메뉴 건너뛰기




Volumn 82, Issue 3, 2012, Pages 408-419

Neurosteroid analog photolabeling of a site in the third transmembrane domain of the β3 subunit of the GABAA receptor

Author keywords

[No Author keywords available]

Indexed keywords

(3ALPHA,5BETA) 6 AZIPREGNANOLONE; 3ALPHA HYDROXY 5ALPHA PREGNAN 20 ONE; 4 AMINOBUTYRIC ACID A RECEPTOR; NEUROSTEROID; REAGENT; TERT BUTYLBICYCLOPHOSPHOROTHIOATE; UNCLASSIFIED DRUG;

EID: 84865244600     PISSN: 0026895X     EISSN: 15210111     Source Type: Journal    
DOI: 10.1124/mol.112.078410     Document Type: Article
Times cited : (65)

References (40)
  • 2
    • 50449086734 scopus 로고    scopus 로고
    • Mutations of the GABA-A receptor α1 subunit M1 domain reveal unexpected complexity for modulation by neuroactive steroids
    • Akk G, Li P, Bracamontes J, Reichert DE, Covey DF, and Steinbach JH (2008) Mutations of the GABA-A receptor α1 subunit M1 domain reveal unexpected complexity for modulation by neuroactive steroids. Mol Pharmacol 74:614-627.
    • (2008) Mol Pharmacol , vol.74 , pp. 614-627
    • Akk, G.1    Li, P.2    Bracamontes, J.3    Reichert, D.E.4    Covey, D.F.5    Steinbach, J.H.6
  • 5
    • 0013787433 scopus 로고
    • Action of some steroids on the central nervous system of the mouse. II. Pharmacology
    • Atkinson RM, Davis B, Pratt MA, Sharpe HM, and Tomich EG (1965) Action of some steroids on the central nervous system of the mouse. II. Pharmacology. J Med Chem 8:426-432.
    • (1965) J Med Chem , vol.8 , pp. 426-432
    • Atkinson, R.M.1    Davis, B.2    Pratt, M.A.3    Sharpe, H.M.4    Tomich, E.G.5
  • 7
    • 0027203297 scopus 로고
    • New photolabeling and crosslinking methods
    • Brunner J (1993) New photolabeling and crosslinking methods. Annu Rev Biochem 62:483-514.
    • (1993) Annu Rev Biochem , vol.62 , pp. 483-514
    • Brunner, J.1
  • 8
    • 0027339979 scopus 로고
    • A receptor subtypes: Ligand binding heterogeneity demonstrated by photoaffinity labeling and autoradiography
    • A receptor subtypes: ligand binding heterogeneity demonstrated by photoaffinity labeling and autoradiography. J Neurochem 61:1479-1491.
    • (1993) J Neurochem , vol.61 , pp. 1479-1491
    • Bureau, M.H.1    Olsen, R.W.2
  • 11
    • 77952956167 scopus 로고    scopus 로고
    • Decoding signalling networks by mass spectrometry-based proteomics
    • Choudhary C and Mann M (2010) Decoding signalling networks by mass spectrometry-based proteomics. Nat Rev Mol Cell Biol 11:427-439.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 427-439
    • Choudhary, C.1    Mann, M.2
  • 14
    • 0030902186 scopus 로고    scopus 로고
    • A receptors comprised of α1β3 and β3 subunits expressed in human embryonic kidney 293 cells
    • A receptors comprised of α1β3 and β3 subunits expressed in human embryonic kidney 293 cells. Br J Pharmacol 120:899-909.
    • (1997) Br J Pharmacol , vol.120 , pp. 899-909
    • Davies, P.A.1    Kirkness, E.F.2    Hales, T.G.3
  • 15
    • 0029870397 scopus 로고    scopus 로고
    • The major site of photoaffinity labeling of the gamma-aminobutyric acid type A receptor by [3H]flunitrazepam is histidine 102 of the alpha subunit
    • Duncalfe LL, Carpenter MR, Smillie LB, Martin IL, and Dunn SM (1996) The major site of photoaffinity labeling of the gamma-aminobutyric acid type A receptor by [3H]flunitrazepam is histidine 102 of the alpha subunit. J Biol Chem 271:9209-9214.
    • (1996) J Biol Chem , vol.271 , pp. 9209-9214
    • Duncalfe, L.L.1    Carpenter, M.R.2    Smillie, L.B.3    Martin, I.L.4    Dunn, S.M.5
  • 16
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar RC (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32:1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 19
    • 79957953215 scopus 로고    scopus 로고
    • Principles of activation and permeation in an anion-selective Cys-loop receptor
    • Hibbs RE and Gouaux E (2011) Principles of activation and permeation in an anion-selective Cys-loop receptor. Nature 474:54-60.
    • (2011) Nature , vol.474 , pp. 54-60
    • Hibbs, R.E.1    Gouaux, E.2
  • 22
    • 53049091572 scopus 로고    scopus 로고
    • A receptor subunits representing strongly hydrophobic transmembrane proteins
    • A receptor subunits representing strongly hydrophobic transmembrane proteins. J Proteome Res 7:3498-3506.
    • (2008) J Proteome Res , vol.7 , pp. 3498-3506
    • Kang, S.U.1    Fuchs, K.2    Sieghart, W.3    Lubec, G.4
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 36749047362 scopus 로고    scopus 로고
    • Photo-leucine incorporation reveals the target of a cyclodepsipeptide inhibitor of cotranslational translocation
    • MacKinnon AL, Garrison JL, Hegde RS, and Taunton J (2007) Photo-leucine incorporation reveals the target of a cyclodepsipeptide inhibitor of cotranslational translocation. J Am Chem Soc 129:14560-14561.
    • (2007) J Am Chem Soc , vol.129 , pp. 14560-14561
    • MacKinnon, A.L.1    Garrison, J.L.2    Hegde, R.S.3    Taunton, J.4
  • 29
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii AI, Keller A, Kolker E, and Aebersold R (2003) A statistical model for identifying proteins by tandem mass spectrometry. Anal Chem 75:4646-4658.
    • (2003) Anal Chem , vol.75 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 30
    • 49849105549 scopus 로고    scopus 로고
    • Label-free detection of differential protein expression by LC/MALDI mass spectrometry
    • Neubert H, Bonnert TP, Rumpel K, Hunt BT, Henle ES, and James IT (2008) Label-free detection of differential protein expression by LC/MALDI mass spectrometry. J Proteome Res 7:2270-2279.
    • (2008) J Proteome Res , vol.7 , pp. 2270-2279
    • Neubert, H.1    Bonnert, T.P.2    Rumpel, K.3    Hunt, B.T.4    Henle, E.S.5    James, I.T.6
  • 31
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame C, Higgins DG, and Heringa J (2000) T-Coffee: a novel method for fast and accurate multiple sequence alignment. J Mol Biol 302:205-217.
    • (2000) J Mol Biol , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 33
    • 0345168214 scopus 로고    scopus 로고
    • Isotope and affinity tags in photoreactive substance P analogues to identify the covalent linkage within the NK-1 receptor by MALDI-TOF analysis
    • Sachon E, Tasseau O, Lavielle S, Sagan S, and Bolbach G (2003) Isotope and affinity tags in photoreactive substance P analogues to identify the covalent linkage within the NK-1 receptor by MALDI-TOF analysis. Anal Chem 75:6536-6543.
    • (2003) Anal Chem , vol.75 , pp. 6536-6543
    • Sachon, E.1    Tasseau, O.2    Lavielle, S.3    Sagan, S.4    Bolbach, G.5
  • 34
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A and Blundell TL (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234:779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 35
    • 0344364894 scopus 로고
    • Anesthetic effect of steroid hormones
    • Selye H (1941) Anesthetic effect of steroid hormones. Proc Soc Exp Biol Med 46:116-121.
    • (1941) Proc Soc Exp Biol Med , vol.46 , pp. 116-121
    • Selye, H.1
  • 36
    • 33749578940 scopus 로고    scopus 로고
    • Statistical potential for assessment and prediction of protein structures
    • Shen MY and Sali A (2006) Statistical potential for assessment and prediction of protein structures. Protein Sci 15:2507-2524.
    • (2006) Protein Sci , vol.15 , pp. 2507-2524
    • Shen, M.Y.1    Sali, A.2
  • 37
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4Å resolution
    • Unwin N (2005) Refined structure of the nicotinic acetylcholine receptor at 4Å resolution. J Mol Biol 346:967-989.
    • (2005) J Mol Biol , vol.346 , pp. 967-989
    • Unwin, N.1
  • 39
    • 55249104730 scopus 로고    scopus 로고
    • Sample preparation and in-solution protease digestion of proteins for chromatography-based proteomic analysis
    • Washburn MP (2008) Sample preparation and in-solution protease digestion of proteins for chromatography-based proteomic analysis. Curr Protoc Protein Sci Chapter 23:23.6.1-23.6.11.
    • (2008) Curr Protoc Protein Sci Chapter , vol.23
    • Washburn, M.P.1
  • 40
    • 25444437909 scopus 로고    scopus 로고
    • Calibration of mass spectrometric peptide mass fingerprint data without specific external or internal calibrants
    • Wolski WE, Lalowski M, Jungblut P, and Reinert K (2005) Calibration of mass spectrometric peptide mass fingerprint data without specific external or internal calibrants. BMC Bioinformatics 6:203.
    • (2005) BMC Bioinformatics , vol.6 , pp. 203
    • Wolski, W.E.1    Lalowski, M.2    Jungblut, P.3    Reinert, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.