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Volumn 5, Issue , 2015, Pages

Dynamic association of PfEMP1 and KAHRP in knobs mediates cytoadherence during Plasmodium invasion

Author keywords

[No Author keywords available]

Indexed keywords

INTRINSICALLY DISORDERED PROTEIN; KNOB PROTEIN, PLASMODIUM FALCIPARUM; PEPTIDE; PROTEIN BINDING; PROTOZOAL PROTEIN; SOLUTION AND SOLUBILITY;

EID: 84923869809     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep08617     Document Type: Article
Times cited : (18)

References (53)
  • 1
    • 84855183249 scopus 로고    scopus 로고
    • Worldwide incidence of malaria in 2009: Estimates, time trends, and a critique of methods
    • Cibulskis, R. E., Aregawi, M., Williams, R., Otten, M. & Dye, C. Worldwide incidence of malaria in 2009: estimates, time trends, and a critique of methods. PLoS Med 8, e1001142 (2011).
    • (2011) PLoS Med , vol.8 , pp. e1001142
    • Cibulskis, R.E.1    Aregawi, M.2    Williams, R.3    Otten, M.4    Dye, C.5
  • 2
    • 0030938126 scopus 로고    scopus 로고
    • Cytoadherence of Plasmodium falciparum to intercellular adhesion molecule 1 and chondroitin-4-sulfate expressed by the syncytiotrophoblast in the human placenta
    • Maubert, B., Guilbert, L. J. & Deloron, P. Cytoadherence of Plasmodium falciparum to intercellular adhesion molecule 1 and chondroitin-4-sulfate expressed by the syncytiotrophoblast in the human placenta. Infect Immun 65, 1251-1257 (1997).
    • (1997) Infect Immun , vol.65 , pp. 1251-1257
    • Maubert, B.1    Guilbert, L.J.2    Deloron, P.3
  • 3
    • 0021884874 scopus 로고
    • Human cerebral malaria. A quantitative ultrastructural analysis of parasitized erythrocyte sequestration
    • MacPherson, G. G., Warrell, M. J., White, N. J., Looareesuwan, S. &Warrell, D. A. Human cerebral malaria. A quantitative ultrastructural analysis of parasitized erythrocyte sequestration. Am J Pathol 119, 385-401 (1985).
    • (1985) Am J Pathol , vol.119 , pp. 385-401
    • MacPherson, G.G.1    Warrell, M.J.2    White, N.J.3    Looareesuwan, S.4    Warrell, D.A.5
  • 4
    • 1942477417 scopus 로고    scopus 로고
    • Malaria and the red blood cell membrane
    • Cooke, B. M., Mohandas, N. & Coppel, R. L. Malaria and the red blood cell membrane. Semin Hematol 41, 173-188 (2004).
    • (2004) Semin Hematol , vol.41 , pp. 173-188
    • Cooke, B.M.1    Mohandas, N.2    Coppel, R.L.3
  • 5
    • 0036096643 scopus 로고    scopus 로고
    • Asexual blood stages of malaria antigens: Cytoadherence
    • Baruch, D. I., Rogerson, S. J. & Cooke, B. M. Asexual blood stages of malaria antigens: cytoadherence. Chem Immunol 80, 144-162 (2002).
    • (2002) Chem Immunol , vol.80 , pp. 144-162
    • Baruch, D.I.1    Rogerson, S.J.2    Cooke, B.M.3
  • 6
    • 0029070914 scopus 로고
    • The large diverse gene family var encodes proteins involved in cytoadherence and antigenic variation of Plasmodium falciparum -infected erythrocytes
    • Su, X. Z. et al. The large diverse gene family var encodes proteins involved in cytoadherence and antigenic variation of Plasmodium falciparum -infected erythrocytes. Cell 82, 89-100 (1995).
    • (1995) Cell , vol.82 , pp. 89-100
    • Su, X.Z.1
  • 7
    • 0029052741 scopus 로고
    • Cloning the P. Falciparum gene encoding PfEMP1, a malarial variant antigen and adherence receptor on the surface of parasitized human erythrocytes
    • Baruch, D. I. et al. Cloning the P. falciparum gene encoding PfEMP1, a malarial variant antigen and adherence receptor on the surface of parasitized human erythrocytes. Cell 82, 77-87 (1995).
    • (1995) Cell , vol.82 , pp. 77-87
    • Baruch, D.I.1
  • 8
    • 0028982168 scopus 로고
    • Switches in expression of Plasmodium falciparum var genes correlate with changes in antigenic and cytoadherent phenotypes of infected erythrocytes
    • Smith, J. D. et al. Switches in expression of Plasmodium falciparum var genes correlate with changes in antigenic and cytoadherent phenotypes of infected erythrocytes. Cell 82, 101-110 (1995).
    • (1995) Cell , vol.82 , pp. 101-110
    • Smith, J.D.1
  • 9
    • 0030904788 scopus 로고    scopus 로고
    • Targeted gene disruption shows that knobs enable malaria-infected red cells to cytoadhere under physiological shear stress
    • Crabb, B. S. et al. Targeted gene disruption shows that knobs enable malaria-infected red cells to cytoadhere under physiological shear stress. Cell 89, 287-296 (1997).
    • (1997) Cell , vol.89 , pp. 287-296
    • Crabb, B.S.1
  • 10
    • 0023156566 scopus 로고
    • Plasmodium falciparum: Identification and localization of a knob protein antigen expressed by a cDNA clone
    • Culvenor, J. G. et al. Plasmodium falciparum: identification and localization of a knob protein antigen expressed by a cDNA clone. Exp Parasitol 63, 58-67 (1987).
    • (1987) Exp Parasitol , vol.63 , pp. 58-67
    • Culvenor, J.G.1
  • 11
    • 0023427830 scopus 로고
    • Primary structure and subcellular localization of the knob-associated histidine-rich protein of Plasmodium falciparum
    • Pologe, L. G., Pavlovec, A., Shio, H. & Ravetch, J. V. Primary structure and subcellular localization of the knob-associated histidine-rich protein of Plasmodium falciparum. Proc Natl Acad Sci U S A 84, 7139-7143 (1987).
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 7139-7143
    • Pologe, L.G.1    Pavlovec, A.2    Shio, H.3    Ravetch, J.V.4
  • 12
    • 0023333815 scopus 로고
    • The complete sequence of the gene for the knob-associated histidine-rich protein from Plasmodium falciparum
    • Triglia, T. et al. The complete sequence of the gene for the knob-associated histidine-rich protein from Plasmodium falciparum. EMBO J 6, 1413-1419 (1987).
    • (1987) EMBO J , vol.6 , pp. 1413-1419
    • Triglia, T.1
  • 13
    • 0033588089 scopus 로고    scopus 로고
    • Mapping the binding domains involved in the interaction between the Plasmodium falciparum knob-associated histidine-rich protein (KAHRP) and the cytoadherence ligand P. Falciparum erythrocyte membrane protein 1 (PfEMP1)
    • Waller, K. L., Cooke, B. M., Nunomura, W., Mohandas, N. & Coppel, R. L. Mapping the binding domains involved in the interaction between the Plasmodium falciparum knob-associated histidine-rich protein (KAHRP) and the cytoadherence ligand P. falciparum erythrocyte membrane protein 1 (PfEMP1). J Biol Chem 274, 23808-23813 (1999).
    • (1999) J Biol Chem , vol.274 , pp. 23808-23813
    • Waller, K.L.1    Cooke, B.M.2    Nunomura, W.3    Mohandas, N.4    Coppel, R.L.5
  • 14
    • 0036139910 scopus 로고    scopus 로고
    • Mapping the domains of the cytoadherence ligand Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) that bind to the knob-associated histidine-rich protein (KAHRP)
    • Waller, K. L., Nunomura, W., Cooke, B. M., Mohandas, N. & Coppel, R. L. Mapping the domains of the cytoadherence ligand Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) that bind to the knob-associated histidine-rich protein (KAHRP). Mol Biochem Parasitol 119, 125-129 (2002).
    • (2002) Mol Biochem Parasitol , vol.119 , pp. 125-129
    • Waller, K.L.1    Nunomura, W.2    Cooke, B.M.3    Mohandas, N.4    Coppel, R.L.5
  • 15
    • 0033737420 scopus 로고    scopus 로고
    • The cytoadherence ligand Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) binds to the P. Falciparum knob-associated histidine-rich protein (KAHRP) by electrostatic interactions
    • Voigt, S. et al. The cytoadherence ligand Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) binds to the P. falciparum knob-associated histidine-rich protein (KAHRP) by electrostatic interactions. Mol Biochem Parasitol 110, 423-428 (2000).
    • (2000) Mol Biochem Parasitol , vol.110 , pp. 423-428
    • Voigt, S.1
  • 16
    • 77955099224 scopus 로고    scopus 로고
    • Temperature-dependent structural changes in intrinsically disordered proteins: Formation of alpha-helices or loss of polyproline II?
    • Kjaergaard, M. et al. Temperature-dependent structural changes in intrinsically disordered proteins: formation of alpha-helices or loss of polyproline II? Protein Sci 19, 1555-1564 (2010).
    • (2010) Protein Sci , vol.19 , pp. 1555-1564
    • Kjaergaard, M.1
  • 17
    • 33748460073 scopus 로고    scopus 로고
    • Heteronuclear NMR identifies a nascent helix in intrinsically disordered dynein intermediate chain: Implications for folding and dimerization
    • Benison, G., Nyarko, A. & Barbar, E. Heteronuclear NMR identifies a nascent helix in intrinsically disordered dynein intermediate chain: implications for folding and dimerization. J Mol Biol 362, 1082-1093 (2006).
    • (2006) J Mol Biol , vol.362 , pp. 1082-1093
    • Benison, G.1    Nyarko, A.2    Barbar, E.3
  • 19
    • 27544456339 scopus 로고    scopus 로고
    • A simple method to predict protein flexibility using secondary chemical shifts
    • Berjanskii, M. V. & Wishart, D. S. A simple method to predict protein flexibility using secondary chemical shifts. J Am Chem Soc 127, 14970-14971 (2005).
    • (2005) J am Chem Soc , vol.127 , pp. 14970-14971
    • Berjanskii, M.V.1    Wishart, D.S.2
  • 20
    • 0027236794 scopus 로고
    • Structural basis of amino acid alpha helix propensity
    • Blaber, M., Zhang, X. J. & Matthews, B. W. Structural basis of amino acid alpha helix propensity. Science 260, 1637-1640 (1993).
    • (1993) Science , vol.260 , pp. 1637-1640
    • Blaber, M.1    Zhang, X.J.2    Matthews, B.W.3
  • 21
    • 0029361842 scopus 로고
    • Relationship of sidechain hydrophobicity and alpha-helical propensity on the stability of the single-stranded amphipathic alpha-helix
    • Monera, O. D., Sereda, T. J., Zhou, N. E., Kay, C. M. & Hodges, R. S. Relationship of sidechain hydrophobicity and alpha-helical propensity on the stability of the single-stranded amphipathic alpha-helix. J Pept Sci 1, 319-329 (1995).
    • (1995) J Pept Sci , vol.1 , pp. 319-329
    • Monera, O.D.1    Sereda, T.J.2    Zhou, N.E.3    Kay, C.M.4    Hodges, R.S.5
  • 22
    • 0015386346 scopus 로고
    • Conformational studies on copolymers of hydroxypropyl-L-glutamine and L-leucine. Circular dichroism studies
    • Chou, P. Y., Wells, M. & Fasman, G. D. Conformational studies on copolymers of hydroxypropyl-L-glutamine and L-leucine. Circular dichroism studies. Biochemistry 11, 3028-3043 (1972).
    • (1972) Biochemistry , vol.11 , pp. 3028-3043
    • Chou, P.Y.1    Wells, M.2    Fasman, G.D.3
  • 23
    • 29544446689 scopus 로고    scopus 로고
    • Weak protein-protein interactions as probed by NMR spectroscopy
    • Vaynberg, J. & Qin, J. Weak protein-protein interactions as probed by NMR spectroscopy. Trends Biotechnol 24, 22-27 (2006).
    • (2006) Trends Biotechnol , vol.24 , pp. 22-27
    • Vaynberg, J.1    Qin, J.2
  • 24
    • 0027633499 scopus 로고
    • Prospects for NMR of large proteins
    • Wagner, G. Prospects for NMR of large proteins. J Biomol NMR 3, 375-385 (1993).
    • (1993) J Biomol NMR , vol.3 , pp. 375-385
    • Wagner, G.1
  • 25
    • 0031451750 scopus 로고    scopus 로고
    • Chemical shift dispersion and secondary structure prediction in unfolded and partly folded proteins
    • Yao, J., Dyson, H. J. & Wright, P. E. Chemical shift dispersion and secondary structure prediction in unfolded and partly folded proteins. FEBS Lett 419, 285-289 (1997).
    • (1997) FEBS Lett , vol.419 , pp. 285-289
    • Yao, J.1    Dyson, H.J.2    Wright, P.E.3
  • 26
    • 79951905332 scopus 로고    scopus 로고
    • Multitude of binding modes attainable by intrinsically disordered proteins: A portrait gallery of disorder-based complexes
    • Uversky, V. N. Multitude of binding modes attainable by intrinsically disordered proteins: a portrait gallery of disorder-based complexes. Chem Soc Rev 40, 1623-1634 (2011).
    • (2011) Chem Soc Rev , vol.40 , pp. 1623-1634
    • Uversky, V.N.1
  • 27
    • 57449091330 scopus 로고    scopus 로고
    • The intrinsically disordered cytoplasmic domain of the T cell receptor zeta chain binds to the nef protein of simian immunodeficiency virus without a disorder-to-order transition
    • Sigalov, A. B., Kim, W. M., Saline, M. & Stern, L. J. The intrinsically disordered cytoplasmic domain of the T cell receptor zeta chain binds to the nef protein of simian immunodeficiency virus without a disorder-to-order transition. Biochemistry 47, 12942-12944 (2008).
    • (2008) Biochemistry , vol.47 , pp. 12942-12944
    • Sigalov, A.B.1    Kim, W.M.2    Saline, M.3    Stern, L.J.4
  • 28
    • 33947254923 scopus 로고    scopus 로고
    • Binding of intrinsically disordered proteins is not necessarily accompanied by a structural transition to a folded form
    • Sigalov, A. B., Zhuravleva, A. V. & Orekhov, V. Y. Binding of intrinsically disordered proteins is not necessarily accompanied by a structural transition to a folded form. Biochimie 89, 419-421 (2007).
    • (2007) Biochimie , vol.89 , pp. 419-421
    • Sigalov, A.B.1    Zhuravleva, A.V.2    Orekhov, V.Y.3
  • 29
    • 1542319866 scopus 로고    scopus 로고
    • Quantitative observation of backbone disorder in native elastin
    • Pometun, M. S., Chekmenev, E. Y. &Wittebort, R. J. Quantitative observation of backbone disorder in native elastin. J Biol Chem 279, 7982-7987 (2004).
    • (2004) J Biol Chem , vol.279 , pp. 7982-7987
    • Pometun, M.S.1    Chekmenev, E.Y.2    Wittebort, R.J.3
  • 30
    • 33745585336 scopus 로고    scopus 로고
    • The role of KAHRP domains in knob formation and cytoadherence of P. Falciparuminfected human erythrocytes
    • Rug, M., Prescott, S. W., Fernandez, K. M., Cooke, B. M.&Cowman, A. F. The role of KAHRP domains in knob formation and cytoadherence of P. falciparuminfected human erythrocytes. Blood 108, 370-378 (2006).
    • (2006) Blood , vol.108 , pp. 370-378
    • Rug, M.1    Prescott, S.W.2    Fernandez, K.M.3    Cooke, B.M.4    Cowman, A.F.5
  • 31
    • 77955203926 scopus 로고    scopus 로고
    • Quantifying colocalization by correlation: The Pearson correlation coefficient is superior to the Mander's overlap coefficient
    • Adler, J. & Parmryd, I. Quantifying colocalization by correlation: the Pearson correlation coefficient is superior to the Mander's overlap coefficient. Cytometry A 77, 733-742 (2010).
    • (2010) Cytometry A , vol.77 , pp. 733-742
    • Adler, J.1    Parmryd, I.2
  • 32
    • 21044459035 scopus 로고    scopus 로고
    • PfEMP1 expression is reduced on the surface of knobless Plasmodium falciparum infected erythrocytes
    • Horrocks, P. et al. PfEMP1 expression is reduced on the surface of knobless Plasmodium falciparum infected erythrocytes. J Cell Sci 118, 2507-2518 (2005).
    • (2005) J Cell Sci , vol.118 , pp. 2507-2518
    • Horrocks, P.1
  • 33
    • 0022363735 scopus 로고
    • Membrane knobs are required for the microcirculatory obstruction induced by Plasmodium falciparum-infected erythrocytes
    • Raventos-Suarez, C., Kaul, D. K., Macaluso, F. &Nagel, R. L. Membrane knobs are required for the microcirculatory obstruction induced by Plasmodium falciparum-infected erythrocytes. Proc Natl Acad Sci U S A 82, 3829-3833 (1985).
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 3829-3833
    • Raventos-Suarez, C.1    Kaul, D.K.2    Macaluso, F.3    Nagel, R.L.4
  • 34
    • 0034105159 scopus 로고    scopus 로고
    • Plasmodium falciparum erythrocyte membrane protein 1 is anchored to the actin-spectrin junction and knob-associated histidine-rich protein in the erythrocyte skeleton
    • Oh, S. S. et al. Plasmodium falciparum erythrocyte membrane protein 1 is anchored to the actin-spectrin junction and knob-associated histidine-rich protein in the erythrocyte skeleton. Mol Biochem Parasitol 108, 237-247 (2000).
    • (2000) Mol Biochem Parasitol , vol.108 , pp. 237-247
    • Oh, S.S.1
  • 35
    • 0021264123 scopus 로고
    • Identification of a strainspecific malarial antigen exposed on the surface of Plasmodium falciparuminfected erythrocytes
    • Leech, J. H., Barnwell, J. W., Miller, L. H. &Howard, R. J. Identification of a strainspecific malarial antigen exposed on the surface of Plasmodium falciparuminfected erythrocytes. J Exp Med 159, 1567-1575 (1984).
    • (1984) J Exp Med , vol.159 , pp. 1567-1575
    • Leech, J.H.1    Barnwell, J.W.2    Miller, L.H.3    Howard, R.J.4
  • 36
    • 65249181659 scopus 로고    scopus 로고
    • Erythrocytic casein kinase II regulates cytoadherence of Plasmodium falciparum-infected red blood cells
    • Hora, R., Bridges, D. J., Craig, A. & Sharma, A. Erythrocytic casein kinase II regulates cytoadherence of Plasmodium falciparum-infected red blood cells. J Biol Chem 284, 6260-6269 (2009).
    • (2009) J Biol Chem , vol.284 , pp. 6260-6269
    • Hora, R.1    Bridges, D.J.2    Craig, A.3    Sharma, A.4
  • 37
    • 84857711352 scopus 로고    scopus 로고
    • Structural analysis of the Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) intracellular domain reveals a conserved interaction epitope
    • Mayer, C., Slater, L., Erat, M. C., Konrat, R. & Vakonakis, I. Structural analysis of the Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) intracellular domain reveals a conserved interaction epitope. J Biol Chem 287, 7182-7189 (2012).
    • (2012) J Biol Chem , vol.287 , pp. 7182-7189
    • Mayer, C.1    Slater, L.2    Erat, M.C.3    Konrat, R.4    Vakonakis, I.5
  • 38
    • 77953211283 scopus 로고    scopus 로고
    • Protein tandem repeats - The more perfect, the less structured
    • Jorda, J., Xue, B., Uversky, V. N. & Kajava, A. V. Protein tandem repeats - the more perfect, the less structured. FEBS J 277, 2673-2682 (2010).
    • (2010) FEBS J , vol.277 , pp. 2673-2682
    • Jorda, J.1    Xue, B.2    Uversky, V.N.3    Kajava, A.V.4
  • 39
    • 56649112976 scopus 로고    scopus 로고
    • Dynamic equilibrium engagement of a polyvalent ligand with a single-site receptor
    • Mittag, T. et al. Dynamic equilibrium engagement of a polyvalent ligand with a single-site receptor. Proc Natl Acad Sci U S A 105, 17772-17777 (2008).
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 17772-17777
    • Mittag, T.1
  • 40
    • 84866089784 scopus 로고    scopus 로고
    • An Exported Heat Shock Protein 40 Associates with Pathogenesis-Related Knobs in Plasmodium falciparum Infected Erythrocytes
    • Acharya, P., Chaubey, S., Grover, M. & Tatu, U. An Exported Heat Shock Protein 40 Associates with Pathogenesis-Related Knobs in Plasmodium falciparum Infected Erythrocytes. PLoS One 7, e44605 (2012).
    • (2012) PLoS One , vol.7 , pp. e44605
    • Acharya, P.1    Chaubey, S.2    Grover, M.3    Tatu, U.4
  • 41
    • 0028240897 scopus 로고
    • A new generation of information retrieval tools for biologists: The example of the ExPASy WWW server
    • Appel, R. D., Bairoch, A. & Hochstrasser, D. F. A new generation of information retrieval tools for biologists: the example of the ExPASy WWW server. Trends Biochem Sci 19, 258-260 (1994).
    • (1994) Trends Biochem Sci , vol.19 , pp. 258-260
    • Appel, R.D.1    Bairoch, A.2    Hochstrasser, D.F.3
  • 42
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. & Doolittle, R. F. A simple method for displaying the hydropathic character of a protein. J Mol Biol 157, 105-132 (1982).
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 43
    • 0024289285 scopus 로고
    • Investigation of the bicinchoninic acid protein assay: Identification of the groups responsible for color formation
    • Wiechelman, K. J., Braun, R. D. & Fitzpatrick, J. D. Investigation of the bicinchoninic acid protein assay: identification of the groups responsible for color formation. Anal Biochem 175, 231-237 (1988).
    • (1988) Anal Biochem , vol.175 , pp. 231-237
    • Wiechelman, K.J.1    Braun, R.D.2    Fitzpatrick, J.D.3
  • 44
    • 33644647902 scopus 로고    scopus 로고
    • Measuring protein concentrations by NMR spectroscopy
    • Wider, G. & Dreier, L. Measuring protein concentrations by NMR spectroscopy. J Am Chem Soc 128, 2571-2576 (2006).
    • (2006) J Am Chem Soc , vol.128 , pp. 2571-2576
    • Wider, G.1    Dreier, L.2
  • 45
    • 33746217517 scopus 로고    scopus 로고
    • Concentration measurements by PULCONusing X-filtered or 2D NMR spectra
    • Dreier, L. & Wider, G. Concentration measurements by PULCONusing X-filtered or 2D NMR spectra. Magn Reson Chem 44 Spec No, S206-212 (2006).
    • (2006) Magn Reson Chem , vol.44 , Issue.SPEC NO , pp. S206-S212
    • Dreier, L.1    Wider, G.2
  • 47
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann, T., Guntert, P. & Wuthrich, K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol 319, 209-227 (2002).
    • (2002) J Mol Biol , vol.319 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 48
    • 0036873589 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS
    • Herrmann, T., Guntert, P. & Wuthrich, K. Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS. J Biomol NMR 24, 171-189 (2002).
    • (2002) J Biomol NMR , vol.24 , pp. 171-189
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 49
    • 68349093958 scopus 로고    scopus 로고
    • TALOS1: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Shen, Y., Delaglio, F., Cornilescu, G. & Bax, A. TALOS1: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44, 213-223 (2009).
    • (2009) J Biomol NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 50
    • 84862776630 scopus 로고    scopus 로고
    • Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106
    • Su, D. et al. Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106. Nature 483, 104-107 (2012).
    • (2012) Nature , vol.483 , pp. 104-107
    • Su, D.1
  • 51
    • 33845937672 scopus 로고    scopus 로고
    • Studying multisite binary and ternary protein interactions by global analysis of isothermal titration calorimetry data in SEDPHAT: Application to adaptor protein complexes in cell signaling
    • Houtman, J. C. et al. Studying multisite binary and ternary protein interactions by global analysis of isothermal titration calorimetry data in SEDPHAT: application to adaptor protein complexes in cell signaling. Protein Sci 16, 30-42 (2007).
    • (2007) Protein Sci , vol.16 , pp. 30-42
    • Houtman, J.C.1
  • 52
    • 84862799382 scopus 로고    scopus 로고
    • Strategies for assessing proton linkage to bimolecular interactions by global analysis of isothermal titration calorimetry data
    • Coussens, N. P., Schuck, P. & Zhao, H. Strategies for assessing proton linkage to bimolecular interactions by global analysis of isothermal titration calorimetry data. J Chem Thermodyn 52, 95-107 (2012).
    • (2012) J Chem Thermodyn , vol.52 , pp. 95-107
    • Coussens, N.P.1    Schuck, P.2    Zhao, H.3
  • 53
    • 84859739785 scopus 로고    scopus 로고
    • Uneven spread of cis- and trans-editing aminoacyl-tRNA synthetase domains within translational compartments of P. Falciparum
    • Khan, S. et al. Uneven spread of cis- and trans-editing aminoacyl-tRNA synthetase domains within translational compartments of P. falciparum. Sci Rep 1, 188 (2011).
    • (2011) Sci Rep , vol.1 , pp. 188
    • Khan, S.1


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