메뉴 건너뛰기




Volumn 5, Issue , 2014, Pages

TRPV4 channel activity is modulated by direct interaction of the ankyrin domain to PI(4,5)P2

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ANKYRIN; INOSITOL 1,4,5 TRISPHOSPHATE; MEMBRANE LIPID; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PHOSPHOLIPID BINDING PROTEIN; VANILLOID RECEPTOR 4; PROTEIN BINDING; TRPV4 PROTEIN, HUMAN; VANILLOID RECEPTOR;

EID: 84923349290     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms5994     Document Type: Article
Times cited : (94)

References (69)
  • 1
    • 84873413090 scopus 로고    scopus 로고
    • The puzzle of TRPV4 channelopathies
    • Nilius, B. & Voets, T. The puzzle of TRPV4 channelopathies. EMBO Rep. 14, 152-163 (2013).
    • (2013) EMBO Rep. , vol.14 , pp. 152-163
    • Nilius, B.1    Voets, T.2
  • 2
    • 77955305225 scopus 로고    scopus 로고
    • The vanilloid transient receptor potential channel TRPV4: From structure to disease
    • Everaerts, W., Nilius, B. & Owsianik, G. The vanilloid transient receptor potential channel TRPV4: From structure to disease. Prog. Biophys. Mol. Biol. 103, 2-17 (2010).
    • (2010) Prog. Biophys. Mol. Biol. , vol.103 , pp. 2-17
    • Everaerts, W.1    Nilius, B.2    Owsianik, G.3
  • 3
    • 0043267987 scopus 로고    scopus 로고
    • Anandamide and arachidonic acid use epoxyeicosatrienoic acids to activate TRPV4 channels
    • Watanabe, H. et al. Anandamide and arachidonic acid use epoxyeicosatrienoic acids to activate TRPV4 channels. Nature 424, 434-438 (2003).
    • (2003) Nature , vol.424 , pp. 434-438
    • Watanabe, H.1
  • 4
    • 77951248588 scopus 로고    scopus 로고
    • A 3.5-nm structure of rat TRPV4 cation channel revealed by Zernike phasecontrast cryoelectron microscopy
    • Shigematsu, H., Sokabe, T., Danev, R., Tominaga, M. & Nagayama, K. A 3.5-nm structure of rat TRPV4 cation channel revealed by Zernike phasecontrast cryoelectron microscopy. J. Biol. Chem. 285, 11210-11218 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 11210-11218
    • Shigematsu, H.1    Sokabe, T.2    Danev, R.3    Tominaga, M.4    Nagayama, K.5
  • 5
    • 33645276591 scopus 로고    scopus 로고
    • Mechanisms of disease: A molecular genetic update on hereditary axonal neuropathies
    • Züchner, S. & Vance, J. M. Mechanisms of disease: A molecular genetic update on hereditary axonal neuropathies. Nat. Clin. Pract. Neurol. 2, 45-53 (2006).
    • (2006) Nat. Clin. Pract. Neurol. , vol.2 , pp. 45-53
    • Züchner, S.1    Vance, J.M.2
  • 6
    • 67649390851 scopus 로고    scopus 로고
    • Diagnosis natural history, and management of charcot-marie-tooth disease
    • Pareyson, D. & Marchesi, C. Diagnosis, natural history, and management of Charcot-Marie-Tooth disease. Lancet Neurol. 8, 654-667 (2009).
    • (2009) Lancet Neurol. , vol.8 , pp. 654-667
    • Pareyson, D.1    Marchesi, C.2
  • 7
    • 75749083221 scopus 로고    scopus 로고
    • Scapuloperoneal spinal muscular atrophy and CMT2C are allelic disorders caused by alterations in TRPV4
    • Deng, H. X. et al. Scapuloperoneal spinal muscular atrophy and CMT2C are allelic disorders caused by alterations in TRPV4. Nat. Genet. 42, 165-169 (2010).
    • (2010) Nat. Genet. , vol.42 , pp. 165-169
    • Deng, H.X.1
  • 8
    • 79952904426 scopus 로고    scopus 로고
    • Trpv4 mutations and cytotoxic hypercalcemia in axonal charcot-marie-tooth neuropathies
    • Klein, C. J. et al. TRPV4 mutations and cytotoxic hypercalcemia in axonal Charcot-Marie-Tooth neuropathies. Neurology 76, 887-894 (2011).
    • (2011) Neurology , vol.76 , pp. 887-894
    • Klein, C.J.1
  • 9
    • 75749139617 scopus 로고    scopus 로고
    • Mutations in TRPV4 cause Charcot-Marie-Tooth disease type 2C
    • Landoure, G. et al. Mutations in TRPV4 cause Charcot-Marie-Tooth disease type 2C. Nat. Genet. 42, 170-174 (2010).
    • (2010) Nat. Genet. , vol.42 , pp. 170-174
    • Landoure, G.1
  • 10
    • 79955758732 scopus 로고    scopus 로고
    • Mutant TRPV4-mediated toxicity is linked to increased constitutive function in axonal neuropathies
    • Fecto, F. et al. Mutant TRPV4-mediated toxicity is linked to increased constitutive function in axonal neuropathies. J. Biol. Chem. 286, 17281-17291 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 17281-17291
    • Fecto, F.1
  • 12
    • 39749130486 scopus 로고    scopus 로고
    • Phosphoinositides and Charcot-Marie-tooth disease: New keys to old questions
    • Suter, U. Phosphoinositides and Charcot-Marie-tooth disease: New keys to old questions. Cell Mol. Life Sci. 64, 3261-3265 (2007).
    • (2007) Cell Mol. Life Sci. , vol.64 , pp. 3261-3265
    • Suter, U.1
  • 13
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • Lemmon, M. A. Membrane recognition by phospholipid-binding domains. Nat. Rev. Mol. Cell Biol. 9, 99-111 (2008).
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 99-111
    • Lemmon, M.A.1
  • 14
    • 0035980759 scopus 로고    scopus 로고
    • Phosphoinositides key molecules for regulation of actin cytoskeletal organization and membrane traffic from the plasma membrane
    • Takenawa, T. & Itoh, T. Phosphoinositides, key molecules for regulation of actin cytoskeletal organization and membrane traffic from the plasma membrane. Biochim. Biophys. Acta 1533, 190-206 (2001).
    • (2001) Biochim. Biophys. Acta , vol.1533 , pp. 190-206
    • Takenawa, T.1    Itoh, T.2
  • 15
    • 28444477387 scopus 로고    scopus 로고
    • Plasma membrane phosphoinositide organization by protein electrostatics
    • McLaughlin, S. & Murray, D. Plasma membrane phosphoinositide organization by protein electrostatics. Nature 438, 605-611 (2005).
    • (2005) Nature , vol.438 , pp. 605-611
    • McLaughlin, S.1    Murray, D.2
  • 16
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
    • Nishizuka, Y. Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science 258, 607-614 (1992).
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 17
    • 20144366550 scopus 로고    scopus 로고
    • Mutations in the pleckstrin homology domain of dynamin 2 cause dominant intermediate Charcot-Marie-Tooth disease
    • Züchner, S. et al. Mutations in the pleckstrin homology domain of dynamin 2 cause dominant intermediate Charcot-Marie-Tooth disease. Nat. Genet. 37, 289-294 (2005).
    • (2005) Nat. Genet. , vol.37 , pp. 289-294
    • Züchner, S.1
  • 18
    • 14844331501 scopus 로고    scopus 로고
    • Molecular motors and mechanisms of directional transport in neurons
    • Hirokawa, N. & Takemura, R. Molecular motors and mechanisms of directional transport in neurons. Nat. Rev. Neurosci. 6, 201-214 (2005).
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 201-214
    • Hirokawa, N.1    Takemura, R.2
  • 19
    • 79953282106 scopus 로고    scopus 로고
    • Phosphatidylinositol phosphates directly bind to neurofilament light chain (NF-L) for the regulation of NF-L self assembly
    • Kim, S. K., Kim, H., Yang, Y. R., Suh, P. G. & Chang, J. S. Phosphatidylinositol phosphates directly bind to neurofilament light chain (NF-L) for the regulation of NF-L self assembly. Exp. Mol. Med. 43, 153-160 (2011).
    • (2011) Exp. Mol. Med. , vol.43 , pp. 153-160
    • Kim, S.K.1    Kim, H.2    Yang, Y.R.3    Suh, P.G.4    Chang, J.S.5
  • 20
    • 84880032361 scopus 로고    scopus 로고
    • Mutations in the PLEKHG5 gene is relevant with autosomal recessive intermediate Charcot-Marie-Tooth disease
    • Kim, H. J. et al. Mutations in the PLEKHG5 gene is relevant with autosomal recessive intermediate Charcot-Marie-Tooth disease. Orphanet J. Rare Dis. 8, 104 (2013).
    • (2013) Orphanet J. Rare Dis. , vol.8 , pp. 104
    • Kim, H.J.1
  • 21
    • 34347213793 scopus 로고    scopus 로고
    • Peripheral nerve demyelination caused by a mutant Rho GTPase guanine nucleotide exchange factor, frabin/FGD4
    • Stendel, C. et al. Peripheral nerve demyelination caused by a mutant Rho GTPase guanine nucleotide exchange factor, frabin/FGD4. Am. J. Hum. Genet. 81, 158-164 (2007).
    • (2007) Am. J. Hum. Genet. , vol.81 , pp. 158-164
    • Stendel, C.1
  • 22
    • 34347240987 scopus 로고    scopus 로고
    • Mutations in FGD4 encoding the Rho GDP/GTP exchange factor FRABIN cause autosomal recessive Charcot-Marie-Tooth type 4H
    • Delague, V. et al. Mutations in FGD4 encoding the Rho GDP/GTP exchange factor FRABIN cause autosomal recessive Charcot-Marie-Tooth type 4H. Am. J. Hum. Genet. 81, 1-16 (2007).
    • (2007) Am. J. Hum. Genet. , vol.81 , pp. 1-16
    • Delague, V.1
  • 23
    • 84864649745 scopus 로고    scopus 로고
    • Structural and biochemical consequences of disease-causing mutations in the ankyrin repeat domain of the human TRPV4 channel
    • Inada, H., Procko, E., Sotomayor, M. & Gaudet, R. Structural and biochemical consequences of disease-causing mutations in the ankyrin repeat domain of the human TRPV4 channel. Biochemistry 51, 6195-6206 (2012).
    • (2012) Biochemistry , vol.51 , pp. 6195-6206
    • Inada, H.1    Procko, E.2    Sotomayor, M.3    Gaudet, R.4
  • 24
    • 34250190946 scopus 로고    scopus 로고
    • The ankyrin repeats of TRPV1 bind multiple ligands and modulate channel sensitivity
    • Lishko, P. V., Procko, E., Jin, X., Phelps, C. B. & Gaudet, R. The ankyrin repeats of TRPV1 bind multiple ligands and modulate channel sensitivity. Neuron 54, 905-918 (2007).
    • (2007) Neuron , vol.54 , pp. 905-918
    • Lishko, P.V.1    Procko, E.2    Jin, X.3    Phelps, C.B.4    Gaudet, R.5
  • 25
    • 75749129360 scopus 로고    scopus 로고
    • Alterations in the ankyrin domain of TRPV4 cause congenital distal SMA, scapuloperoneal SMA and HMSN2C
    • Auer-Grumbach, M. et al. Alterations in the ankyrin domain of TRPV4 cause congenital distal SMA, scapuloperoneal SMA and HMSN2C. Nat. Genet. 42, 160-164 (2010).
    • (2010) Nat. Genet. , vol.42 , pp. 160-164
    • Auer-Grumbach, M.1
  • 26
    • 0037134482 scopus 로고    scopus 로고
    • Activation of TRPV4 channels (hVRL-2/mTRP12) by phorbol derivatives
    • Watanabe, H. et al. Activation of TRPV4 channels (hVRL-2/mTRP12) by phorbol derivatives. J. Biol. Chem. 277, 13569-13577 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 13569-13577
    • Watanabe, H.1
  • 27
    • 67349183758 scopus 로고    scopus 로고
    • Phosphoinositide regulation of non-canonical transient receptor potential channels
    • Rohacs, T. Phosphoinositide regulation of non-canonical transient receptor potential channels. Cell Calcium 45, 554-565 (2009).
    • (2009) Cell Calcium , vol.45 , pp. 554-565
    • Rohacs, T.1
  • 28
    • 0029617615 scopus 로고
    • Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain
    • Ferguson, K. M., Lemmon, M. A., Schlessinger, J. & Sigler, P. B. Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. Cell 83, 1037-1046 (1995).
    • (1995) Cell , vol.83 , pp. 1037-1046
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4
  • 30
    • 0042861412 scopus 로고    scopus 로고
    • Retrograde regulation of synaptic vesicle endocytosis and recycling
    • Micheva, K. D., Buchanan, J., Holz, R. W. & Smith, S. J. Retrograde regulation of synaptic vesicle endocytosis and recycling. Nat. Neurosci. 6, 925-932 (2003).
    • (2003) Nat. Neurosci. , vol.6 , pp. 925-932
    • Micheva, K.D.1    Buchanan, J.2    Holz, R.W.3    Smith, S.J.4
  • 31
    • 0038394476 scopus 로고    scopus 로고
    • + release channels by Gbg
    • + release channels by Gbg. Curr. Biol. 13, 872-876 (2003).
    • (2003) Curr. Biol. , vol.13 , pp. 872-876
    • Zeng, W.1
  • 32
    • 42049092996 scopus 로고    scopus 로고
    • IP3 sensitizes TRPV4 channel to the mechano-and osmotransducing messenger 5'-6'-epoxyeicosatrienoic acid
    • Fernandes, J. et al. IP3 sensitizes TRPV4 channel to the mechano-and osmotransducing messenger 5'-6'-epoxyeicosatrienoic acid. J. Cell Biol. 181, 143-155 (2008).
    • (2008) J. Cell Biol. , vol.181 , pp. 143-155
    • Fernandes, J.1
  • 33
    • 67249137553 scopus 로고    scopus 로고
    • A distinct pool of phosphatidylinositol 4,5-bisphosphate in caveolae revealed by a nanoscale labeling technique
    • Fujita, A., Cheng, J., Tauchi-Sato, K., Takenawa, T. & Fujimoto, T. A distinct pool of phosphatidylinositol 4,5-bisphosphate in caveolae revealed by a nanoscale labeling technique. Proc. Natl Acad. Sci. USA 106, 9256-9261 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 9256-9261
    • Fujita, A.1    Cheng, J.2    Tauchi-Sato, K.3    Takenawa, T.4    Fujimoto, T.5
  • 34
    • 0037033077 scopus 로고    scopus 로고
    • Heat-evoked activation of TRPV4 channels in a HEK293 cell expression system and in native mouse aorta endothelial cells
    • Watanabe, H. et al. Heat-evoked activation of TRPV4 channels in a HEK293 cell expression system and in native mouse aorta endothelial cells. J. Biol. Chem. 277, 47044-47051 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 47044-47051
    • Watanabe, H.1
  • 35
    • 0023262465 scopus 로고
    • + -dependent a1-adrenergic stimulation of pineal phospholipase A2 activity
    • + -dependent a1-adrenergic stimulation of pineal phospholipase A2 activity. J. Biol. Chem. 262, 11764-11770 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 11764-11770
    • Ho, A.K.1    Klein, D.C.2
  • 36
    • 0025284773 scopus 로고
    • Diminished protein kinase C-activated arachidonate metabolism accompanies rat macrophage differentiation in the lung
    • Peters-Golden, M., McNish, R. W., Brieland, J. K. & Fantone, J. C. Diminished protein kinase C-activated arachidonate metabolism accompanies rat macrophage differentiation in the lung. J. Immunol. 144, 4320-4326 (1990).
    • (1990) J. Immunol. , vol.144 , pp. 4320-4326
    • Peters-Golden, M.1    McNish, R.W.2    Brieland, J.K.3    Fantone, J.C.4
  • 37
    • 0028138215 scopus 로고
    • 1,3-Dioctanoylglycerol 1,3-DiC8) is as effective as 1,2-dioctanoylglycerol (1,2-DiC8) in priming phospholipase A2 activation in human platelets and neutrophils
    • Murthy, M., Rao, G. H. & Reddy, S. 1,3-Dioctanoylglycerol (1,3-DiC8) is as effective as 1,2-dioctanoylglycerol (1,2-DiC8) in priming phospholipase A2 activation in human platelets and neutrophils. Biochem. Med. Metab. Biol. 52, 89-96 (1994).
    • (1994) Biochem. Med. Metab. Biol. , vol.52 , pp. 89-96
    • Murthy, M.1    Rao, G.H.2    Reddy, S.3
  • 39
    • 73649104785 scopus 로고    scopus 로고
    • Differential regulation of TRPV1, TRPV3, and TRPV4 sensitivity through a conserved binding site on the ankyrin repeat domain
    • Phelps, C. B., Wang, R. R., Choo, S. S. & Gaudet, R. Differential regulation of TRPV1, TRPV3, and TRPV4 sensitivity through a conserved binding site on the ankyrin repeat domain. J. Biol. Chem. 285, 731-740 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 731-740
    • Phelps, C.B.1    Wang, R.R.2    Choo, S.S.3    Gaudet, R.4
  • 40
    • 84889607320 scopus 로고    scopus 로고
    • Structure of the TRPV1 ion channel determined by electron cryo-microscopy
    • Liao, M., Cao, E., Julius, D. & Cheng, Y. Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504, 107-112 (2013).
    • (2013) Nature , vol.504 , pp. 107-112
    • Liao, M.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 41
    • 84889594608 scopus 로고    scopus 로고
    • TRPV1 structures in distinct conformations reveal activation mechanisms
    • Cao, E., Liao, M., Cheng, Y. & Julius, D. TRPV1 structures in distinct conformations reveal activation mechanisms. Nature 504, 113-118 (2013).
    • (2013) Nature , vol.504 , pp. 113-118
    • Cao, E.1    Liao, M.2    Cheng, Y.3    Julius, D.4
  • 42
    • 84893757446 scopus 로고    scopus 로고
    • Structural insight into the assembly of TRPV channels
    • Huynh, K. W. et al. Structural insight into the assembly of TRPV channels. Structure. 22, 260-268 (2013).
    • (2013) Structure. , vol.22 , pp. 260-268
    • Huynh, K.W.1
  • 43
    • 33644969008 scopus 로고    scopus 로고
    • Human TRPV4 channel splice variants revealed a key role of ankyrin domains in multimerization and trafficking
    • Arniges, M., Fernández-Fernández, J. M., Albrecht, N., Schaefer, M. & Valverde, M. A. Human TRPV4 channel splice variants revealed a key role of ankyrin domains in multimerization and trafficking. J. Biol. Chem. 281, 1580-1586 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 1580-1586
    • Arniges, M.1    Fernández-Fernández, J.M.2    Albrecht, N.3    Schaefer, M.4    Valverde, M.A.5
  • 44
    • 84878677214 scopus 로고    scopus 로고
    • Phosphatidylinositol-4,5-biphosphate-dependent rearrangement of TRPV4 cytosolic tails enables channel activation by physiological stimuli
    • Garcia-Elias, A. et al. Phosphatidylinositol-4,5-biphosphate-dependent rearrangement of TRPV4 cytosolic tails enables channel activation by physiological stimuli. Proc. Natl Acad. Sci. USA 110, 9553-9558 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 9553-9558
    • Garcia-Elias, A.1
  • 45
    • 2942718545 scopus 로고    scopus 로고
    • PI-loting membrane traffic
    • De Matteis, M. A. & Godi, A. PI-loting membrane traffic. Nat. Cell Biol. 6, 487-492 (2004).
    • (2004) Nat. Cell Biol. , vol.6 , pp. 487-492
    • De Matteis, M.A.1    Godi, A.2
  • 46
    • 0346435090 scopus 로고    scopus 로고
    • Microfilament-associated protein 7 increases the membrane expression of transient receptor potential vanilloid 4 (TRPV4)
    • Suzuki, M., Hirao, A. & Mizuno, A. Microfilament-associated protein 7 increases the membrane expression of transient receptor potential vanilloid 4 (TRPV4). J. Biol. Chem. 278, 51448-51453 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 51448-51453
    • Suzuki, M.1    Hirao, A.2    Mizuno, A.3
  • 47
    • 37549002929 scopus 로고    scopus 로고
    • OS-9 regulates the transit and polyubiquitination of TRPV4 in the endoplasmic reticulum
    • Wang, Y. et al. OS-9 regulates the transit and polyubiquitination of TRPV4 in the endoplasmic reticulum. J. Biol. Chem. 282, 36561-36570 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 36561-36570
    • Wang, Y.1
  • 48
    • 84857794759 scopus 로고    scopus 로고
    • Synergistic BAR-NPF interactions in actin-driven membrane remodeling
    • Suetsugu, S. & Gautreau, A. Synergistic BAR-NPF interactions in actin-driven membrane remodeling. Trends Cell Biol. 22, 141-150 (2012).
    • (2012) Trends Cell Biol. , vol.22 , pp. 141-150
    • Suetsugu, S.1    Gautreau, A.2
  • 49
    • 2442706456 scopus 로고    scopus 로고
    • The ankyrin repeat as molecular architecture for protein recognition
    • Mosavi, L. K., Cammett, T. J., Desrosiers, D. C. & Peng, Z. Y. The ankyrin repeat as molecular architecture for protein recognition. Protein Sci. 13, 1435-1448 (2004).
    • (2004) Protein Sci. , vol.13 , pp. 1435-1448
    • Mosavi, L.K.1    Cammett, T.J.2    Desrosiers, D.C.3    Peng, Z.Y.4
  • 50
    • 84855465067 scopus 로고    scopus 로고
    • An ankyrin-repeat ubiquitin-binding domain determines TRABID's specificity for atypical ubiquitin chains
    • Licchesi, J. D. et al. An ankyrin-repeat ubiquitin-binding domain determines TRABID's specificity for atypical ubiquitin chains. Nat. Struct. Mol. Biol. 19, 62-71 (2012).
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 62-71
    • Licchesi, J.D.1
  • 51
    • 2342624119 scopus 로고    scopus 로고
    • High-affinity binders selected from designed ankyrin repeat protein libraries
    • Binz, H. K. et al. High-affinity binders selected from designed ankyrin repeat protein libraries. Nat. Biotechnol. 22, 575-582 (2004).
    • (2004) Nat. Biotechnol. , vol.22 , pp. 575-582
    • Binz, H.K.1
  • 52
    • 0023835720 scopus 로고
    • Mitogenesis in response to PDGF and bombesin abolished by microinjection of antibody to PIP2
    • Matuoka, K., Fukami, K., Nakanishi, O., Kawai, S. & Takenawa, T. Mitogenesis in response to PDGF and bombesin abolished by microinjection of antibody to PIP2. Science 239, 640-643 (1988).
    • (1988) Science , vol.239 , pp. 640-643
    • Matuoka, K.1    Fukami, K.2    Nakanishi, O.3    Kawai, S.4    Takenawa, T.5
  • 53
    • 78651348672 scopus 로고    scopus 로고
    • Phosphoinositide-incorporated lipid-protein nanodiscs: A tool for studying protein-lipid interactions
    • Kobashigawa, Y., Harada, K., Yoshida, N., Ogura, K. & Inagaki, F. Phosphoinositide-incorporated lipid-protein nanodiscs: A tool for studying protein-lipid interactions. Anal. Biochem. 410, 77-83 (2011).
    • (2011) Anal. Biochem. , vol.410 , pp. 77-83
    • Kobashigawa, Y.1    Harada, K.2    Yoshida, N.3    Ogura, K.4    Inagaki, F.5
  • 54
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 55
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 56
    • 14244272868 scopus 로고    scopus 로고
    • Phenix: Building new software for automated crystallographic structure determination
    • Adams, P. D. et al. PHENIX: Building new software for automated crystallographic structure determination. Acta Crystallogr. D Biol. Crystallogr 58, 1948-1954 (2002).
    • (2002) Acta Crystallogr. D Biol. Crystallogr , vol.58 , pp. 1948-1954
    • Adams, P.D.1
  • 57
  • 58
    • 70349932423 scopus 로고    scopus 로고
    • AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility
    • Morris, G. M. et al. AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility. J. Comput. Chem. 30, 2785-2791 (2009).
    • (2009) J. Comput. Chem. , vol.30 , pp. 2785-2791
    • Morris, G.M.1
  • 59
    • 27344436659 scopus 로고    scopus 로고
    • Scalable molecular dynamics with NAMD
    • Phillips, J. C. et al. Scalable molecular dynamics with NAMD. J. Comput. Chem. 26, 1781-1802 (2005).
    • (2005) J. Comput. Chem. , vol.26 , pp. 1781-1802
    • Phillips, J.C.1
  • 60
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • MacKerell, A. D. et al. All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. B 102, 3586-3616 (1998).
    • (1998) J. Phys. Chem. B , vol.102 , pp. 3586-3616
    • Mackerell, A.D.1
  • 61
    • 3142714765 scopus 로고    scopus 로고
    • Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations
    • MacKerell, A. D., Feig, M. & Brooks, C. L. Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations. J. Comput. Chem. 25, 1400-1415 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1400-1415
    • Mackerell, A.D.1    Feig, M.2    Brooks, C.L.3
  • 62
    • 77953377650 scopus 로고    scopus 로고
    • Update of the CHARMM all-atom additive force field for lipids: Validation on six lipid types
    • Klauda, J. B. et al. Update of the CHARMM all-atom additive force field for lipids: Validation on six lipid types. J. Phys. Chem. B 114, 7830-7843 (2010).
    • (2010) J. Phys. Chem. B , vol.114 , pp. 7830-7843
    • Klauda, J.B.1
  • 63
    • 80053944070 scopus 로고    scopus 로고
    • CHARMM additive all-atom force field for carbohydrate derivatives and its utility in polysaccharide and carbohydrate-protein modeling
    • Guvench, O. et al. CHARMM additive all-atom force field for carbohydrate derivatives and its utility in polysaccharide and carbohydrate-protein modeling. J. Chem. Theory Comput. 7, 3162-3180 (2011).
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 3162-3180
    • Guvench, O.1
  • 64
    • 44649133131 scopus 로고    scopus 로고
    • Extrinsic fluorescent dyes as tools for protein characterization
    • Hawe, A., Sutter, M. & Jiskoot, W. Extrinsic fluorescent dyes as tools for protein characterization. Pharm. Res. 25, 1487-1499 (2008).
    • (2008) Pharm. Res. , vol.25 , pp. 1487-1499
    • Hawe, A.1    Sutter, M.2    Jiskoot, W.3
  • 65
    • 80052960971 scopus 로고    scopus 로고
    • TRPA1 underlies a sensing mechanism for O2
    • Takahashi, N. et al. TRPA1 underlies a sensing mechanism for O2. Nat. Chem. Biol. 7, 701-711 (2011).
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 701-711
    • Takahashi, N.1
  • 66
    • 48349103354 scopus 로고    scopus 로고
    • Gain-of-function mutations in TRPV4 cause autosomal dominant brachyolmia
    • Rock, M. J. et al. Gain-of-function mutations in TRPV4 cause autosomal dominant brachyolmia. Nat. Genet. 40, 999-1003 (2008).
    • (2008) Nat. Genet. , vol.40 , pp. 999-1003
    • Rock, M.J.1
  • 67
    • 0038049930 scopus 로고    scopus 로고
    • The TRPV4 channel: Structure-function relationship and promiscuous gating behaviour
    • Nilius, B., Watanabe, H. & Vriens, J. The TRPV4 channel: Structure-function relationship and promiscuous gating behaviour. Pflügers Archiv. 446, 298-303 (2003).
    • (2003) Pflügers Archiv. , vol.446 , pp. 298-303
    • Nilius, B.1    Watanabe, H.2    Vriens, J.3
  • 68
    • 27244438579 scopus 로고    scopus 로고
    • Low mobility of phosphatidylinositol 4, 5-bisphosphate underlies receptor specificity of Gq-mediated ion channel regulation in atrial myocytes
    • Cho, H. et al. Low mobility of phosphatidylinositol 4, 5-bisphosphate underlies receptor specificity of Gq-mediated ion channel regulation in atrial myocytes. Proc. Natl Acad. Sci. USA 102, 15241-15246 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 15241-15246
    • Cho, H.1
  • 69
    • 0023278627 scopus 로고
    • Rapid increases in cytosolic free calcium in response to muscarinic stimulation of rat parotid acinar cells
    • Merritt, J. E. & Rink, T. J. Rapid increases in cytosolic free calcium in response to muscarinic stimulation of rat parotid acinar cells. J. Biol. Chem. 262, 4958-4960 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 4958-4960
    • Merritt, J.E.1    Rink, T.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.