메뉴 건너뛰기




Volumn 10, Issue 10, 2014, Pages

Cyclophilin A Associates with Enterovirus-71 Virus Capsid and Plays an Essential Role in Viral Infection as an Uncoating Regulator

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOPHILIN A; CYCLOPHILIN A INHIBITOR; CYCLOPHILIN INHIBITOR; HOST FACTOR; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; VIRUS RNA; ANTIVIRUS AGENT; CAPSID PROTEIN;

EID: 84908339254     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1004422     Document Type: Article
Times cited : (73)

References (51)
  • 1
    • 0025893168 scopus 로고
    • Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
    • Liu J, Farmer JD, JrLane WS, Friedman J, Weissman I, et al. (1991) Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell 66: 807–815.
    • (1991) Cell , vol.66 , pp. 807-815
    • Liu, J.1    Farmer, J.D.2    Lane, W.S.3    Friedman, J.4    Weissman, I.5
  • 3
    • 70049114748 scopus 로고    scopus 로고
    • Target cell cyclophilins facilitate human papillomavirus type 16 infection
    • Bienkowska-Haba M, Patel HD, Sapp M, (2009) Target cell cyclophilins facilitate human papillomavirus type 16 infection. PLoS Pathog 5: e1000524.
    • (2009) PLoS Pathog , vol.5 , pp. e1000524
    • Bienkowska-Haba, M.1    Patel, H.D.2    Sapp, M.3
  • 4
    • 0027971782 scopus 로고
    • Functional association of cyclophilin A with HIV-1 virions
    • Thali M, Bukovsky A, Kondo E, Rosenwirth B, Walsh CT, et al. (1994) Functional association of cyclophilin A with HIV-1 virions. Nature 372: 363–365.
    • (1994) Nature , vol.372 , pp. 363-365
    • Thali, M.1    Bukovsky, A.2    Kondo, E.3    Rosenwirth, B.4    Walsh, C.T.5
  • 5
    • 0027940713 scopus 로고
    • Specific incorporation of cyclophilin A into HIV-1 virions
    • Franke EK, Yuan HE, Luban J, (1994) Specific incorporation of cyclophilin A into HIV-1 virions. Nature 372: 359–362.
    • (1994) Nature , vol.372 , pp. 359-362
    • Franke, E.K.1    Yuan, H.E.2    Luban, J.3
  • 6
    • 0242321995 scopus 로고    scopus 로고
    • Structural characterization of the HIV-1 Vpr N terminus: evidence of cis/trans-proline isomerism
    • Bruns K, Fossen T, Wray V, Henklein P, Tessmer U, et al. (2003) Structural characterization of the HIV-1 Vpr N terminus: evidence of cis/trans-proline isomerism. J Biol Chem 278: 43188–43201.
    • (2003) J Biol Chem , vol.278 , pp. 43188-43201
    • Bruns, K.1    Fossen, T.2    Wray, V.3    Henklein, P.4    Tessmer, U.5
  • 7
    • 0029948529 scopus 로고    scopus 로고
    • Binding of the human immunodeficiency virus type 1 Gag polyprotein to cyclophilin A is mediated by the central region of capsid and requires Gag dimerization
    • Colgan J, Yuan HE, Franke EK, Luban J, (1996) Binding of the human immunodeficiency virus type 1 Gag polyprotein to cyclophilin A is mediated by the central region of capsid and requires Gag dimerization. J Virol 70: 4299–4310.
    • (1996) J Virol , vol.70 , pp. 4299-4310
    • Colgan, J.1    Yuan, H.E.2    Franke, E.K.3    Luban, J.4
  • 9
    • 84871947594 scopus 로고    scopus 로고
    • The host proteins transportin SR2/TNPO3 and cyclophilin A exert opposing effects on HIV-1 uncoating
    • Shah VB, Shi J, Hout DR, Oztop I, Krishnan L, et al. (2013) The host proteins transportin SR2/TNPO3 and cyclophilin A exert opposing effects on HIV-1 uncoating. J Virol 87: 422–432.
    • (2013) J Virol , vol.87 , pp. 422-432
    • Shah, V.B.1    Shi, J.2    Hout, D.R.3    Oztop, I.4    Krishnan, L.5
  • 10
    • 21244433445 scopus 로고    scopus 로고
    • Cyclophilin B is a functional regulator of hepatitis C virus RNA polymerase
    • Watashi K, Ishii N, Hijikata M, Inoue D, Murata T, et al. (2005) Cyclophilin B is a functional regulator of hepatitis C virus RNA polymerase. Mol Cell 19: 111–122.
    • (2005) Mol Cell , vol.19 , pp. 111-122
    • Watashi, K.1    Ishii, N.2    Hijikata, M.3    Inoue, D.4    Murata, T.5
  • 11
    • 43949123575 scopus 로고    scopus 로고
    • Cyclophilin A is an essential cofactor for hepatitis C virus infection and the principal mediator of cyclosporine resistance in vitro
    • Yang F, Robotham JM, Nelson HB, Irsigler A, Kenworthy R, et al. (2008) Cyclophilin A is an essential cofactor for hepatitis C virus infection and the principal mediator of cyclosporine resistance in vitro. J Virol 82: 5269–5278.
    • (2008) J Virol , vol.82 , pp. 5269-5278
    • Yang, F.1    Robotham, J.M.2    Nelson, H.B.3    Irsigler, A.4    Kenworthy, R.5
  • 12
    • 70049096419 scopus 로고    scopus 로고
    • Essential role of cyclophilin A for hepatitis C virus replication and virus production and possible link to polyprotein cleavage kinetics
    • Kaul A, Stauffer S, Berger C, Pertel T, Schmitt J, et al. (2009) Essential role of cyclophilin A for hepatitis C virus replication and virus production and possible link to polyprotein cleavage kinetics. PLoS Pathog 5: e1000546.
    • (2009) PLoS Pathog , vol.5 , pp. e1000546
    • Kaul, A.1    Stauffer, S.2    Berger, C.3    Pertel, T.4    Schmitt, J.5
  • 13
    • 67449093865 scopus 로고    scopus 로고
    • Critical role of cyclophilin A and its prolyl-peptidyl isomerase activity in the structure and function of the hepatitis C virus replication complex
    • Liu Z, Yang F, Robotham JM, Tang H, (2009) Critical role of cyclophilin A and its prolyl-peptidyl isomerase activity in the structure and function of the hepatitis C virus replication complex. J Virol 83: 6554–6565.
    • (2009) J Virol , vol.83 , pp. 6554-6565
    • Liu, Z.1    Yang, F.2    Robotham, J.M.3    Tang, H.4
  • 14
    • 72949100768 scopus 로고    scopus 로고
    • Cyclosporine A inhibits hepatitis C virus nonstructural protein 2 through cyclophilin A
    • Ciesek S, Steinmann E, Wedemeyer H, Manns MP, Neyts J, et al. (2009) Cyclosporine A inhibits hepatitis C virus nonstructural protein 2 through cyclophilin A. Hepatology 50: 1638–1645.
    • (2009) Hepatology , vol.50 , pp. 1638-1645
    • Ciesek, S.1    Steinmann, E.2    Wedemeyer, H.3    Manns, M.P.4    Neyts, J.5
  • 15
    • 67649412015 scopus 로고    scopus 로고
    • Hepatitis C virus NS5A protein is a substrate for the peptidyl-prolyl cis/trans isomerase activity of cyclophilins A and B
    • Hanoulle X, Badillo A, Wieruszeski JM, Verdegem D, Landrieu I, et al. (2009) Hepatitis C virus NS5A protein is a substrate for the peptidyl-prolyl cis/trans isomerase activity of cyclophilins A and B. J Biol Chem 284: 13589–13601.
    • (2009) J Biol Chem , vol.284 , pp. 13589-13601
    • Hanoulle, X.1    Badillo, A.2    Wieruszeski, J.M.3    Verdegem, D.4    Landrieu, I.5
  • 16
    • 38349162328 scopus 로고    scopus 로고
    • Identification of residues required for RNA replication in domains II and III of the hepatitis C virus NS5A protein
    • Tellinghuisen TL, Foss KL, Treadaway JC, Rice CM, (2008) Identification of residues required for RNA replication in domains II and III of the hepatitis C virus NS5A protein. J Virol 82: 1073–1083.
    • (2008) J Virol , vol.82 , pp. 1073-1083
    • Tellinghuisen, T.L.1    Foss, K.L.2    Treadaway, J.C.3    Rice, C.M.4
  • 17
    • 84866170686 scopus 로고    scopus 로고
    • Cyclophilins facilitate dissociation of the human papillomavirus type 16 capsid protein L1 from the L2/DNA complex following virus entry
    • Bienkowska-Haba M, Williams C, Kim SM, Garcea RL, Sapp M, (2012) Cyclophilins facilitate dissociation of the human papillomavirus type 16 capsid protein L1 from the L2/DNA complex following virus entry. J Virol 86: 9875–9887.
    • (2012) J Virol , vol.86 , pp. 9875-9887
    • Bienkowska-Haba, M.1    Williams, C.2    Kim, S.M.3    Garcea, R.L.4    Sapp, M.5
  • 18
    • 84870666504 scopus 로고    scopus 로고
    • Enterovirus 71 VPg uridylation uses a two-molecular mechanism of 3D polymerase
    • Sun Y, Wang Y, Shan C, Chen C, Xu P, et al. (2012) Enterovirus 71 VPg uridylation uses a two-molecular mechanism of 3D polymerase. J Virol 86: 13662–13671.
    • (2012) J Virol , vol.86 , pp. 13662-13671
    • Sun, Y.1    Wang, Y.2    Shan, C.3    Chen, C.4    Xu, P.5
  • 19
    • 84895076942 scopus 로고    scopus 로고
    • Current progress in antiviral strategies
    • Lou Z, Sun Y, Rao Z, (2013) Current progress in antiviral strategies. Trends in Pharmacological Sciences 35: 86–102 10.1016/j.tips.2013.1011.1006.
    • (2013) Trends in Pharmacological Sciences , vol.35 , pp. 86-102
    • Lou, Z.1    Sun, Y.2    Rao, Z.3
  • 20
    • 84877616491 scopus 로고    scopus 로고
    • Crystal Structure of Enterovirus 71 RNA-Dependent RNA Polymerase Complexed with Its Protein Primer VPg: Implication for a trans Mechanism of VPg Uridylylation
    • Chen C, Wang Y, Shan C, Sun Y, Xu P, et al. (2013) Crystal Structure of Enterovirus 71 RNA-Dependent RNA Polymerase Complexed with Its Protein Primer VPg: Implication for a trans Mechanism of VPg Uridylylation. J Virol 87: 5755–5768.
    • (2013) J Virol , vol.87 , pp. 5755-5768
    • Chen, C.1    Wang, Y.2    Shan, C.3    Sun, Y.4    Xu, P.5
  • 21
    • 84863116544 scopus 로고    scopus 로고
    • Molecular determinants of enterovirus 71 viral entry: cleft around GLN-172 on VP1 protein interacts with variable region on scavenge receptor B 2
    • Chen P, Song Z, Qi Y, Feng X, Xu N, et al. (2012) Molecular determinants of enterovirus 71 viral entry: cleft around GLN-172 on VP1 protein interacts with variable region on scavenge receptor B 2. J Biol Chem 287: 6406–6420.
    • (2012) J Biol Chem , vol.287 , pp. 6406-6420
    • Chen, P.1    Song, Z.2    Qi, Y.3    Feng, X.4    Xu, N.5
  • 23
    • 67650491431 scopus 로고    scopus 로고
    • Human P-selectin glycoprotein ligand-1 is a functional receptor for enterovirus 71
    • Nishimura Y, Shimojima M, Tano Y, Miyamura T, Wakita T, et al. (2009) Human P-selectin glycoprotein ligand-1 is a functional receptor for enterovirus 71. Nat Med 15: 794–797.
    • (2009) Nat Med , vol.15 , pp. 794-797
    • Nishimura, Y.1    Shimojima, M.2    Tano, Y.3    Miyamura, T.4    Wakita, T.5
  • 24
    • 67650446350 scopus 로고    scopus 로고
    • Scavenger receptor B2 is a cellular receptor for enterovirus 71
    • Yamayoshi S, Yamashita Y, Li J, Hanagata N, Minowa T, et al. (2009) Scavenger receptor B2 is a cellular receptor for enterovirus 71. Nat Med 15: 798–801.
    • (2009) Nat Med , vol.15 , pp. 798-801
    • Yamayoshi, S.1    Yamashita, Y.2    Li, J.3    Hanagata, N.4    Minowa, T.5
  • 25
    • 84889609917 scopus 로고    scopus 로고
    • Structure of LIMP-2 provides functional insights with implications for SR-BI and CD36
    • Neculai D, Schwake M, Ravichandran M, Zunke F, Collins RF, et al. (2013) Structure of LIMP-2 provides functional insights with implications for SR-BI and CD36. Nature.
    • (2013) Nature
    • Neculai, D.1    Schwake, M.2    Ravichandran, M.3    Zunke, F.4    Collins, R.F.5
  • 26
    • 84871962446 scopus 로고    scopus 로고
    • Enterovirus 71 uses cell surface heparan sulfate glycosaminoglycan as an attachment receptor
    • Tan CW, Poh CL, Sam IC, Chan YF, (2013) Enterovirus 71 uses cell surface heparan sulfate glycosaminoglycan as an attachment receptor. J Virol 87: 611–620.
    • (2013) J Virol , vol.87 , pp. 611-620
    • Tan, C.W.1    Poh, C.L.2    Sam, I.C.3    Chan, Y.F.4
  • 27
    • 80655125503 scopus 로고    scopus 로고
    • Annexin II binds to capsid protein VP1 of enterovirus 71 and enhances viral infectivity
    • Yang SL, Chou YT, Wu CN, Ho MS, (2011) Annexin II binds to capsid protein VP1 of enterovirus 71 and enhances viral infectivity. J Virol 85: 11809–11820.
    • (2011) J Virol , vol.85 , pp. 11809-11820
    • Yang, S.L.1    Chou, Y.T.2    Wu, C.N.3    Ho, M.S.4
  • 28
    • 69949084535 scopus 로고    scopus 로고
    • Discovering potent small molecule inhibitors of cyclophilin A using de novo drug design approach
    • Ni S, Yuan Y, Huang J, Mao X, Lv M, et al. (2009) Discovering potent small molecule inhibitors of cyclophilin A using de novo drug design approach. J Med Chem 52: 5295–5298.
    • (2009) J Med Chem , vol.52 , pp. 5295-5298
    • Ni, S.1    Yuan, Y.2    Huang, J.3    Mao, X.4    Lv, M.5
  • 29
    • 84883795344 scopus 로고    scopus 로고
    • Structural perspective on the formation of ribonucleoprotein complex in negative-sense single-stranded RNA viruses
    • Zhou H, Sun Y, Guo Y, Lou Z, (2013) Structural perspective on the formation of ribonucleoprotein complex in negative-sense single-stranded RNA viruses. Trends Microbiol 21: 475–484.
    • (2013) Trends Microbiol , vol.21 , pp. 475-484
    • Zhou, H.1    Sun, Y.2    Guo, Y.3    Lou, Z.4
  • 30
    • 64049094864 scopus 로고    scopus 로고
    • Cyclophilin A interacts with influenza A virus M1 protein and impairs the early stage of the viral replication
    • Liu X, Sun L, Yu M, Wang Z, Xu C, et al. (2009) Cyclophilin A interacts with influenza A virus M1 protein and impairs the early stage of the viral replication. Cell Microbiol 11: 730–741.
    • (2009) Cell Microbiol , vol.11 , pp. 730-741
    • Liu, X.1    Sun, L.2    Yu, M.3    Wang, Z.4    Xu, C.5
  • 31
    • 84863012269 scopus 로고    scopus 로고
    • Cyclophilin A restricts influenza A virus replication through degradation of the M1 protein
    • Liu X, Zhao Z, Xu C, Sun L, Chen J, et al. (2012) Cyclophilin A restricts influenza A virus replication through degradation of the M1 protein. PLoS One 7: e31063.
    • (2012) PLoS One , vol.7 , pp. e31063
    • Liu, X.1    Zhao, Z.2    Xu, C.3    Sun, L.4    Chen, J.5
  • 33
    • 0027071803 scopus 로고
    • Active site mutants of human cyclophilin A separate peptidyl-prolyl isomerase activity from cyclosporin A binding and calcineurin inhibition
    • Zydowsky LD, Etzkorn FA, Chang HY, Ferguson SB, Stolz LA, et al. (1992) Active site mutants of human cyclophilin A separate peptidyl-prolyl isomerase activity from cyclosporin A binding and calcineurin inhibition. Protein Sci 1: 1092–1099.
    • (1992) Protein Sci , vol.1 , pp. 1092-1099
    • Zydowsky, L.D.1    Etzkorn, F.A.2    Chang, H.Y.3    Ferguson, S.B.4    Stolz, L.A.5
  • 34
    • 67650550814 scopus 로고    scopus 로고
    • The isomerase active site of cyclophilin A is critical for hepatitis C virus replication
    • Chatterji U, Bobardt M, Selvarajah S, Yang F, Tang H, et al. (2009) The isomerase active site of cyclophilin A is critical for hepatitis C virus replication. J Biol Chem 284: 16998–17005.
    • (2009) J Biol Chem , vol.284 , pp. 16998-17005
    • Chatterji, U.1    Bobardt, M.2    Selvarajah, S.3    Yang, F.4    Tang, H.5
  • 35
    • 84861316194 scopus 로고    scopus 로고
    • A sensor-adaptor mechanism for enterovirus uncoating from structures of EV71
    • Wang X, Peng W, Ren J, Hu Z, Xu J, et al. (2012) A sensor-adaptor mechanism for enterovirus uncoating from structures of EV71. Nat Struct Mol Biol 19: 424–429.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 424-429
    • Wang, X.1    Peng, W.2    Ren, J.3    Hu, Z.4    Xu, J.5
  • 36
    • 84895890904 scopus 로고    scopus 로고
    • More-powerful virus inhibitors from structure-based analysis of HEV71 capsid-binding molecules
    • De Colibus L, Wang X, Spyrou JA, Kelly J, Ren J, et al. (2014) More-powerful virus inhibitors from structure-based analysis of HEV71 capsid-binding molecules. Nat Struct Mol Biol 21: 282–288.
    • (2014) Nat Struct Mol Biol , vol.21 , pp. 282-288
    • De Colibus, L.1    Wang, X.2    Spyrou, J.A.3    Kelly, J.4    Ren, J.5
  • 37
    • 84884804710 scopus 로고    scopus 로고
    • Enterovirus 71 Binding to PSGL-1 on Leukocytes: VP1-145 Acts as a Molecular Switch to Control Receptor Interaction
    • Nishimura Y, Lee K, Hafenstein S, Kataoka C, Wakita T, et al. (2013) Enterovirus 71 Binding to PSGL-1 on Leukocytes: VP1-145 Acts as a Molecular Switch to Control Receptor Interaction. PLoS Pathogen 9: e1003511.
    • (2013) PLoS Pathogen , vol.9 , pp. e1003511
    • Nishimura, Y.1    Lee, K.2    Hafenstein, S.3    Kataoka, C.4    Wakita, T.5
  • 38
    • 84886921164 scopus 로고    scopus 로고
    • A strain-specific epitope of Enterovirus 71 identified by cryoEM of the complex with Fab from 2 neutralizing antibody
    • Lee H, Cifuente JO, Ashley RE, Conway JF, Makhov AM, et al. (2013) A strain-specific epitope of Enterovirus 71 identified by cryoEM of the complex with Fab from 2 neutralizing antibody. J Virol 87: 11363–11370.
    • (2013) J Virol , vol.87 , pp. 11363-11370
    • Lee, H.1    Cifuente, J.O.2    Ashley, R.E.3    Conway, J.F.4    Makhov, A.M.5
  • 39
    • 80052233389 scopus 로고    scopus 로고
    • Endosome maturation
    • Huotari J, Helenius A, (2011) Endosome maturation. Embo J 30: 3481–3500.
    • (2011) Embo J , vol.30 , pp. 3481-3500
    • Huotari, J.1    Helenius, A.2
  • 41
    • 34548440352 scopus 로고    scopus 로고
    • Preferential chemotaxis of activated human CD4+ T cells by extracellular cyclophilin A
    • Damsker JM, Bukrinsky MI, Constant SL, (2007) Preferential chemotaxis of activated human CD4+ T cells by extracellular cyclophilin A. J Leukoc Biol 82: 613–618.
    • (2007) J Leukoc Biol , vol.82 , pp. 613-618
    • Damsker, J.M.1    Bukrinsky, M.I.2    Constant, S.L.3
  • 42
    • 77956591150 scopus 로고    scopus 로고
    • Structural and functional analysis of prehistoric lentiviruses uncovers an ancient molecular interface
    • Goldstone DC, Yap MW, Robertson LE, Haire LF, Taylor WR, et al. (2010) Structural and functional analysis of prehistoric lentiviruses uncovers an ancient molecular interface. Cell Host Microbe 8: 248–259.
    • (2010) Cell Host Microbe , vol.8 , pp. 248-259
    • Goldstone, D.C.1    Yap, M.W.2    Robertson, L.E.3    Haire, L.F.4    Taylor, W.R.5
  • 43
    • 79960417577 scopus 로고    scopus 로고
    • Single amino acid changes in the virus capsid permit coxsackievirus B3 to bind decay-accelerating factor
    • Pan J, Narayanan B, Shah S, Yoder JD, Cifuente JO, et al. (2011) Single amino acid changes in the virus capsid permit coxsackievirus B3 to bind decay-accelerating factor. J Virol 85: 7436–7443.
    • (2011) J Virol , vol.85 , pp. 7436-7443
    • Pan, J.1    Narayanan, B.2    Shah, S.3    Yoder, J.D.4    Cifuente, J.O.5
  • 44
    • 84888054227 scopus 로고    scopus 로고
    • HIV-1 evades innate immune recognition through specific cofactor recruitment
    • Rasaiyaah J, Tan CP, Fletcher AJ, Price AJ, Blondeau C, et al. (2013) HIV-1 evades innate immune recognition through specific cofactor recruitment. Nature 503: 402–405.
    • (2013) Nature , vol.503 , pp. 402-405
    • Rasaiyaah, J.1    Tan, C.P.2    Fletcher, A.J.3    Price, A.J.4    Blondeau, C.5
  • 45
    • 70350319201 scopus 로고    scopus 로고
    • Target cell type-dependent modulation of human immunodeficiency virus type 1 capsid disassembly by cyclophilin A
    • Li Y, Kar AK, Sodroski J, (2009) Target cell type-dependent modulation of human immunodeficiency virus type 1 capsid disassembly by cyclophilin A. J Virol 83: 10951–10962.
    • (2009) J Virol , vol.83 , pp. 10951-10962
    • Li, Y.1    Kar, A.K.2    Sodroski, J.3
  • 46
    • 0037035859 scopus 로고    scopus 로고
    • Characterization of a Vero cell-adapted virulent strain of enterovirus 71 suitable for use as a vaccine candidate
    • Lin YC, Wu CN, Shih SR, Ho MS, (2002) Characterization of a Vero cell-adapted virulent strain of enterovirus 71 suitable for use as a vaccine candidate. Vaccine 20: 2485–2493.
    • (2002) Vaccine , vol.20 , pp. 2485-2493
    • Lin, Y.C.1    Wu, C.N.2    Shih, S.R.3    Ho, M.S.4
  • 48
    • 84864574433 scopus 로고    scopus 로고
    • Identification of site-specific adaptations conferring increased neural cell tropism during human enterovirus 71 infection
    • Cordey S, Petty TJ, Schibler M, Martinez Y, Gerlach D, et al. (2012) Identification of site-specific adaptations conferring increased neural cell tropism during human enterovirus 71 infection. PLoS Pathog 8: e1002826.
    • (2012) PLoS Pathog , vol.8 , pp. e1002826
    • Cordey, S.1    Petty, T.J.2    Schibler, M.3    Martinez, Y.4    Gerlach, D.5
  • 49
    • 0024959449 scopus 로고
    • Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
    • Fischer G, Wittmann-Liebold B, Lang K, Kiefhaber T, Schmid FX, (1989) Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature 337: 476–478.
    • (1989) Nature , vol.337 , pp. 476-478
    • Fischer, G.1    Wittmann-Liebold, B.2    Lang, K.3    Kiefhaber, T.4    Schmid, F.X.5
  • 51
    • 0025728450 scopus 로고
    • Peptidyl-prolyl cis-trans isomerase activity as studied by dynamic proton NMR spectroscopy
    • Hubner D, Drakenberg T, Forsen S, Fischer G, (1991) Peptidyl-prolyl cis-trans isomerase activity as studied by dynamic proton NMR spectroscopy. FEBS Lett 284: 79–81.
    • (1991) FEBS Lett , vol.284 , pp. 79-81
    • Hubner, D.1    Drakenberg, T.2    Forsen, S.3    Fischer, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.