메뉴 건너뛰기




Volumn 416, Issue 3, 2012, Pages 328-334

Thermodynamic measurements of bilayer insertion of a single transmembrane helix chaperoned by fluorinated surfactants

Author keywords

bilayer insertion; free energy; helical backbone; transmembrane helices; WALP peptides

Indexed keywords

CHAPERONE; CHOLINE; DETERGENT; DYE; HYDROCARBON; OLEOYLPALMITOYLLECITHIN; ORGANIC SOLVENT; SINGLE TRANSMEMBRANE HELIX CHAPERONE; SURFACTANT; UNCLASSIFIED DRUG; WATER;

EID: 84856725828     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.12.037     Document Type: Article
Times cited : (15)

References (56)
  • 2
    • 2542452829 scopus 로고    scopus 로고
    • Cotranslational membrane protein biogenesis at the endoplasmic reticulum
    • DOI 10.1074/jbc.R400002200
    • Alder N.N., and Johnson A.E. Cotranslational membrane protein biogenesis at the endoplasmic reticulum J. Biol. Chem. 279 2004 22787 22790 (Pubitemid 38685576)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.22 , pp. 22787-22790
    • Alder, N.N.1    Johnson, A.E.2
  • 3
    • 4644356464 scopus 로고    scopus 로고
    • Membrane-protein integration and the role of the translocation channel
    • DOI 10.1016/j.tcb.2004.09.002, PII S096289240400234X
    • Rapoport T.A., Goder V., Heinrich S.U., and Matlack K.E.S. Membrane-protein integration and the role of the translocation channel Trends Cell Biol. 14 2004 568 575 (Pubitemid 39296619)
    • (2004) Trends in Cell Biology , vol.14 , Issue.10 , pp. 568-575
    • Rapoport, T.A.1    Goder, V.2    Heinrich, S.U.3    Matlack, K.E.S.4
  • 5
    • 0033543208 scopus 로고    scopus 로고
    • Anthrax protective antigen: Prepore-to-pore conversion
    • Miller C.J., Elliott J.L., and Collier R.J. Anthrax protective antigen: prepore-to-pore conversion Biochemistry 38 1999 10432 10441
    • (1999) Biochemistry , vol.38 , pp. 10432-10441
    • Miller, C.J.1    Elliott, J.L.2    Collier, R.J.3
  • 6
    • 0033615736 scopus 로고    scopus 로고
    • The mechanism of membrane insertion for a cholesterol-dependent cytolysin: A novel paradigm for pore-forming toxins
    • DOI 10.1016/S0092-8674(00)81660-8
    • Shatursky O., Heuck A.P., Shepard L.A., Rossjohn J., Parker M.W., Johnson A.E., and Tweten R.K. The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for pore-forming toxins Cell 99 1999 293 299 (Pubitemid 29519908)
    • (1999) Cell , vol.99 , Issue.3 , pp. 293-299
    • Shatursky, O.1    Heuck, A.P.2    Shepard, L.A.3    Rossjohn, J.4    Parker, M.W.5    Johnson, A.E.6    Tweten, R.K.7
  • 9
    • 0033621164 scopus 로고    scopus 로고
    • Kinetic description of structural changes linked to membrane import of the colicin E1 channel protein
    • Zakharov S.D., Lindeberg M., and Cramer W.A. Kinetic description of structural changes linked to membrane import of the colicin E1 channel protein Biochemistry 38 1999 11325 11332
    • (1999) Biochemistry , vol.38 , pp. 11325-11332
    • Zakharov, S.D.1    Lindeberg, M.2    Cramer, W.A.3
  • 10
    • 0033609909 scopus 로고    scopus 로고
    • Adventures in membrane protein topology: A study of the membrane-bound state of colicin E1
    • Tory M.C., and Merrill A.R. Adventures in membrane protein topology: a study of the membrane-bound state of colicin E1 J. Biol. Chem. 274 1999 24539 24549
    • (1999) J. Biol. Chem. , vol.274 , pp. 24539-24549
    • Tory, M.C.1    Merrill, A.R.2
  • 12
    • 70350359860 scopus 로고    scopus 로고
    • Biogenesis of tail-anchored proteins: The beginning for the end?
    • Rabu C., Schmid V., Schwappach B., and High S. Biogenesis of tail-anchored proteins: the beginning for the end? J. Cell Sci. 122 2009 3605 3612
    • (2009) J. Cell Sci. , vol.122 , pp. 3605-3612
    • Rabu, C.1    Schmid, V.2    Schwappach, B.3    High, S.4
  • 13
    • 77950624268 scopus 로고    scopus 로고
    • Helix insertion into bilayers and the evolution of membrane proteins
    • Renthal R. Helix insertion into bilayers and the evolution of membrane proteins Cell. Mol. Life Sci. 67 2010 1077 1088
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 1077-1088
    • Renthal, R.1
  • 14
    • 0030963602 scopus 로고    scopus 로고
    • Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis
    • Hsu Y.T., Wolter K.G., and Youle R.J. Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis Proc. Natl Acad. Sci. USA 94 1997 3668 3672
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 3668-3672
    • Hsu, Y.T.1    Wolter, K.G.2    Youle, R.J.3
  • 15
    • 33750619845 scopus 로고    scopus 로고
    • How do Bax and Bak lead to permeabilization of the outer mitochondrial membrane?
    • DOI 10.1016/j.ceb.2006.10.004, PII S0955067406001578
    • Antignani A., and Youle R.J. How do Bax and Bak lead to permeabilization of the outer mitochondrial membrane? Curr. Opin. Cell Biol. 18 2006 685 689 (Pubitemid 44692478)
    • (2006) Current Opinion in Cell Biology , vol.18 , Issue.6 , pp. 685-689
    • Antignani, A.1    Youle, R.J.2
  • 16
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: Opposing activities that mediate cell death
    • Youle R.J., and Strasser A. The BCL-2 protein family: opposing activities that mediate cell death Nat. Rev., Mol. Cell Biol. 9 2008 47 59
    • (2008) Nat. Rev., Mol. Cell Biol. , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 18
    • 27844476903 scopus 로고    scopus 로고
    • Do protein-lipid interactions determine the recognition of transmembrane helices at the ER translocon?
    • DOI 10.1042/BST20051012
    • White S.H., and von Heijne G. Do protein-lipid interactions determine the recognition of transmembrane helices at the ER translocon? Biochem. Soc. Trans. 33 2005 1012 1015 (Pubitemid 41659102)
    • (2005) Biochemical Society Transactions , vol.33 , Issue.5 , pp. 1012-1015
    • White, S.H.1    Von Heijne, G.2
  • 19
    • 13444274461 scopus 로고    scopus 로고
    • Border crossing
    • Bowie J.U. Border crossing Nature 433 2005 367 369
    • (2005) Nature , vol.433 , pp. 367-369
    • Bowie, J.U.1
  • 20
    • 0346749514 scopus 로고    scopus 로고
    • Reversible Topological Organization within a Polytopic Membrane Protein is Governed by a Change in Membrane Phospholipid Composition
    • DOI 10.1074/jbc.M309840200
    • Zhang W., Bogdanov M., Pi J., Pittard A.J., and Dowhan W. Reversible topological organization within a polytopic membrane protein is governed by a change in membrane phospholipid composition J. Biol. Chem. 278 2003 50128 50135 (Pubitemid 37548850)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.50 , pp. 50128-50135
    • Zhang, W.1    Bogdanov, M.2    Pi, J.3    Pittard, A.J.4    Dowhan, W.5
  • 23
    • 65649102996 scopus 로고    scopus 로고
    • Lipid-protein interactions drive membrane protein topogenesis in accordance with the positive inside rule
    • Bogdanov M., Xie J., and Dowhan W. Lipid-protein interactions drive membrane protein topogenesis in accordance with the positive inside rule J. Biol. Chem. 284 2009 9637 9641
    • (2009) J. Biol. Chem. , vol.284 , pp. 9637-9641
    • Bogdanov, M.1    Xie, J.2    Dowhan, W.3
  • 25
    • 67650732710 scopus 로고    scopus 로고
    • Lipid-dependent membrane protein topogenesis
    • Dowhan W., and Bogdanov M. Lipid-dependent membrane protein topogenesis Annu. Rev. Biochem. 78 2009 515 540
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 515-540
    • Dowhan, W.1    Bogdanov, M.2
  • 26
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • DOI 10.1038/nsb1096-842
    • Wimley W.C., and White S.H. Experimentally determined hydrophobicity scale for proteins at membrane interfaces Nat. Struct. Biol. 3 1996 842 848 (Pubitemid 26330634)
    • (1996) Nature Structural Biology , vol.3 , Issue.10 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 27
    • 0032321726 scopus 로고    scopus 로고
    • Protein folding in membranes: Determining energetics of peptide-bilayer interactions
    • DOI 10.1016/S0076-6879(98)95035-2
    • White S.H., Wimley W.C., Ladokhin A.S., and Hristova K. Protein folding in membranes: determining the energetics of peptide-bilayer interactions Methods Enzymol. 295 1998 62 87 (Pubitemid 29349909)
    • (1998) Methods in Enzymology , vol.295 , pp. 62-87
    • White, S.H.1    Wimley, W.C.2    Ladokhin, A.S.3    Hristova, K.4
  • 29
    • 0035827137 scopus 로고    scopus 로고
    • Protein chemistry at membrane interfaces: Non-additivity of electrostatic and hydrophobic interactions
    • DOI 10.1006/jmbi.2001.4684
    • Ladokhin A.S., and White S.H. Protein chemistry at membrane interfaces: non-additivity of electrostatic and hydrophobic interactions J. Mol. Biol. 309 2001 543 552 (Pubitemid 32595090)
    • (2001) Journal of Molecular Biology , vol.309 , Issue.3 , pp. 543-552
    • Ladokhin, A.S.1    White, S.H.2
  • 30
    • 34548214197 scopus 로고    scopus 로고
    • Is lipid bilayer binding a common property of inhibitor cysteine knot ion-channel blockers?
    • Posokhov Y.O., Gottlieb P.A., Morales M.J., Sachs F., and Ladokhin A.S. Is lipid bilayer binding a common property of inhibitor cysteine knot ion-channel blockers? Biophys. J. 93 2007 L20 L22
    • (2007) Biophys. J. , vol.93
    • Posokhov, Y.O.1    Gottlieb, P.A.2    Morales, M.J.3    Sachs, F.4    Ladokhin, A.S.5
  • 32
    • 0033613815 scopus 로고    scopus 로고
    • Folding of amphipathic α-helices on membranes: Energetics of helix formation by melittin
    • DOI 10.1006/jmbi.1998.2346
    • Ladokhin A.S., and White S.H. Folding of amphipathic α-helices on membranes: energetics of helix formation by melittin J. Mol. Biol. 285 1999 1363 1369 (Pubitemid 29060439)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.4 , pp. 1363-1369
    • Ladokhin, A.S.1    White, S.H.2
  • 33
    • 34250195381 scopus 로고    scopus 로고
    • Folding Amphipathic Helices Into Membranes: Amphiphilicity Trumps Hydrophobicity
    • DOI 10.1016/j.jmb.2007.05.016, PII S0022283607006262
    • Fernandez-Vidal M., Jayasinghe S., Ladokhin A.S., and White S.H. Folding amphipathic helices into membranes: amphiphilicity trumps hydrophobicity J. Mol. Biol. 370 2007 459 470 (Pubitemid 46898437)
    • (2007) Journal of Molecular Biology , vol.370 , Issue.3 , pp. 459-470
    • Fernandez-Vidal, M.1    Jayasinghe, S.2    Ladokhin, A.S.3    White, S.H.4
  • 34
    • 84855457273 scopus 로고    scopus 로고
    • Hydrogen-bond energetics drive helix formation in membrane interfaces
    • Almeida P.F., Ladokhin A.S., and White S.H. Hydrogen-bond energetics drive helix formation in membrane interfaces Biochim. Biophys. Acta 1818 2012 178 182
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 178-182
    • Almeida, P.F.1    Ladokhin, A.S.2    White, S.H.3
  • 35
    • 0034681908 scopus 로고    scopus 로고
    • Designing transmembrane α-helices that insert spontaneously
    • DOI 10.1021/bi992746j
    • Wimley W.C., and White S.H. Designing transmembrane alpha-helices that insert spontaneously Biochemistry 39 2000 4432 4442 (Pubitemid 30212660)
    • (2000) Biochemistry , vol.39 , Issue.15 , pp. 4432-4442
    • Wimley, W.C.1    White, S.H.2
  • 36
    • 2442442435 scopus 로고    scopus 로고
    • Interfacial Folding and Membrane Insertion of a Designed Helical Peptide
    • DOI 10.1021/bi0361259
    • Ladokhin A.S., and White S.H. Interfacial folding and membrane insertion of a designed helical peptide Biochemistry 43 2004 5782 5791 (Pubitemid 38623612)
    • (2004) Biochemistry , vol.43 , Issue.19 , pp. 5782-5791
    • Ladokhin, A.S.1    White, S.H.2
  • 37
    • 34848885103 scopus 로고    scopus 로고
    • A monomeric membrane peptide that lives in three worlds: In solution, attached to, and inserted across lipid bilayers
    • DOI 10.1529/biophysj.107.109967
    • Reshetnyak Y.K., Segala M., Andreev O.A., and Engelman D.M. A monomeric membrane peptide that lives in three worlds: in solution, attached to, and inserted across lipid bilayers Biophys. J. 93 2007 2363 2372 (Pubitemid 47511136)
    • (2007) Biophysical Journal , vol.93 , Issue.7 , pp. 2363-2372
    • Reshetnyak, Y.K.1    Segala, M.2    Andreev, O.A.3    Engelman, D.M.4
  • 38
    • 0032075801 scopus 로고    scopus 로고
    • Stabilization of integral membrane proteins in aqueous solution using fluorinated surfactants
    • DOI 10.1016/S0300-9084(00)80017-6
    • Chabaud E., Barthelemy P., Mora N., Popot J.L., and Pucci B. Stabilization of integral membrane proteins in aqueous solution using fluorinated surfactants Biochimie 80 1998 515 530 (Pubitemid 28425398)
    • (1998) Biochimie , vol.80 , Issue.5-6 , pp. 515-530
    • Chabaud, E.1    Barthelemy, P.2    Mora, N.3    Popot, J.L.4    Pucci, B.5
  • 39
    • 1942532324 scopus 로고    scopus 로고
    • Hemifluorinated surfactants: A non-dissociating environment for handling membrane proteins in aqueous solutions?
    • DOI 10.1016/S0014-5793(04)00227-3, PII S0014579304002273
    • Breyton C., Chabaud E., Chaudier Y., Pucci B., and Popot J.L. Hemifluorinated surfactants: a non-dissociating environment for handling membrane proteins in aqueous solutions? FEBS Lett. 564 2004 312 318 (Pubitemid 38520939)
    • (2004) FEBS Letters , vol.564 , Issue.3 , pp. 312-318
    • Breyton, C.1    Chabaud, E.2    Chaudier, Y.3    Pucci, B.4    Popot, J.-L.5
  • 40
    • 33746647787 scopus 로고    scopus 로고
    • Peptides in lipid bilayers: The power of simple models
    • DOI 10.1016/j.sbi.2006.06.007, PII S0959440X06001114
    • Killian J.A., and Nyholm T.K. Peptides in lipid bilayers: the power of simple models Curr. Opin. Struct. Biol. 16 2006 473 479 (Pubitemid 44149068)
    • (2006) Current Opinion in Structural Biology , vol.16 , Issue.4 , pp. 473-479
    • Killian, J.A.1    Nyholm, T.K.2
  • 41
    • 77952093470 scopus 로고    scopus 로고
    • Orientation and dynamics of transmembrane peptides: The power of simple models
    • Holt A., and Killian J.A. Orientation and dynamics of transmembrane peptides: the power of simple models Eur. Biophys. J. 39 2010 609 621
    • (2010) Eur. Biophys. J. , vol.39 , pp. 609-621
    • Holt, A.1    Killian, J.A.2
  • 42
    • 33644530973 scopus 로고    scopus 로고
    • Chaperoning of insertion of membrane proteins into lipid bilayers by hemifluorinated surfactants: Application to diphtheria toxin
    • Palchevskyy S.S., Posokhov Y.O., Olivier B., Popot J.L., Pucci B., and Ladokhin A.S. Chaperoning of insertion of membrane proteins into lipid bilayers by hemifluorinated surfactants: application to diphtheria toxin Biochemistry 45 2006 2629 2635
    • (2006) Biochemistry , vol.45 , pp. 2629-2635
    • Palchevskyy, S.S.1    Posokhov, Y.O.2    Olivier, B.3    Popot, J.L.4    Pucci, B.5    Ladokhin, A.S.6
  • 43
    • 44849136504 scopus 로고    scopus 로고
    • Interactions of fluorinated surfactants with diphtheria toxin T-domain: Testing new media for studies of membrane proteins
    • Rodnin M.V., Posokhov Y.O., Contino-Pepin C., Brettmann J., Kyrychenko A., and Palchevskyy S.S. Interactions of fluorinated surfactants with diphtheria toxin T-domain: testing new media for studies of membrane proteins Biophys. J. 94 2008 4348 4357
    • (2008) Biophys. J. , vol.94 , pp. 4348-4357
    • Rodnin, M.V.1    Posokhov, Y.O.2    Contino-Pepin, C.3    Brettmann, J.4    Kyrychenko, A.5    Palchevskyy, S.S.6
  • 44
    • 56049103995 scopus 로고    scopus 로고
    • FCS study of the thermodynamics of membrane protein insertion into the lipid bilayer chaperoned by fluorinated surfactants
    • Posokhov Y.O., Rodnin M.V., Das S.K., Pucci B., and Ladokhin A.S. FCS study of the thermodynamics of membrane protein insertion into the lipid bilayer chaperoned by fluorinated surfactants Biophys. J. 95 2008 L54 L56
    • (2008) Biophys. J. , vol.95
    • Posokhov, Y.O.1    Rodnin, M.V.2    Das, S.K.3    Pucci, B.4    Ladokhin, A.S.5
  • 45
    • 80053424267 scopus 로고    scopus 로고
    • Fluorescence spectroscopy in thermodynamic and kinetic analysis of pH-dependent membrane protein insertion
    • Ladokhin A.S. Fluorescence spectroscopy in thermodynamic and kinetic analysis of pH-dependent membrane protein insertion Methods Enzymol. 466 2009 19 42
    • (2009) Methods Enzymol. , vol.466 , pp. 19-42
    • Ladokhin, A.S.1
  • 46
    • 4143120995 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy studies of peptide and protein binding phospholipid vesicles
    • DOI 10.1529/biophysj.104.039958
    • Rusu L., Gambhir A., McLaughlin S., and Radler J. Fluorescence correlation spectroscopy studies of peptide and protein binding to phospholipid vesicles Biophys. J. 87 2004 1044 1053 (Pubitemid 39095083)
    • (2004) Biophysical Journal , vol.87 , Issue.2 , pp. 1044-1053
    • Rusu, L.1    Gambhir, A.2    McLaughlin, S.3    Radler, J.4
  • 47
    • 33744788870 scopus 로고    scopus 로고
    • Quantification of α-synuclein binding to lipid vesicles using fluorescence correlation spectroscopy
    • DOI 10.1529/biophysj.105.079251
    • Rhoades E., Ramlall T.F., Webb W.W., and Eliezer D. Quantification of alpha-synuclein binding to lipid vesicles using fluorescence correlation spectroscopy Biophys. J. 90 2006 4692 4700 (Pubitemid 43830913)
    • (2006) Biophysical Journal , vol.90 , Issue.12 , pp. 4692-4700
    • Rhoades, E.1    Ramlall, T.F.2    Webb, W.W.3    Eliezer, D.4
  • 48
    • 42949116926 scopus 로고    scopus 로고
    • Membrane insertion pathway of annexin B12: Thermodynamic and kinetic characterization by fluorescence correlation spectroscopy and fluorescence quenching
    • DOI 10.1021/bi702223c
    • Posokhov Y.O., Rodnin M.V., Lu L., and Ladokhin A.S. Membrane insertion pathway of annexin B12: thermodynamic and kinetic characterization by fluorescence correlation spectroscopy and fluorescence quenching Biochemistry 47 2008 5078 5087 (Pubitemid 351620746)
    • (2008) Biochemistry , vol.47 , Issue.18 , pp. 5078-5087
    • Posokhov, Y.O.1    Rodnin, M.V.2    Lu, L.3    Ladokhin, A.S.4
  • 49
    • 68849090174 scopus 로고    scopus 로고
    • Kinetic intermediate reveals staggered pH-dependent transitions along the membrane insertion pathway of the diphtheria toxin T-domain
    • Kyrychenko A., Posokhov Y.O., Rodnin M.V., and Ladokhin A.S. Kinetic intermediate reveals staggered pH-dependent transitions along the membrane insertion pathway of the diphtheria toxin T-domain Biochemistry 48 2009 7584 7594
    • (2009) Biochemistry , vol.48 , pp. 7584-7594
    • Kyrychenko, A.1    Posokhov, Y.O.2    Rodnin, M.V.3    Ladokhin, A.S.4
  • 50
    • 79955669407 scopus 로고    scopus 로고
    • Membrane partitioning: "Classical" and "nonclassical" hydrophobic effects
    • Fernandez-Vidal M., White S.H., and Ladokhin A.S. Membrane partitioning: "classical" and "nonclassical" hydrophobic effects J. Membr. Biol. 239 2011 5 14
    • (2011) J. Membr. Biol. , vol.239 , pp. 5-14
    • Fernandez-Vidal, M.1    White, S.H.2    Ladokhin, A.S.3
  • 51
    • 0032536194 scopus 로고    scopus 로고
    • Group additive contributions to the alcohol-induced α-helix formation of melittin: Implication for the mechanism of the alcohol effects on proteins
    • DOI 10.1006/jmbi.1997.1468
    • Hirota N., Mizuno K., and Goto Y. Group additive contributions to the alcohol-induced α-helix formation of melittin: implication for the mechanism of the alcohol effects on proteins J. Mol. Biol. 275 1998 365 378 (Pubitemid 28030010)
    • (1998) Journal of Molecular Biology , vol.275 , Issue.2 , pp. 365-378
    • Hirota, N.1    Mizuno, K.2    Goto, Y.3
  • 52
    • 79959928058 scopus 로고    scopus 로고
    • Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers
    • Moon C.P., and Fleming K.G. Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers Proc. Natl Acad. Sci. USA 108 2011 10174 10177
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 10174-10177
    • Moon, C.P.1    Fleming, K.G.2
  • 53
    • 0002001503 scopus 로고    scopus 로고
    • The liquid-crystallographic structure of fluid lipid bilayer membranes
    • K.M. Merz, B. Roux, Birkhäuser Boston, MA
    • White S.H., and Wiener M.C. The liquid-crystallographic structure of fluid lipid bilayer membranes K.M. Merz, B. Roux, Membrane Structure and Dynamics 1996 Birkhäuser Boston, MA 127 144
    • (1996) Membrane Structure and Dynamics , pp. 127-144
    • White, S.H.1    Wiener, M.C.2
  • 55
    • 0035812599 scopus 로고    scopus 로고
    • Energetics, stability, and prediction of transmembrane helices
    • DOI 10.1006/jmbi.2001.5008
    • Jayasinghe S., Hristova K., and White S.H. Energetics, stability, and prediction of transmembrane helices J. Mol. Biol. 312 2001 927 934 (Pubitemid 32980315)
    • (2001) Journal of Molecular Biology , vol.312 , Issue.5 , pp. 927-934
    • Jayasinghe, S.1    Hristova, K.2    White, S.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.