtay, A.1    Arad, Z.2
  • 90
    • 84878549241 scopus 로고    scopus 로고
    • Rapid cortisol signaling in response to acute stress involves changes in plasma membrane order in rainbow trout liver
    • L. Dindia, E. Faught, Z. Leonenko, R. Thomas, and M.M. Vijayan Rapid cortisol signaling in response to acute stress involves changes in plasma membrane order in rainbow trout liver Am. J. Physiol. Endocrinol. Metab. 304 2013 E1157 E1166
    • (2013) Am. J. Physiol. Endocrinol. Metab. , vol.304
    • Dindia, L.1    Faught, E.2    Leonenko, Z.3    Thomas, R.4    Vijayan, M.M.5
  • 91
    • 84867324809 scopus 로고    scopus 로고
    • Novel nongenomic signaling by glucocorticoid may involve changes to liver membrane order in rainbow trout
    • L. Dindia, J. Murray, E. Faught, T.L. Davis, Z. Leonenko, and M.M. Vijayan Novel nongenomic signaling by glucocorticoid may involve changes to liver membrane order in rainbow trout PLoS One 7 2012
    • (2012) PLoS One , vol.7
    • Dindia, L.1    Murray, J.2    Faught, E.3    Davis, T.L.4    Leonenko, Z.5    Vijayan, M.M.6
  • 92
    • 77954944583 scopus 로고    scopus 로고
    • Interaction mechanism of cortisol and catecholamines with structural components of erythrocyte membranes
    • L.E. Panin, P.V. Mokrushnikov, V.G. Kunitsyn, and B.N. Zaitsev Interaction mechanism of cortisol and catecholamines with structural components of erythrocyte membranes J. Phys. Chem. B 114 2010 9462
    • (2010) J. Phys. Chem. B , vol.114 , pp. 9462
    • Panin, L.E.1    Mokrushnikov, P.V.2    Kunitsyn, V.G.3    Zaitsev, B.N.4
  • 94
    • 0016637033 scopus 로고
    • Single dose metyrapone test - 11 beta-hydroxylase inhibition by metyrapone and reduced metyrapone assayed by radioimmunoassay
    • A.W. Meikle, S.C. West, J.A. Weed, and F.H. Tyler Single dose metyrapone test - 11 beta-hydroxylase inhibition by metyrapone and reduced metyrapone assayed by radioimmunoassay J. Clin. Endocrinol. Metab. 40 1975 290
    • (1975) J. Clin. Endocrinol. Metab. , vol.40 , pp. 290
    • Meikle, A.W.1    West, S.C.2    Weed, J.A.3    Tyler, F.H.4
  • 96
    • 84255190048 scopus 로고    scopus 로고
    • Hormonal modulation of the heat shock response: Insights from fish with divergent cortisol stress responses
    • S. LeBlanc, E. Hoglund, K.M. Gilmour, and S. Currie Hormonal modulation of the heat shock response: insights from fish with divergent cortisol stress responses Am. J. Physiol. Regul. Integr. Comp. Physiol. 302 2012 R184 R192
    • (2012) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.302
    • Leblanc, S.1    Hoglund, E.2    Gilmour, K.M.3    Currie, S.4
  • 98
    • 0036724685 scopus 로고    scopus 로고
    • Glucocorticoid-mediated attenuation of the hsp70 response in trout hepatocytes involves the proteasome
    • A.N. Boone, and M.M. Vijayan Glucocorticoid-mediated attenuation of the hsp70 response in trout hepatocytes involves the proteasome Am. J. Physiol. Regul. Integr. Comp. Physiol. 283 2002 R680 R687
    • (2002) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.283
    • Boone, A.N.1    Vijayan, M.M.2
  • 100
    • 67649236110 scopus 로고    scopus 로고
    • Lipid rafts constrain basal alpha(1A)-adrenergic receptor signaling by maintaining receptor in an inactive conformation
    • B.L. Lei, D.P. Morris, M.P. Smith, and D.A. Schwinn Lipid rafts constrain basal alpha(1A)-adrenergic receptor signaling by maintaining receptor in an inactive conformation Cell. Signal. 21 2009 1532
    • (2009) Cell. Signal. , vol.21 , pp. 1532
    • Lei, B.L.1    Morris, D.P.2    Smith, M.P.3    Schwinn, D.A.4
  • 101
    • 0036482874 scopus 로고    scopus 로고
    • Rate sensitivity of shear-induced changes in the lateral diffusion of endothelial cell membrane lipids: A role for membrane perturbation in shear-induced MAPK activation
    • P.J. Butler, T.C. Tsou, J.Y.S. Li, S. Usami, and S. Chien Rate sensitivity of shear-induced changes in the lateral diffusion of endothelial cell membrane lipids: a role for membrane perturbation in shear-induced MAPK activation FASEB J. 15 2001 216
    • (2001) FASEB J. , vol.15 , pp. 216
    • Butler, P.J.1    Tsou, T.C.2    Li, J.Y.S.3    Usami, S.4    Chien, S.5
  • 102
    • 33644872354 scopus 로고    scopus 로고
    • Phosphorylation of HSF1 by MAPK-activated protein kinase 2 on serine 121, inhibits transcriptional activity and promotes HSP90 binding
    • X.Z. Wang, M.A. Khaleque, M.J. Zhao, R. Zhong, M. Gaestel, and S.K. Calderwood Phosphorylation of HSF1 by MAPK-activated protein kinase 2 on serine 121, inhibits transcriptional activity and promotes HSP90 binding J. Biol. Chem. 281 2006 782
    • (2006) J. Biol. Chem. , vol.281 , pp. 782
    • Wang, X.Z.1    Khaleque, M.A.2    Zhao, M.J.3    Zhong, R.4    Gaestel, M.5    Calderwood, S.K.6
  • 103
    • 0030988941 scopus 로고    scopus 로고
    • Repression of the heat shock factor 1 transcriptional activation domain is modulated by constitutive phosphorylation
    • M.P. Kline, and R.I. Morimoto Repression of the heat shock factor 1 transcriptional activation domain is modulated by constitutive phosphorylation Mol. Cell. Biol. 17 1997 2107
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2107
    • Kline, M.P.1    Morimoto, R.I.2
  • 104
    • 0029804194 scopus 로고    scopus 로고
    • Repression of human heat shock factor 1 activity at control temperature by phosphorylation
    • U. Knauf, E.M. Newton, J. Kyriakis, and R.E. Kingston Repression of human heat shock factor 1 activity at control temperature by phosphorylation Genes Dev. 10 1996 2782
    • (1996) Genes Dev. , vol.10 , pp. 2782
    • Knauf, U.1    Newton, E.M.2    Kyriakis, J.3    Kingston, R.E.4
  • 105
    • 0034194472 scopus 로고    scopus 로고
    • Influence of membrane physical state on the lysosomal proton permeability
    • G.J. Zhang, H.W. Liu, L. Yang, Y.G. Zhong, and Y.Z. Zheng Influence of membrane physical state on the lysosomal proton permeability J. Membr. Biol. 175 2000 53
    • (2000) J. Membr. Biol. , vol.175 , pp. 53
    • Zhang, G.J.1    Liu, H.W.2    Yang, L.3    Zhong, Y.G.4    Zheng, Y.Z.5
  • 106
    • 0022410034 scopus 로고
    • Relationship between fluidity and ionic permeability of bilayers from natural mixtures of phospholipids
    • M. Rossignol, T. Uso, and P. Thomas Relationship between fluidity and ionic permeability of bilayers from natural mixtures of phospholipids J. Membr. Biol. 87 1985 269
    • (1985) J. Membr. Biol. , vol.87 , pp. 269
    • Rossignol, M.1    Uso, T.2    Thomas, P.3
  • 107
    • 0024503168 scopus 로고
    • Proton flux mechanisms in model and biological membranes
    • D.W. Deamer, and J.W. Nichols Proton flux mechanisms in model and biological membranes J. Membr. Biol. 107 1989 91
    • (1989) J. Membr. Biol. , vol.107 , pp. 91
    • Deamer, D.W.1    Nichols, J.W.2
  • 108
    • 0029782010 scopus 로고    scopus 로고
    • Proton transport across transient single-file water pores in a lipid membrane studied by molecular dynamics simulations
    • S.J. Marrink, F. Jahnig, and H.J. Berendsen Proton transport across transient single-file water pores in a lipid membrane studied by molecular dynamics simulations Biophys. J. 71 1996 632
    • (1996) Biophys. J. , vol.71 , pp. 632
    • Marrink, S.J.1    Jahnig, F.2    Berendsen, H.J.3
  • 109
    • 0022728447 scopus 로고
    • Permeability of lipid bilayers to water and ionic solutes
    • D.W. Deamer, and J. Bramhall Permeability of lipid bilayers to water and ionic solutes Chem. Phys. Lipids 40 1986 167
    • (1986) Chem. Phys. Lipids , vol.40 , pp. 167
    • Deamer, D.W.1    Bramhall, J.2
  • 110
    • 0028086058 scopus 로고
    • Interaction of Serratia marcescens hemolysin (ShlA) with artificial and erythrocyte membranes. Demonstration of the formation of aqueous multistate channels
    • R. Schonherr, M. Hilger, S. Broer, R. Benz, and V. Braun Interaction of Serratia marcescens hemolysin (ShlA) with artificial and erythrocyte membranes. Demonstration of the formation of aqueous multistate channels Eur. J. Biochem. 223 1994 655
    • (1994) Eur. J. Biochem. , vol.223 , pp. 655
    • Schonherr, R.1    Hilger, M.2    Broer, S.3    Benz, R.4    Braun, V.5
  • 111
    • 0024539836 scopus 로고
    • Proton permeability and lipid dynamics of gastric and duodenal apical membrane vesicles
    • J.M. Wilkes, H.J. Ballard, D.T. Dryden, and B.H. Hirst Proton permeability and lipid dynamics of gastric and duodenal apical membrane vesicles Am. J. Physiol. 256 1989 G553 G562
    • (1989) Am. J. Physiol. , vol.256
    • Wilkes, J.M.1    Ballard, H.J.2    Dryden, D.T.3    Hirst, B.H.4
  • 112
    • 0029893721 scopus 로고    scopus 로고
    • Bile acid-induced increase of rat colonic apical membrane fluidity and proton permeability
    • O. Schroder, W. Rathner, W.F. Caspary, and J. Stein Bile acid-induced increase of rat colonic apical membrane fluidity and proton permeability Z. Gastroenterol. 34 1996 365
    • (1996) Z. Gastroenterol. , vol.34 , pp. 365
    • Schroder, O.1    Rathner, W.2    Caspary, W.F.3    Stein, J.4
  • 113
    • 28244493434 scopus 로고    scopus 로고
    • The hyperfluidization of mammalian cell membranes acts as a signal to initiate the heat shock protein response
    • G. Balogh, I. Horvath, E. Nagy, Z. Hoyk, S. Benko, O. Bensaude, and L. Vigh The hyperfluidization of mammalian cell membranes acts as a signal to initiate the heat shock protein response FEBS J. 272 2005 6077
    • (2005) FEBS J. , vol.272 , pp. 6077
    • Balogh, G.1    Horvath, I.2    Nagy, E.3    Hoyk, Z.4    Benko, S.5    Bensaude, O.6    Vigh, L.7
  • 115
    • 0035091628 scopus 로고    scopus 로고
    • Structure-specific membrane-fluidizing effect of propofol
    • H. Tsuchiya Structure-specific membrane-fluidizing effect of propofol Clin. Exp. Pharmacol. Physiol. 28 2001 292
    • (2001) Clin. Exp. Pharmacol. Physiol. , vol.28 , pp. 292
    • Tsuchiya, H.1
  • 116
    • 78649749950 scopus 로고    scopus 로고
    • Molecular dynamics simulations of local anesthetic articaine in a lipid bilayer
    • E.H. Mojumdar, and A.P. Lyubartsev Molecular dynamics simulations of local anesthetic articaine in a lipid bilayer Biophys. Chem. 153 2010 27
    • (2010) Biophys. Chem. , vol.153 , pp. 27
    • Mojumdar, E.H.1    Lyubartsev, A.P.2
  • 117
    • 84878746587 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the interactions of medicinal plant extracts and drugs with lipid bilayer membranes
    • W. Kopec, J. Telenius, and H. Khandelia Molecular dynamics simulations of the interactions of medicinal plant extracts and drugs with lipid bilayer membranes FEBS J. 280 2013 2785
    • (2013) FEBS J. , vol.280 , pp. 2785
    • Kopec, W.1    Telenius, J.2    Khandelia, H.3
  • 118
  • 120
    • 85172633626 scopus 로고    scopus 로고
    • Modelling of lipid membranes and membrane interacting compounds
    • Elsevier Ireland
    • S. Piotto, S. Concilio, and P. Iannelli Modelling of lipid membranes and membrane interacting compounds Chemistry and Physics of Lipids vol. 143 2006 Elsevier Ireland 62 63
    • (2006) Chemistry and Physics of Lipids , vol.143 , pp. 62-63
    • Piotto, S.1    Concilio, S.2    Iannelli, P.3
  • 121
    • 10344223464 scopus 로고    scopus 로고
    • Making optimal use of empirical energy functions: Force-field parameterization in crystal space
    • E. Krieger, T. Darden, S.B. Nabuurs, A. Finkelstein, and G. Vriend Making optimal use of empirical energy functions: force-field parameterization in crystal space Proteins 57 2004 678
    • (2004) Proteins , vol.57 , pp. 678
    • Krieger, E.1    Darden, T.2    Nabuurs, S.B.3    Finkelstein, A.4    Vriend, G.5
  • 124
    • 33751157086 scopus 로고
    • Conductor-like screening model for real solvents - A new approach to the quantitative calculation of solvation phenomena
    • A. Klamt Conductor-like screening model for real solvents - a new approach to the quantitative calculation of solvation phenomena J. Phys. Chem. 99 1995 2224
    • (1995) J. Phys. Chem. , vol.99 , pp. 2224
    • Klamt, A.1
  • 125
    • 0025390935 scopus 로고
    • Special Issue - Mopac - A semiempirical molecular-orbital program
    • J.J.P. Stewart Special Issue - Mopac - a semiempirical molecular-orbital program J. Comput. Aided Mol. Des. 4 1990 1
    • (1990) J. Comput. Aided Mol. Des. , vol.4 , pp. 1
    • Stewart, J.J.P.1
  • 129
    • 50349141358 scopus 로고
    • Treatment of staphylococcal infections with penicillin by intermittent sterilisation
    • J.W. Bigger Treatment of staphylococcal infections with penicillin by intermittent sterilisation Lancet 2 1944 497
    • (1944) Lancet , vol.2 , pp. 497
    • Bigger, J.W.1
  • 130
    • 33747174575 scopus 로고    scopus 로고
    • Microbial cell individuality and the underlying sources of heterogeneity
    • S.V. Avery Microbial cell individuality and the underlying sources of heterogeneity Nat. Rev. Microbiol. 4 2006 577
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 577
    • Avery, S.V.1
  • 131
    • 65249157060 scopus 로고    scopus 로고
    • Single-cell profiling reveals the origin of phenotypic variability in adipogenesis
    • T.T. Le, and J.X. Cheng Single-cell profiling reveals the origin of phenotypic variability in adipogenesis PLoS One 4 2009
    • (2009) PLoS One , vol.4
    • Le, T.T.1    Cheng, J.X.2
  • 133
    • 0037104993 scopus 로고    scopus 로고
    • Stress and the single cell: Intrapopulation diversity is a mechanism to ensure survival upon exposure to stress
    • I.R. Booth Stress and the single cell: intrapopulation diversity is a mechanism to ensure survival upon exposure to stress Int. J. Food Microbiol. 78 2002 19
    • (2002) Int. J. Food Microbiol. , vol.78 , pp. 19
    • Booth, I.R.1
  • 135
    • 0035014797 scopus 로고    scopus 로고
    • Heterogeneity of stress gene expression and stress resistance among individual cells of Saccharomyces cerevisiae
    • P.V. Attfield, H.Y. Choi, D.A. Veal, and P.J. Bell Heterogeneity of stress gene expression and stress resistance among individual cells of Saccharomyces cerevisiae Mol. Microbiol. 40 2001 1000
    • (2001) Mol. Microbiol. , vol.40 , pp. 1000
    • Attfield, P.V.1    Choi, H.Y.2    Veal, D.A.3    Bell, P.J.4
  • 136
    • 0036178356 scopus 로고    scopus 로고
    • Phenotypic heterogeneity: Differential stress resistance among individual cells of the yeast Saccharomyces cerevisiae
    • E.R. Sumner, and S.V. Avery Phenotypic heterogeneity: differential stress resistance among individual cells of the yeast Saccharomyces cerevisiae Microbiology 148 2002 345
    • (2002) Microbiology , vol.148 , pp. 345
    • Sumner, E.R.1    Avery, S.V.2
  • 137
    • 0032569851 scopus 로고    scopus 로고
    • Hsp90 as a capacitor for morphological evolution
    • S.L. Rutherford, and S. Lindquist Hsp90 as a capacitor for morphological evolution Nature 396 1998 336
    • (1998) Nature , vol.396 , pp. 336
    • Rutherford, S.L.1    Lindquist, S.2
  • 138
    • 0042154192 scopus 로고    scopus 로고
    • Evolutionary capacitance as a general feature of complex gene networks
    • A. Bergman, and M.L. Siegal Evolutionary capacitance as a general feature of complex gene networks Nature 424 2003 549
    • (2003) Nature , vol.424 , pp. 549
    • Bergman, A.1    Siegal, M.L.2
  • 139
    • 0033027056 scopus 로고    scopus 로고
    • Physiological states of individual Salmonella Typhimurium cells monitored by in situ reverse transcription-PCR
    • K. Holmstrom, T. Tolker-Nielsen, and S. Molin Physiological states of individual Salmonella Typhimurium cells monitored by in situ reverse transcription-PCR J. Bacteriol. 181 1999 1733
    • (1999) J. Bacteriol. , vol.181 , pp. 1733
    • Holmstrom, K.1    Tolker-Nielsen, T.2    Molin, S.3
  • 140
    • 0023147386 scopus 로고
    • Effect of cell-cycle position on thermotolerance in Saccharomyces- cerevisiae
    • J. Plesset, J.R. Ludwig, B.S. Cox, and C.S. Mclaughlin Effect of cell-cycle position on thermotolerance in Saccharomyces-cerevisiae J. Bacteriol. 169 1987 779
    • (1987) J. Bacteriol. , vol.169 , pp. 779
    • Plesset, J.1    Ludwig, J.R.2    Cox, B.S.3    McLaughlin, C.S.4
  • 141
    • 0038612842 scopus 로고    scopus 로고
    • Oscillatory nucleocytoplasmic shuttling of the general stress response transcriptional activators Msn2 and Msn4 in Saccharomyces cerevisiae
    • M. Jacquet, G. Renault, S. Lallet, J. De Mey, and A. Goldbeter Oscillatory nucleocytoplasmic shuttling of the general stress response transcriptional activators Msn2 and Msn4 in Saccharomyces cerevisiae J. Cell Biol. 161 2003 497
    • (2003) J. Cell Biol. , vol.161 , pp. 497
    • Jacquet, M.1    Renault, G.2    Lallet, S.3    De Mey, J.4    Goldbeter, A.5
  • 142
    • 27944487902 scopus 로고    scopus 로고
    • Logic of the yeast metabolic cycle: Temporal compartmentalization of cellular processes
    • B.P. Tu, A. Kudlicki, M. Rowicka, and S.L. McKnight Logic of the yeast metabolic cycle: temporal compartmentalization of cellular processes Science 310 2005 1152
    • (2005) Science , vol.310 , pp. 1152
    • Tu, B.P.1    Kudlicki, A.2    Rowicka, M.3    McKnight, S.L.4
  • 143
    • 0035196372 scopus 로고    scopus 로고
    • Analysis of the upstream regulatory region of the GTS1 gene required for its oscillatory expression
    • H. Tonozuka, J.Q. Wang, K. Mitsui, T. Saito, Y. Hamada, and K. Tsurugi Analysis of the upstream regulatory region of the GTS1 gene required for its oscillatory expression J. Biochem. 130 2001 589
    • (2001) J. Biochem. , vol.130 , pp. 589
    • Tonozuka, H.1    Wang, J.Q.2    Mitsui, K.3    Saito, T.4    Hamada, Y.5    Tsurugi, K.6
  • 144
    • 0034255690 scopus 로고    scopus 로고
    • Cellular stress responses oscillate in synchronization with the ultradian oscillation of energy metabolism in the yeast Saccharomyces cerevisiae
    • J.Q. Wang, W.D. Liu, T. Uno, H. Tonozuka, K. Mitsui, and K. Tsurugi Cellular stress responses oscillate in synchronization with the ultradian oscillation of energy metabolism in the yeast Saccharomyces cerevisiae FEMS Microbiol. Lett. 189 2000 9
    • (2000) FEMS Microbiol. Lett. , vol.189 , pp. 9
    • Wang, J.Q.1    Liu, W.D.2    Uno, T.3    Tonozuka, H.4    Mitsui, K.5    Tsurugi, K.6
  • 145
    • 0032502723 scopus 로고    scopus 로고
    • Hydrogen peroxide causes RAD9-dependent cell cycle arrest in G2 in Saccharomyces cerevisiae whereas menadione causes G1 arrest independent of RAD9 function
    • J.A. Flattery-O'Brien, and I.W. Dawes Hydrogen peroxide causes RAD9-dependent cell cycle arrest in G2 in Saccharomyces cerevisiae whereas menadione causes G1 arrest independent of RAD9 function J. Biol. Chem. 273 1998 8564
    • (1998) J. Biol. Chem. , vol.273 , pp. 8564
    • Flattery-O'Brien, J.A.1    Dawes, I.W.2
  • 151
    • 84867962537 scopus 로고    scopus 로고
    • Expanding the horizons of lipidomics. Towards fluxolipidomics
    • M. Lagarde, N. Bernoud-Hubac, and M. Guichardant Expanding the horizons of lipidomics. Towards fluxolipidomics Mol. Membr. Biol. 29 2012 222
    • (2012) Mol. Membr. Biol. , vol.29 , pp. 222
    • Lagarde, M.1    Bernoud-Hubac, N.2    Guichardant, M.3
  • 152
    • 84155172923 scopus 로고    scopus 로고
    • Multi-dimensional mass spectrometry-based shotgun lipidomics and novel strategies for lipidomic analyses
    • X.L. Han, K. Yang, and R.W. Gross Multi-dimensional mass spectrometry-based shotgun lipidomics and novel strategies for lipidomic analyses Mass Spectrom. Rev. 31 2012 134
    • (2012) Mass Spectrom. Rev. , vol.31 , pp. 134
    • Han, X.L.1    Yang, K.2    Gross, R.W.3
  • 155
    • 0031452645 scopus 로고    scopus 로고
    • Involvement of yeast sphingolipids in the heat stress response of Saccharomyces cerevisiae
    • G.M. Jenkins, A. Richards, T. Wahl, C.G. Mao, L. Obeid, and Y. Hannun Involvement of yeast sphingolipids in the heat stress response of Saccharomyces cerevisiae J. Biol. Chem. 272 1997 32566
    • (1997) J. Biol. Chem. , vol.272 , pp. 32566
    • Jenkins, G.M.1    Richards, A.2    Wahl, T.3    Mao, C.G.4    Obeid, L.5    Hannun, Y.6
  • 156
    • 27844446183 scopus 로고    scopus 로고
    • Using genomic and lipidomic strategies to investigate sphingolipid function in the yeast heat-stress response
    • L.A. Cowart, and Y.A. Hannun Using genomic and lipidomic strategies to investigate sphingolipid function in the yeast heat-stress response Biochem. Soc. Trans. 33 2005 1166
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 1166
    • Cowart, L.A.1    Hannun, Y.A.2
  • 157
    • 84855291351 scopus 로고    scopus 로고
    • Direct infusion mass spectrometry of oxylipin-containing Arabidopsis membrane lipids reveals varied patterns in different stress responses
    • H.S. Vu, P. Tamura, N.A. Galeva, R. Chaturvedi, M.R. Roth, T.D. Williams, X. Wang, J. Shah, and R. Welti Direct infusion mass spectrometry of oxylipin-containing Arabidopsis membrane lipids reveals varied patterns in different stress responses Plant Physiol. 158 2012 324
    • (2012) Plant Physiol. , vol.158 , pp. 324
    • Vu, H.S.1    Tamura, P.2    Galeva, N.A.3    Chaturvedi, R.4    Roth, M.R.5    Williams, T.D.6    Wang, X.7    Shah, J.8    Welti, R.9
  • 158
    • 77951009331 scopus 로고    scopus 로고
    • Osmotic stress-induced phosphoinositide and inositol phosphate signalling in plants
    • T. Munnik, and J.E. Vermeer Osmotic stress-induced phosphoinositide and inositol phosphate signalling in plants Plant Cell Environ. 33 2010 655
    • (2010) Plant Cell Environ. , vol.33 , pp. 655
    • Munnik, T.1    Vermeer, J.E.2
  • 159
    • 84890555941 scopus 로고    scopus 로고
    • Rapid phosphatidic acid accumulation in response to low temperature stress in Arabidopsis is generated through diacylglycerol kinase
    • S.A. Arisz, R. van Wijk, W. Roels, J.K. Zhu, M.A. Haring, and T. Munnik Rapid phosphatidic acid accumulation in response to low temperature stress in Arabidopsis is generated through diacylglycerol kinase Front. Plant Sci. 4 2013 1
    • (2013) Front. Plant Sci. , vol.4 , pp. 1
    • Arisz, S.A.1    Van Wijk, R.2    Roels, W.3    Zhu, J.K.4    Haring, M.A.5    Munnik, T.6
  • 165
    • 77954955686 scopus 로고    scopus 로고
    • Heat shock factors: Integrators of cell stress, development and lifespan
    • M. Akerfelt, R.I. Morimoto, and L. Sistonen Heat shock factors: integrators of cell stress, development and lifespan Nat. Rev. Mol. Cell Biol. 11 2010 545
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 545
    • Akerfelt, M.1    Morimoto, R.I.2    Sistonen, L.3
  • 167
    • 79959463520 scopus 로고    scopus 로고
    • Regulation of HSF1 function in the heat stress response: Implications in aging and disease
    • J. Anckar, and L. Sistonen Regulation of HSF1 function in the heat stress response: implications in aging and disease Annu. Rev. Biochem. 80 2011 1089
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 1089
    • Anckar, J.1    Sistonen, L.2
  • 171
    • 0026794255 scopus 로고
    • Activity of the epidermal-growth-factor receptor and phospholipase C-gamma 1 in heat-stressed fibroblasts and A-431 cells
    • S.M. Liu, and G. Carpenter Activity of the epidermal-growth-factor
    • (1992) Biochem. J. , vol.286 , Issue.PART 2 , pp. 541
    • Liu, S.M.1    Carpenter, G.2
  • 172
    • 0027192188 scopus 로고
    • Inducers of the heat shock response stimulate phospholipase C and phospholipase A2 activity in mammalian cells
    • S.K. Calderwood, and M.A. Stevenson Inducers of the heat shock response stimulate phospholipase C and phospholipase A2 activity in mammalian cells J. Cell. Physiol. 155 1993 248
    • (1993) J. Cell. Physiol. , vol.155 , pp. 248
    • Calderwood, S.K.1    Stevenson, M.A.2
  • 174
    • 84856712884 scopus 로고    scopus 로고
    • Phosphoinositide-specific phospholipase C9 is involved in the thermotolerance of Arabidopsis
    • S.Z. Zheng, Y.L. Liu, B. Li, Z.L. Shang, R.G. Zhou, and D.Y. Sun Phosphoinositide-specific phospholipase C9 is involved in the thermotolerance of Arabidopsis Plant J. 69 2012 689
    • (2012) Plant J. , vol.69 , pp. 689
    • Zheng, S.Z.1    Liu, Y.L.2    Li, B.3    Shang, Z.L.4    Zhou, R.G.5    Sun, D.Y.6
  • 176
    • 77955614363 scopus 로고    scopus 로고
    • A review on the monoacylglycerol lipase: At the interface between fat and endocannabinoid signalling
    • G. Labar, J. Wouters, and D.M. Lambert A review on the monoacylglycerol lipase: at the interface between fat and endocannabinoid signalling Curr. Med. Chem. 17 2010 2588
    • (2010) Curr. Med. Chem. , vol.17 , pp. 2588
    • Labar, G.1    Wouters, J.2    Lambert, D.M.3
  • 177
  • 178
    • 67349096688 scopus 로고    scopus 로고
    • PKC and PLA2: Probing the complexities of the calcium network
    • D.B. van Rossum, and R.L. Patterson PKC and PLA2: probing the complexities of the calcium network Cell Calcium 45 2009 535
    • (2009) Cell Calcium , vol.45 , pp. 535
    • Van Rossum, D.B.1    Patterson, R.L.2
  • 180
    • 37249087851 scopus 로고    scopus 로고
    • Small G proteins in insulin action: Rab and Rho families at the crossroads of signal transduction and GLUT4 vesicle traffic
    • S. Ishikura, A. Koshkina, and A. Klip Small G proteins in insulin action: Rab and Rho families at the crossroads of signal transduction and GLUT4 vesicle traffic Acta Physiol. (Oxf.) 192 2008 61
    • (2008) Acta Physiol. (Oxf.) , vol.192 , pp. 61
    • Ishikura, S.1    Koshkina, A.2    Klip, A.3
  • 181
    • 0034687548 scopus 로고    scopus 로고
    • Activation of Akt is induced by heat shock and involved in suppression of heat-shock-induced apoptosis of NIH3T3 cells
    • O.S. Bang, B.G. Ha, E.K. Park, and S.S. Kang Activation of Akt is induced by heat shock and involved in suppression of heat-shock-induced apoptosis of NIH3T3 cells Biochem. Biophys. Res. Commun. 278 2000 306
    • (2000) Biochem. Biophys. Res. Commun. , vol.278 , pp. 306
    • Bang, O.S.1    Ha, B.G.2    Park, E.K.3    Kang, S.S.4
  • 182
    • 84871750894 scopus 로고    scopus 로고
    • MTOR is essential for the proteotoxic stress response, HSF1 activation and heat shock protein synthesis
    • S.D. Chou, T. Prince, J. Gong, and S.K. Calderwood mTOR is essential for the proteotoxic stress response, HSF1 activation and heat shock protein synthesis PLoS One 7 2012 e39679
    • (2012) PLoS One , vol.7 , pp. 39679
    • Chou, S.D.1    Prince, T.2    Gong, J.3    Calderwood, S.K.4
  • 183
    • 0035910574 scopus 로고    scopus 로고
    • Implication of a small GTPase Rac1 in the activation of c-Jun N-terminal kinase and heat shock factor in response to heat shock
    • S.I. Han, S.Y. Oh, S.H. Woo, K.H. Kim, J.H. Kim, H.D. Kim, and H.S. Kang Implication of a small GTPase Rac1 in the activation of c-Jun N-terminal kinase and heat shock factor in response to heat shock J. Biol. Chem. 276 2001 1889
    • (2001) J. Biol. Chem. , vol.276 , pp. 1889
    • Han, S.I.1    Oh, S.Y.2    Woo, S.H.3    Kim, K.H.4    Kim, J.H.5    Kim, H.D.6    Kang, H.S.7
  • 184
    • 0030680132 scopus 로고    scopus 로고
    • Heat shock activates c-Src tyrosine kinases and phosphatidylinositol 3-kinase in NIH3T3 fibroblasts
    • R.Z. Lin, Z.W. Hu, J.H. Chin, and B.B. Hoffman Heat shock activates c-Src tyrosine kinases and phosphatidylinositol 3-kinase in NIH3T3 fibroblasts J. Biol. Chem. 272 1997 31196
    • (1997) J. Biol. Chem. , vol.272 , pp. 31196
    • Lin, R.Z.1    Hu, Z.W.2    Chin, J.H.3    Hoffman, B.B.4
  • 185
    • 57549118558 scopus 로고    scopus 로고
    • The pharmacological challenge to tame the transient receptor potential vanilloid-1 (TRPV1) nocisensor
    • P. Holzer The pharmacological challenge to tame the transient receptor potential vanilloid-1 (TRPV1) nocisensor Br. J. Pharmacol. 155 2008 1145
    • (2008) Br. J. Pharmacol. , vol.155 , pp. 1145
    • Holzer, P.1
  • 186
    • 0029558130 scopus 로고
    • Ceramide formation during heat shock: A potential mediator of alpha B-crystallin transcription
    • Y. Chang, A. Abe, and J.A. Shayman Ceramide formation during heat shock: a potential mediator of alpha B-crystallin transcription Proc. Natl. Acad. Sci. U. S. A. 92 1995 12275
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 12275
    • Chang, Y.1    Abe, A.2    Shayman, J.A.3
  • 187
    • 34250851353 scopus 로고    scopus 로고
    • Doxorubicin enhances TRAIL-induced cell death via ceramide-enriched membrane platforms
    • C.A. Dumitru, A. Carpinteiro, T. Trarbach, U.R. Hengge, and E. Gulbins Doxorubicin enhances TRAIL-induced cell death via ceramide-enriched membrane platforms Apoptosis 12 2007 1533
    • (2007) Apoptosis , vol.12 , pp. 1533
    • Dumitru, C.A.1    Carpinteiro, A.2    Trarbach, T.3    Hengge, U.R.4    Gulbins, E.5
  • 189
    • 34249657837 scopus 로고    scopus 로고
    • Activation of acid sphingomyelinase by protein kinase Cdelta-mediated phosphorylation
    • Y.H. Zeidan, and Y.A. Hannun Activation of acid sphingomyelinase by protein kinase Cdelta-mediated phosphorylation J. Biol. Chem. 282 2007 11549
    • (2007) J. Biol. Chem. , vol.282 , pp. 11549
    • Zeidan, Y.H.1    Hannun, Y.A.2
  • 190
    • 38549152194 scopus 로고    scopus 로고
    • Principles of bioactive lipid signalling: Lessons from sphingolipids
    • Y.A. Hannun, and L.M. Obeid Principles of bioactive lipid signalling: lessons from sphingolipids Nat. Rev. Mol. Cell Biol. 9 2008 139
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 139
    • Hannun, Y.A.1    Obeid, L.M.2
  • 191
    • 50049090026 scopus 로고    scopus 로고
    • Ceramidases: Regulators of cellular responses mediated by ceramide, sphingosine, and sphingosine-1-phosphate
    • C. Mao, and L.M. Obeid Ceramidases: regulators of cellular responses mediated by ceramide, sphingosine, and sphingosine-1-phosphate Biochim. Biophys. Acta 1781 2008 424
    • (2008) Biochim. Biophys. Acta , vol.1781 , pp. 424
    • Mao, C.1    Obeid, L.M.2
  • 192
    • 0033178453 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate regulates heat shock protein 27 induction by a p38 MAP kinase-dependent mechanism in aortic smooth muscle cells
    • O. Kozawa, K. Tanabe, H. Ito, H. Matsuno, M. Niwa, K. Kato, and T. Uematsu Sphingosine 1-phosphate regulates heat shock protein 27 induction by a p38 MAP kinase-dependent mechanism in aortic smooth muscle cells Exp. Cell Res. 250 1999 376
    • (1999) Exp. Cell Res. , vol.250 , pp. 376
    • Kozawa, O.1    Tanabe, K.2    Ito, H.3    Matsuno, H.4    Niwa, M.5    Kato, K.6    Uematsu, T.7
  • 193
    • 33746437999 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase/Akt plays a role in sphingosine 1-phosphate-stimulated HSP27 induction in osteoblasts
    • S. Takai, H. Tokuda, R. Matsushima-Nishiwaki, Y. Hanai, K. Kato, and O. Kozawa Phosphatidylinositol 3-kinase/Akt plays a role in sphingosine 1-phosphate-stimulated HSP27 induction in osteoblasts J. Cell. Biochem. 98 2006 1249
    • (2006) J. Cell. Biochem. , vol.98 , pp. 1249
    • Takai, S.1    Tokuda, H.2    Matsushima-Nishiwaki, R.3    Hanai, Y.4    Kato, K.5    Kozawa, O.6
  • 196
    • 34250742501 scopus 로고    scopus 로고
    • Biological aspects of ceramide-enriched membrane domains
    • H. Grassme, J. Riethmuller, and E. Gulbins Biological aspects of ceramide-enriched membrane domains Prog. Lipid Res. 46 2007 161
    • (2007) Prog. Lipid Res. , vol.46 , pp. 161
    • Grassme, H.1    Riethmuller, J.2    Gulbins, E.3
  • 197
    • 33644555869 scopus 로고    scopus 로고
    • Sphingolipids differentially regulate mitogen-activated protein kinases and intracellular Ca2 + in vascular smooth muscle: Effects on CREB activation
    • F.A. Mathieson, and G.F. Nixon Sphingolipids differentially regulate mitogen-activated protein kinases and intracellular Ca2 + in vascular smooth muscle: effects on CREB activation Br. J. Pharmacol. 147 2006 351
    • (2006) Br. J. Pharmacol. , vol.147 , pp. 351
    • Mathieson, F.A.1    Nixon, G.F.2
  • 199
    • 0026739577 scopus 로고
    • In vitro activation of heat shock transcription factor by 4-hydroxynonenal
    • F. Cajone, and M. Crescente In vitro activation of heat shock transcription factor by 4-hydroxynonenal Chem. Biol. Interact. 84 1992 97
    • (1992) Chem. Biol. Interact. , vol.84 , pp. 97
    • Cajone, F.1    Crescente, M.2
  • 200
    • 36348938843 scopus 로고    scopus 로고
    • Heat shock factor 1 attenuates 4-Hydroxynonenal-mediated apoptosis: Critical role for heat shock protein 70 induction and stabilization of Bcl-XL
    • A.T. Jacobs, and L.J. Marnett Heat shock factor 1 attenuates 4-Hydroxynonenal-mediated apoptosis: critical role for heat shock protein 70 induction and stabilization of Bcl-XL J. Biol. Chem. 282 2007 33412
    • (2007) J. Biol. Chem. , vol.282 , pp. 33412
    • Jacobs, A.T.1    Marnett, L.J.2
  • 202
    • 37848999061 scopus 로고    scopus 로고
    • 4-Hydroxynonenal self-limits fas-mediated DISC-independent apoptosis by promoting export of Daxx from the nucleus to the cytosol and its binding to Fas
    • R. Sharma, A. Sharma, S. Dwivedi, P. Zimniak, S. Awasthi, and Y.C. Awasthi 4-Hydroxynonenal self-limits fas-mediated DISC-independent apoptosis by promoting export of Daxx from the nucleus to the cytosol and its binding to Fas Biochemistry 47 2008 143
    • (2008) Biochemistry , vol.47 , pp. 143
    • Sharma, R.1    Sharma, A.2    Dwivedi, S.3    Zimniak, P.4    Awasthi, S.5    Awasthi, Y.C.6
  • 203
    • 84885448184 scopus 로고    scopus 로고
    • Crotonaldehyde induces heat shock protein 72 expression that mediates anti-apoptotic effects in human endothelial cells
    • D.S. Ryu, H. Yang, S.E. Lee, C.S. Park, Y.H. Jin, and Y.S. Park Crotonaldehyde induces heat shock protein 72 expression that mediates anti-apoptotic effects in human endothelial cells Toxicol. Lett. 223 2013 116
    • (2013) Toxicol. Lett. , vol.223 , pp. 116
    • Ryu, D.S.1    Yang, H.2    Lee, S.E.3    Park, C.S.4    Jin, Y.H.5    Park, Y.S.6
  • 205
    • 0032528185 scopus 로고    scopus 로고
    • Enhanced expression of heat shock protein 70 (hsp70) and heat shock factor 1 (HSF1) activation in rheumatoid arthritis synovial tissue. Differential regulation of hsp70 expression and hsf1 activation in synovial fibroblasts by proinflammatory cytokines, shear stress, and antiinflammatory drugs
    • G. Schett, K. Redlich, Q. Xu, P. Bizan, M. Groger, M. Tohidast-Akrad, H. Kiener, J. Smolen, and G. Steiner Enhanced expression of heat shock protein 70 (hsp70) and heat shock factor 1 (HSF1) activation in rheumatoid arthritis synovial tissue. Differential regulation of hsp70 expression and hsf1 activation in synovial fibroblasts by proinflammatory cytokines, shear stress, and antiinflammatory drugs J. Clin. Invest. 102 1998 302
    • (1998) J. Clin. Invest. , vol.102 , pp. 302
    • Schett, G.1    Redlich, K.2    Xu, Q.3    Bizan, P.4    Groger, M.5    Tohidast-Akrad, M.6    Kiener, H.7    Smolen, J.8    Steiner, G.9
  • 208
    • 0342890792 scopus 로고
    • Adaptation of membrane fluidity of rye and wheat seedlings according to temperature
    • L. Vigh, I. Horvath, T. Farkas, L.I. Horvath, and A. Belea Adaptation of membrane fluidity of rye and wheat seedlings according to temperature Phytochemistry 18 1979 787
    • (1979) Phytochemistry , vol.18 , pp. 787
    • Vigh, L.1    Horvath, I.2    Farkas, T.3    Horvath, L.I.4    Belea, A.5
  • 209
    • 79551664341 scopus 로고    scopus 로고
    • Membrane lipid composition affects plant heat sensing and modulates Ca (2 +)-dependent heat shock response
    • Y. Saidi, M. Peter, A. Finka, C. Cicekli, L. Vigh, and P. Goloubinoff Membrane lipid composition affects plant heat sensing and modulates Ca (2 +)-dependent heat shock response Plant Signal. Behav. 5 2010
    • (2010) Plant Signal. Behav. , vol.5
    • Saidi, Y.1    Peter, M.2    Finka, A.3    Cicekli, C.4    Vigh, L.5    Goloubinoff, P.6
  • 215
    • 32644441610 scopus 로고    scopus 로고
    • Exogenous heat shock protein 70 binds macrophage lipid raft microdomain and stimulates phagocytosis, processing, and MHC-II presentation of antigens
    • R.B. Wang, J.T. Kovalchin, P. Muhlenkamp, and R.Y. Chandawarkar Exogenous heat shock protein 70 binds macrophage lipid raft microdomain and stimulates phagocytosis, processing, and MHC-II presentation of antigens Blood 107 2006 1636
    • (2006) Blood , vol.107 , pp. 1636
    • Wang, R.B.1    Kovalchin, J.T.2    Muhlenkamp, P.3    Chandawarkar, R.Y.4
  • 216
    • 0037484291 scopus 로고    scopus 로고
    • Expression of the molecular chaperone Hsp70 in detergent-resistant microdomains correlates with its membrane delivery and release
    • A.H. Broquet, G. Thomas, J. Masliah, G. Trugnan, and M. Bachelet Expression of the molecular chaperone Hsp70 in detergent-resistant microdomains correlates with its membrane delivery and release J. Biol. Chem. 278 2003 21601
    • (2003) J. Biol. Chem. , vol.278 , pp. 21601
    • Broquet, A.H.1    Thomas, G.2    Masliah, J.3    Trugnan, G.4    Bachelet, M.5
  • 217
    • 77949670044 scopus 로고    scopus 로고
    • Genetic modification of the Salmonella membrane physical state alters the pattern of heat shock response
    • A. Porta, Z. Torok, I. Horvath, S. Franceschelli, L. Vigh, and B. Maresca Genetic modification of the Salmonella membrane physical state alters the pattern of heat shock response J. Bacteriol. 192 2010 1988
    • (2010) J. Bacteriol. , vol.192 , pp. 1988
    • Porta, A.1    Torok, Z.2    Horvath, I.3    Franceschelli, S.4    Vigh, L.5    Maresca, B.6
  • 218
    • 33646910257 scopus 로고    scopus 로고
    • Biochemical characterization of a delta12 acyl-lipid desaturase after overexpression of the enzyme in Escherichia coli
    • S. Panpoom, D.A. Los, and N. Murata Biochemical characterization of a delta12 acyl-lipid desaturase after overexpression of the enzyme in Escherichia coli Biochim. Biophys. Acta 1390 1998 323
    • (1998) Biochim. Biophys. Acta , vol.1390 , pp. 323
    • Panpoom, S.1    Los, D.A.2    Murata, N.3
  • 219
    • 84877879914 scopus 로고    scopus 로고
    • Endothelial cell and model membranes respond to shear stress by rapidly decreasing the order of their lipid phases
    • K. Yamamoto, and J. Ando Endothelial cell and model membranes respond to shear stress by rapidly decreasing the order of their lipid phases J. Cell Sci. 126 2013 1227
    • (2013) J. Cell Sci. , vol.126 , pp. 1227
    • Yamamoto, K.1    Ando, J.2
  • 220
    • 0018348831 scopus 로고
    • Relationship of growth temperature and thermotropic lipid phase-changes in cytoplasmic and outer membranes from Escherichia-coli-K12
    • A.S. Janoff, A. Haug, and E.J. Mcgroarty Relationship of growth temperature and thermotropic lipid phase-changes in cytoplasmic and outer membranes from Escherichia-coli-K12 Biochim. Biophys. Acta 555 1979 56
    • (1979) Biochim. Biophys. Acta , vol.555 , pp. 56
    • Janoff, A.S.1    Haug, A.2    McGroarty, E.J.3
  • 221
    • 29144469368 scopus 로고    scopus 로고
    • Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones
    • A. de Marco, L. Vigh, S. Diamant, and P. Goloubinoff Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones Cell Stress Chaperones 10 2005 329
    • (2005) Cell Stress Chaperones , vol.10 , pp. 329
    • De Marco, A.1    Vigh, L.2    Diamant, S.3    Goloubinoff, P.4
  • 222
    • 0028838436 scopus 로고
    • Matrix-assisted laser-desorption ionization mass-spectrometry (MALDI-MS)
    • J.T. Stults Matrix-assisted laser-desorption ionization mass-spectrometry (MALDI-MS) Curr. Opin. Struct. Biol. 5 1995 691
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 691
    • Stults, J.T.1
  • 223
    • 0034120638 scopus 로고    scopus 로고
    • Matrix assisted laser desorption/ionization-time of flight-mass spectrometry analysis of proteins detected by anti-phosphotyrosine antibody on two-dimensional-gels of fibrolast cell lysates after tumor necrosis factor-alpha stimulation
    • M. Yanagida, Y. Miura, K. Yagasaki, M. Taoka, T. Isobe, and N. Takahashi Matrix assisted laser desorption/ionization-time of flight-mass spectrometry analysis of proteins detected by anti-phosphotyrosine antibody on two-dimensional-gels of fibrolast cell lysates after tumor necrosis factor-alpha stimulation Electrophoresis 21 2000 1890
    • (2000) Electrophoresis , vol.21 , pp. 1890
    • Yanagida, M.1    Miura, Y.2    Yagasaki, K.3    Taoka, M.4    Isobe, T.5    Takahashi, N.6
  • 225
    • 21244435631 scopus 로고    scopus 로고
    • The PhoP/PhoQ system controls the intramacrophage type three secretion system of Salmonella enterica
    • J.J. Bijlsma, and E.A. Groisman The PhoP/PhoQ system controls the intramacrophage type three secretion system of Salmonella enterica Mol. Microbiol. 57 2005 85
    • (2005) Mol. Microbiol. , vol.57 , pp. 85
    • Bijlsma, J.J.1    Groisman, E.A.2
  • 226
    • 44649203366 scopus 로고    scopus 로고
    • The Salmonella PmrAB regulon: Lipopolysaccharide modifications, antimicrobial peptide resistance and more
    • J.S. Gunn The Salmonella PmrAB regulon: lipopolysaccharide modifications, antimicrobial peptide resistance and more Trends Microbiol. 16 2008 284
    • (2008) Trends Microbiol. , vol.16 , pp. 284
    • Gunn, J.S.1
  • 231
    • 0028834230 scopus 로고
    • A temperature-sensitive strain of histoplasma-capsulatum has an altered delta(9)-fatty acid desaturase gene
    • S. Gargano, G. Dilallo, G.S. Kobayashi, and B. Maresca A temperature-sensitive strain of histoplasma-capsulatum has an altered delta(9)-fatty acid desaturase gene Lipids 30 1995 899
    • (1995) Lipids , vol.30 , pp. 899
    • Gargano, S.1    Dilallo, G.2    Kobayashi, G.S.3    Maresca, B.4
  • 232
    • 0029816651 scopus 로고    scopus 로고
    • Cellular immune responses to recombinant heat shock protein 70 from Histoplasma capsulatum
    • R. Allendoerfer, B. Maresca, and G.S. Deepe Cellular immune responses to recombinant heat shock protein 70 from Histoplasma capsulatum Infect. Immun. 64 1996 4123
    • (1996) Infect. Immun. , vol.64 , pp. 4123
    • Allendoerfer, R.1    Maresca, B.2    Deepe, G.S.3
  • 233
    • 0028173175 scopus 로고
    • Hsp70 in parasites - As an inducible protective protein and as an antigen
    • B. Maresca, and G.S. Kobayashi Hsp70 in parasites - as an inducible protective protein and as an antigen Experientia 50 1994 1067
    • (1994) Experientia , vol.50 , pp. 1067
    • Maresca, B.1    Kobayashi, G.S.2
  • 234
    • 33748627985 scopus 로고    scopus 로고
    • The PhoP/PhoQ two-component system stabilizes the alternative sigma factor RpoS in Salmonella enterica
    • X. Tu, T. Latifi, A. Bougdour, S. Gottesman, and E.A. Groisman The PhoP/PhoQ two-component system stabilizes the alternative sigma factor RpoS in Salmonella enterica Proc. Natl. Acad. Sci. U. S. A. 103 2006 13503
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 13503
    • Tu, X.1    Latifi, T.2    Bougdour, A.3    Gottesman, S.4    Groisman, E.A.5
  • 236
    • 34250561475 scopus 로고
    • A new puffing pattern induced by temperature shock and DNP in Drosophila
    • F. Ritossa A new puffing pattern induced by temperature shock and DNP in Drosophila Experientia 18 1962 571
    • (1962) Experientia , vol.18 , pp. 571
    • Ritossa, F.1
  • 237
    • 0023732689 scopus 로고
    • Hyperthermia protects against light damage in the rat retina
    • M.F. Barbe, M. Tytell, D.J. Gower, and W.J. Welch Hyperthermia protects against light damage in the rat retina Science 241 1988 1817
    • (1988) Science , vol.241 , pp. 1817
    • Barbe, M.F.1    Tytell, M.2    Gower, D.J.3    Welch, W.J.4
  • 238
    • 0036086736 scopus 로고    scopus 로고
    • Optimal timing and temperature for hyperthermic preconditioning in an animal model of fecal peritonitis
    • B.M. Gulluoglu, B.S. Aksoy, E.S. Ozveri, M. Yuksel, E.E. Demiralp, and A.O. Aktan Optimal timing and temperature for hyperthermic preconditioning in an animal model of fecal peritonitis J. Invest. Surg. 15 2002 117
    • (2002) J. Invest. Surg. , vol.15 , pp. 117
    • Gulluoglu, B.M.1    Aksoy, B.S.2    Ozveri, E.S.3    Yuksel, M.4    Demiralp, E.E.5    Aktan, A.O.6
  • 239
    • 0036250141 scopus 로고    scopus 로고
    • Neuroprotective effects of hyperthermic preconditioning on infarcted volume after middle cerebral artery occlusion in rats: Role of adenosine receptors
    • H. Xu, M. Aibiki, and J. Nagoya Neuroprotective effects of hyperthermic preconditioning on infarcted volume after middle cerebral artery occlusion in rats: role of adenosine receptors Crit. Care Med. 30 2002 1126
    • (2002) Crit. Care Med. , vol.30 , pp. 1126
    • Xu, H.1    Aibiki, M.2    Nagoya, J.3
  • 240
    • 0032491193 scopus 로고    scopus 로고
    • Whole-body hyperthermia provides biphasic cardioprotection against ischemia/reperfusion injury in the rat
    • N. Yamashita, S. Hoshida, N. Taniguchi, T. Kuzuya, and M. Hori Whole-body hyperthermia provides biphasic cardioprotection against ischemia/reperfusion injury in the rat Circulation 98 1998 1414
    • (1998) Circulation , vol.98 , pp. 1414
    • Yamashita, N.1    Hoshida, S.2    Taniguchi, N.3    Kuzuya, T.4    Hori, M.5
  • 247
    • 0033575998 scopus 로고    scopus 로고
    • Hot-tub therapy for type 2 diabetes mellitus
    • P.L. Hooper Hot-tub therapy for type 2 diabetes mellitus N. Engl. J. Med. 341 1999 924
    • (1999) N. Engl. J. Med. , vol.341 , pp. 924
    • Hooper, P.L.1
  • 251
    • 0033631841 scopus 로고    scopus 로고
    • Cecal ligation and double puncture impairs heat shock protein 70 (HSP-70) expression in the lungs of rats
    • Y.G. Weiss, A. Bouwman, B. Gehan, G. Schears, N. Raj, and C.S. Deutschman Cecal ligation and double puncture impairs heat shock protein 70 (HSP-70) expression in the lungs of rats Shock 13 2000 19
    • (2000) Shock , vol.13 , pp. 19
    • Weiss, Y.G.1    Bouwman, A.2    Gehan, B.3    Schears, G.4    Raj, N.5    Deutschman, C.S.6
  • 252
    • 33745528140 scopus 로고    scopus 로고
    • Proteomic analysis of altered protein expression in skeletal muscle of rats in a hypermetabolic state induced by burn sepsis
    • X.B. Duan, F. Berthiaume, D. Yarmush, and M.L. Yarmush Proteomic analysis of altered protein expression in skeletal muscle of rats in a hypermetabolic state induced by burn sepsis Biochem. J. 397 2006 149
    • (2006) Biochem. J. , vol.397 , pp. 149
    • Duan, X.B.1    Berthiaume, F.2    Yarmush, D.3    Yarmush, M.L.4
  • 253
    • 77955710022 scopus 로고    scopus 로고
    • Ascitic fluid and serum from rats with acute pancreatitis injure rat pancreatic tissues and alter the expression of heat shock protein 60
    • Y.Y. Li, X.J. Li, S.A. Lv, K. Li, Y.N. Li, Z.R. Gao, J.Y. Feng, C.J. Chen, and C. Schaefer Ascitic fluid and serum from rats with acute pancreatitis injure rat pancreatic tissues and alter the expression of heat shock protein 60 Cell Stress Chaperones 15 2010 583
    • (2010) Cell Stress Chaperones , vol.15 , pp. 583
    • Li, Y.Y.1    Li, X.J.2    Lv, S.A.3    Li, K.4    Li, Y.N.5    Gao, Z.R.6    Feng, J.Y.7    Chen, C.J.8    Schaefer, C.9
  • 254
    • 14844356006 scopus 로고    scopus 로고
    • Loss of defense against stress: Diabetes and heat shock proteins
    • P.L. Hooper, and J.J. Hooper Loss of defense against stress: diabetes and heat shock proteins Diabetes Technol. Ther. 7 2005 204
    • (2005) Diabetes Technol. Ther. , vol.7 , pp. 204
    • Hooper, P.L.1    Hooper, J.J.2
  • 255
    • 0036227062 scopus 로고    scopus 로고
    • Decreased expression of heat shock protein 72 in skeletal muscle of patients with type 2 diabetes correlates with insulin resistance
    • I. Kurucz, A. Morva, A. Vaag, K.F. Eriksson, X.D. Huang, L. Groop, and L. Koranyi Decreased expression of heat shock protein 72 in skeletal muscle of patients with type 2 diabetes correlates with insulin resistance Diabetes 51 2002 1102
    • (2002) Diabetes , vol.51 , pp. 1102
    • Kurucz, I.1    Morva, A.2    Vaag, A.3    Eriksson, K.F.4    Huang, X.D.5    Groop, L.6    Koranyi, L.7
  • 256
    • 36549058329 scopus 로고    scopus 로고
    • Translational inhibition of colonic epithelial heat shock proteins by IFN-gamma and TNF-alpha in intestinal inflammation
    • S. Hu, M.J. Ciancio, M. Lahav, M. Fujiya, L. Lichtenstein, S. Anant, M.W. Musch, and E.B. Chang Translational inhibition of colonic epithelial heat shock proteins by IFN-gamma and TNF-alpha in intestinal inflammation Gastroenterology 133 2007 1893
    • (2007) Gastroenterology , vol.133 , pp. 1893
    • Hu, S.1    Ciancio, M.J.2    Lahav, M.3    Fujiya, M.4    Lichtenstein, L.5    Anant, S.6    Musch, M.W.7    Chang, E.B.8
  • 257
    • 4544373279 scopus 로고    scopus 로고
    • Heat shock proteins 60 and 70 expression of cutaneous lichen planus: Comparison with normal skin and psoriasis vulgaris
    • D. Bayramgurler, S.K. Ozkara, R. Apaydin, C. Ercin, and N. Bilen Heat shock proteins 60 and 70 expression of cutaneous lichen planus: comparison with normal skin and psoriasis vulgaris J. Cutan. Pathol. 31 2004 586
    • (2004) J. Cutan. Pathol. , vol.31 , pp. 586
    • Bayramgurler, D.1    Ozkara, S.K.2    Apaydin, R.3    Ercin, C.4    Bilen, N.5
  • 258
  • 262
    • 77951798140 scopus 로고    scopus 로고
    • Reduced heat shock protein 70 in airway smooth muscle in patients with chronic obstructive pulmonary disease
    • J.G. Xie, J.P. Zhao, C.F. Xiao, Y.J. Xu, S.F. Yang, and W. Ni Reduced heat shock protein 70 in airway smooth muscle in patients with chronic obstructive pulmonary disease Exp. Lung Res. 36 2010 219
    • (2010) Exp. Lung Res. , vol.36 , pp. 219
    • Xie, J.G.1    Zhao, J.P.2    Xiao, C.F.3    Xu, Y.J.4    Yang, S.F.5    Ni, W.6
  • 263
    • 35548998775 scopus 로고    scopus 로고
    • Chaperonopathies by defect, excess, or mistake
    • A.J. Macario, and M.E. Conway de Chaperonopathies by defect, excess, or mistake Ann. N. Y. Acad. Sci. 1113 2007 178
    • (2007) Ann. N. Y. Acad. Sci. , vol.1113 , pp. 178
    • Macario, A.J.1    De Conway, M.E.2
  • 264
    • 78650009053 scopus 로고    scopus 로고
    • Advanced drug delivery of N-acetylcarnosine (N-acetyl-beta-alanyl-L- histidine), carcinine (beta-alanylhistamine) and L-carnosine (beta-alanyl-L-histidine) in targeting peptide compounds as pharmacological chaperones for use in tissue engineering, human disease management and therapy: From in vitro to the clinic
    • M.A. Babizhayev, and Y.E. Yegorov Advanced drug delivery of N-acetylcarnosine (N-acetyl-beta-alanyl-L-histidine), carcinine (beta-alanylhistamine) and L-carnosine (beta-alanyl-L-histidine) in targeting peptide compounds as pharmacological chaperones for use in tissue engineering, human disease management and therapy: from in vitro to the clinic Recent Pat Drug Deliv. Formul. 4 2010 198
    • (2010) Recent Pat Drug Deliv. Formul. , vol.4 , pp. 198
    • Babizhayev, M.A.1    Yegorov, Y.E.2
  • 268
    • 84866684724 scopus 로고    scopus 로고
    • Tolerogenic dendritic cells that inhibit autoimmune arthritis can be induced by a combination of carvacrol and thermal stress
    • R. Spiering, Z.R. van der, J. Wagenaar, D. Kapetis, F. Zolezzi, E.W. van, and F. Broere Tolerogenic dendritic cells that inhibit autoimmune arthritis can be induced by a combination of carvacrol and thermal stress PLoS One 7 2012 e46336
    • (2012) PLoS One , vol.7 , pp. 46336
    • Spiering, R.1    Van Der, Z.R.2    Wagenaar, J.3    Kapetis, D.4    Zolezzi, F.5    Van, E.W.6    Broere, F.7
  • 271
  • 272
    • 84868146609 scopus 로고    scopus 로고
    • Loss of stress response as a consequence of viral infection: Implications for disease and therapy
    • P.L. Hooper, L.E. Hightower, and P.L. Hooper Loss of stress response as a consequence of viral infection: implications for disease and therapy Cell Stress Chaperones 17 2012 647
    • (2012) Cell Stress Chaperones , vol.17 , pp. 647
    • Hooper, P.L.1    Hightower, L.E.2    Hooper, P.L.3
  • 274
    • 77950653993 scopus 로고    scopus 로고
    • Waon therapy for cardiovascular disease - Innovative therapy for the 21(st) century
    • M. Miyata, and C. Tei Waon therapy for cardiovascular disease - innovative therapy for the 21(st) century Circ. J. 74 2010 617
    • (2010) Circ. J. , vol.74 , pp. 617
    • Miyata, M.1    Tei, C.2
  • 275
    • 84867482908 scopus 로고    scopus 로고
    • Role of the transient receptor potential vanilloid type 1 receptor and stretch-activated ion channels in nitric oxide release from endothelial cells of the aorta and heart in rats
    • J.C. Torres-Narvaez, L.D. Mondragon, E.V. Lopez, I. Perez-Torres, J.A.D. Juarez, J. Suarez, and G.P. Hernandez Role of the transient receptor potential vanilloid type 1 receptor and stretch-activated ion channels in nitric oxide release from endothelial cells of the aorta and heart in rats Exp. Clin. Cardiol. 17 2012 89
    • (2012) Exp. Clin. Cardiol. , vol.17 , pp. 89
    • Torres-Narvaez, J.C.1    Mondragon, L.D.2    Lopez, E.V.3    Perez-Torres, I.4    Juarez, J.A.D.5    Suarez, J.6    Hernandez, G.P.7
  • 276
    • 25144469765 scopus 로고    scopus 로고
    • Geranylgeranylacetone protects membranes against nonsteroidal anti-inflammatory drugs
    • H. Ushijima, K. Tanaka, M. Takeda, T. Katsu, S. Mima, and T. Mizushima Geranylgeranylacetone protects membranes against nonsteroidal anti-inflammatory drugs Mol. Pharmacol. 68 2005 1156
    • (2005) Mol. Pharmacol. , vol.68 , pp. 1156
    • Ushijima, H.1    Tanaka, K.2    Takeda, M.3    Katsu, T.4    Mima, S.5    Mizushima, T.6
  • 277
    • 78149467191 scopus 로고    scopus 로고
    • Xenohormesis: Health benefits from an eon of plant stress response evolution
    • P.L. Hooper, P.L. Hooper, M. Tytell, and L. Vigh Xenohormesis: health benefits from an eon of plant stress response evolution Cell Stress Chaperones 15 2010 761
    • (2010) Cell Stress Chaperones , vol.15 , pp. 761
    • Hooper, P.L.1    Hooper, P.L.2    Tytell, M.3    Vigh, L.4
  • 278
    • 67349132352 scopus 로고    scopus 로고
    • Adaptogens exert a stress-protective effect by modulation of expression of molecular chaperones
    • A. Panossian, G. Wikman, P. Kaur, and A. Asea Adaptogens exert a stress-protective effect by modulation of expression of molecular chaperones Phytomedicine 16 2009 617
    • (2009) Phytomedicine , vol.16 , pp. 617
    • Panossian, A.1    Wikman, G.2    Kaur, P.3    Asea, A.4
  • 279
    • 77957901415 scopus 로고    scopus 로고
    • Heat shock proteins (chaperones) in fish and shellfish and their potential role in relation to fish health: A review
    • R.J. Roberts, C. Agius, C. Saliba, P. Bossier, and Y.Y. Sung Heat shock proteins (chaperones) in fish and shellfish and their potential role in relation to fish health: a review J. Fish Dis. 33 2010 789
    • (2010) J. Fish Dis. , vol.33 , pp. 789
    • Roberts, R.J.1    Agius, C.2    Saliba, C.3    Bossier, P.4    Sung, Y.Y.5
  • 280
    • 3042635548 scopus 로고    scopus 로고
    • Effect of Opuntia ficus indica on symptoms of the alcohol hangover
    • J. Wiese, S. McPherson, M.C. Odden, and M.G. Shlipak Effect of Opuntia ficus indica on symptoms of the alcohol hangover Arch. Intern. Med. 164 2004 1334
    • (2004) Arch. Intern. Med. , vol.164 , pp. 1334
    • Wiese, J.1    McPherson, S.2    Odden, M.C.3    Shlipak, M.G.4
  • 284
    • 0030760940 scopus 로고    scopus 로고
    • Bimoclomol (BRLP-42) ameliorates peripheral neuropathy in streptozotocin-induced diabetic rats
    • K. Biro, A. Jednakovits, T. Kukorelli, E. Hegedus, and L. Koranyi Bimoclomol (BRLP-42) ameliorates peripheral neuropathy in streptozotocin-induced diabetic rats Brain Res. Bull. 44 1997 259
    • (1997) Brain Res. Bull. , vol.44 , pp. 259
    • Biro, K.1    Jednakovits, A.2    Kukorelli, T.3    Hegedus, E.4    Koranyi, L.5
  • 285
    • 0032557842 scopus 로고    scopus 로고
    • Bimoclomol improves early electrophysiological signs of retinopathy in diabetic rats
    • K. Biro, J. Palhalmi, A.J. Toth, T. Kukorelli, and G. Juhasz Bimoclomol improves early electrophysiological signs of retinopathy in diabetic rats Neuroreport 9 1998 2029
    • (1998) Neuroreport , vol.9 , pp. 2029
    • Biro, K.1    Palhalmi, J.2    Toth, A.J.3    Kukorelli, T.4    Juhasz, G.5
  • 287
    • 0033954867 scopus 로고    scopus 로고
    • BGP-15, a nicotinic amidoxime derivate protecting heart from ischemia reperfusion injury through modulation of poly(ADP-ribose) polymerase
    • E. Szabados, P. Literati-Nagy, B. Farkas, and B. Sumegi BGP-15, a nicotinic amidoxime derivate protecting heart from ischemia reperfusion injury through modulation of poly(ADP-ribose) polymerase Biochem. Pharmacol. 59 2000 937
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 937
    • Szabados, E.1    Literati-Nagy, P.2    Farkas, B.3    Sumegi, B.4
  • 289
    • 0031964929 scopus 로고    scopus 로고
    • Bimoclomol protects against vascular consequences of experimental subarachnoid hemorrhage in rats
    • F. Erdo, and S.L. Erdo Bimoclomol protects against vascular consequences of experimental subarachnoid hemorrhage in rats Brain Res. Bull. 45 1998 163
    • (1998) Brain Res. Bull. , vol.45 , pp. 163
    • Erdo, F.1    Erdo, S.L.2
  • 292
    • 0034714508 scopus 로고    scopus 로고
    • Effect of subchronic bimoclomol treatment on vascular responsiveness and heat shock protein production in spontaneously hypertensive rats
    • A. Jednakovits, I. Kurucz, and P.P. Nanasi Effect of subchronic bimoclomol treatment on vascular responsiveness and heat shock protein production in spontaneously hypertensive rats Life Sci. 67 2000 1791
    • (2000) Life Sci. , vol.67 , pp. 1791
    • Jednakovits, A.1    Kurucz, I.2    Nanasi, P.P.3
  • 294
    • 77954106884 scopus 로고    scopus 로고
    • Arimoclomol, a coinducer of heat shock proteins for the potential treatment of amyotrophic lateral sclerosis
    • J. Phukan Arimoclomol, a coinducer of heat shock proteins for the potential treatment of amyotrophic lateral sclerosis Idrugs 13 2010 482
    • (2010) Idrugs , vol.13 , pp. 482
    • Phukan, J.1
  • 295
    • 84934435239 scopus 로고    scopus 로고
    • A heat-shock protein co-inducer treatment improves behavioral performance in rats exposed to hypoxia
    • (Xxxii)
    • K. Xu, X.Y. Sun, B.O. Erokwu, I. Cernak, and J.C. LaManna A heat-shock protein co-inducer treatment improves behavioral performance in rats exposed to hypoxia Oxygen Transp. Tissue 701 2011 313 (Xxxii)
    • (2011) Oxygen Transp. Tissue , vol.701 , pp. 313
    • Xu, K.1    Sun, X.Y.2    Erokwu, B.O.3    Cernak, I.4    Lamanna, J.C.5
  • 297
    • 78149464449 scopus 로고    scopus 로고
    • Neuroprotective effect of small heat shock protein, Hsp27, after acute and chronic alcohol administration
    • M.E. Toth, S. Gonda, L. Vigh, and M. Santha Neuroprotective effect of small heat shock protein, Hsp27, after acute and chronic alcohol administration Cell Stress Chaperones 15 2010 807
    • (2010) Cell Stress Chaperones , vol.15 , pp. 807
    • Toth, M.E.1    Gonda, S.2    Vigh, L.3    Santha, M.4
  • 300
    • 77954760957 scopus 로고    scopus 로고
    • Heat shock protein 70 protects against bleomycin-induced pulmonary fibrosis in mice
    • K.I. Tanaka, Y. Tanaka, T. Namba, A. Azuma, and T. Mizushima Heat shock protein 70 protects against bleomycin-induced pulmonary fibrosis in mice Biochem. Pharmacol. 80 2010 920
    • (2010) Biochem. Pharmacol. , vol.80 , pp. 920
    • Tanaka, K.I.1    Tanaka, Y.2    Namba, T.3    Azuma, A.4    Mizushima, T.5
  • 303
    • 51449117213 scopus 로고    scopus 로고
    • Low-dose sevoflurane inhalation enhances late cardioprotection from the anti-ulcer drug geranylgeranylacetone
    • H. Kitahata, J. Nozaki, S. Kawahito, T. Tomino, and S. Oshita Low-dose sevoflurane inhalation enhances late cardioprotection from the anti-ulcer drug geranylgeranylacetone Anesth. Analg. 107 2008 755
    • (2008) Anesth. Analg. , vol.107 , pp. 755
    • Kitahata, H.1    Nozaki, J.2    Kawahito, S.3    Tomino, T.4    Oshita, S.5
  • 304
    • 57849122454 scopus 로고    scopus 로고
    • Geranylgeranylacetone prevents acute liver damage after massive hepatectomy in rats through suppression of a CXC chemokine GRO1 and induction of heat shock proteins
    • H. Kanemura, K. Kusumoto, H. Miyake, S. Tashiro, K. Rokutan, and M. Shimada Geranylgeranylacetone prevents acute liver damage after massive hepatectomy in rats through suppression of a CXC chemokine GRO1 and induction of heat shock proteins J. Gastrointest. Surg. 13 2009 66
    • (2009) J. Gastrointest. Surg. , vol.13 , pp. 66
    • Kanemura, H.1    Kusumoto, K.2    Miyake, H.3    Tashiro, S.4    Rokutan, K.5    Shimada, M.6
  • 306
    • 33846703692 scopus 로고    scopus 로고
    • Pharmacological induction of heat shock protein exerts neuroprotective effects in experimental intracerebral hemorrhage
    • D.I. Sinn, K. Chu, S.T. Lee, E.C. Song, K.H. Jung, E.H. Kim, D.K. Park, K.M. Kang, M. Kim, and J.K. Roh Pharmacological induction of heat shock protein exerts neuroprotective effects in experimental intracerebral hemorrhage Brain Res. 1135 2007 167
    • (2007) Brain Res. , vol.1135 , pp. 167
    • Sinn, D.I.1    Chu, K.2    Lee, S.T.3    Song, E.C.4    Jung, K.H.5    Kim, E.H.6    Park, D.K.7    Kang, K.M.8    Kim, M.9    Roh, J.K.10
  • 307
    • 33644668963 scopus 로고    scopus 로고
    • Geranylgeranylacetone, a noninvasive heat shock protein inducer, induces protein kinase C and leads to neuroprotection against cerebral infarction in rats
    • S. Uchida, M. Fujiki, Y. Nagai, T. Abe, and H. Kobayashi Geranylgeranylacetone, a noninvasive heat shock protein inducer, induces protein kinase C and leads to neuroprotection against cerebral infarction in rats Neurosci. Lett. 396 2006 220
    • (2006) Neurosci. Lett. , vol.396 , pp. 220
    • Uchida, S.1    Fujiki, M.2    Nagai, Y.3    Abe, T.4    Kobayashi, H.5
  • 311
    • 27644440326 scopus 로고    scopus 로고
    • Oral administration of geranylgeranylacetone improves survival rate in a rat endotoxin shock model: Administration timing and heat shock protein 70 induction
    • J. Nakada, T. Matsura, N. Okazaki, T. Nishida, A. Togawa, Y. Minami, Y. Inagaki, H. Ito, K. Yamada, and Y. Ishibe Oral administration of geranylgeranylacetone improves survival rate in a rat endotoxin shock model: administration timing and heat shock protein 70 induction Shock 24 2005 482
    • (2005) Shock , vol.24 , pp. 482
    • Nakada, J.1    Matsura, T.2    Okazaki, N.3    Nishida, T.4    Togawa, A.5    Minami, Y.6    Inagaki, Y.7    Ito, H.8    Yamada, K.9    Ishibe, Y.10
  • 312
    • 0037408438 scopus 로고    scopus 로고
    • Retinal ganglion cell protection with geranylgeranylacetone, a heat shock protein inducer, in a rat glaucoma model
    • Y. Ishii, J.M.K. Kwong, and J. Caprioli Retinal ganglion cell protection with geranylgeranylacetone, a heat shock protein inducer, in a rat glaucoma model Invest. Ophthalmol. Vis. Sci. 44 2003 1982
    • (2003) Invest. Ophthalmol. Vis. Sci. , vol.44 , pp. 1982
    • Ishii, Y.1    Kwong, J.M.K.2    Caprioli, J.3
  • 313
    • 79952754823 scopus 로고    scopus 로고
    • Heat shock protein 70 (HSP70) is critical for the photoreceptor stress response after retinal detachment via modulating anti-apoptotic Akt kinase
    • M. Kayama, T. Nakazawa, A. Thanos, Y. Morizane, Y. Murakami, S. Theodoropoulou, T. Abe, D. Vavvas, and J.W. Miller Heat shock protein 70 (HSP70) is critical for the photoreceptor stress response after retinal detachment via modulating anti-apoptotic Akt kinase Am. J. Pathol. 178 2011 1080
    • (2011) Am. J. Pathol. , vol.178 , pp. 1080
    • Kayama, M.1    Nakazawa, T.2    Thanos, A.3    Morizane, Y.4    Murakami, Y.5    Theodoropoulou, S.6    Abe, T.7    Vavvas, D.8    Miller, J.W.9
  • 314
    • 0042924435 scopus 로고    scopus 로고
    • Antiviral effects of geranylgeranylacetone: Enhancement of MxA expression and phosphorylation of PKR during influenza virus infection
    • M. Unoshima, H. Iwasaka, J. Eto, Y. Takita-Sonoda, T. Noguchi, and R. Nishizono Antiviral effects of geranylgeranylacetone: enhancement of MxA expression and phosphorylation of PKR during influenza virus infection Antimicrob. Agents Chemother. 47 2003 2914
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 2914
    • Unoshima, M.1    Iwasaka, H.2    Eto, J.3    Takita-Sonoda, Y.4    Noguchi, T.5    Nishizono, R.6
  • 315
    • 77949509086 scopus 로고    scopus 로고
    • Geranylgeranylacetone preconditioning may attenuate heat-induced inflammation and multiorgan dysfunction in rats
    • Y.Q. Zhao, J.T. Gao, S.H. Liu, Y. Wu, M.T. Lin, and M. Fan Geranylgeranylacetone preconditioning may attenuate heat-induced inflammation and multiorgan dysfunction in rats J. Pharm. Pharmacol. 62 2010 99
    • (2010) J. Pharm. Pharmacol. , vol.62 , pp. 99
    • Zhao, Y.Q.1    Gao, J.T.2    Liu, S.H.3    Wu, Y.4    Lin, M.T.5    Fan, M.6
  • 317
    • 66149153033 scopus 로고    scopus 로고
    • Lipoic acid increases heat shock protein expression and inhibits stress kinase activation to improve insulin signaling in skeletal muscle from high-fat-fed rats
    • A.A. Gupte, G.L. Bomhoff, J.K. Morris, B.K. Gorres, and P.C. Geiger Lipoic acid increases heat shock protein expression and inhibits stress kinase activation to improve insulin signaling in skeletal muscle from high-fat-fed rats J. Appl. Physiol. 106 2009 1425
    • (2009) J. Appl. Physiol. , vol.106 , pp. 1425
    • Gupte, A.A.1    Bomhoff, G.L.2    Morris, J.K.3    Gorres, B.K.4    Geiger, P.C.5
  • 318
    • 84881654000 scopus 로고    scopus 로고
    • Lipoic acid in animal models and clinical use in diabetic retinopathy
    • M. Nebbioso, F. Pranno, and N. Pescosolido Lipoic acid in animal models and clinical use in diabetic retinopathy Expert. Opin. Pharmacother. 14 2013 1829
    • (2013) Expert. Opin. Pharmacother. , vol.14 , pp. 1829
    • Nebbioso, M.1    Pranno, F.2    Pescosolido, N.3
  • 319
    • 84891669984 scopus 로고    scopus 로고
    • Alpha lipoic acid and glycaemic control in diabetic neuropathies at type 2 diabetes treatment
    • K. Ibrahimpasic Alpha lipoic acid and glycaemic control in diabetic neuropathies at type 2 diabetes treatment Med. Arh. 67 2013 7
    • (2013) Med. Arh. , vol.67 , pp. 7
    • Ibrahimpasic, K.1
  • 320
    • 84862272469 scopus 로고    scopus 로고
    • Cardiac fibrosis and dysfunction in experimental diabetic cardiomyopathy are ameliorated by alpha-lipoic acid
    • C.J. Li, L. Lv, H. Li, and D.M. Yu Cardiac fibrosis and dysfunction in experimental diabetic cardiomyopathy are ameliorated by alpha-lipoic acid Cardiovasc. Diabetol. 11 2012
    • (2012) Cardiovasc. Diabetol. , vol.11
    • Li, C.J.1    Lv, L.2    Li, H.3    Yu, D.M.4
  • 321
    • 84891622415 scopus 로고    scopus 로고
    • Comparative evaluation of short- and long-term treatment of periodontitis with alpha-lipoic acid
    • Y. Lakhtin Comparative evaluation of short- and long-term treatment of periodontitis with alpha-lipoic acid Georgian Med. News 218 2013 19
    • (2013) Georgian Med. News , vol.218 , pp. 19
    • Lakhtin, Y.1
  • 323
    • 84870826742 scopus 로고    scopus 로고
    • Hepato-protective effects of alpha lipoic acid besides its role in preventing fatty liver disease
    • S. Kapoor Hepato-protective effects of alpha lipoic acid besides its role in preventing fatty liver disease Liver Int. 33 2013 162
    • (2013) Liver Int. , vol.33 , pp. 162
    • Kapoor, S.1
  • 324
    • 84870203851 scopus 로고    scopus 로고
    • Alpha-lipoic acid reduces hypertension and increases baroreflex sensitivity in renovascular hypertensive rats
    • T.M. Queiroz, D.D. Guimaraes, L.G. Mendes, and V.A. Braga Alpha-lipoic acid reduces hypertension and increases baroreflex sensitivity in renovascular hypertensive rats Molecules 17 2012 13357
    • (2012) Molecules , vol.17 , pp. 13357
    • Queiroz, T.M.1    Guimaraes, D.D.2    Mendes, L.G.3    Braga, V.A.4
  • 325
    • 84870063331 scopus 로고    scopus 로고
    • The oxidative damage and inflammation caused by pesticides are reverted by lipoic acid in rat brain
    • M. Astiz, M.J.T. de Alaniz, and C.A. Marra The oxidative damage and inflammation caused by pesticides are reverted by lipoic acid in rat brain Neurochem. Int. 61 2012 1231
    • (2012) Neurochem. Int. , vol.61 , pp. 1231
    • Astiz, M.1    De Alaniz, M.J.T.2    Marra, C.A.3
  • 328
    • 84861796305 scopus 로고    scopus 로고
    • Effect of (R)-alpha-lipoic acid supplementation on serum lipids and antioxidative ability in patients with age-related macular degeneration
    • Y.D. Sun, Y.D. Dong, R. Fan, L.L. Zhai, Y.L. Bai, and L.H. Jia Effect of (R)-alpha-lipoic acid supplementation on serum lipids and antioxidative ability in patients with age-related macular degeneration Ann. Nutr. Metab. 60 2012 293
    • (2012) Ann. Nutr. Metab. , vol.60 , pp. 293
    • Sun, Y.D.1    Dong, Y.D.2    Fan, R.3    Zhai, L.L.4    Bai, Y.L.5    Jia, L.H.6
  • 329
    • 84855388628 scopus 로고    scopus 로고
    • Evaluation of protective and curative role of alpha-lipoic acid and selenium in gentamicin-induced nephrotoxicity in rabbits
    • A. Tahira, U. Saleem, S. Mahmood, F.K. Hashmi, K. Hussain, N.I. Bukhari, and B. Ahmad Evaluation of protective and curative role of alpha-lipoic acid and selenium in gentamicin-induced nephrotoxicity in rabbits Pak. J. Pharm. Sci. 25 2012 103
    • (2012) Pak. J. Pharm. Sci. , vol.25 , pp. 103
    • Tahira, A.1    Saleem, U.2    Mahmood, S.3    Hashmi, F.K.4    Hussain, K.5    Bukhari, N.I.6    Ahmad, B.7
  • 330
    • 41149155892 scopus 로고    scopus 로고
    • Treatment of obese diabetic mice with a heme oxygenase inducer reduces visceral and subcutaneous adiposity, increases adiponectin levels, and improves insulin sensitivity and glucose tolerance
    • M. Li, D.H. Kim, P.L. Tsenovoy, S.J. Peterson, R. Rezzani, L.F. Rodella, W.S. Aronow, S. Ikehara, and N.G. Abraham Treatment of obese diabetic mice with a heme oxygenase inducer reduces visceral and subcutaneous adiposity, increases adiponectin levels, and improves insulin sensitivity and glucose tolerance Diabetes 57 2008 1526
    • (2008) Diabetes , vol.57 , pp. 1526
    • Li, M.1    Kim, D.H.2    Tsenovoy, P.L.3    Peterson, S.J.4    Rezzani, R.5    Rodella, L.F.6    Aronow, W.S.7    Ikehara, S.8    Abraham, N.G.9
  • 332
    • 84860284564 scopus 로고    scopus 로고
    • High-fat diet exacerbates renal dysfunction in SHR: Reversal by induction of HO-1-adiponectin axis
    • J. Cao, K. Inoue, K. Sodhi, N. Puri, S.J. Peterson, R. Rezzani, and N.G. Abraham High-fat diet exacerbates renal dysfunction in SHR: reversal by induction of HO-1-adiponectin axis Obesity 20 2012 945
    • (2012) Obesity , vol.20 , pp. 945
    • Cao, J.1    Inoue, K.2    Sodhi, K.3    Puri, N.4    Peterson, S.J.5    Rezzani, R.6    Abraham, N.G.7
  • 338
    • 34948892667 scopus 로고    scopus 로고
    • Heme oxygenase-1 protects against radiocontrast-induced acute kidney injury by regulating anti-apoptotic proteins
    • A.I. Goodman, R. Olszanecki, L.M. Yang, S. Quan, M. Li, S. Omura, D.E. Stec, and N.G. Abraham Heme oxygenase-1 protects against radiocontrast-induced acute kidney injury by regulating anti-apoptotic proteins Kidney Int. 72 2007 945
    • (2007) Kidney Int. , vol.72 , pp. 945
    • Goodman, A.I.1    Olszanecki, R.2    Yang, L.M.3    Quan, S.4    Li, M.5    Omura, S.6    Stec, D.E.7    Abraham, N.G.8
  • 340
    • 77957316569 scopus 로고    scopus 로고
    • Restoring endoplasmic reticulum function by chemical chaperones: An emerging therapeutic approach for metabolic diseases
    • F. Engin, and G.S. Hotamisligil Restoring endoplasmic reticulum function by chemical chaperones: an emerging therapeutic approach for metabolic diseases Diabetes Obes. Metab. 12 2010 108
    • (2010) Diabetes Obes. Metab. , vol.12 , pp. 108
    • Engin, F.1    Hotamisligil, G.S.2
  • 341
    • 84861083677 scopus 로고    scopus 로고
    • Potent aminocyclitol glucocerebrosidase inhibitors are subnanomolar pharmacological chaperones for treating Gaucher disease
    • A. Trapero, P. Gonzalez-Bulnes, T.D. Butters, and A. Llebaria Potent aminocyclitol glucocerebrosidase inhibitors are subnanomolar pharmacological chaperones for treating Gaucher disease J. Med. Chem. 55 2012 4479
    • (2012) J. Med. Chem. , vol.55 , pp. 4479
    • Trapero, A.1    Gonzalez-Bulnes, P.2    Butters, T.D.3    Llebaria, A.4
  • 342
    • 84876793140 scopus 로고    scopus 로고
    • Chaperone therapy update: Fabry disease, GM1-gangliosidosis and Gaucher disease
    • Y. Suzuki Chaperone therapy update: Fabry disease, GM1-gangliosidosis and Gaucher disease Brain Dev. 35 2013 515
    • (2013) Brain Dev. , vol.35 , pp. 515
    • Suzuki, Y.1
  • 346
    • 77951928481 scopus 로고    scopus 로고
    • Palmitoyl:protein thioesterase (PPT1) inhibitors can act as pharmacological chaperones in infantile Batten disease
    • G. Dawson, C. Schroeder, and P.E. Dawson Palmitoyl:protein thioesterase (PPT1) inhibitors can act as pharmacological chaperones in infantile Batten disease Biochem. Biophys. Res. Commun. 395 2010 66
    • (2010) Biochem. Biophys. Res. Commun. , vol.395 , pp. 66
    • Dawson, G.1    Schroeder, C.2    Dawson, P.E.3
  • 348
    • 50249175120 scopus 로고    scopus 로고
    • Chemical and biological approaches synergize to ameliorate protein-folding diseases
    • T.W. Mu, D.S.T. Ong, Y.J. Wang, W.E. Balch, J.R. Yates, L. Segatori, and J.W. Kelly Chemical and biological approaches synergize to ameliorate protein-folding diseases Cell 134 2008 769
    • (2008) Cell , vol.134 , pp. 769
    • Mu, T.W.1    Ong, D.S.T.2    Wang, Y.J.3    Balch, W.E.4    Yates, J.R.5    Segatori, L.6    Kelly, J.W.7
  • 349
    • 47349111938 scopus 로고    scopus 로고
    • Unfolding the therapeutic potential of chemical chaperones for age-related macular degeneration
    • T. Sauer, M. Patel, C.C. Chan, and J. Tuo Unfolding the therapeutic potential of chemical chaperones for age-related macular degeneration Expert Rev. Ophthalmol. 3 2008 29
    • (2008) Expert Rev. Ophthalmol. , vol.3 , pp. 29
    • Sauer, T.1    Patel, M.2    Chan, C.C.3    Tuo, J.4


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