메뉴 건너뛰기




Volumn 7, Issue 10, 2008, Pages 4465-4474

Human regulatory protein Ki-1/57 has characteristics of an intrinsically unstructured protein

Author keywords

Circular dichroism; Hydrodynamic characterization; Intrinsically unstructured protein (iup); Limited proteolysis; Protein protein interaction; SAXS

Indexed keywords

CD30 ANTIGEN; RECOMBINANT ANTIGEN; RNA; HABP4 PROTEIN, HUMAN; MYOGENIC FACTOR; PROTEINASE K;

EID: 55949137920     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr8005342     Document Type: Article
Times cited : (19)

References (64)
  • 1
    • 0019981972 scopus 로고
    • Production of a monoclonal antibody specific for Hodgin and Sternberg-Reed cells of Hodgkin's disease and a subset of normal lymphoid cells
    • Schwab, U.; Stein, H.; Gerdes, J.; Lemke, H.; Kirchner, H.; Schaadt, M.; Diehl, V. Production of a monoclonal antibody specific for Hodgin and Sternberg-Reed cells of Hodgkin's disease and a subset of normal lymphoid cells. Nature 1982, 299, 65-67.
    • (1982) Nature , vol.299 , pp. 65-67
    • Schwab, U.1    Stein, H.2    Gerdes, J.3    Lemke, H.4    Kirchner, H.5    Schaadt, M.6    Diehl, V.7
  • 2
    • 0024373338 scopus 로고
    • The Hodgkin-associated Ki-1 antigen exists in an intracellular and a membrane-bound form
    • Hansen, H.; Lemke, H.; Bredfeldt, G.; Könnecke, I.; Havsteen, B. The Hodgkin-associated Ki-1 antigen exists in an intracellular and a membrane-bound form. Biol. Chem. Hoppe-Seyler 1989, 370, 409-416.
    • (1989) Biol. Chem. Hoppe-Seyler , vol.370 , pp. 409-416
    • Hansen, H.1    Lemke, H.2    Bredfeldt, G.3    Könnecke, I.4    Havsteen, B.5
  • 3
    • 0025318253 scopus 로고
    • Protein kinase activity of the intracellular but not the membrane-associated form of the Ki-1 antigen (CD30)
    • Hansen, H.; Bredfeldt, G.; Havsteen, B.; Lemke, H. Protein kinase activity of the intracellular but not the membrane-associated form of the Ki-1 antigen (CD30). Res. Immunol. 1990, 141, 13-31.
    • (1990) Res. Immunol , vol.141 , pp. 13-31
    • Hansen, H.1    Bredfeldt, G.2    Havsteen, B.3    Lemke, H.4
  • 5
    • 0026563520 scopus 로고
    • Cellular localization and processing of the two molecular forms of the Hodgkin-associated Ki-1 (CD30) antigen
    • Rohde, D.; Hansen, H.; Hafner, M.; Lange, H.; Mielke, V.; Hansmann, M. L.; Lemke, H. Cellular localization and processing of the two molecular forms of the Hodgkin-associated Ki-1 (CD30) antigen. Am. J. Pathol. 1992, 140, 473-482.
    • (1992) Am. J. Pathol , vol.140 , pp. 473-482
    • Rohde, D.1    Hansen, H.2    Hafner, M.3    Lange, H.4    Mielke, V.5    Hansmann, M.L.6    Lemke, H.7
  • 6
    • 0034703020 scopus 로고    scopus 로고
    • Molecular characterization of a novel intracellular hyaluro-an-binding protein
    • Huang, L.; Grammatikakis, N.; Yoneda, M.; Banerjee, S. D.; Toole, B. P. Molecular characterization of a novel intracellular hyaluro-an-binding protein. J. Biol. Chem. 2000, 275, 29829-29839.
    • (2000) J. Biol. Chem , vol.275 , pp. 29829-29839
    • Huang, L.1    Grammatikakis, N.2    Yoneda, M.3    Banerjee, S.D.4    Toole, B.P.5
  • 7
    • 0037413848 scopus 로고    scopus 로고
    • Characterization of a new family of proteins that interact with the C-terminal region of the chromatin-remodeling factor CHD-3
    • Lemos, T. A.; Passos, D. O.; Nery, F. C.; Kobarg, J. Characterization of a new family of proteins that interact with the C-terminal region of the chromatin-remodeling factor CHD-3. FEBS Lett. 2003, 533, 14-20.
    • (2003) FEBS Lett , vol.533 , pp. 14-20
    • Lemos, T.A.1    Passos, D.O.2    Nery, F.C.3    Kobarg, J.4
  • 8
    • 31744447890 scopus 로고    scopus 로고
    • CGI-55 interacts with nuclear proteins and co-localizes to p80-coilin positive-coiled bodies in the nucleus
    • Lemos, T. A.; Kobarg, J. CGI-55 interacts with nuclear proteins and co-localizes to p80-coilin positive-coiled bodies in the nucleus. Cell Biochem. Biophys. 2006, 44, 463-74.
    • (2006) Cell Biochem. Biophys , vol.44 , pp. 463-474
    • Lemos, T.A.1    Kobarg, J.2
  • 9
    • 31744431606 scopus 로고    scopus 로고
    • Evidence for the interaction of the regulatory protein Ki-1/57 with p53 and its interacting proteins
    • Nery, F. C; Rui, E.; Kuniyoshi, T. M.; Kobarg, J. Evidence for the interaction of the regulatory protein Ki-1/57 with p53 and its interacting proteins. Biochem. Biophys. Res. Commun. 2006, 341, 847-855.
    • (2006) Biochem. Biophys. Res. Commun , vol.341 , pp. 847-855
    • Nery, F.C.1    Rui, E.2    Kuniyoshi, T.M.3    Kobarg, J.4
  • 10
    • 33747431911 scopus 로고    scopus 로고
    • Passos, D. O.; Bressan, G. G; Nery, F. C; Kobarg, J. Ki-1/57 interacts with PRMT1 and is a substrate for arginine methylation. FEBS J. 2006, 273, 3946-61.
    • Passos, D. O.; Bressan, G. G; Nery, F. C; Kobarg, J. Ki-1/57 interacts with PRMT1 and is a substrate for arginine methylation. FEBS J. 2006, 273, 3946-61.
  • 11
    • 1642565088 scopus 로고    scopus 로고
    • Nery, F. C; Passos, D. O.; Garcia, V. S.; Kobarg, J. Ki-1/57 interacts with RACK1 and is a substrate for the phosphorylation by phorbol 12-myristate 13-acetate activated protein kinase C. J. Biol. Chem. 2004, 279, 11444-11455.
    • Nery, F. C; Passos, D. O.; Garcia, V. S.; Kobarg, J. Ki-1/57 interacts with RACK1 and is a substrate for the phosphorylation by phorbol 12-myristate 13-acetate activated protein kinase C. J. Biol. Chem. 2004, 279, 11444-11455.
  • 12
    • 33746034124 scopus 로고    scopus 로고
    • Nery, F. C; Bressan, G. C; Alborghetti, M. R.; Passos, D. O.; Kuniyoshi, T. M.; Ramos, C. H. I.; Oyama, S.; Kobarg, J. A spectroscopic analysis of the interaction between the human regulatory proteins RACK1 and Ki-1/57. Biol. Chem. 2006, 387, 577- 582.
    • Nery, F. C; Bressan, G. C; Alborghetti, M. R.; Passos, D. O.; Kuniyoshi, T. M.; Ramos, C. H. I.; Oyama, S.; Kobarg, J. A spectroscopic analysis of the interaction between the human regulatory proteins RACK1 and Ki-1/57. Biol. Chem. 2006, 387, 577- 582.
  • 14
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson, H. J.; Wright, P. E. Intrinsically unstructured proteins and their functions. Nat. Rev., Mol. Cell. Biol. 2005, 6, 197-208.
    • (2005) Nat. Rev., Mol. Cell. Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 15
    • 37749053887 scopus 로고    scopus 로고
    • Fuzzy complexes: Polymorphism and structural disorder in protein-protein interactions
    • Tompa, P.; Fuxreiter, M. Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions. Trends Biochem. Sci. 2008, 33, 2-8.
    • (2008) Trends Biochem. Sci , vol.33 , pp. 2-8
    • Tompa, P.1    Fuxreiter, M.2
  • 17
    • 0002086583 scopus 로고
    • Nucleotide binding proteins
    • Balaban, M, Ed, Elsevier/North-Holland: New York
    • Schulz, G. E. Nucleotide binding proteins. In Molecular Mechanism of Biological Recognition; Balaban, M., Ed.; Elsevier/North-Holland: New York, 1979; pp 79-94.
    • (1979) Molecular Mechanism of Biological Recognition , pp. 79-94
    • Schulz, G.E.1
  • 20
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • Tompa, P. The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett. 2005, 579, 3346- 54.
    • (2005) FEBS Lett , vol.579 , pp. 3346-3354
    • Tompa, P.1
  • 21
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa, P. Intrinsically unstructured proteins. Trends Biochem. Sci. 2002, 27, 527-33.
    • (2002) Trends Biochem. Sci , vol.27 , pp. 527-533
    • Tompa, P.1
  • 22
    • 0034669882 scopus 로고    scopus 로고
    • Uversky, V. N.; Gillespie, J. R.; Fink, A. L. Why are natively unfolded proteins unstructured under physiologic conditions. Proteins 2000, 41, 415-27.
    • Uversky, V. N.; Gillespie, J. R.; Fink, A. L. Why are "natively unfolded" proteins unstructured under physiologic conditions. Proteins 2000, 41, 415-27.
  • 23
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded
    • Uversky, V. N. What does it mean to be natively unfolded. Eur. J. Biochem. 2002, 269, 2-12.
    • (2002) Eur. J. Biochem , vol.269 , pp. 2-12
    • Uversky, V.N.1
  • 24
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson, H. J.; Wright, P. E. Coupling of folding and binding for unstructured proteins. Curr. Opin. Struct. Biol. 2002, 12, 54-60.
    • (2002) Curr. Opin. Struct. Biol , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 27
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward, J. J.; Sodhi, J. S.; McGuffin, L. J.; Buxton, B. F.; Jones, D. T. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J. Mol. Biol. 2004, 337, 635-645.
    • (2004) J. Mol. Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 28
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin, L. J.; Bryson, K.; Jones, D. T. The PSIPRED protein structure prediction server. Bioinformatics 2000, 16, 404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 29
    • 0037705413 scopus 로고    scopus 로고
    • The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphopro- tein
    • Longhi, S.; Receveur-Bréchot, V.; Karlin, D.; Johansson, K.; Darbon, H.; Bhella, D.; Yeo, R.; Finet, S.; Canard, B. The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphopro- tein. J. Biol. Chem. 2003, 278, 18638-48.
    • (2003) J. Biol. Chem , vol.278 , pp. 18638-18648
    • Longhi, S.1    Receveur-Bréchot, V.2    Karlin, D.3    Johansson, K.4    Darbon, H.5    Bhella, D.6    Yeo, R.7    Finet, S.8    Canard, B.9
  • 30
    • 10044296373 scopus 로고    scopus 로고
    • SAXS study of the PIR domain from the Grbl4 molecular adaptor: A natively unfolded protein with a transient structure primer
    • Moncoq, K.; Broutin, I.; Craescu, C. T.; Vachette, P.; Ducruix, A.; Durand, D. SAXS study of the PIR domain from the Grbl4 molecular adaptor: a natively unfolded protein with a transient structure primer. Biophys. J. 2004, 87, 4056-64.
    • (2004) Biophys. J , vol.87 , pp. 4056-4064
    • Moncoq, K.1    Broutin, I.2    Craescu, C.T.3    Vachette, P.4    Ducruix, A.5    Durand, D.6
  • 31
    • 34247891557 scopus 로고    scopus 로고
    • Structural characterization of flexible proteins using small-angle X-ray scattering
    • Bernadó, P.; Mylonas, E.; Petoukhov, M. V.; Blackledge, M.; Svergun, D. I. Structural characterization of flexible proteins using small-angle X-ray scattering. J. Am. Chem. Soc. 2007, 129, 5656- 64.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 5656-5664
    • Bernadó, P.1    Mylonas, E.2    Petoukhov, M.V.3    Blackledge, M.4    Svergun, D.I.5
  • 33
    • 0002556772 scopus 로고
    • Glatter, O, Kratky, O, Eds, Academic Press: New York
    • Kirste, R. G.; Oberthür, R. C. In Small Angle X-Ray Scattering; Glatter, O., Kratky, O., Eds.; Academic Press: New York, 1982; pp 387-431.
    • (1982) Small Angle X-Ray Scattering , pp. 387-431
    • Kirste, R.G.1    Oberthür, R.C.2
  • 36
    • 0033001996 scopus 로고    scopus 로고
    • Svergun, D. I. solution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 1999, 76, 2879-2886.
    • Svergun, D. I. solution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 1999, 76, 2879-2886.
  • 37
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun, D. I.; Petoukhov, M. V.; Koch, M. H. Determination of domain structure of proteins from X-ray solution scattering. Biophys. J. 2001, 80, 2946-2953.
    • (2001) Biophys. J , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3
  • 38
    • 0242571958 scopus 로고    scopus 로고
    • Small-angle scattering studies of biological macromolecules in solution
    • Svergun, D. I.; Koch, M. H. J. Small-angle scattering studies of biological macromolecules in solution. Rep. Prog. Phys. 2003, 66, 1735-1782.
    • (2003) Rep. Prog. Phys , vol.66 , pp. 1735-1782
    • Svergun, D.I.1    Koch, M.H.J.2
  • 39
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov, V. V.; Svergun, D. I. Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Crystallogr. 2003, 36, 860-864.
    • (2003) J. Appl. Crystallogr , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 42
    • 0035443198 scopus 로고    scopus 로고
    • Biophysical studies by ultracentrifugation
    • Laue, T. Biophysical studies by ultracentrifugation. Curr. Opin. Struct. Biol. 2001, 11, 579-583.
    • (2001) Curr. Opin. Struct. Biol , vol.11 , pp. 579-583
    • Laue, T.1
  • 43
    • 0036707991 scopus 로고    scopus 로고
    • Modern analytical ultracentrifugation in protein science: A tutorial review
    • Lebowitz, J.; Lewis, M. S.; Schuck, P. Modern analytical ultracentrifugation in protein science: A tutorial review. Protein Sci. 2002, 11, 2067-2079.
    • (2002) Protein Sci , vol.11 , pp. 2067-2079
    • Lebowitz, J.1    Lewis, M.S.2    Schuck, P.3
  • 44
    • 0037031842 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein
    • Denning, D. P.; Uversky, V.; Patel, S. S.; Fink, A. L.; Rexach, M. The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein. J. Biol. Chem. 2002, 277, 33447-55.
    • (2002) J. Biol. Chem , vol.277 , pp. 33447-33455
    • Denning, D.P.1    Uversky, V.2    Patel, S.S.3    Fink, A.L.4    Rexach, M.5
  • 45
    • 0035793586 scopus 로고    scopus 로고
    • Identification and cDNA cloning of a novel RNAbinding protein that interacts with the cyclic nucleotideresponsive sequence in the type-1 plasminogen activator inhibitor mRNA
    • Heaton, J. H.; Dlakic, W. M.; Dlakic, M.; Gelehrter, T. D. Identification and cDNA cloning of a novel RNAbinding protein that interacts with the cyclic nucleotideresponsive sequence in the type-1 plasminogen activator inhibitor mRNA. J. Biol. Chem. 2001, 276, 3341-3347.
    • (2001) J. Biol. Chem , vol.276 , pp. 3341-3347
    • Heaton, J.H.1    Dlakic, W.M.2    Dlakic, M.3    Gelehrter, T.D.4
  • 46
    • 0030816685 scopus 로고    scopus 로고
    • Mechanism of helix induction by trifluoroethanol: A framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water
    • Luo, P.; Baldwin, R. L. Mechanism of helix induction by trifluoroethanol: a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water. Biochemistry 1997, 36, 8413-21.
    • (1997) Biochemistry , vol.36 , pp. 8413-8421
    • Luo, P.1    Baldwin, R.L.2
  • 47
    • 24944546549 scopus 로고    scopus 로고
    • Coupled folding and binding with α helix-forming molecular recognition elements
    • Oldfield, C. J.; Cheng, Y.; Cortese, M. S.; Romero, P.; Uversky, V. N.; Dunker, A. K. Coupled folding and binding with α helix-forming molecular recognition elements. Biochemistry 2005, 44, 12454-70.
    • (2005) Biochemistry , vol.44 , pp. 12454-12470
    • Oldfield, C.J.1    Cheng, Y.2    Cortese, M.S.3    Romero, P.4    Uversky, V.N.5    Dunker, A.K.6
  • 48
    • 0035799707 scopus 로고    scopus 로고
    • Lethality and centrality in protein networks
    • Jeong, H.; Mason, S. P.; Barabasi, A. L.; Oltvai, Z. N. Lethality and centrality in protein networks. Nature 2001, 411, 41-42.
    • (2001) Nature , vol.411 , pp. 41-42
    • Jeong, H.1    Mason, S.P.2    Barabasi, A.L.3    Oltvai, Z.N.4
  • 50
    • 33645214608 scopus 로고    scopus 로고
    • Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks
    • Patil, A.; Nakamura, H. Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks. FEBS Lett. 2006, 580, 2041-2045.
    • (2006) FEBS Lett , vol.580 , pp. 2041-2045
    • Patil, A.1    Nakamura, H.2
  • 51
    • 10844264054 scopus 로고    scopus 로고
    • Two new sealed sample cells for small angle X-ray scattering from macromolecules in solution and complex fluids using synchrotron radiation
    • Cavalcanti, L. P.; Torriani, I. L.; Plivelic, T. S.; Oliveira, C. L. P.; Kellermann, G.; Neuenschwander, R. Two new sealed sample cells for small angle X-ray scattering from macromolecules in solution and complex fluids using synchrotron radiation. R. Rev. Sci. Inst. 2004, 75, 4541-4546.
    • (2004) R. Rev. Sci. Inst , vol.75 , pp. 4541-4546
    • Cavalcanti, L.P.1    Torriani, I.L.2    Plivelic, T.S.3    Oliveira, C.L.P.4    Kellermann, G.5    Neuenschwander, R.6
  • 53
    • 34248397195 scopus 로고    scopus 로고
    • Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering
    • Mylonas, E.; Svergun, D. I. Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering. J. Appl. Cryst. 2001, 40, 245-249.
    • (2001) J. Appl. Cryst , vol.40 , pp. 245-249
    • Mylonas, E.1    Svergun, D.I.2
  • 54
    • 0003519476 scopus 로고
    • Translated by Walker, C. B, Yudowitch, K. L, John Wiley & Sons: New York
    • Guinier, A.; Fournet, G. In Small angle scattering of X-rays; Translated by Walker, C. B.; Yudowitch, K. L.; John Wiley & Sons: New York, 1955; pp 5-78.
    • (1955) Small angle scattering of X-rays , pp. 5-78
    • Guinier, A.1    Fournet, G.2
  • 56
    • 33644606089 scopus 로고
    • Molecular-weight determination by light scattering
    • Debye, P. J. Molecular-weight determination by light scattering. Phys. Colloid. Chem. 1947, 51, 18-32.
    • (1947) Phys. Colloid. Chem , vol.51 , pp. 18-32
    • Debye, P.J.1
  • 58
    • 0034966446 scopus 로고    scopus 로고
    • Heat-induced unfolding of neocarzinostatin, a small all-beta protein investigated by small-angle X-ray scattering
    • Perez, J.; Vachette, P.; Russo, D.; Desmadril, M.; Durand, D. Heat-induced unfolding of neocarzinostatin, a small all-beta protein investigated by small-angle X-ray scattering. J. Mol. Biol. 2001, 308, 721-743.
    • (2001) J. Mol. Biol , vol.308 , pp. 721-743
    • Perez, J.1    Vachette, P.2    Russo, D.3    Desmadril, M.4    Durand, D.5
  • 59
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun, D. I. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Cryst. 1992, 25, 495-503.
    • (1992) J. Appl. Cryst , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 61
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • Schuck, P. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys. J. 2000, 78, 1606-19.
    • (2000) Biophys. J , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 62
    • 0036154258 scopus 로고    scopus 로고
    • Size-Distribution Analysis of Proteins by Analytical Ultracentrifugation: Strategies and Application to Model Systems
    • Schuck, P.; Perugini, M. A.; Gonzales, N. R.; Howlett, G. J.; Schubert, D. Size-Distribution Analysis of Proteins by Analytical Ultracentrifugation: Strategies and Application to Model Systems. Biophys. J. 2002, 82, 1096-1111.
    • (2002) Biophys. J , vol.82 , pp. 1096-1111
    • Schuck, P.1    Perugini, M.A.2    Gonzales, N.R.3    Howlett, G.J.4    Schubert, D.5
  • 63
    • 0037224504 scopus 로고    scopus 로고
    • Identification and characterization of proteins that selectively interact with isoforms of the mRNA binding protein AUF1 (hnRNP D)
    • Moraes, K. C; Quaresma, A. J.; Maehnss, K.; Kobarg, J. Identification and characterization of proteins that selectively interact with isoforms of the mRNA binding protein AUF1 (hnRNP D). Biol. Chem. 2003, 384, 25-37.
    • (2003) Biol. Chem , vol.384 , pp. 25-37
    • Moraes, K.C.1    Quaresma, A.J.2    Maehnss, K.3    Kobarg, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.