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Volumn 59, Issue , 2015, Pages 43-70

Biological membranes

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN;

EID: 84978399721     PISSN: 00711365     EISSN: None     Source Type: Journal    
DOI: 10.1042/BSE0590043     Document Type: Article
Times cited : (221)

References (31)
  • 2
    • 0016753216 scopus 로고
    • Transfer of proteins across membranes. 1. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma
    • Blobel, G. and Dobberstein, B. (1975) Transfer of proteins across membranes. 1. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J. Cell Biol. 67, 835-851.
    • (1975) J. Cell Biol. , vol.67 , pp. 835-851
    • Blobel, G.1    Dobberstein, B.2
  • 3
    • 0001174553 scopus 로고
    • Ribosome-membrane interaction in eukaryotic cells
    • Blobel, G. and Sabatini, D.D. (1971) Ribosome-membrane interaction in eukaryotic cells. Biomembranes 2, 193-195.
    • (1971) Biomembranes , vol.2 , pp. 193-195
    • Blobel, G.1    Sabatini, D.D.2
  • 4
    • 0842324801 scopus 로고    scopus 로고
    • The mechanisms of vesicle budding and fusion
    • Bonifacino, J.S. and Glick, B.S. (2004) The mechanisms of vesicle budding and fusion. Cell 116, 153-166.
    • (2004) Cell , vol.116 , pp. 153-166
    • Bonifacino, J.S.1    Glick, B.S.2
  • 5
    • 80054970860 scopus 로고    scopus 로고
    • Retrieval from the ER-Golgi intermediate compartment is key to the targeting of C-terminally anchored ER-resident proteins
    • Butler, J., Watson, H.R., Lee, A.G., Schuppe, H.J. and East, J.M. (2011) Retrieval from the ER-Golgi intermediate compartment is key to the targeting of C-terminally anchored ER-resident proteins. J. Cell Biochem. 112, 3543-3548.
    • (2011) J. Cell Biochem. , vol.112 , pp. 3543-3548
    • Butler, J.1    Watson, H.R.2    Lee, A.G.3    Schuppe, H.J.4    East, J.M.5
  • 6
    • 0037391107 scopus 로고    scopus 로고
    • Membrane protein crystallization
    • Caffrey, M. (2003) Membrane protein crystallization. J. Struct. Biol. 142, 108-132.
    • (2003) J. Struct. Biol. , vol.142 , pp. 108-132
    • Caffrey, M.1
  • 7
    • 33646576217 scopus 로고    scopus 로고
    • Proteins involved in lipid translocation in eukaryotic cells
    • Devaux, P.F., López-Montero, I. and Bryde, S. (2006) Proteins involved in lipid translocation in eukaryotic cells. Chem. Phys. Lipids 141, 119-132.
    • (2006) Chem. Phys. Lipids , vol.141 , pp. 119-132
    • Devaux, P.F.1    López-Montero, I.2    Bryde, S.3
  • 8
    • 78650280529 scopus 로고    scopus 로고
    • Viral channel forming proteins modeling the target
    • Fischer, W.B. and Hsu, H.-J. (2011) Viral channel forming proteins modeling the target. Biochim. Biophys. Acta 1808, 561-571.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 561-571
    • Fischer, W.B.1    Hsu, H.-J.2
  • 9
    • 0343800636 scopus 로고
    • On bimolecular layers of lipoids on the chromocytes of the blood
    • Gorter, E. and Grendel, F. (1925) On bimolecular layers of lipoids on the chromocytes of the blood. J. Exp. Med. 41, 439-443.
    • (1925) J. Exp. Med. , vol.41 , pp. 439-443
    • Gorter, E.1    Grendel, F.2
  • 10
    • 79955811328 scopus 로고    scopus 로고
    • Recent progress in the study of G protein-coupled receptors with molecular dynamics computer simulations
    • Grossfield, A. (2011) Recent progress in the study of G protein-coupled receptors with molecular dynamics computer simulations. Biochim. Biophys. Acta 1808, 1868-1878.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 1868-1878
    • Grossfield, A.1
  • 12
    • 84872295116 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptors: From basic science to therapeutics
    • Hurst, R., Rollema, H. and Bertrand, D. (2013) Nicotinic acetylcholine receptors: From basic science to therapeutics. Pharmacol. Ther. 137, 22-54.
    • (2013) Pharmacol. Ther. , vol.137 , pp. 22-54
    • Hurst, R.1    Rollema, H.2    Bertrand, D.3
  • 13
    • 40849113435 scopus 로고    scopus 로고
    • The Ca2+ ATPase of cardiac sarcoplasmic reticulum: Physiological role and relevance to diseases
    • Inesi, G., Prasad, A.M. and Pilankatta, R. (2008) The Ca2+ ATPase of cardiac sarcoplasmic reticulum: Physiological role and relevance to diseases. Biochem. Biophys. Res. Commun. 369, 182-187.
    • (2008) Biochem. Biophys. Res. Commun. , vol.369 , pp. 182-187
    • Inesi, G.1    Prasad, A.M.2    Pilankatta, R.3
  • 14
    • 0001266102 scopus 로고
    • A threedimensional model of the myoglobin molecule obtained by X-ray analysis
    • Kendrew, J.C., Bodo, G., Dintzis, H.M., Parrish, R.G., Wyckoff, H. and Phillips, D.C. (1958) A threedimensional model of the myoglobin molecule obtained by X-ray analysis. Nature 181, 662-666.
    • (1958) Nature , vol.181 , pp. 662-666
    • Kendrew, J.C.1    Bodo, G.2    Dintzis, H.M.3    Parrish, R.G.4    Wyckoff, H.5    Phillips, D.C.6
  • 15
    • 0025975875 scopus 로고
    • Disposition of intracellular cholesterol in human fibroblasts
    • Lange, Y. (1991) Disposition of intracellular cholesterol in human fibroblasts. J. Lipid Res. 32, 329-339.
    • (1991) J. Lipid Res. , vol.32 , pp. 329-339
    • Lange, Y.1
  • 16
    • 7044241302 scopus 로고    scopus 로고
    • How lipids affect the activities of integral membrane proteins
    • Lee, A.G. (2004) How lipids affect the activities of integral membrane proteins. Biochim. Biophys. Acta 1666, 62-87.
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 62-87
    • Lee, A.G.1
  • 18
    • 77950596053 scopus 로고    scopus 로고
    • Driving membrane curvature in clathrin-dependent and clathrin-independent endocytosis
    • Lundmark, R. and Carlsson, S.R. (2010) Driving membrane curvature in clathrin-dependent and clathrin-independent endocytosis. Semin. Cell Dev. Biol. 21, 363-370.
    • (2010) Semin. Cell Dev. Biol. , vol.21 , pp. 363-370
    • Lundmark, R.1    Carlsson, S.R.2
  • 19
    • 80051788173 scopus 로고    scopus 로고
    • Urban planning of the endoplasmic reticulum (ER): How diverse mechanisms segregate the many functions of the ER
    • Lynes, E.M. and Simmen, T. (2011) Urban planning of the endoplasmic reticulum (ER): How diverse mechanisms segregate the many functions of the ER. Biochim. Biophys. Acta 1813, 1893-1905.
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 1893-1905
    • Lynes, E.M.1    Simmen, T.2
  • 21
    • 84861779104 scopus 로고    scopus 로고
    • How SNARE molecules mediate membrane fusion: Recent insights from molecular simulations
    • Risselada, H.J. and Grubmüller, H. (2012) How SNARE molecules mediate membrane fusion: Recent insights from molecular simulations. Curr. Opin. Struct. Biol. 22, 187-196.
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 187-196
    • Risselada, H.J.1    Grubmüller, H.2
  • 23
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer, S.J. and Nicolson, G.L. (1972) The fluid mosaic model of the structure of cell membranes. Science 175, 720-731.
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 24
    • 82955185523 scopus 로고    scopus 로고
    • Lipid-protein interactions in biological membranes: A dynamic perspective
    • Smith, A.W. (2012) Lipid-protein interactions in biological membranes: A dynamic perspective. Biochim. Biophys. Acta 1818, 172-177.
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 172-177
    • Smith, A.W.1
  • 25
    • 84865436871 scopus 로고    scopus 로고
    • A crystal clear solution for determining G-protein-coupled receptor structures
    • Tate, C.G. (2012) A crystal clear solution for determining G-protein-coupled receptor structures. Trends Biochem. Sci. 37, 343-352.
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 343-352
    • Tate, C.G.1
  • 26
    • 84877704954 scopus 로고    scopus 로고
    • Botulinum neurotoxins: Mechanism of action
    • Tighe, A.P. and Schiavo, G. (2013) Botulinum neurotoxins: Mechanism of action. Toxicon 67, 87-93.
    • (2013) Toxicon , vol.67 , pp. 87-93
    • Tighe, A.P.1    Schiavo, G.2
  • 27
    • 78349305715 scopus 로고    scopus 로고
    • Dynamics and flexibility of G-protein-coupled receptor conformations and their relevance to drug design
    • Vaidehi, N. (2010) Dynamics and flexibility of G-protein-coupled receptor conformations and their relevance to drug design. Drug Discov. Today 15, 951-957.
    • (2010) Drug Discov. Today , vol.15 , pp. 951-957
    • Vaidehi, N.1
  • 28
    • 78651095014 scopus 로고    scopus 로고
    • Lipid map of the mammalian cell
    • van Meer, G. and de Kroon, A.I. (2011) Lipid map of the mammalian cell. J. Cell Sci. 124, 5-8.
    • (2011) J. Cell Sci. , vol.124 , pp. 5-8
    • Van Meer, G.1    De Kroon, A.I.2
  • 29
    • 79955628672 scopus 로고    scopus 로고
    • The localization of the ER retrieval sequence for the calcium pump SERCA1
    • Watson, H.R., Butler, J., Schuppe, H.J., Lee, A.G. and East, J.M. (2011) The localization of the ER retrieval sequence for the calcium pump SERCA1. Mol. Membr. Biol. 28, 216-226.
    • (2011) Mol. Membr. Biol. , vol.28 , pp. 216-226
    • Watson, H.R.1    Butler, J.2    Schuppe, H.J.3    Lee, A.G.4    East, J.M.5
  • 30
    • 66249121383 scopus 로고    scopus 로고
    • Biophysical dissection of membrane proteins
    • White, S.H. (2009) Biophysical dissection of membrane proteins. Nature 459, 344-346.
    • (2009) Nature , vol.459 , pp. 344-346
    • White, S.H.1
  • 31
    • 0041428149 scopus 로고    scopus 로고
    • The versatile β-barrel membrane protein
    • Wimley, W.C. (2003) The versatile β-barrel membrane protein. Curr. Opin. Struct. Biol. 13, 404-411.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 404-411
    • Wimley, W.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.