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Volumn 10, Issue , 2010, Pages

The intriguing Cyclophilin A-HIV-1 Vpr interaction: Prolyl cis/trans isomerisation catalysis and specific binding

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOPHILIN A; ISOMERASE; PROLINE; VPR PROTEIN; PEPTIDYLPROLYL ISOMERASE; VPR PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 77957259243     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-10-31     Document Type: Article
Times cited : (14)

References (48)
  • 1
    • 0027429412 scopus 로고
    • Incorporation of Vpr into Human Immunodeficiency Virus Type 1 Virions: Requirement for the p6 Region of gag and Mutational Analysis
    • 8230445
    • Incorporation of Vpr into Human Immunodeficiency Virus Type 1 Virions: Requirement for the p6 Region of gag and Mutational Analysis. W Paxton RI Connor NR Landau, J Virol 1993 67 7229 37 8230445
    • (1993) J Virol , vol.67 , pp. 7229-37
    • Paxton, W.1    Connor, R.I.2    Landau, N.R.3
  • 3
    • 0027410459 scopus 로고
    • Induction of cell differentiation by human immunodeficiency virus 1 vpr
    • 10.1016/0092-8674(93)90073-Y. 8440020
    • Induction of cell differentiation by human immunodeficiency virus 1 vpr. DN Levy LS Fernandes WV Williams DB Weiner, Cell 1993 72 541 550 10.1016/0092-8674(93)90073-Y 8440020
    • (1993) Cell , vol.72 , pp. 541-550
    • Levy, D.N.1    Fernandes, L.S.2    Williams, W.V.3    Weiner, D.B.4
  • 4
    • 0028813107 scopus 로고
    • The Human Immunodeficiency Virus Type 1 vpr Gene Prevents Cell Proliferation during Chronic Infection
    • 7815556
    • The Human Immunodeficiency Virus Type 1 vpr Gene Prevents Cell Proliferation during Chronic Infection. ME Rogel LI Wu M Emerman, J Virol 1995 69 882 888 7815556
    • (1995) J Virol , vol.69 , pp. 882-888
    • Rogel, M.E.1    Wu, L.I.2    Emerman, M.3
  • 5
    • 0030920243 scopus 로고    scopus 로고
    • Human Immunodeficiency Virus Type 1 Vpr Induces Apoptosis following Cell Cycle Arrest
    • 9188632
    • Human Immunodeficiency Virus Type 1 Vpr Induces Apoptosis following Cell Cycle Arrest. SA Stewart B Poon JBM Jowett ISY Chen, J Virol 1997 71 5579 92 9188632
    • (1997) J Virol , vol.71 , pp. 5579-92
    • Stewart, S.A.1    Poon, B.2    Jowett, J.B.M.3    Chen, I.S.Y.4
  • 7
    • 0034644649 scopus 로고    scopus 로고
    • Functional and structural characterization of synthetic HIV-1 Vpr that transduces cells, localizes to the nucleus, and induces G(2) cell cycle arrest
    • 10.1074/jbc.M004044200. 10903315
    • Functional and structural characterization of synthetic HIV-1 Vpr that transduces cells, localizes to the nucleus, and induces G(2) cell cycle arrest. P Henklein K Bruns MP Sherman U Tessmer K Licha J Kopp CMC de Noronha WC Greene V Wray U Schubert, J Biol Chem 2000 275 32016 32026 10.1074/jbc.M004044200 10903315
    • (2000) J Biol Chem , vol.275 , pp. 32016-32026
    • Henklein, P.1    Bruns, K.2    Sherman, M.P.3    Tessmer, U.4    Licha, K.5    Kopp, J.6    De Noronha, C.M.C.7    Greene, W.C.8    Wray, V.9    Schubert, U.10
  • 8
    • 0035798131 scopus 로고    scopus 로고
    • Dynamic Distruption in Nuclear Envelope Architecture and Integrity Induced by HIV-1 Vpr
    • 10.1126/science.1063957. 11691994
    • Dynamic Distruption in Nuclear Envelope Architecture and Integrity Induced by HIV-1 Vpr. CMC de Noronha MP Sherman HW Lin MV Cavrois RD Moir RD Goldman WC Greene, Science 2001 294 1105 1108 10.1126/science.1063957 11691994
    • (2001) Science , vol.294 , pp. 1105-1108
    • De Noronha, C.M.C.1    Sherman, M.P.2    Lin, H.W.3    Cavrois, M.V.4    Moir, R.D.5    Goldman, R.D.6    Greene, W.C.7
  • 10
    • 33645767939 scopus 로고    scopus 로고
    • 2 Arrest and Binding to Cyclophilin A Are Independent Phenotypes of Human Immunodeficiency Virus Type 1 Vpr
    • 10.1128/JVI.80.8.3694-3700.2006. 16571786
    • 2 Arrest and Binding to Cyclophilin A Are Independent Phenotypes of Human Immunodeficiency Virus Type 1 Vpr. O Ardon ES Zimmermann JL Andersen JL DeHart J Blackett V Planelles, J Virol 2006 80 3694 3700 10.1128/JVI.80.8.3694-3700.2006 16571786
    • (2006) J Virol , vol.80 , pp. 3694-3700
    • Ardon, O.1    Zimmermann, E.S.2    Andersen, J.L.3    Dehart, J.L.4    Blackett, J.5    Planelles, V.6
  • 11
    • 34249284179 scopus 로고    scopus 로고
    • Role of cyclophilin A in HIV replication
    • DOI 10.2217/17460794.2.1.65
    • Role of cyclophilin A in HIV replication. J Votteler V Wray U Schubert, Future Virol 2007 2 65 78 10.2217/17460794.2.1.65 (Pubitemid 46813453)
    • (2007) Future Virology , vol.2 , Issue.1 , pp. 65-78
    • Votteler, J.1    Wray, V.2    Schubert, U.3
  • 12
    • 0037117555 scopus 로고    scopus 로고
    • Catalysis of cis/trans isomerisation in native HIV-1 capsid by human CypA
    • 10.1073/pnas.082100499. 11929983
    • Catalysis of cis/trans isomerisation in native HIV-1 capsid by human CypA. DA Bosco EZ Eisenmesser S Pochapsky WI Sundsquist D Kern, PNAS 2002 99 5247 5252 10.1073/pnas.082100499 11929983
    • (2002) PNAS , vol.99 , pp. 5247-5252
    • Bosco, D.A.1    Eisenmesser, E.Z.2    Pochapsky, S.3    Sundsquist, W.I.4    Kern, D.5
  • 13
    • 2442670432 scopus 로고    scopus 로고
    • Catalysis and Binding of Cyclophilin A with Different HIV-1 Capsid Constructs
    • 10.1021/bi049841z. 15147195
    • Catalysis and Binding of Cyclophilin A with Different HIV-1 Capsid Constructs. DA Bosco D Kern, Biochemistry 2004 43 6110 6119 10.1021/bi049841z 15147195
    • (2004) Biochemistry , vol.43 , pp. 6110-6119
    • Bosco, D.A.1    Kern, D.2
  • 16
    • 0028965266 scopus 로고
    • Mode of action of SDZ NIM 811, a nonimmunosuppressive cyclosporine A analog with activity against human immunodeficiency virus (HIV) type 1: Interference with HIV Protein-cyclophilin A interactions
    • 7884893
    • Mode of action of SDZ NIM 811, a nonimmunosuppressive cyclosporine A analog with activity against human immunodeficiency virus (HIV) type 1: interference with HIV Protein-cyclophilin A interactions. A Billich F Hammerschmid P Peichl R Wenger G Zenke V Quesniaux B Rosenwirth, J Virol 1995 69 2451 2461 7884893
    • (1995) J Virol , vol.69 , pp. 2451-2461
    • Billich, A.1    Hammerschmid, F.2    Peichl, P.3    Wenger, R.4    Zenke, G.5    Quesniaux, V.6    Rosenwirth, B.7
  • 17
    • 0030219974 scopus 로고    scopus 로고
    • Inhibition of HIV-1 replication by cyclosporine A or related compounds correlates with the ability to disrupt the Gag-cyclophilin A interaction
    • 10.1006/viro.1996.0421. 8806510
    • Inhibition of HIV-1 replication by cyclosporine A or related compounds correlates with the ability to disrupt the Gag-cyclophilin A interaction. EK Franke J Luban, Virology 1996 222 279 282 10.1006/viro.1996.0421 8806510
    • (1996) Virology , vol.222 , pp. 279-282
    • Franke, E.K.1    Luban, J.2
  • 18
    • 0030760256 scopus 로고    scopus 로고
    • Active-site residues of cyclophilin A are crucial for its incorporation into human immunodeficiency virus type 1 virions
    • 9261445
    • Active-site residues of cyclophilin A are crucial for its incorporation into human immunodeficiency virus type 1 virions. T Dorfman A Weimann A Borsetti CT Walsh HG Göttlinger, J Virol 1997 71 7110 7113 9261445
    • (1997) J Virol , vol.71 , pp. 7110-7113
    • Dorfman, T.1    Weimann, A.2    Borsetti, A.3    Walsh, C.T.4    Göttlinger, H.G.5
  • 19
    • 0242321995 scopus 로고    scopus 로고
    • Structural Characterization of the HIV-1 Vpr N Terminus
    • 10.1074/jbc.M305413200. 12881523
    • Structural Characterization of the HIV-1 Vpr N Terminus. K Bruns T Fossen V Wray P Henklein U Tessmer U Schubert, J Biol Chem 2003 278 43188 43201 10.1074/jbc.M305413200 12881523
    • (2003) J Biol Chem , vol.278 , pp. 43188-43201
    • Bruns, K.1    Fossen, T.2    Wray, V.3    Henklein, P.4    Tessmer, U.5    Schubert, U.6
  • 20
    • 0027940713 scopus 로고
    • Specific incorporation of cyclophilin A into HIV-1 virions
    • 10.1038/372359a0. 7969494
    • Specific incorporation of cyclophilin A into HIV-1 virions. EK Franke HEH Yuan J Luban, Nature 1994 372 359 362 10.1038/372359a0 7969494
    • (1994) Nature , vol.372 , pp. 359-362
    • Franke, E.K.1    Yuan, H.E.H.2    Luban, J.3
  • 21
    • 0025373627 scopus 로고
    • Substrate Specificities of the Peptidyl Prolyl Cis- Trans Isomerase Activity of Cyclophilin and FK-506 Binding Protein: Evidence for the Existence of a Family of Distinct Enzymes
    • 10.1021/bi00468a001. 1693856
    • Substrate Specificities of the Peptidyl Prolyl Cis- Trans Isomerase Activity of Cyclophilin and FK-506 Binding Protein: Evidence for the Existence of a Family of Distinct Enzymes. RK Harrison RL Stein, Biochemistry 1990 29 3813 3816 10.1021/bi00468a001 1693856
    • (1990) Biochemistry , vol.29 , pp. 3813-3816
    • Harrison, R.K.1    Stein, R.L.2
  • 22
    • 0033605133 scopus 로고    scopus 로고
    • Maturation-induced Conformational Changes of HIV-1 Capsid Protein and Identification of Two High Affinity Sites for Cyclophilins in the C-termainal Domain
    • 10.1074/jbc.274.9.5326. 10026140
    • Maturation-induced Conformational Changes of HIV-1 Capsid Protein and Identification of Two High Affinity Sites for Cyclophilins in the C-termainal Domain. MM Endrich P Gehrig H Gehrig, J Biol Chem 1999 274 5326 5332 10.1074/jbc.274.9.5326 10026140
    • (1999) J Biol Chem , vol.274 , pp. 5326-5332
    • Endrich, M.M.1    Gehrig, P.2    Gehrig, H.3
  • 23
    • 0027321984 scopus 로고
    • The cis/trans interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin
    • DOI 10.1016/0014-5793(93)81338-Z
    • The cis/trans interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin. D Kern T Drakenberg M Wikström S Forsèn H Bang G Fischer, FEBS 1993 323 198 202 10.1016/0014-5793(93) 81338-Z (Pubitemid 23153468)
    • (1993) FEBS Letters , vol.323 , Issue.3 , pp. 198-202
    • Kern, D.1    Drakenberg, T.2    Wikstrom, M.3    Forsen, S.4    Bang, H.5    Fischer, G.6
  • 24
    • 0036360507 scopus 로고    scopus 로고
    • NMR structure of the HIV-1 regulatory protein Vpr in H2O/trifluoroethanol - Comparison with the Vpr N-terminal (1-51) and C-terminal (52-96) domains
    • 10.1046/j.1432-1033.2002.03067.x. 12153575
    • NMR structure of the HIV-1 regulatory protein Vpr in H2O/trifluoroethanol - Comparison with the Vpr N-terminal (1-51) and C-terminal (52-96) domains. K Wecker N Morellet S Bouaziz BP Roques, Eur J Biochem 2002 269 3779 3788 10.1046/j.1432-1033.2002.03067.x 12153575
    • (2002) Eur J Biochem , vol.269 , pp. 3779-3788
    • Wecker, K.1    Morellet, N.2    Bouaziz, S.3    Roques, B.P.4
  • 25
    • 0037436404 scopus 로고    scopus 로고
    • NMR structure of the HIV-1 regulatory protein Vpr
    • 10.1016/S0022-2836(03)00060-3. 12614620
    • NMR structure of the HIV-1 regulatory protein Vpr. N Morellet S Bouaziz P Petitjean BP Roques, J Mol Biol 2003 327 215 227 10.1016/S0022-2836(03)00060-3 12614620
    • (2003) J Mol Biol , vol.327 , pp. 215-227
    • Morellet, N.1    Bouaziz, S.2    Petitjean, P.3    Roques, B.P.4
  • 28
    • 34548155662 scopus 로고    scopus 로고
    • Proline 35 of human immunodeficiency virus type 1 (HIV-1) Vpr regulates the integrity of the N-terminal helix and the incorporation of Vpr into virus particles and supports the replication of R5-tropic HIV-1 in human lymphoid tissue ex vivo
    • 10.1128/JVI.02803-06. 17553868
    • Proline 35 of human immunodeficiency virus type 1 (HIV-1) Vpr regulates the integrity of the N-terminal helix and the incorporation of Vpr into virus particles and supports the replication of R5-tropic HIV-1 in human lymphoid tissue ex vivo. J Votteler N Studtrucker S Sörgel J Münch E Rücker F Kirchhoff B Schick P Henklein T Fossen K Bruns A Sharma V Wray U Schubert, J Virol 2007 81 9572 9576 10.1128/JVI.02803-06 17553868
    • (2007) J Virol , vol.81 , pp. 9572-9576
    • Votteler, J.1    Studtrucker, N.2    Sörgel, S.3    Münch, J.4    Rücker, E.5    Kirchhoff, F.6    Schick, B.7    Henklein, P.8    Fossen, T.9    Bruns, K.10    Sharma, A.11    Wray, V.12    Schubert, U.13
  • 29
    • 84985715908 scopus 로고
    • NMR Studies of the Rates of Proline Cis-Trans Isomerisation in Oligopeptides
    • 10.1002/bip.1981.360201209
    • NMR Studies of the Rates of Proline Cis-Trans Isomerisation in Oligopeptides. C Grathwohl K Wüthrich, Biopolymers 1981 20 2623 2633 10.1002/bip.1981.360201209
    • (1981) Biopolymers , vol.20 , pp. 2623-2633
    • Grathwohl, C.1    Wüthrich, K.2
  • 30
    • 33847010532 scopus 로고    scopus 로고
    • Prolyl cis-trans isomerisation as a molecular timer in Crk signaling
    • 10.1016/j.molcel.2007.02.005. 17317620
    • Prolyl cis-trans isomerisation as a molecular timer in Crk signaling. LK Nicholson KP Lu, Mol Cell 2007 25 483 485 10.1016/j.molcel.2007.02.005 17317620
    • (2007) Mol Cell , vol.25 , pp. 483-485
    • Nicholson, L.K.1    Lu, K.P.2
  • 31
    • 0025144288 scopus 로고
    • Peptidyl-Prolyl Cis-Trans Isomerase Activity of Cyclophilin Studied by One-Dimensional 'H Nuclear Magnetic Resonance Spectroscopy
    • 10.1021/ja00174a064
    • Peptidyl-Prolyl Cis-Trans Isomerase Activity of Cyclophilin Studied by One-Dimensional 'H Nuclear Magnetic Resonance Spectroscopy. VL Hsu RE Handschumacher IM Armitage, J Am Chem Soc 1990 112 6145 6141 10.1021/ja00174a064
    • (1990) J Am Chem Soc , vol.112 , pp. 6145-6141
    • Hsu, V.L.1    Handschumacher, R.E.2    Armitage, I.M.3
  • 32
    • 0025728450 scopus 로고
    • Peptidyl-prolyl cis-trans isomerase activity as studied by dynamic proton NMR spectroscopy
    • 10.1016/0014-5793(91)80766-V
    • Peptidyl-prolyl cis-trans isomerase activity as studied by dynamic proton NMR spectroscopy. D Hübner T Drakenberg S Forsén G Fischer, FEBS 1991 284 79 81 10.1016/0014-5793(91)80766-V
    • (1991) FEBS , vol.284 , pp. 79-81
    • Hübner, D.1    Drakenberg, T.2    Forsén, S.3    Fischer, G.4
  • 33
    • 0028877264 scopus 로고
    • Kinetic Analysis of Cyclophilin-Catalyzed Prolyl CisRrans Isomerisation by Dynamic NMR Spectroscopy
    • 10.1021/bi00041a039. 7577948
    • Kinetic Analysis of Cyclophilin-Catalyzed Prolyl CisRrans Isomerisation by Dynamic NMR Spectroscopy. D Kern G Kern G Scherer G Fischer T Drakenberg, Biochemistry 1995 34 13594 13602 10.1021/bi00041a039 7577948
    • (1995) Biochemistry , vol.34 , pp. 13594-13602
    • Kern, D.1    Kern, G.2    Scherer, G.3    Fischer, G.4    Drakenberg, T.5
  • 34
    • 0030931434 scopus 로고    scopus 로고
    • Conformational state of a 25-mer peptide from the cyclophilin-binding loop of the HIV type 1 capsid protein
    • 9337866
    • Conformational state of a 25-mer peptide from the cyclophilin-binding loop of the HIV type 1 capsid protein. U Reimer M Drewello M Jakob G Fischer M Schutkowski, Biochem J 1997 326 181 185 9337866
    • (1997) Biochem J , vol.326 , pp. 181-185
    • Reimer, U.1    Drewello, M.2    Jakob, M.3    Fischer, G.4    Schutkowski, M.5
  • 35
    • 0030880581 scopus 로고    scopus 로고
    • HIV protease substrate conformation: Modulation by cyclophilin A
    • DOI 10.1016/S0014-5793(97)00974-5, PII S0014579397009745
    • HIV protease substrate conformation: modulation by cyclophilin A. MA McCornack LT Kakalis C Caserta RE Handschumacher IM Armitage, FEBS Lett 1997 414 88 10.1016/S0014-5793(97)00974-5 (Pubitemid 27380360)
    • (1997) FEBS Letters , vol.414 , Issue.1 , pp. 84-88
    • McCornack, M.A.1    Kakalis, L.T.2    Caserta, C.3    Handschumacher, R.E.4    Armitage, I.M.5
  • 36
    • 0015024541 scopus 로고
    • Substrate anchoring and the catalytic power of enzymes
    • 10.1073/pnas.68.3.563. 5276762
    • Substrate anchoring and the catalytic power of enzymes. J Reuben, PNAS 1971 68 563 565 10.1073/pnas.68.3.563 5276762
    • (1971) PNAS , vol.68 , pp. 563-565
    • Reuben, J.1
  • 37
    • 0037154884 scopus 로고    scopus 로고
    • Enzyme Dynamics during Catalysis
    • 10.1126/science.1066176. 11859194
    • Enzyme Dynamics During Catalysis. EZ Eisenmesser DA Bosco M Akke D Kern, Science 2002 295 1520 1523 10.1126/science.1066176 11859194
    • (2002) Science , vol.295 , pp. 1520-1523
    • Eisenmesser, E.Z.1    Bosco, D.A.2    Akke, M.3    Kern, D.4
  • 38
    • 37549010341 scopus 로고    scopus 로고
    • Survey of the year 2006 commercial optical biosensor literature
    • 10.1002/jmr.862. 18074396
    • Survey of the year 2006 commercial optical biosensor literature. RL Rich DG Myszka, J Mol Recognit 2007 20 300 366 10.1002/jmr.862 18074396
    • (2007) J Mol Recognit , vol.20 , pp. 300-366
    • Rich, R.L.1    Myszka, D.G.2
  • 39
    • 0030448994 scopus 로고    scopus 로고
    • Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid
    • 10.1016/S0092-8674(00)81823-1. 8980234
    • Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid. TR Gamble FF Vajdos SH Yoo DK Worthylake M Houseweart WI Sundquist CP Hill, Cell 1996 87 1285 1294 10.1016/S0092-8674(00)81823-1 8980234
    • (1996) Cell , vol.87 , pp. 1285-1294
    • Gamble, T.R.1    Vajdos, F.F.2    Yoo, S.H.3    Worthylake, D.K.4    Houseweart, M.5    Sundquist, W.I.6    Hill, C.P.7
  • 40
    • 0030666230 scopus 로고    scopus 로고
    • Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein
    • 10.1002/pro.5560061103
    • Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein. FF Vajdos S Yoo M Houseweart WI Sundquist CP Hill, Prot Sci 1997 6 2297 2307 10.1002/pro.5560061103
    • (1997) Prot Sci , vol.6 , pp. 2297-2307
    • Vajdos, F.F.1    Yoo, S.2    Houseweart, M.3    Sundquist, W.I.4    Hill, C.P.5
  • 41
    • 21244444702 scopus 로고    scopus 로고
    • Cyclophilin A binds to linear peptide motifs containing a consensus that is present in many human proteins
    • 10.1074/jbc.M503405200. 15845542
    • Cyclophilin A binds to linear peptide motifs containing a consensus that is present in many human proteins. K Piotukh W Gu M Kofler D Labudde V Helms C Freund, J Biol Chem 2005 280 23668 23674 10.1074/jbc.M503405200 15845542
    • (2005) J Biol Chem , vol.280 , pp. 23668-23674
    • Piotukh, K.1    Gu, W.2    Kofler, M.3    Labudde, D.4    Helms, V.5    Freund, C.6
  • 42
    • 0025216877 scopus 로고
    • Cloning, expression, and purification of human cyclophilin in Escherichia coli and assessment of the catalytic role of cysteines by site-directed mutagenesis
    • 10.1073/pnas.87.6.2304. 2179953
    • Cloning, expression, and purification of human cyclophilin in Escherichia coli and assessment of the catalytic role of cysteines by site-directed mutagenesis. J Liu MW Albers CM Chen SL Schreiber CT Walsh, Proc Natl Acad Sci USA 1990 87 2304 2308 10.1073/pnas.87.6.2304 2179953
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 2304-2308
    • Liu, J.1    Albers, M.W.2    Chen, C.M.3    Schreiber, S.L.4    Walsh, C.T.5
  • 43
    • 0041925439 scopus 로고    scopus 로고
    • In Vitro Assembly Properties of Wild-Type and Cyclophilin-Binding Defective Human Immunodeficiency Virus Capsid Proteins in the Presence and Absence of Cyclophilin A
    • 10.1006/viro.1999.9668. 10208938
    • In Vitro Assembly Properties of Wild-Type and Cyclophilin-Binding Defective Human Immunodeficiency Virus Capsid Proteins in the Presence and Absence of Cyclophilin A. M Grättinger H Hohenberg D Thomas T Wilk B Müller HG Kräusslich, Virology 1999 257 247 260 10.1006/viro.1999.9668 10208938
    • (1999) Virology , vol.257 , pp. 247-260
    • Grättinger, M.1    Hohenberg, H.2    Thomas, D.3    Wilk, T.4    Müller, B.5    Kräusslich, H.G.6
  • 44
    • 79960698472 scopus 로고
    • Water Suppression That Works. Excitation Sculpting Using Arbitrary Wave-Forms and Pulsed-Field Gradients
    • 10.1006/jmra.1995.1047
    • Water Suppression That Works. Excitation Sculpting Using Arbitrary Wave-Forms and Pulsed-Field Gradients. TL Hwang AJ Shaka, J Magn Reson 1995 112 275 279 10.1006/jmra.1995.1047
    • (1995) J Magn Reson , vol.112 , pp. 275-279
    • Hwang, T.L.1    Shaka, A.J.2
  • 45
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. A Bax DG Davis, J Magn Reson 1985 65 355 360
    • (1985) J Magn Reson , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 47
    • 0004040543 scopus 로고    scopus 로고
    • University of California, San Francisco
    • SPARKY 3. TD Goddard DG Kneller, University of California, San Francisco http://www.cgl.ucsf.edu/home/sparky/
    • SPARKY 3
    • Goddard, T.D.1    Kneller, D.G.2


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