메뉴 건너뛰기




Volumn 287, Issue 9, 2012, Pages 6169-6176

Identification of in vivo disulfide conformation of TRPA1 ion channel

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION MECHANISMS; ANKYRIN; CONFORMATION CHANGE; CYSTEINE RESIDUES; DISULFIDE BONDING; DISULFIDE BONDS; IN-VITRO; IN-VIVO; ION CHANNEL; LIGAND BINDING; N-TERMINAL DOMAINS; N-TERMINALS; NOCICEPTION; PROTEIN CONFORMATION; SENSORY NEURONS; TRANSIENT RECEPTOR POTENTIALS;

EID: 84863178659     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.329748     Document Type: Article
Times cited : (63)

References (34)
  • 3
    • 1842475312 scopus 로고    scopus 로고
    • Noxious cold ion channel TRPA1 is activated by pungent compounds and bradykinin
    • DOI 10.1016/S0896-6273(04)00150-3, PII S0896627304001503
    • Bandell, M., Story, G. M., Hwang, S. W., Viswanath, V., Eid, S. R., Petrus, M. J., Earley, T. J., and Patapoutian, A. (2004) Noxious cold ion channel TRPA1 is activated by pungent compounds and bradykinin. Neuron 41, 849-857 (Pubitemid 38429729)
    • (2004) Neuron , vol.41 , Issue.6 , pp. 849-857
    • Bandell, M.1    Story, G.M.2    Hwang, S.W.3    Viswanath, V.4    Eid, S.R.5    Petrus, M.J.6    Earley, T.J.7    Patapoutian, A.8
  • 4
    • 33846692923 scopus 로고    scopus 로고
    • Noxious compounds activate TRPA1 ion channels through covalent modification of cysteines
    • DOI 10.1038/nature05544, PII NATURE05544
    • Macpherson, L. J., Dubin, A. E., Evans, M. J., Marr, F., Schultz, P. G., Cravatt, B. F., and Patapoutian, A. (2007) Noxious compounds activate TRPA1 ion channels through covalent modification of cysteines. Nature 445, 541-545 (Pubitemid 46197634)
    • (2007) Nature , vol.445 , Issue.7127 , pp. 541-545
    • Macpherson, L.J.1    Dubin, A.E.2    Evans, M.J.3    Marr, F.4    Schultz, P.G.5    Cravatt, B.F.6    Patapoutian, A.7
  • 6
    • 55749115431 scopus 로고    scopus 로고
    • Molecular characterization of TRPA1 channel activation by cysteine-reactive inflammatory mediators
    • Takahashi, N., Mizuno, Y., Kozai, D., Yamamoto, S., Kiyonaka, S., Shibata, T., Uchida, K., and Mori, Y. (2008) Molecular characterization of TRPA1 channel activation by cysteine-reactive inflammatory mediators. Channels 2, 287-298
    • (2008) Channels , vol.2 , pp. 287-298
    • Takahashi, N.1    Mizuno, Y.2    Kozai, D.3    Yamamoto, S.4    Kiyonaka, S.5    Shibata, T.6    Uchida, K.7    Mori, Y.8
  • 7
    • 33846807748 scopus 로고    scopus 로고
    • Transient receptor potential cation channels in disease
    • DOI 10.1152/physrev.00021.2006
    • Nilius, B., Owsianik, G., Voets, T., and Peters, J. A. (2007) Transient receptor potential cation channels in disease. Physiol. Rev. 87, 165-217 (Pubitemid 46207713)
    • (2007) Physiological Reviews , vol.87 , Issue.1 , pp. 165-217
    • Nilius, B.1    Owsianik, G.2    Voets, T.3    Peters, J.A.4
  • 10
    • 81755185888 scopus 로고    scopus 로고
    • Cytoplasmic ankyrin repeats of transient receptor potential A1 (TRPA1) dictate sensitivity to thermal and chemical stimuli
    • Cordero-Morales, J. F., Gracheva, E. O., and Julius, D. (2011) Cytoplasmic ankyrin repeats of transient receptor potential A1 (TRPA1) dictate sensitivity to thermal and chemical stimuli. Proc. Natl. Acad. Sci. U.S.A. 108, E1184-E1191
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108
    • Cordero-Morales, J.F.1    Gracheva, E.O.2    Julius, D.3
  • 11
    • 33846661523 scopus 로고    scopus 로고
    • Chemical biology: Sticky spices
    • Caterina, M. J. (2007) Chemical biology: sticky spices. Nature 445, 491-492
    • (2007) Nature , vol.445 , pp. 491-492
    • Caterina, M.J.1
  • 12
    • 80055073153 scopus 로고    scopus 로고
    • Molecular architecture and subunit organization of TRPA1 ion channel revealed by electron microscopy
    • Cvetkov, T. L., Huynh, K. W., Cohen, M. R., and Moiseenkova-Bell, V. Y. (2011) Molecular architecture and subunit organization of TRPA1 ion channel revealed by electron microscopy. J. Biol. Chem. 286, 38168-38176
    • (2011) J. Biol. Chem. , vol.286 , pp. 38168-38176
    • Cvetkov, T.L.1    Huynh, K.W.2    Cohen, M.R.3    Moiseenkova-Bell, V.Y.4
  • 13
    • 0141849083 scopus 로고    scopus 로고
    • Overexpression and purification of the vanilloid receptor in yeast (Saccharomyces cerevisiae)
    • DOI 10.1016/j.bbrc.2003.09.011
    • Moiseenkova, V. Y., Hellmich, H. L., and Christensen, B. N. (2003) Overexpression and purification of the vanilloid receptor in yeast (Saccharomyces cerevisiae). Biochem. Biophys. Res. Commun. 310, 196-201 (Pubitemid 37162782)
    • (2003) Biochemical and Biophysical Research Communications , vol.310 , Issue.1 , pp. 196-201
    • Moiseenkova, V.Yu.1    Hellmich, H.L.2    Christensen, B.N.3
  • 14
    • 38649131282 scopus 로고    scopus 로고
    • Identification and characterization of disulfide bonds in proteins and peptides from tandem MS data by use of the MassMatrix MS/MS search engine
    • DOI 10.1021/pr070363z
    • Xu, H., Zhang, L., and Freitas, M. A. (2008) Identification and characterization of disulfide bonds in proteins and peptides from tandem MS data by use of the MassMatrix MS/MS search engine. J. Proteome Res. 7, 138-144 (Pubitemid 351171125)
    • (2008) Journal of Proteome Research , vol.7 , Issue.1 , pp. 138-144
    • Xu, H.1    Zhang, L.2    Freitas, M.A.3
  • 15
    • 65349143654 scopus 로고    scopus 로고
    • 3 database search algorithm for automated analysis of phosphopeptide tandem mass spectra
    • 3 database search algorithm for automated analysis of phosphopeptide tandem mass spectra. Proteomics 9, 1763-1770
    • (2009) Proteomics , vol.9 , pp. 1763-1770
    • Xu, H.1    Wang, L.2    Sallans, L.3    Freitas, M.A.4
  • 16
    • 63049105321 scopus 로고    scopus 로고
    • MassMatrix: A database search program for rapid characterization of proteins and peptides from tandem mass spectrometry data
    • Xu, H., and Freitas, M. A. (2009) MassMatrix: a database search program for rapid characterization of proteins and peptides from tandem mass spectrometry data. Proteomics 9, 1548-1555
    • (2009) Proteomics , vol.9 , pp. 1548-1555
    • Xu, H.1    Freitas, M.A.2
  • 17
    • 64549113013 scopus 로고    scopus 로고
    • Hot on the trail of TRP channel structure
    • Moiseenkova-Bell, V. Y., and Wensel, T. G. (2009) Hot on the trail of TRP channel structure. J. Gen. Physiol. 133, 239-244
    • (2009) J. Gen. Physiol. , vol.133 , pp. 239-244
    • Moiseenkova-Bell, V.Y.1    Wensel, T.G.2
  • 18
    • 79959788691 scopus 로고    scopus 로고
    • Functional and structural studies of TRP channels heterologously expressed in budding yeast
    • Moiseenkova-Bell, V., and Wensel, T. G. (2011) Functional and structural studies of TRP channels heterologously expressed in budding yeast. Adv. Exp. Med. Biol. 704, 25-40
    • (2011) Adv. Exp. Med. Biol. , vol.704 , pp. 25-40
    • Moiseenkova-Bell, V.1    Wensel, T.G.2
  • 19
    • 42949117400 scopus 로고    scopus 로고
    • A Yeast Genetic Screen Reveals a Critical Role for the Pore Helix Domain in TRP Channel Gating
    • DOI 10.1016/j.neuron.2008.04.012, PII S0896627308003383
    • Myers, B. R., Bohlen, C. J., and Julius, D. (2008) A yeast genetic screen reveals a critical role for the pore helix domain in TRP channel gating. Neuron 58, 362-373 (Pubitemid 351615191)
    • (2008) Neuron , vol.58 , Issue.3 , pp. 362-373
    • Myers, B.R.1    Bohlen, C.J.2    Julius, D.3
  • 20
    • 59449106080 scopus 로고    scopus 로고
    • Multiple unbiased prospective screens identify TRP channels and their conserved gating elements
    • Myers, B. R., Saimi, Y., Julius, D., and Kung, C. (2008) Multiple unbiased prospective screens identify TRP channels and their conserved gating elements. J. Gen. Physiol. 132, 481-486
    • (2008) J. Gen. Physiol. , vol.132 , pp. 481-486
    • Myers, B.R.1    Saimi, Y.2    Julius, D.3    Kung, C.4
  • 21
    • 27944442839 scopus 로고    scopus 로고
    • Disulfide relays and phosphorylative cascades: Partners in redox-mediated signaling pathways
    • DOI 10.1038/sj.cdd.4401754, PII 4401754
    • Filomeni, G., Rotilio, G., and Ciriolo, M. R. (2005) Disulfide relays and phosphorylative cascades: partners in redox-mediated signaling pathways. Cell Death Differ. 12, 1555-1563 (Pubitemid 41679161)
    • (2005) Cell Death and Differentiation , vol.12 , Issue.12 , pp. 1555-1563
    • Filomeni, G.1    Rotilio, G.2    Ciriolo, M.R.3
  • 22
    • 50849135137 scopus 로고    scopus 로고
    • Glutathione-dependent redox status of frataxin-deficient cells in a yeast model of Friedreich's ataxia
    • Auchère, F., Santos, R., Planamente, S., Lesuisse, E., and Camadro, J. M. (2008) Glutathione-dependent redox status of frataxin-deficient cells in a yeast model of Friedreich's ataxia. Hum. Mol. Genet 17, 2790-2802
    • (2008) Hum. Mol. Genet , vol.17 , pp. 2790-2802
    • Auchère, F.1    Santos, R.2    Planamente, S.3    Lesuisse, E.4    Camadro, J.M.5
  • 23
    • 3543079758 scopus 로고    scopus 로고
    • An examination of quinone toxicity using the yeast Saccharomyces cerevisiae model system
    • DOI 10.1016/j.tox.2004.04.016, PII S0300483X04002707
    • Rodriguez, C. E., Shinyashiki, M., Froines, J., Yu, R. C., Fukuto, J. M., and Cho, A. K. (2004) An examination of quinone toxicity using the yeast Saccharomyces cerevisiae model system. Toxicology 201, 185-196 (Pubitemid 39023945)
    • (2004) Toxicology , vol.201 , Issue.1-3 , pp. 185-196
    • Rodriguez, C.E.1    Shinyashiki, M.2    Froines, J.3    Yu, R.C.4    Fukuto, J.M.5    Cho, A.K.6
  • 24
    • 80052039000 scopus 로고    scopus 로고
    • Redox regulation in respiring Saccharomyces cerevisiae
    • Murray, D. B., Haynes, K., and Tomita, M. (2011) Redox regulation in respiring Saccharomyces cerevisiae. Biochim. Biophys. Acta 1810, 945-958
    • (2011) Biochim. Biophys. Acta , vol.1810 , pp. 945-958
    • Murray, D.B.1    Haynes, K.2    Tomita, M.3
  • 25
    • 57649183232 scopus 로고    scopus 로고
    • The redox environment in the mitochondrial intermembrane space is maintained separately from the cytosol and matrix
    • Hu, J., Dong, L., and Outten, C. E. (2008) The redox environment in the mitochondrial intermembrane space is maintained separately from the cytosol and matrix. J. Biol. Chem. 283, 29126-29134
    • (2008) J. Biol. Chem. , vol.283 , pp. 29126-29134
    • Hu, J.1    Dong, L.2    Outten, C.E.3
  • 28
    • 51349088530 scopus 로고    scopus 로고
    • Molecular mechanisms and clinical implications of reversible protein S-glutathionylation
    • Mieyal, J. J., Gallogly, M. M., Qanungo, S., Sabens, E. A., and Shelton, M. D. (2008) Molecular mechanisms and clinical implications of reversible protein S-glutathionylation. Antioxid. Redox Signal. 10, 1941-1988
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 1941-1988
    • Mieyal, J.J.1    Gallogly, M.M.2    Qanungo, S.3    Sabens, E.A.4    Shelton, M.D.5
  • 29
    • 66649131057 scopus 로고    scopus 로고
    • Crystal structure of the human lymphoid tyrosine phosphatase catalytic domain: Insights into redox regulation
    • Tsai, S. J., Sen, U., Zhao, L., Greenleaf, W. B., Dasgupta, J., Fiorillo, E., Orrú, V., Bottini, N., and Chen, X. S. (2009) Crystal structure of the human lymphoid tyrosine phosphatase catalytic domain: insights into redox regulation . Biochemistry 48, 4838-4845
    • (2009) Biochemistry , vol.48 , pp. 4838-4845
    • Tsai, S.J.1    Sen, U.2    Zhao, L.3    Greenleaf, W.B.4    Dasgupta, J.5    Fiorillo, E.6    Orrú, V.7    Bottini, N.8    Chen, X.S.9
  • 30
    • 33746049192 scopus 로고    scopus 로고
    • Redox regulation of MAPkinase phosphatase 3
    • Seth, D., and Rudolph, J. (2006) Redox regulation of MAPkinase phosphatase 3. Biochemistry 45, 8476-8487
    • (2006) Biochemistry , vol.45 , pp. 8476-8487
    • Seth, D.1    Rudolph, J.2
  • 31
    • 0041323072 scopus 로고    scopus 로고
    • Catalytic and chemical competence of regulation of Cdc25 phosphatase by oxidation/reduction
    • DOI 10.1021/bi0345081
    • Sohn, J., and Rudolph, J. (2003) Catalytic and chemical competence of regulation of Cdc25 phosphatase by oxidation/reduction. Biochemistry 42, 10060-10070 (Pubitemid 37052026)
    • (2003) Biochemistry , vol.42 , Issue.34 , pp. 10060-10070
    • Sohn, J.1    Rudolph, J.2
  • 32
    • 64349117191 scopus 로고    scopus 로고
    • Redox regulation of SH2 domain-containing protein-tyrosine phosphatases by two backdoor cysteines
    • Chen, C. Y., Willard, D., and Rudolph, J. (2009) Redox regulation of SH2 domain-containing protein-tyrosine phosphatases by two backdoor cysteines. Biochemistry 48, 1399-1409
    • (2009) Biochemistry , vol.48 , pp. 1399-1409
    • Chen, C.Y.1    Willard, D.2    Rudolph, J.3
  • 34
    • 53849108437 scopus 로고    scopus 로고
    • Molecular modeling of the full-length human TRPV1 channel in closed and desensitized states
    • Fernández-Ballester, G., and Ferrer-Montiel, A. (2008) Molecular modeling of the full-length human TRPV1 channel in closed and desensitized states. J. Membr. Biol. 223, 161-172
    • (2008) J. Membr. Biol. , vol.223 , pp. 161-172
    • Fernández-Ballester, G.1    Ferrer-Montiel, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.