메뉴 건너뛰기




Volumn 19, Issue 6, 2014, Pages 877-886

Interaction of heat shock protein 70 with membranes depends on the lipid environment

Author keywords

Hsp70; Liposomes; Membranes; Stress

Indexed keywords

HEAT SHOCK PROTEIN 70; LIPOSOME; PHOSPHATIDYLSERINE; RECOMBINANT PROTEIN;

EID: 84939881101     PISSN: 13558145     EISSN: 14661268     Source Type: Journal    
DOI: 10.1007/s12192-014-0511-x     Document Type: Article
Times cited : (55)

References (55)
  • 1
    • 0010389517 scopus 로고    scopus 로고
    • Aggregation of hsp70 and hsc70 in vivo is distinct and temperature-dependent and their chaperone function is directly related to non-aggregated forms
    • COI: 1:CAS:528:DyaK1MXlt1Krtw%3D%3D, PID: 9914533
    • Angelidis CE, Lazaridis I, Pagoulatos GN (1999) Aggregation of hsp70 and hsc70 in vivo is distinct and temperature-dependent and their chaperone function is directly related to non-aggregated forms. Eur J Biochem 259:505–512
    • (1999) Eur J Biochem , vol.259 , pp. 505-512
    • Angelidis, C.E.1    Lazaridis, I.2    Pagoulatos, G.N.3
  • 3
    • 0034613163 scopus 로고    scopus 로고
    • ATP and ADP modulate a cation channel formed by Hsc70 in acidic phospholipid membranes
    • COI: 1:CAS:528:DC%2BD3cXntlCjtbc%3D, PID: 10899168
    • Arispe N, De Maio A (2000) ATP and ADP modulate a cation channel formed by Hsc70 in acidic phospholipid membranes. J Biol Chem 275:30839–30843
    • (2000) J Biol Chem , vol.275 , pp. 30839-30843
    • Arispe, N.1    De Maio, A.2
  • 4
    • 0027490362 scopus 로고
    • Giant multilevel cation channels formed by Alzheimer disease amyloid beta-protein [A beta P-(1–40)] in bilayer membranes
    • COI: 1:CAS:528:DyaK2cXnsVOisQ%3D%3D, PID: 7504270
    • Arispe N, Pollard HB, Rojas E (1993) Giant multilevel cation channels formed by Alzheimer disease amyloid beta-protein [A beta P-(1–40)] in bilayer membranes. Proc Natl Acad Sci U S A 90:10573–10577
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 10573-10577
    • Arispe, N.1    Pollard, H.B.2    Rojas, E.3
  • 5
    • 0029670048 scopus 로고    scopus 로고
    • Zn2+ interaction with Alzheimer amyloid beta protein calcium channels
    • COI: 1:CAS:528:DyaK28Xht1entLg%3D, PID: 8643694
    • Arispe N, Pollard HB, Rojas E (1996) Zn2+ interaction with Alzheimer amyloid beta protein calcium channels. Proc Natl Acad Sci U S A 93:1710–1715
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 1710-1715
    • Arispe, N.1    Pollard, H.B.2    Rojas, E.3
  • 6
    • 7744222195 scopus 로고    scopus 로고
    • Hsc70 and Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability
    • COI: 1:CAS:528:DC%2BD2cXpslCjsb4%3D, PID: 15522909
    • Arispe N, Doh M, Simakova O, Kurganov B, De Maio A (2004) Hsc70 and Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability. FASEB J 18:1636–1645
    • (2004) FASEB J , vol.18 , pp. 1636-1645
    • Arispe, N.1    Doh, M.2    Simakova, O.3    Kurganov, B.4    De Maio, A.5
  • 7
    • 0029746254 scopus 로고    scopus 로고
    • Effect of nucleotides, peptides, and unfolded proteins on the self-association of the molecular chaperone HSC70
    • COI: 1:CAS:528:DyaK28XkslCisr4%3D, PID: 8702492
    • Benaroudj N, Triniolles F, Ladjimi MM (1996) Effect of nucleotides, peptides, and unfolded proteins on the self-association of the molecular chaperone HSC70. J Biol Chem 271:18471–18476
    • (1996) J Biol Chem , vol.271 , pp. 18471-18476
    • Benaroudj, N.1    Triniolles, F.2    Ladjimi, M.M.3
  • 8
    • 0347319182 scopus 로고    scopus 로고
    • Membrane binding, structure, and localization of cecropin-mellitin hybrid peptides: a site-directed spin-labeling study
    • COI: 1:CAS:528:DC%2BD2cXlsV2msA%3D%3D, PID: 14695274
    • Bhargava K, Feix JB (2004) Membrane binding, structure, and localization of cecropin-mellitin hybrid peptides: a site-directed spin-labeling study. Biophys J 86:329–336
    • (2004) Biophys J , vol.86 , pp. 329-336
    • Bhargava, K.1    Feix, J.B.2
  • 9
    • 0031869555 scopus 로고    scopus 로고
    • Differential Hsp70 plasma-membrane expression on primary human tumors and metastases in mice with severe combined immunodeficiency
    • COI: 1:CAS:528:DyaK1cXltlKkurw%3D, PID: 9714069
    • Botzler C, Schmidt J, Luz A, Jennen L, Issels R, Multhoff G (1998) Differential Hsp70 plasma-membrane expression on primary human tumors and metastases in mice with severe combined immunodeficiency. Int J Cancer 77:942–948
    • (1998) Int J Cancer , vol.77 , pp. 942-948
    • Botzler, C.1    Schmidt, J.2    Luz, A.3    Jennen, L.4    Issels, R.5    Multhoff, G.6
  • 10
    • 0037484291 scopus 로고    scopus 로고
    • Expression of the molecular chaperone Hsp70 in detergent-resistant microdomains correlates with its membrane delivery and release
    • COI: 1:CAS:528:DC%2BD3sXksVems7k%3D, PID: 12682040
    • Broquet AH, Thomas G, Masliah J, Trugnan G, Bachelet M (2003) Expression of the molecular chaperone Hsp70 in detergent-resistant microdomains correlates with its membrane delivery and release. J Biol Chem 278:21601–21606
    • (2003) J Biol Chem , vol.278 , pp. 21601-21606
    • Broquet, A.H.1    Thomas, G.2    Masliah, J.3    Trugnan, G.4    Bachelet, M.5
  • 11
    • 77955658694 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid-beta peptide analogue alters the ps-dynamics of phospholipid membranes
    • COI: 1:CAS:528:DC%2BC3cXhtVaqt7vL, PID: 20603101
    • Buchsteiner A, Hauss T, Dante S, Dencher NA (2010) Alzheimer's disease amyloid-beta peptide analogue alters the ps-dynamics of phospholipid membranes. Biochim Biophys Acta 1798:1969–1976
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 1969-1976
    • Buchsteiner, A.1    Hauss, T.2    Dante, S.3    Dencher, N.A.4
  • 12
    • 44649169371 scopus 로고    scopus 로고
    • Crystal structures of the 70-kDa heat shock proteins in domain disjoining conformation
    • COI: 1:CAS:528:DC%2BD1cXmtlyms74%3D, PID: 18400763
    • Chang YW, Sun YJ, Wang C, Hsiao CD (2008) Crystal structures of the 70-kDa heat shock proteins in domain disjoining conformation. J Biol Chem 283:15502–15511
    • (2008) J Biol Chem , vol.283 , pp. 15502-15511
    • Chang, Y.W.1    Sun, Y.J.2    Wang, C.3    Hsiao, C.D.4
  • 13
    • 24744445805 scopus 로고    scopus 로고
    • Association of heat shock proteins and neuronal membrane components with lipid rafts from the rat brain
    • COI: 1:CAS:528:DC%2BD2MXnsVCjtLg%3D, PID: 15948182
    • Chen S, Bawa D, Besshoh S, Gurd JW, Brown IR (2005) Association of heat shock proteins and neuronal membrane components with lipid rafts from the rat brain. J Neurosci Res 81:522–529
    • (2005) J Neurosci Res , vol.81 , pp. 522-529
    • Chen, S.1    Bawa, D.2    Besshoh, S.3    Gurd, J.W.4    Brown, I.R.5
  • 14
    • 0032608038 scopus 로고    scopus 로고
    • Heat shock proteins: facts, thoughts, and dreams
    • PID: 9921710
    • De Maio A (1999) Heat shock proteins: facts, thoughts, and dreams. Shock 11:1–12
    • (1999) Shock , vol.11 , pp. 1-12
    • De Maio, A.1
  • 15
    • 79958748545 scopus 로고    scopus 로고
    • Extracellular heat shock proteins, cellular export vesicles and the Stress Observation System: a form of communication during injury, infection, and cell damage
    • COI: 1:CAS:528:DC%2BC3MXkt12qsLc%3D, PID: 20963644
    • De Maio A (2011) Extracellular heat shock proteins, cellular export vesicles and the Stress Observation System: a form of communication during injury, infection, and cell damage. Cell Stress Chaperones 16:235–249
    • (2011) Cell Stress Chaperones , vol.16 , pp. 235-249
    • De Maio, A.1
  • 16
    • 84885665868 scopus 로고    scopus 로고
    • Extracellular heat shock proteins: a new location, a new function
    • PID: 23807250
    • De Maio A, Vazquez D (2013) Extracellular heat shock proteins: a new location, a new function. Shock 40:239–246
    • (2013) Shock , vol.40 , pp. 239-246
    • De Maio, A.1    Vazquez, D.2
  • 17
    • 72749098602 scopus 로고    scopus 로고
    • Fluorescence and UV resonance raman study of peptide-vesicle interactions of human cathelicidin LL-37 and its F6W and F17W mutants
    • COI: 1:CAS:528:DC%2BD1MXhtlOksrfN, PID: 19894716
    • Gable JE, Schlamadinger DE, Cogen AL, Gallo RL, Kim JE (2009) Fluorescence and UV resonance raman study of peptide-vesicle interactions of human cathelicidin LL-37 and its F6W and F17W mutants. Biochemistry 48:11264–11272
    • (2009) Biochemistry , vol.48 , pp. 11264-11272
    • Gable, J.E.1    Schlamadinger, D.E.2    Cogen, A.L.3    Gallo, R.L.4    Kim, J.E.5
  • 18
    • 0029953178 scopus 로고    scopus 로고
    • Effect of constitutive 70-kDa heat shock protein polymerization on its interaction with protein substrate
    • COI: 1:CAS:528:DyaK28Xkt1CjsLY%3D, PID: 8663341
    • Gao B, Eisenberg E, Greene L (1996) Effect of constitutive 70-kDa heat shock protein polymerization on its interaction with protein substrate. J Biol Chem 271:16792–16797
    • (1996) J Biol Chem , vol.271 , pp. 16792-16797
    • Gao, B.1    Eisenberg, E.2    Greene, L.3
  • 19
    • 20444431560 scopus 로고    scopus 로고
    • Heat shock protein 70 surface-positive tumor exosomes stimulate migratory and cytolytic activity of natural killer cells
    • COI: 1:CAS:528:DC%2BD2MXltFemu7w%3D, PID: 15958569
    • Gastpar R, Gehrmann M, Bausero MA, Asea A, Gross C, Schroeder JA, Multhoff G (2005) Heat shock protein 70 surface-positive tumor exosomes stimulate migratory and cytolytic activity of natural killer cells. Cancer Res 65:5238–5247
    • (2005) Cancer Res , vol.65 , pp. 5238-5247
    • Gastpar, R.1    Gehrmann, M.2    Bausero, M.A.3    Asea, A.4    Gross, C.5    Schroeder, J.A.6    Multhoff, G.7
  • 20
    • 0022541510 scopus 로고
    • Purification and initial characterization of the 71-kilodalton rat heat-shock protein and its cognate as fatty acid binding proteins
    • COI: 1:CAS:528:DyaL28Xit1Sqtbo%3D, PID: 3730359
    • Guidon PT Jr, Hightower LE (1986) Purification and initial characterization of the 71-kilodalton rat heat-shock protein and its cognate as fatty acid binding proteins. Biochemistry 25:3231–3239
    • (1986) Biochemistry , vol.25 , pp. 3231-3239
    • Guidon, P.T.1    Hightower, L.E.2
  • 21
    • 49349091518 scopus 로고    scopus 로고
    • In vitro multimerization and membrane insertion of bacterial outer membrane secretin PulD
    • COI: 1:CAS:528:DC%2BD1cXhtVSitbzF, PID: 18616949
    • Guilvout I, Chami M, Berrier C, Ghazi A, Engel A, Pugsley AP, Bayan N (2008) In vitro multimerization and membrane insertion of bacterial outer membrane secretin PulD. J Mol Biol 382:13–23
    • (2008) J Mol Biol , vol.382 , pp. 13-23
    • Guilvout, I.1    Chami, M.2    Berrier, C.3    Ghazi, A.4    Engel, A.5    Pugsley, A.P.6    Bayan, N.7
  • 22
    • 66849143696 scopus 로고    scopus 로고
    • Converging concepts of protein folding in vitro and in vivo
    • COI: 1:CAS:528:DC%2BD1MXms12ms7c%3D
    • Hartl FU, Hayer-Hartl M (2009) Converging concepts of protein folding in vitro and in vivo. Nat Structural Mol Biol 16:574–581
    • (2009) Nat Structural Mol Biol , vol.16 , pp. 574-581
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 23
    • 0033636662 scopus 로고    scopus 로고
    • Mechanism of membrane insertion of a multimeric beta-barrel protein: perfringolysin O creates a pore using ordered and coupled conformational changes
    • COI: 1:CAS:528:DC%2BD3cXosV2mt7g%3D, PID: 11106760
    • Heuck AP, Hotze EM, Tweten RK, Johnson AE (2000) Mechanism of membrane insertion of a multimeric beta-barrel protein: perfringolysin O creates a pore using ordered and coupled conformational changes. Mol Cell 6:1233–1242
    • (2000) Mol Cell , vol.6 , pp. 1233-1242
    • Heuck, A.P.1    Hotze, E.M.2    Tweten, R.K.3    Johnson, A.E.4
  • 24
    • 0024541931 scopus 로고
    • Selective release from cultured mammalian cells of heat-shock (stress) proteins that resemble glia-axon transfer proteins
    • COI: 1:CAS:528:DyaL1MXhtlaltbg%3D, PID: 2918030
    • Hightower LE, Guidon PT Jr (1989) Selective release from cultured mammalian cells of heat-shock (stress) proteins that resemble glia-axon transfer proteins. J Cell Physiol 138:257–266
    • (1989) J Cell Physiol , vol.138 , pp. 257-266
    • Hightower, L.E.1    Guidon, P.T.2
  • 26
    • 0038076054 scopus 로고    scopus 로고
    • X-ray structure of a voltage-dependent K + channel
    • COI: 1:CAS:528:DC%2BD3sXjtlSrtro%3D, PID: 12721618
    • Jiang Y, Lee A, Chen J, Ruta V, Cadene M, Chait BT, MacKinnon R (2003) X-ray structure of a voltage-dependent K + channel. Nature 423:33–41
    • (2003) Nature , vol.423 , pp. 33-41
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Ruta, V.4    Cadene, M.5    Chait, B.T.6    MacKinnon, R.7
  • 27
    • 0026669643 scopus 로고
    • Constitutive HSP70: oligomerization and its dependence on ATP binding
    • COI: 1:CAS:528:DyaK3sXnsFKjug%3D%3D, PID: 1429855
    • Kim D, Lee YJ, Corry PM (1992) Constitutive HSP70: oligomerization and its dependence on ATP binding. J Cell Physiol 153:353–361
    • (1992) J Cell Physiol , vol.153 , pp. 353-361
    • Kim, D.1    Lee, Y.J.2    Corry, P.M.3
  • 28
    • 27344442574 scopus 로고    scopus 로고
    • Structure of the KvAP voltage-dependent K + channel and its dependence on the lipid membrane
    • COI: 1:CAS:528:DC%2BD2MXht1ShtrvI, PID: 16223877
    • Lee SY, Lee A, Chen J, MacKinnon R (2005) Structure of the KvAP voltage-dependent K + channel and its dependence on the lipid membrane. Proc Natl Acad Sci U S A 102:15441–15446
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 15441-15446
    • Lee, S.Y.1    Lee, A.2    Chen, J.3    MacKinnon, R.4
  • 29
    • 77952761421 scopus 로고    scopus 로고
    • Membrane-mediated peptide conformation change from alpha-monomers to beta-aggregates
    • COI: 1:CAS:528:DC%2BC3cXosFCisbo%3D, PID: 20483332
    • Lee CC, Sun Y, Huang HW (2010) Membrane-mediated peptide conformation change from alpha-monomers to beta-aggregates. Biophys J 98:2236–2245
    • (2010) Biophys J , vol.98 , pp. 2236-2245
    • Lee, C.C.1    Sun, Y.2    Huang, H.W.3
  • 30
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent Shaker family K + channel
    • COI: 1:CAS:528:DC%2BD2MXmvFSks7o%3D, PID: 16002581
    • Long SB, Campbell EB, MacKinnon R (2005) Crystal structure of a mammalian voltage-dependent Shaker family K + channel. Science 309:897–903
    • (2005) Science , vol.309 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    MacKinnon, R.3
  • 31
    • 36248982122 scopus 로고    scopus 로고
    • Atomic structure of a voltage-dependent K + channel in a lipid membrane-like environment
    • COI: 1:CAS:528:DC%2BD2sXhtlajs7%2FN, PID: 18004376
    • Long SB, Tao X, Campbell EB, MacKinnon R (2007) Atomic structure of a voltage-dependent K + channel in a lipid membrane-like environment. Nature 450:376–382
    • (2007) Nature , vol.450 , pp. 376-382
    • Long, S.B.1    Tao, X.2    Campbell, E.B.3    MacKinnon, R.4
  • 32
    • 84894607190 scopus 로고    scopus 로고
    • Human heat shock protein 70 (Hsp70) as a peripheral membrane protein
    • COI: 1:CAS:528:DC%2BC2cXjslOmuro%3D, PID: 24480410
    • Mahalka AK, Kirkegaard T, Jukola LT, Jaatela M, Kinnunen PKJ (2014) Human heat shock protein 70 (Hsp70) as a peripheral membrane protein. Biochim Biophys Acta 1838:1344–1361
    • (2014) Biochim Biophys Acta , vol.1838 , pp. 1344-1361
    • Mahalka, A.K.1    Kirkegaard, T.2    Jukola, L.T.3    Jaatela, M.4    Kinnunen, P.K.J.5
  • 33
    • 0033936317 scopus 로고    scopus 로고
    • Multistep mechanism of substrate binding determines chaperone activity of Hsp70
    • COI: 1:CAS:528:DC%2BD3cXkslKnur0%3D, PID: 10876246
    • Mayer MP, Schroder H, Rudiger S, Paal K, Laufen T, Bukau B (2000) Multistep mechanism of substrate binding determines chaperone activity of Hsp70. Nat Struct Biol 7:586–593
    • (2000) Nat Struct Biol , vol.7 , pp. 586-593
    • Mayer, M.P.1    Schroder, H.2    Rudiger, S.3    Paal, K.4    Laufen, T.5    Bukau, B.6
  • 34
    • 0030044018 scopus 로고    scopus 로고
    • Pore formation by the cytotoxic islet amyloid peptide amylin
    • COI: 1:CAS:528:DyaK28XnsF2lug%3D%3D, PID: 8567648
    • Mirzabekov TA, Lin MC, Kagan BL (1996) Pore formation by the cytotoxic islet amyloid peptide amylin. J Biol Chem 271:1988–1992
    • (1996) J Biol Chem , vol.271 , pp. 1988-1992
    • Mirzabekov, T.A.1    Lin, M.C.2    Kagan, B.L.3
  • 35
    • 34848859541 scopus 로고    scopus 로고
    • Heat shock protein 70 (Hsp70): membrane location, export and immunological relevance
    • COI: 1:CAS:528:DC%2BD2sXhtFers7%2FO, PID: 17920520
    • Multhoff G (2007) Heat shock protein 70 (Hsp70): membrane location, export and immunological relevance. Methods 43:229–237
    • (2007) Methods , vol.43 , pp. 229-237
    • Multhoff, G.1
  • 36
    • 0030224714 scopus 로고    scopus 로고
    • Cell surface expression of heat shock proteins and the immune response
    • COI: 1:CAS:528:DyaK28XmsFChu7c%3D, PID: 9222602
    • Multhoff G, Hightower LE (1996) Cell surface expression of heat shock proteins and the immune response. Cell Stress Chaperones 1:167–176
    • (1996) Cell Stress Chaperones , vol.1 , pp. 167-176
    • Multhoff, G.1    Hightower, L.E.2
  • 37
    • 0031132876 scopus 로고    scopus 로고
    • Heat shock protein 72 on tumor cells: a recognition structure for natural killer cells
    • COI: 1:CAS:528:DyaK2sXivVCksb0%3D, PID: 9126997
    • Multhoff G, Botzler C, Jennen L, Schmidt J, Elwart J, Issels R (1997) Heat shock protein 72 on tumor cells: a recognition structure for natural killer cells. J Immunol 158:4341–4350
    • (1997) J Immunol , vol.158 , pp. 4341-4350
    • Multhoff, G.1    Botzler, C.2    Jennen, L.3    Schmidt, J.4    Elwart, J.5    Issels, R.6
  • 38
    • 55849145075 scopus 로고    scopus 로고
    • Unconventional mechanisms of protein transport to the cell surface of eukaryotic cells
    • COI: 1:CAS:528:DC%2BD1cXhtlOgtbbJ, PID: 18590485
    • Nickel W, Seedorf M (2008) Unconventional mechanisms of protein transport to the cell surface of eukaryotic cells. Annu Rev Cell Dev Biol 24:287–308
    • (2008) Annu Rev Cell Dev Biol , vol.24 , pp. 287-308
    • Nickel, W.1    Seedorf, M.2
  • 39
    • 84876525138 scopus 로고    scopus 로고
    • Folding of outer membrane proteins
    • COI: 1:CAS:528:DC%2BC38XhslejtbfJ, PID: 23131493
    • Otzen DE, Andersen KK (2013) Folding of outer membrane proteins. Arch Biochem Biophys 531:34–43
    • (2013) Arch Biochem Biophys , vol.531 , pp. 34-43
    • Otzen, D.E.1    Andersen, K.K.2
  • 40
    • 0026578171 scopus 로고
    • Identification of annexins as calcium channels in biological membranes
    • COI: 1:CAS:528:DyaK38XksVars7c%3D, PID: 1319252
    • Rojas E, Arispe N, Haigler HT, Burns AL, Pollard HB (1992) Identification of annexins as calcium channels in biological membranes. Bone Miner 17:214–218
    • (1992) Bone Miner , vol.17 , pp. 214-218
    • Rojas, E.1    Arispe, N.2    Haigler, H.T.3    Burns, A.L.4    Pollard, H.B.5
  • 41
    • 68849112162 scopus 로고    scopus 로고
    • Binding of heat shock protein 70 to extracellular phosphatidylserine promotes killing of normoxic and hypoxic tumor cells
    • COI: 1:CAS:528:DC%2BD1MXpvFOltrg%3D, PID: 19289606
    • Schilling D, Gehrmann M, Steinem C, De Maio A, Pockley AG, Abend M, Molls M, Multhoff G (2009) Binding of heat shock protein 70 to extracellular phosphatidylserine promotes killing of normoxic and hypoxic tumor cells. FASEB J 23:2467–2477
    • (2009) FASEB J , vol.23 , pp. 2467-2477
    • Schilling, D.1    Gehrmann, M.2    Steinem, C.3    De Maio, A.4    Pockley, A.G.5    Abend, M.6    Molls, M.7    Multhoff, G.8
  • 42
    • 79955654072 scopus 로고    scopus 로고
    • Arginine in membranes: the connection between molecular dynamics simulations and translocon-mediated insertion experiments
    • COI: 1:CAS:528:DC%2BC3MXht1Clsbs%3D, PID: 21127848
    • Schow EV, Freites JA, Cheng P, Bernsel A, von Heijne G, White SH, Tobias DJ (2011) Arginine in membranes: the connection between molecular dynamics simulations and translocon-mediated insertion experiments. J Membr Biol 239:35–48
    • (2011) J Membr Biol , vol.239 , pp. 35-48
    • Schow, E.V.1    Freites, J.A.2    Cheng, P.3    Bernsel, A.4    von Heijne, G.5    White, S.H.6    Tobias, D.J.7
  • 43
    • 0033932639 scopus 로고    scopus 로고
    • Beta-Barrel membrane proteins
    • COI: 1:CAS:528:DC%2BD3cXlvFOmt70%3D, PID: 10981633
    • Schulz GE (2000) Beta-Barrel membrane proteins. Curr Opin Struct Biol 10:443–447
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 443-447
    • Schulz, G.E.1
  • 44
    • 33947324465 scopus 로고    scopus 로고
    • Correct folding of the beta-barrel of the human membrane protein VDAC requires a lipid bilayer
    • COI: 1:CAS:528:DC%2BD2sXjsVeqt7s%3D, PID: 17336328
    • Shanmugavadivu B, Apell HJ, Meins T, Zeth K, Kleinschmidt JH (2007) Correct folding of the beta-barrel of the human membrane protein VDAC requires a lipid bilayer. J Mol Biol 368:66–78
    • (2007) J Mol Biol , vol.368 , pp. 66-78
    • Shanmugavadivu, B.1    Apell, H.J.2    Meins, T.3    Zeth, K.4    Kleinschmidt, J.H.5
  • 45
    • 0033615736 scopus 로고    scopus 로고
    • The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for pore-forming toxins
    • COI: 1:CAS:528:DyaK1MXnt1Gqs70%3D, PID: 10555145
    • Shatursky O, Heuck AP, Shepard LA, Rossjohn J, Parker MW, Johnson AE, Tweten RK (1999) The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for pore-forming toxins. Cell 99:293–299
    • (1999) Cell , vol.99 , 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
  • 46
    • 0034702810 scopus 로고    scopus 로고
    • The mechanism of pore assembly for a cholesterol-dependent cytolysin: formation of a large prepore complex precedes the insertion of the transmembrane beta-hairpins
    • COI: 1:CAS:528:DC%2BD3cXltVOjsb0%3D, PID: 10956018
    • Shepard LA, Shatursky O, Johnson AE, Tweten RK (2000) The mechanism of pore assembly for a cholesterol-dependent cytolysin: formation of a large prepore complex precedes the insertion of the transmembrane beta-hairpins. Biochemistry 39:10284–10293
    • (2000) Biochemistry , vol.39 , pp. 10284-10293
    • Shepard, L.A.1    Shatursky, O.2    Johnson, A.E.3    Tweten, R.K.4
  • 47
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • COI: 1:CAS:528:DC%2BD3MXivVGjtbo%3D, PID: 11413487
    • Simons K, Toomre D (2000) Lipid rafts and signal transduction. Nat Rev Mol Cell Biol 1:31–39
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 31-39
    • Simons, K.1    Toomre, D.2
  • 48
    • 36749026606 scopus 로고    scopus 로고
    • The process of folding proteins into membranes: challenges and progress
    • COI: 1:CAS:528:DC%2BD2sXhsVSktb%2FO, PID: 17971290
    • Stanley AM, Fleming KG (2008) The process of folding proteins into membranes: challenges and progress. Arch Biochem Biophys 469:46–66
    • (2008) Arch Biochem Biophys , vol.469 , pp. 46-66
    • Stanley, A.M.1    Fleming, K.G.2
  • 49
    • 68849129712 scopus 로고    scopus 로고
    • Membrane vesicles as conveyors of immune responses
    • COI: 1:CAS:528:DC%2BD1MXmvVWntr0%3D, PID: 19498381
    • Thery C, Ostrowski M, Segura E (2009) Membrane vesicles as conveyors of immune responses. Nat Rev Immunol 9:581–593
    • (2009) Nat Rev Immunol , vol.9 , pp. 581-593
    • Thery, C.1    Ostrowski, M.2    Segura, E.3
  • 50
    • 44849084963 scopus 로고    scopus 로고
    • Hsp70 translocates into the plasma membrane after stress and is released into the extracellular environment in a membrane-associated form that activates macrophages
    • COI: 1:CAS:528:DC%2BD1cXisl2jtLc%3D, PID: 18322243
    • Vega VL, Rodriguez-Silva M, Frey T, Gehrmann M, Diaz JC, Multhoff G, Arispe N, De Maio A (2008) Hsp70 translocates into the plasma membrane after stress and is released into the extracellular environment in a membrane-associated form that activates macrophages. J Immunol 180:4299–4307
    • (2008) J Immunol , vol.180 , pp. 4299-4307
    • Vega, V.L.1    Rodriguez-Silva, M.2    Frey, T.3    Gehrmann, M.4    Diaz, J.C.5    Multhoff, G.6    Arispe, N.7    De Maio, A.8
  • 51
    • 84869864369 scopus 로고    scopus 로고
    • OmpA can form folded and unfolded oligomers
    • COI: 1:CAS:528:DC%2BC38XhvV2rs7%2FI, PID: 22982243
    • Wang H, Andersen KK, Vad BS, Otzen DE (2013) OmpA can form folded and unfolded oligomers. Biochim Biophys Acta 1834:127–136
    • (2013) Biochim Biophys Acta , vol.1834 , pp. 127-136
    • Wang, H.1    Andersen, K.K.2    Vad, B.S.3    Otzen, D.E.4
  • 52
    • 0031740601 scopus 로고    scopus 로고
    • Hydrophobic interactions of peptides with membrane interfaces
    • White SH, Wimley WC (1998) Hydrophobic interactions of peptides with membrane interfaces. Biochim Biophys Acta 376:339–352
    • (1998) Biochim Biophys Acta , vol.376 , pp. 339-352
    • White, S.H.1    Wimley, W.C.2
  • 53
    • 0026729232 scopus 로고
    • Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. III. Complete structure
    • COI: 1:CAS:528:DyaK38XhvV2rtL4%3D, PID: 1547331
    • Wiener MC, White SH (1992) Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. III. Complete structure. Biophys J 61:434–447
    • (1992) Biophys J , vol.61 , pp. 434-447
    • Wiener, M.C.1    White, S.H.2
  • 54
    • 0032540234 scopus 로고    scopus 로고
    • Folding of beta-sheet membrane proteins: a hydrophobic hexapeptide model
    • COI: 1:CAS:528:DyaK1cXivF2ntbc%3D, PID: 9571025
    • Wimley WC, Hristova K, Ladokhin AS, Silvestro L, Axelsen PH, White SH (1998) Folding of beta-sheet membrane proteins: a hydrophobic hexapeptide model. J Mol Biol 277:1091–1110
    • (1998) J Mol Biol , vol.277 , pp. 1091-1110
    • Wimley, W.C.1    Hristova, K.2    Ladokhin, A.S.3    Silvestro, L.4    Axelsen, P.H.5    White, S.H.6
  • 55
    • 84870716717 scopus 로고    scopus 로고
    • Structure and dynamics of the two amphipathic arginine-rich peptides RW9 and RL9 in a lipid environment investigated by solid-state NMR and MD simulations
    • COI: 1:CAS:528:DC%2BC3sXhtVOisg%3D%3D, PID: 23174351
    • Witte K, Olausson BE, Walrant A, Alves ID, Vogel A (2013) Structure and dynamics of the two amphipathic arginine-rich peptides RW9 and RL9 in a lipid environment investigated by solid-state NMR and MD simulations. Biochim Biophys Acta 1828:824–833
    • (2013) Biochim Biophys Acta , vol.1828 , pp. 824-833
    • Witte, K.1    Olausson, B.E.2    Walrant, A.3    Alves, I.D.4    Vogel, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.