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Volumn 110, Issue 45, 2013, Pages

Reply to Subramaniam, van Heel, and Henderson: Validity of the cryo-electron microscopy structures of the HIV-1 envelope glycoprotein complex

Author keywords

[No Author keywords available]

Indexed keywords

INOSITOL TRIPHOSPHATE RECEPTOR; INOSITOL TRISPHOSPHATE; RECEPTOR; UNCLASSIFIED DRUG; VIRUS ENVELOPE PROTEIN;

EID: 84887299506     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1316666110     Document Type: Letter
Times cited : (15)

References (23)
  • 1
    • 84887297231 scopus 로고    scopus 로고
    • Structure of trimeric hiv-1 envelope glycoproteins
    • Subramaniam S (2013) Structure of trimeric HIV-1 envelope glycoproteins. Proc Natl Acad Sci USA 110:E4172-E4174.
    • (2013) Proc Natl Acad Sci USA , vol.110
    • Subramaniam, S.1
  • 2
    • 84887282198 scopus 로고    scopus 로고
    • Finding trimeric hiv-1 envelope glycoproteins in random noise
    • van Heel M (2013) Finding trimeric HIV-1 envelope glycoproteins in random noise. Proc Natl Acad Sci USA 110:E4175-E4177.
    • (2013) Proc Natl Acad Sci USA , vol.110
    • Van Heel, M.1
  • 3
    • 84887271303 scopus 로고    scopus 로고
    • Avoiding the pitfalls of single particle cryoem: Einstein from noise
    • Henderson R (2013) Avoiding the pitfalls of single particle cryoEM: Einstein from noise. Proc Natl Acad Sci USA 110:18037-18041.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 18037-18041
    • Henderson, R.1
  • 4
    • 84866061123 scopus 로고    scopus 로고
    • Subunit organization of the membrane-bound hiv-1 envelope glycoprotein trimer
    • Mao Y, et al. (2012) Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer. Nat Struct Mol Biol 19(9): 893-899.
    • (2012) Nat Struct Mol Biol , vol.19 , Issue.9 , pp. 893-899
    • Mao, Y.1
  • 5
    • 84880678141 scopus 로고    scopus 로고
    • Molecular architecture of the uncleaved hiv-1 envelope glycoprotein trimer
    • Mao Y, et al. (2013) Molecular architecture of the uncleaved HIV-1 envelope glycoprotein trimer. Proc Natl Acad Sci USA 110(30): 12438-12443.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.30 , pp. 12438-12443
    • Mao, Y.1
  • 8
    • 84887300161 scopus 로고    scopus 로고
    • or contact Dr. Ardan Patwardhan (ardan@ebi.ac.uk)
    • http://www.ebi.ac.uk/ardan/aspera/em-aspera-demo.htmlor contact Dr. Ardan Patwardhan (ardan@ebi.ac.uk).
  • 9
    • 51549085335 scopus 로고    scopus 로고
    • Particle-verification for single-particle, reference-based reconstruction using multivariate data analysis and classification
    • Shaikh TR, Trujillo R, LeBarron JS, Baxter WT, Frank J (2008) Particle-verification for single-particle, reference-based reconstruction using multivariate data analysis and classification. J Struct Biol 164(1): 41-48.
    • (2008) J Struct Biol , vol.164 , Issue.1 , pp. 41-48
    • Shaikh, T.R.1    Trujillo, R.2    Lebarron, J.S.3    Baxter, W.T.4    Frank, J.5
  • 10
    • 16244396466 scopus 로고    scopus 로고
    • Maximum-likelihood multi-reference refinement for electron microscopy images
    • Scheres SH, et al. (2005) Maximum-likelihood multi-reference refinement for electron microscopy images. J Mol Biol 348(1):139-149.
    • (2005) J Mol Biol , vol.348 , Issue.1 , pp. 139-149
    • Scheres, S.H.1
  • 11
    • 0031704540 scopus 로고    scopus 로고
    • A maximum-likelihood approach to singleparticle image refinement
    • Sigworth FJ (1998) A maximum-likelihood approach to singleparticle image refinement. J Struct Biol 122(3):328-339.
    • (1998) J Struct Biol , vol.122 , Issue.3 , pp. 328-339
    • Sigworth, F.J.1
  • 12
    • 0037404096 scopus 로고    scopus 로고
    • An approach to examining model dependence in em reconstructions using cross-validation
    • Shaikh TR, Hegerl R, Frank J (2003) An approach to examining model dependence in EM reconstructions using cross-validation. J Struct Biol 142(2):301-310.
    • (2003) J Struct Biol , vol.142 , Issue.2 , pp. 301-310
    • Shaikh, T.R.1    Hegerl, R.2    Frank, J.3
  • 13
    • 84878860950 scopus 로고    scopus 로고
    • Validation of cryo-em structure of ipr1 channel
    • Murray SC, et al. (2013) Validation of cryo-EM structure of IPR1 channel. Structure 21(6):900-909.
    • (2013) Structure , vol.21 , Issue.6 , pp. 900-909
    • Murray, S.C.1
  • 14
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal PB, Henderson R (2003) Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J Mol Biol 333(4):721-745.
    • (2003) J Mol Biol , vol.333 , Issue.4 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 15
    • 80855132610 scopus 로고    scopus 로고
    • Tilt-pair analysis of images from a range of different specimens in single-particle electron cryomicroscopy
    • Henderson R, et al. (2011) Tilt-pair analysis of images from a range of different specimens in single-particle electron cryomicroscopy. J Mol Biol 413(5):1028-1046.
    • (2011) J Mol Biol , vol.413 , Issue.5 , pp. 1028-1046
    • Henderson, R.1
  • 16
    • 84868444740 scopus 로고    scopus 로고
    • Relion: Implementation of a bayesian approach to cryo-em structure determination
    • Scheres SH (2012) RELION: Implementation of a Bayesian approach to cryo-EM structure determination. J Struct Biol 180(3):519-530.
    • (2012) J Struct Biol , vol.180 , Issue.3 , pp. 519-530
    • Scheres, S.H.1
  • 17
    • 0033777020 scopus 로고    scopus 로고
    • Resolution measurement in structures derived from single particles
    • Grigorieff N (2000) Resolution measurement in structures derived from single particles. Acta Crystallogr D Biol Crystallogr 56(Pt 10):1270-1277.
    • (2000) Acta Crystallogr D Biol Crystallogr , vol.56 , Issue.PART 10 , pp. 1270-1277
    • Grigorieff, N.1
  • 18
    • 84866078359 scopus 로고    scopus 로고
    • Prevention of overfitting in cryo-em structure determination
    • Scheres SHW, Chen S (2012) Prevention of overfitting in cryo-EM structure determination. Nat Methods 9(9):853-854.
    • (2012) Nat Methods , vol.9 , Issue.9 , pp. 853-854
    • Scheres, S.H.W.1    Chen, S.2
  • 20
    • 84864603281 scopus 로고    scopus 로고
    • Structural mechanism of trimeric hiv-1 envelope glycoprotein activation
    • Tran EE, et al. (2012) Structural mechanism of trimeric HIV-1 envelope glycoprotein activation. PLoS Pathog 8(7):e1002797.
    • (2012) PLoS Pathog , vol.8 , Issue.7
    • Tran, E.E.1
  • 21
    • 84872189908 scopus 로고    scopus 로고
    • Molecular structures of trimeric hiv-1 env in complex with small antibody derivatives
    • Meyerson JR, et al. (2013) Molecular structures of trimeric HIV-1 Env in complex with small antibody derivatives. Proc Natl Acad Sci USA 110(2):513-518.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.2 , pp. 513-518
    • Meyerson, J.R.1
  • 22
    • 27744597054 scopus 로고    scopus 로고
    • Structure of a v3-containing hiv-1 gp120 core
    • Huang CC, et al. (2005) Structure of a V3-containing HIV-1 gp120 core. Science 310(5750):1025-1028.
    • (2005) Science , vol.310 , Issue.5750 , pp. 1025-1028
    • Huang, C.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.