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Volumn 288, Issue 16, 2013, Pages 11294-11303

Structural sensitivity of a prokaryotic pentameric ligand-gated ion channel to its membrane environment

Author keywords

[No Author keywords available]

Indexed keywords

LIGAND-GATED ION CHANNELS; MOLECULAR FEATURE; STRUCTURAL SENSITIVITY; THERMALLY STABLE;

EID: 84876543856     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.458133     Document Type: Article
Times cited : (32)

References (51)
  • 1
    • 33645302360 scopus 로고    scopus 로고
    • Recent advances in Cys-loop receptor structure and function
    • Sine, S. M., and Engel, A. G. (2006) Recent advances in Cys-loop receptor structure and function. Nature 440, 448-455.
    • (2006) Nature , vol.440 , pp. 448-455
    • Sine, S.M.1    Engel, A.G.2
  • 2
    • 69949159308 scopus 로고    scopus 로고
    • Nicotinic receptors. Allosteric transitions and therapeutic targets in the nervous system
    • Taly, A., Corringer, P. J., Guedin, D., Lestage, P., and Changeux, J. P. (2009) Nicotinic receptors. Allosteric transitions and therapeutic targets in the nervous system. Nat. Rev. Drug Discov. 8, 733-750.
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 733-750
    • Taly, A.1    Corringer, P.J.2    Guedin, D.3    Lestage, P.4    Changeux, J.P.5
  • 3
    • 84864060207 scopus 로고    scopus 로고
    • End-plate acetylcholine receptor. Structure, mechanism, pharmacology, and disease
    • Sine, S. M. (2012) End-plate acetylcholine receptor. Structure, mechanism, pharmacology, and disease. Physiol. Rev. 92, 1189-1234.
    • (2012) Physiol. Rev. , vol.92 , pp. 1189-1234
    • Sine, S.M.1
  • 4
    • 84863791625 scopus 로고    scopus 로고
    • Conscious processing. Implications for general anesthesia
    • Changeux, J. P. (2012) Conscious processing. Implications for general anesthesia. Curr. Opin. Anaesthesiol. 25, 397-404.
    • (2012) Curr. Opin. Anaesthesiol. , vol.25 , pp. 397-404
    • Changeux, J.P.1
  • 5
    • 78149498460 scopus 로고    scopus 로고
    • 3D structure and allosteric modulation of the transmembrane domain of pentameric ligand-gated ion channels
    • Baenziger, J. E., and Corringer, P. J. (2011) 3D structure and allosteric modulation of the transmembrane domain of pentameric ligand-gated ion channels. Neuropharmacology 60, 116-125.
    • (2011) Neuropharmacology , vol.60 , pp. 116-125
    • Baenziger, J.E.1    Corringer, P.J.2
  • 6
    • 0019182731 scopus 로고
    • Reconstitution of a functional acetylcholine receptor. Conservation of the conformational and allosteric transitions and recovery of the permeability response; Role of lipids
    • Heidmann, T., Sobel, A., Popot, J. L., and Changeux, J. P. (1980) Reconstitution of a functional acetylcholine receptor. Conservation of the conformational and allosteric transitions and recovery of the permeability response; role of lipids. Eur. J. Biochem. 110, 35-55.
    • (1980) Eur. J. Biochem. , vol.110 , pp. 35-55
    • Heidmann, T.1    Sobel, A.2    Popot, J.L.3    Changeux, J.P.4
  • 7
    • 0033954766 scopus 로고    scopus 로고
    • Effect of membrane lipid composition on the conformational equilibria of the nicotinic acetylcholine receptor
    • Baenziger, J. E., Morris, M. L., Darsaut, T. E., and Ryan, S. E. (2000) Effect of membrane lipid composition on the conformational equilibria of the nicotinic acetylcholine receptor. J. Biol. Chem. 275, 777-784.
    • (2000) J. Biol. Chem. , vol.275 , pp. 777-784
    • Baenziger, J.E.1    Morris, M.L.2    Darsaut, T.E.3    Ryan, S.E.4
  • 8
    • 33645549694 scopus 로고    scopus 로고
    • Assessing the lipid requirements of the Torpedo californica nicotinic acetylcholine receptor
    • Hamouda, A. K., Sanghvi, M., Sauls, D., Machu, T. K., and Blanton, M. P. (2006) Assessing the lipid requirements of the Torpedo californica nicotinic acetylcholine receptor. Biochemistry 45, 4327-4337.
    • (2006) Biochemistry , vol.45 , pp. 4327-4337
    • Hamouda, A.K.1    Sanghvi, M.2    Sauls, D.3    MacHu, T.K.4    Blanton, M.P.5
  • 9
    • 0022552318 scopus 로고
    • Correlation between acetylcholine receptor function and structural properties of membranes
    • Fong, T. M., and McNamee, M. G. (1986) Correlation between acetylcholine receptor function and structural properties of membranes. Biochemistry 25, 830-840.
    • (1986) Biochemistry , vol.25 , pp. 830-840
    • Fong, T.M.1    McNamee, M.G.2
  • 10
    • 0020376564 scopus 로고
    • Effects of lipids on acetylcholine receptor. Essential need of cholesterol for maintenance of agonistinduced state transitions in lipid vesicles
    • Criado, M., Eibl, H., and Barrantes, F. J. (1982) Effects of lipids on acetylcholine receptor. Essential need of cholesterol for maintenance of agonistinduced state transitions in lipid vesicles. Biochemistry 21, 3622-3629.
    • (1982) Biochemistry , vol.21 , pp. 3622-3629
    • Criado, M.1    Eibl, H.2    Barrantes, F.J.3
  • 11
    • 67650516762 scopus 로고    scopus 로고
    • A lipid-dependent uncoupled conformation of the acetylcholine receptor
    • daCosta, C. J., and Baenziger, J. E. (2009) A lipid-dependent uncoupled conformation of the acetylcholine receptor. J. Biol. Chem. 284, 17819-17825.
    • (2009) J. Biol. Chem. , vol.284 , pp. 17819-17825
    • Da Costa, C.J.1    Baenziger, J.E.2
  • 12
    • 84876529429 scopus 로고    scopus 로고
    • Molecular mechanisms of acetylcholine receptor-lipid interactions. from model membranes to huma biology
    • Baenziger, J. E., and daCosta, C. J. (2013) Molecular mechanisms of acetylcholine receptor-lipid interactions. From model membranes to huma biology. Biophys. Rev. 5, 1-9.
    • (2013) Biophys. Rev. , vol.5 , pp. 1-9
    • Baenziger, J.E.1    Da Costa, C.J.2
  • 15
    • 41149168686 scopus 로고    scopus 로고
    • X-ray structure of a prokaryotic pentameric ligand-gated ion channel
    • Hilf, R. J., and Dutzler, R. (2008) X-ray structure of a prokaryotic pentameric ligand-gated ion channel. Nature 452, 375-379.
    • (2008) Nature , vol.452 , pp. 375-379
    • Hilf, R.J.1    Dutzler, R.2
  • 16
    • 58149267953 scopus 로고    scopus 로고
    • X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation
    • Bocquet, N., Nury, H., Baaden, M., Le Poupon, C., Changeux, J. P., Delarue, M., and Corringer, P. J. (2009) X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation. Nature 457, 111-114.
    • (2009) Nature , vol.457 , pp. 111-114
    • Bocquet, N.1    Nury, H.2    Baaden, M.3    Le Poupon, C.4    Changeux, J.P.5    Delarue, M.6    Corringer, P.J.7
  • 17
    • 58149242730 scopus 로고    scopus 로고
    • Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel
    • Hilf, R. J., and Dutzler, R. (2009) Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel. Nature 457, 115-118.
    • (2009) Nature , vol.457 , pp. 115-118
    • Hilf, R.J.1    Dutzler, R.2
  • 18
    • 84868258417 scopus 로고    scopus 로고
    • Conformational transitions underlying pore opening and desensitization in membrane-embedded GLIC
    • Velisetty, P., Chalamalasetti, S. V., and Chakrapani, S. (2012) Conformational transitions underlying pore opening and desensitization in membrane-embedded GLIC. J. Biol. Chem. 287, 36864-36872.
    • (2012) J. Biol. Chem. , vol.287 , pp. 36864-36872
    • Velisetty, P.1    Chalamalasetti, S.V.2    Chakrapani, S.3
  • 19
    • 49449114708 scopus 로고    scopus 로고
    • Expression, purification, and structural characterization of CfrA, a putative iron transporter from Campylobacter jejuni
    • Carswell, C. L., Rigden, M. D., and Baenziger, J. E. (2008) Expression, purification, and structural characterization of CfrA, a putative iron transporter from Campylobacter jejuni. J. Bacteriol. 190, 5650-5662.
    • (2008) J. Bacteriol. , vol.190 , pp. 5650-5662
    • Carswell, C.L.1    Rigden, M.D.2    Baenziger, J.E.3
  • 20
    • 65249190326 scopus 로고    scopus 로고
    • Structural characterization of the osmosensor ProP
    • Sayeed, W. M., and Baenziger, J. E. (2009) Structural characterization of the osmosensor ProP. Biochim. Biophys. Acta 1788, 1108-1115.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1108-1115
    • Sayeed, W.M.1    Baenziger, J.E.2
  • 21
    • 31044432386 scopus 로고    scopus 로고
    • Cholesterol interacts with transmembrane -helices M1, M3, and M4 of the Torpedo nicotinic acetylcholine receptor. Photolabeling studies using [3H]azicholesterol
    • Hamouda, A. K., Chiara, D. C., Sauls, D., Cohen, J. B., and Blanton, M. P. (2006) Cholesterol interacts with transmembrane -helices M1, M3, and M4 of the Torpedo nicotinic acetylcholine receptor. Photolabeling studies using [3H]azicholesterol. Biochemistry 45, 976-986.
    • (2006) Biochemistry , vol.45 , pp. 976-986
    • Hamouda, A.K.1    Chiara, D.C.2    Sauls, D.3    Cohen, J.B.4    Blanton, M.P.5
  • 22
    • 0000374434 scopus 로고    scopus 로고
    • The selective enhancement and subsequent subtraction of atmospheric water vapour contributions from Fourier transform infrared spectra of proteins
    • Reid, S. E., Moffat, D. J., and Baenziger, J. E. (1996) The selective enhancement and subsequent subtraction of atmospheric water vapour contributions from Fourier transform infrared spectra of proteins. Spectrochim. Acta A 52, 1347-1356.
    • (1996) Spectrochim. Acta A , vol.52 , pp. 1347-1356
    • Reid, S.E.1    Moffat, D.J.2    Baenziger, J.E.3
  • 23
    • 84859186479 scopus 로고    scopus 로고
    • Bupropion binds to two sites in the Torpedo nicotinic acetylcholine receptor transmembrane domain. A photoaffinity labeling study with the bupropion analogue [125I]-SADU-3-72
    • Pandhare, A., Hamouda, A. K., Staggs, B., Aggarwal, S., Duddempudi, P. K., Lever, J. R., Lapinsky, D. J., Jansen, M., Cohen, J. B., and Blanton, M. P. (2012) Bupropion binds to two sites in the Torpedo nicotinic acetylcholine receptor transmembrane domain. A photoaffinity labeling study with the bupropion analogue [125I]-SADU-3-72. Biochemistry 51, 2425-2435.
    • (2012) Biochemistry , vol.51 , pp. 2425-2435
    • Pandhare, A.1    Hamouda, A.K.2    Staggs, B.3    Aggarwal, S.4    Duddempudi, P.K.5    Lever, J.R.6    Lapinsky, D.J.7    Jansen, M.8    Cohen, J.B.9    Blanton, M.P.10
  • 24
    • 0037240246 scopus 로고    scopus 로고
    • A rapid method for assessing lipid:protein and detergent:protein ratios in membrane-protein crystallization
    • daCosta, C. J., and Baenziger, J. E. (2003) A rapid method for assessing lipid:protein and detergent:protein ratios in membrane-protein crystallization. Acta Crystallogr. D Biol. Crystallogr. 59, 77-83.
    • (2003) Acta Crystallogr. D Biol. Crystallogr. , vol.59 , pp. 77-83
    • Da Costa, C.J.1    Baenziger, J.E.2
  • 25
    • 0035968206 scopus 로고    scopus 로고
    • Structure of the pore-forming transmembrane domain of a ligand-gated ion channel
    • Méthot, N., Ritchie, B. D., Blanton, M. P., and Baenziger, J. E. (2001) Structure of the pore-forming transmembrane domain of a ligand-gated ion channel. J. Biol. Chem. 276, 23726-23732.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23726-23732
    • Méthot, N.1    Ritchie, B.D.2    Blanton, M.P.3    Baenziger, J.E.4
  • 26
    • 0030894826 scopus 로고    scopus 로고
    • Desensitization of the nicotinic acetylcholine receptor mainly involves a structural change in solvent-accessible regions of the polypeptide backbone
    • Baenziger, J. E., and Chew, J. P. (1997) Desensitization of the nicotinic acetylcholine receptor mainly involves a structural change in solvent-accessible regions of the polypeptide backbone. Biochemistry 36, 3617-3624.
    • (1997) Biochemistry , vol.36 , pp. 3617-3624
    • Baenziger, J.E.1    Chew, J.P.2
  • 28
    • 0028800463 scopus 로고
    • Fourier transform infrared and hydrogen/deuterium exchange reveal an exchange-resistant core of α-helical peptide hydrogens in the nicotinic acetylcholine receptor
    • Baenziger, J. E., and Méthot, N. (1995) Fourier transform infrared and hydrogen/deuterium exchange reveal an exchange-resistant core of α-helical peptide hydrogens in the nicotinic acetylcholine receptor. J. Biol. Chem. 270, 29129-29137.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29129-29137
    • Baenziger, J.E.1    Méthot, N.2
  • 29
    • 71749098387 scopus 로고    scopus 로고
    • Anionic lipids allosterically modulate multiple nicotinic acetylcholine receptor conformational equilibria
    • daCosta, C. J., Medaglia, S. A., Lavigne, N., Wang, S., Carswell, C. L., and Baenziger, J. E. (2009) Anionic lipids allosterically modulate multiple nicotinic acetylcholine receptor conformational equilibria. J. Biol. Chem. 284, 33841-33849.
    • (2009) J. Biol. Chem. , vol.284 , pp. 33841-33849
    • Da Costa, C.J.1    Medaglia, S.A.2    Lavigne, N.3    Wang, S.4    Carswell, C.L.5    Baenziger, J.E.6
  • 30
    • 84865696393 scopus 로고    scopus 로고
    • Gating movement of acetylcholine receptor caught by plunge-freezing
    • Unwin, N., and Fujiyoshi, Y. (2012) Gating movement of acetylcholine receptor caught by plunge-freezing. J. Mol. Biol. 422, 617-634.
    • (2012) J. Mol. Biol. , vol.422 , pp. 617-634
    • Unwin, N.1    Fujiyoshi, Y.2
  • 31
    • 40049099087 scopus 로고    scopus 로고
    • Microscale fluorescent thermal stability assay for membrane proteins
    • Alexandrov, A. I., Mileni, M., Chien, E. Y., Hanson, M. A., and Stevens, R. C. (2008) Microscale fluorescent thermal stability assay for membrane proteins. Structure 16, 351-359.
    • (2008) Structure , vol.16 , pp. 351-359
    • Alexandrov, A.I.1    Mileni, M.2    Chien, E.Y.3    Hanson, M.A.4    Stevens, R.C.5
  • 33
    • 0028825381 scopus 로고
    • Structure of both the ligand-and lipid-dependent channel-inactive states of the nicotinic acetylcholine receptor probed by FTIR spectroscopy and hydrogen exchange
    • Méthot, N., Demers, C. N., and Baenziger, J. E. (1995) Structure of both the ligand-and lipid-dependent channel-inactive states of the nicotinic acetylcholine receptor probed by FTIR spectroscopy and hydrogen exchange. Biochemistry 34, 15142-15149.
    • (1995) Biochemistry , vol.34 , pp. 15142-15149
    • Méthot, N.1    Demers, C.N.2    Baenziger, J.E.3
  • 34
    • 0021152857 scopus 로고
    • Functional properties of the acetylcholine receptor incorporated in model lipid membranes. Differential effects of chain length and head group of phospholipids on receptor affinity states and receptor-mediated ion translocation
    • Criado, M., Eibl, H., and Barrantes, F. J. (1984) Functional properties of the acetylcholine receptor incorporated in model lipid membranes. Differential effects of chain length and head group of phospholipids on receptor affinity states and receptor-mediated ion translocation. J. Biol. Chem. 259, 9188-9198.
    • (1984) J. Biol. Chem. , vol.259 , pp. 9188-9198
    • Criado, M.1    Eibl, H.2    Barrantes, F.J.3
  • 35
    • 0030734157 scopus 로고    scopus 로고
    • The cholesterol dependence of activation and fast desensitization of the nicotinic acetylcholine receptor
    • Rankin, S. E., Addona, G. H., Kloczewiak, M. A., Bugge, B., and Miller, K. W. (1997) The cholesterol dependence of activation and fast desensitization of the nicotinic acetylcholine receptor. Biophys. J. 73, 2446-2455.
    • (1997) Biophys. J. , vol.73 , pp. 2446-2455
    • Rankin, S.E.1    Addona, G.H.2    Kloczewiak, M.A.3    Bugge, B.4    Miller, K.W.5
  • 36
    • 0029768099 scopus 로고    scopus 로고
    • Structural effects of neutral and anionic lipids on the nicotinic acetylcholine receptor. An infrared difference spectroscopy study
    • Ryan, S. E., Demers, C. N., Chew, J. P., and Baenziger, J. E. (1996) Structural effects of neutral and anionic lipids on the nicotinic acetylcholine receptor. An infrared difference spectroscopy study. J. Biol. Chem. 271, 24590-24597.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24590-24597
    • Ryan, S.E.1    Demers, C.N.2    Chew, J.P.3    Baenziger, J.E.4
  • 37
    • 0024278441 scopus 로고
    • Annular and nonannular binding sites for cholesterol associated with the nicotinic acetylcholine receptor
    • Jones, O. T., and McNamee, M. G. (1988) Annular and nonannular binding sites for cholesterol associated with the nicotinic acetylcholine receptor. Biochemistry 27, 2364-2374.
    • (1988) Biochemistry , vol.27 , pp. 2364-2374
    • Jones, O.T.1    McNamee, M.G.2
  • 38
    • 0019404213 scopus 로고
    • Phospholipid chain immobilization and steroid rotational immobilization in acetylcholine receptor-rich membranes from Torpedo marmorata
    • Marsh, D., Watts, A., and Barrantes, F. J. (1981) Phospholipid chain immobilization and steroid rotational immobilization in acetylcholine receptor-rich membranes from Torpedo marmorata. Biochim. Biophys. Acta 645, 97-101.
    • (1981) Biochim. Biophys. Acta , vol.645 , pp. 97-101
    • Marsh, D.1    Watts, A.2    Barrantes, F.J.3
  • 39
    • 0021110283 scopus 로고
    • Lipid-protein interactions in reconstituted membranes containing acetylcholine receptor
    • Ellena, J. F., Blazing, M. A., and McNamee, M. G. (1983) Lipid-protein interactions in reconstituted membranes containing acetylcholine receptor. Biochemistry 22, 5523-5535.
    • (1983) Biochemistry , vol.22 , pp. 5523-5535
    • Ellena, J.F.1    Blazing, M.A.2    McNamee, M.G.3
  • 40
    • 26944443142 scopus 로고    scopus 로고
    • Identification of the prokaryotic ligand-gated ion channels and their implications for the mechanisms and origins of animal Cys-loop ion channels
    • Tasneem, A., Iyer, L. M., Jakobsson, E., and Aravind, L. (2005) Identification of the prokaryotic ligand-gated ion channels and their implications for the mechanisms and origins of animal Cys-loop ion channels. Genome Biol. 6, R4.
    • (2005) Genome Biol. , vol.6
    • Tasneem, A.1    Iyer, L.M.2    Jakobsson, E.3    Aravind, L.4
  • 42
    • 74049110470 scopus 로고    scopus 로고
    • Anesthetic sensitivity of the Gloeobacter violaceus proton-gated ion channel
    • Weng, Y., Yang, L., Corringer, P. J., and Sonner, J. M. (2010) Anesthetic sensitivity of the Gloeobacter violaceus proton-gated ion channel. Anesth. Analg. 110, 59-63.
    • (2010) Anesth. Analg. , vol.110 , pp. 59-63
    • Weng, Y.1    Yang, L.2    Corringer, P.J.3    Sonner, J.M.4
  • 43
    • 0037155917 scopus 로고    scopus 로고
    • Dissecting the chemistry of nicotinic receptor-ligand interactions with infrared difference spectroscopy
    • Ryan, S. E., Hill, D. G., and Baenziger, J. E. (2002) Dissecting the chemistry of nicotinic receptor-ligand interactions with infrared difference spectroscopy. J. Biol. Chem. 277, 10420-10426.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10420-10426
    • Ryan, S.E.1    Hill, D.G.2    Baenziger, J.E.3
  • 45
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4A resolution
    • Unwin, N. (2005) Refined structure of the nicotinic acetylcholine receptor at 4A resolution. J. Mol. Biol. 346, 967-989.
    • (2005) J. Mol. Biol. , vol.346 , pp. 967-989
    • Unwin, N.1
  • 46
    • 33750481856 scopus 로고    scopus 로고
    • Structure and dynamics of the M4transmembrane domain of the acetylcholine receptor in lipid bilayers. Insights into receptor assembly and function
    • De Almeida, R. F., Loura, L. M., Prieto, M., Watts, A., Fedorov, A., and Barrantes, F. J. (2006) Structure and dynamics of the M4transmembrane domain of the acetylcholine receptor in lipid bilayers. Insights into receptor assembly and function. Mol. Membr. Biol. 23, 305-315.
    • (2006) Mol. Membr. Biol. , vol.23 , pp. 305-315
    • De Almeida, R.F.1    Loura, L.M.2    Prieto, M.3    Watts, A.4    Fedorov, A.5    Barrantes, F.J.6
  • 47
    • 13644270375 scopus 로고    scopus 로고
    • Conformational dynamics of the nicotinic acetylcholine receptor channel. A 35-ns molecular dynamics simulation study
    • Xu, Y., Barrantes, F. J., Luo, X., Chen, K., Shen, J., and Jiang, H. (2005) Conformational dynamics of the nicotinic acetylcholine receptor channel. A 35-ns molecular dynamics simulation study. J. Am. Chem. Soc. 127, 1291-1299.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 1291-1299
    • Xu, Y.1    Barrantes, F.J.2    Luo, X.3    Chen, K.4    Shen, J.5    Jiang, H.6
  • 49
    • 84890114038 scopus 로고    scopus 로고
    • Intra-membrane proton binding site linked to activation of a bacterial pentameric ion channel
    • Wang, H. L., Cheng, X., and Sine, S. M. (2011) Intra-membrane proton binding site linked to activation of a bacterial pentameric ion channel. J. Biol. Chem.
    • (2011) J. Biol. Chem.
    • Wang, H.L.1    Cheng, X.2    Sine, S.M.3
  • 50
    • 80053407923 scopus 로고    scopus 로고
    • Engineering a prokaryotic Cys-loop receptor with a third functional domain
    • Goyal, R., Salahudeen, A. A., and Jansen, M. (2011) Engineering a prokaryotic Cys-loop receptor with a third functional domain. J. Biol. Chem. 286, 34635-34642.
    • (2011) J. Biol. Chem. , vol.286 , pp. 34635-34642
    • Goyal, R.1    Salahudeen, A.A.2    Jansen, M.3
  • 51
    • 84861537525 scopus 로고    scopus 로고
    • Desensitization mechanism in prokaryotic ligand-gated ion channel
    • Velisetty, P., and Chakrapani, S. (2012) Desensitization mechanism in prokaryotic ligand-gated ion channel. J. Biol. Chem. 287, 18467-18477.
    • (2012) J. Biol. Chem. , vol.287 , pp. 18467-18477
    • Velisetty, P.1    Chakrapani, S.2


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