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Volumn 210, Issue 2, 2011, Pages 159-170

Solution NMR spectroscopy of supra-molecular systems, why bother? A methyl-TROSY view

Author keywords

HMQC; Methyl labeling; Methyl TROSY; Proteasome; Protein dynamics; Supra molecular systems

Indexed keywords

HMQC; METHYL LABELING; METHYL-TROSY; PROTEASOMES; PROTEIN DYNAMICS; SUPRA-MOLECULAR SYSTEMS;

EID: 79955910554     PISSN: 10907807     EISSN: 10960856     Source Type: Journal    
DOI: 10.1016/j.jmr.2011.03.008     Document Type: Article
Times cited : (66)

References (62)
  • 3
    • 0021755973 scopus 로고
    • X-ray structure analysis of a membrane protein complex. Electron density map at 3 A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis
    • J. Deisenhofer, O. Epp, K. Miki, R. Huber, and H. Michel X-ray structure analysis of a membrane protein complex. Electron density map at 3 A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis J. Mol. Biol. 180 1984 385 398
    • (1984) J. Mol. Biol. , vol.180 , pp. 385-398
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 5
    • 0028114231 scopus 로고
    • Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria
    • J.P. Abrahams, A.G. Leslie, R. Lutter, and J.E. Walker Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria Nature 370 1994 621 628
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 7
    • 0035827346 scopus 로고    scopus 로고
    • Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution
    • DOI 10.1126/science.1059493
    • P. Cramer, D.A. Bushnell, and R.D. Kornberg Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution Science 292 2001 1863 1876 (Pubitemid 32538356)
    • (2001) Science , vol.292 , Issue.5523 , pp. 1863-1876
    • Cramer, P.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 9
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 A resolution
    • DOI 10.1126/science.289.5481.905
    • N. Ban, P. Nissen, J. Hansen, P.B. Moore, and T.A. Steitz The complete atomic structure of the large ribosomal subunit at 2.4 A resolution Science 289 2000 905 920 (Pubitemid 30659939)
    • (2000) Science , vol.289 , Issue.5481 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 12
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 resolution
    • J. Lowe, D. Stock, B. Jap, P. Zwickl, W. Baumeister, and R. Huber Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 resolution Science 268 1995 533 539
    • (1995) Science , vol.268 , pp. 533-539
    • Lowe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 13
    • 70350336247 scopus 로고    scopus 로고
    • The yeast exosome functions as a macromolecular cage to channel RNA substrates for degradation
    • F. Bonneau, J. Basquin, J. Ebert, E. Lorentzen, and E. Conti The yeast exosome functions as a macromolecular cage to channel RNA substrates for degradation Cell 139 2009 547 559
    • (2009) Cell , vol.139 , pp. 547-559
    • Bonneau, F.1    Basquin, J.2    Ebert, J.3    Lorentzen, E.4    Conti, E.5
  • 15
    • 0037038365 scopus 로고    scopus 로고
    • Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy
    • DOI 10.1038/nature01070
    • F. Castellani, B. van Rossum, A. Diehl, M. Schubert, K. Rehbein, and H. Oschkinat Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy Nature 420 2002 98 102 (Pubitemid 35291447)
    • (2002) Nature , vol.420 , Issue.6911 , pp. 98-102
    • Castellani, F.1    Van Rossum, B.2    Diehl, A.3    Schubert, M.4    Rehbein, K.5    Oschklnat, H.6
  • 16
    • 40849120669 scopus 로고    scopus 로고
    • Amyloid fibrils of the HET-s(218-289) prion form a β solenoid with a triangular hydrophobic core
    • DOI 10.1126/science.1151839
    • C. Wasmer, A. Lange, H. Van Melckebeke, A.B. Siemer, R. Riek, and B.H. Meier Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core Science 319 2008 1523 1526 (Pubitemid 351398180)
    • (2008) Science , vol.319 , Issue.5869 , pp. 1523-1526
    • Wasmer, C.1    Lange, A.2    Van Melckebeke, H.3    Siemer, A.B.4    Riek, R.5    Meier, B.H.6
  • 17
    • 0028019827 scopus 로고
    • Multidimensional nuclear magnetic resonance methods for protein studies
    • DOI 10.1016/S0959-440X(94)90173-2
    • A. Bax Multidimensional nuclear magnetic resonance methods for protein studies Curr. Opin. Struct. Biol. 4 1994 738 744 (Pubitemid 24325294)
    • (1994) Current Opinion in Structural Biology , vol.4 , Issue.5 , pp. 738-744
    • Bax, A.1
  • 18
    • 0025871254 scopus 로고
    • Structures of larger proteins in solution: Three- and four-dimensional heteronuclear NMR spectroscopy
    • G.M. Clore, and A.M. Gronenborn Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy Science 252 1991 1390 1399 (Pubitemid 21917051)
    • (1991) Science , vol.252 , Issue.5011 , pp. 1390-1399
    • Clore, G.M.1    Gronenborn, A.M.2
  • 19
  • 20
    • 62049086246 scopus 로고    scopus 로고
    • Application of methyl-TROSY NMR to test allosteric models describing effects of nucleotide binding to aspartate transcarbamoylase
    • A. Velyvis, H.K. Schachman, and L.E. Kay Application of methyl-TROSY NMR to test allosteric models describing effects of nucleotide binding to aspartate transcarbamoylase J. Mol. Biol. 387 2009 540 547
    • (2009) J. Mol. Biol. , vol.387 , pp. 540-547
    • Velyvis, A.1    Schachman, H.K.2    Kay, L.E.3
  • 21
    • 46049107832 scopus 로고    scopus 로고
    • TROSY-based NMR evidence for a novel class of 20S proteasome inhibitors
    • DOI 10.1021/bi8005913
    • R. Sprangers, X. Li, X. Mao, J.L. Rubinstein, A.D. Schimmer, and L.E. Kay TROSY-based NMR evidence for a novel class of 20S proteasome inhibitors Biochemistry 47 2008 6727 6734 (Pubitemid 351898927)
    • (2008) Biochemistry , vol.47 , Issue.26 , pp. 6727-6734
    • Sprangers, R.1    Li, X.2    Mao, X.3    Rubinstein, J.L.4    Schimmer, A.D.5    Kay, L.E.6
  • 23
    • 36049046667 scopus 로고    scopus 로고
    • Structural Basis for Signal-Sequence Recognition by the Translocase Motor SecA as Determined by NMR
    • DOI 10.1016/j.cell.2007.09.039, PII S009286740701269X
    • I. Gelis, A.M. Bonvin, D. Keramisanou, M. Koukaki, G. Gouridis, S. Karamanou, A. Economou, and C.G. Kalodimos Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR Cell 131 2007 756 769 (Pubitemid 350087200)
    • (2007) Cell , vol.131 , Issue.4 , pp. 756-769
    • Gelis, I.1    Bonvin, A.M.J.J.2    Keramisanou, D.3    Koukaki, M.4    Gouridis, G.5    Karamanou, S.6    Economou, A.7    Kalodimos, C.G.8
  • 24
    • 0032898682 scopus 로고    scopus 로고
    • 2H-labeled proteins
    • DOI 10.1023/A:1008393201236
    • N.K. Goto, K.H. Gardner, G.A. Mueller, R.C. Willis, and L.E. Kay A robust and cost-effective method for the production of Val, Leu, Ile (δ1) methyl-protonated 15N-, 13C-, 2H-labeled proteins J. Biomol. NMR 13 1999 369 374 (Pubitemid 29210329)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.4 , pp. 369-374
    • Goto, N.K.1    Gardner, K.H.2    Mueller, G.A.3    Willis, R.C.4    Kay, L.E.5
  • 25
    • 1242308875 scopus 로고    scopus 로고
    • An isotope labeling strategy for methyl TROSY spectroscopy
    • DOI 10.1023/B:JNMR.0000013824.93994.1f
    • V. Tugarinov, and L.E. Kay An isotope labeling strategy for methyl TROSY spectroscopy J. Biomol. NMR 28 2004 165 172 (Pubitemid 38232795)
    • (2004) Journal of Biomolecular NMR , vol.28 , Issue.2 , pp. 165-172
    • Tugarinov, V.1    Kay, L.E.2
  • 26
    • 58149463865 scopus 로고    scopus 로고
    • An efficient protocol for the complete incorporation of methyl-protonated alanine in perdeuterated protein
    • I. Ayala, R. Sounier, N. Use, P. Gans, and J. Boisbouvier An efficient protocol for the complete incorporation of methyl-protonated alanine in perdeuterated protein J. Biomol. NMR 43 2009 111 119
    • (2009) J. Biomol. NMR , vol.43 , pp. 111-119
    • Ayala, I.1    Sounier, R.2    Use, N.3    Gans, P.4    Boisbouvier, J.5
  • 27
    • 37849041010 scopus 로고    scopus 로고
    • A new labeling method for methyl transverse relaxation-optimized spectroscopy NMR spectra of alanine residues
    • R.L. Isaacson, P.J. Simpson, M. Liu, E. Cota, X. Zhang, P. Freemont, and S. Matthews A new labeling method for methyl transverse relaxation-optimized spectroscopy NMR spectra of alanine residues J. Am. Chem. Soc. 129 2007 15428 15429
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 15428-15429
    • Isaacson, R.L.1    Simpson, P.J.2    Liu, M.3    Cota, E.4    Zhang, X.5    Freemont, P.6    Matthews, S.7
  • 28
    • 34249023900 scopus 로고    scopus 로고
    • 13C-methyl-group-labeled methionine precursor as a useful tool for simplifying protein structural analysis by NMR spectroscopy
    • DOI 10.1002/cbic.200600551
    • M. Fischer, K. Kloiber, J. Hausler, K. Ledolter, R. Konrat, and W. Schmid Synthesis of a 13C-methyl-group-labeled methionine precursor as a useful tool for simplifying protein structural analysis by NMR spectroscopy ChemBioChem 8 2007 610 612 (Pubitemid 47194850)
    • (2007) ChemBioChem , vol.8 , Issue.6 , pp. 610-612
    • Fischer, M.1    Kloiber, K.2    Hausler, J.3    Ledolter, K.4    Konrat, R.5    Schmid, W.6
  • 29
    • 78149412689 scopus 로고    scopus 로고
    • A simple strategy for (1)(3)C, (1)H labeling at the Ile-gamma2 methyl position in highly deuterated proteins
    • A.M. Ruschak, A. Velyvis, L.E. Kay, A simple strategy for (1)(3)C, (1)H labeling at the Ile-gamma2 methyl position in highly deuterated proteins, J. Biomol. NMR 48 129-135.
    • J. Biomol. NMR , vol.48 , pp. 129-135
    • Ruschak, A.M.1    Velyvis, A.2    Kay, L.E.3
  • 31
    • 0041930989 scopus 로고    scopus 로고
    • 13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes
    • DOI 10.1021/ja030153x
    • V. Tugarinov, P. Hwang, J. Ollerenshaw, and L.E. Kay Cross-correlated relaxation enhanced 1H-13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes J. Am. Chem. Soc. 125 2003 10420 10428 (Pubitemid 37022252)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.34 , pp. 10420-10428
    • Tugarinov, V.1    Hwang, P.M.2    Ollerenshaw, J.E.3    Kay, L.E.4
  • 32
    • 44949272393 scopus 로고
    • 2 and NOE measurements in macromolecules
    • 2 and NOE measurements in macromolecules J. Magn. Reson. 95 1991 536 547
    • (1991) J. Magn. Reson. , vol.95 , pp. 536-547
    • Kay, L.E.1    Torchia, D.A.2
  • 33
    • 33644757144 scopus 로고
    • Correlation of proton and nitrogen-15 chemical shifts by multiple quantum NMR
    • A. Bax, R.H. Griffey, and B.L. Hawkings Correlation of proton and nitrogen-15 chemical shifts by multiple quantum NMR J. Magn. Reson. 55 1983 301 315
    • (1983) J. Magn. Reson. , vol.55 , pp. 301-315
    • Bax, A.1    Griffey, R.H.2    Hawkings, B.L.3
  • 34
    • 0002616982 scopus 로고
    • Sensitivity enhanced detection of weak nuclei using heteronuclear multiple quantum coherence
    • L. Mueller Sensitivity enhanced detection of weak nuclei using heteronuclear multiple quantum coherence J. Am. Chem. Soc. 101 1979 4481 4484
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 4481-4484
    • Mueller, L.1
  • 35
    • 0030612833 scopus 로고    scopus 로고
    • 2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • 2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution Proc. Natl Acad. Sci. USA 94 1997 12366 12371
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wüthrich, K.4
  • 36
    • 22144435546 scopus 로고    scopus 로고
    • The contact interface of a 120 kD CheA-CheW complex by methyl TROSY interaction spectroscopy
    • DOI 10.1021/ja052517m
    • D.J. Hamel, and F.W. Dahlquist The contact interface of a 120 kD CheA-CheW complex by methyl TROSY interaction spectroscopy J. Am. Chem. Soc. 127 2005 9676 9677 (Pubitemid 40981519)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.27 , pp. 9676-9677
    • Hamel, D.J.1    Dahlquist, F.W.2
  • 38
    • 33846928691 scopus 로고    scopus 로고
    • Quantitative dynamics and binding studies of the 20S proteasome by NMR
    • DOI 10.1038/nature05512, PII NATURE05512
    • R. Sprangers, and L.E. Kay Quantitative dynamics and binding studies of the 20S proteasome by NMR Nature 445 2007 618 622 (Pubitemid 46232877)
    • (2007) Nature , vol.445 , Issue.7128 , pp. 618-622
    • Sprangers, R.1    Kay, L.E.2
  • 39
    • 77950497745 scopus 로고    scopus 로고
    • Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR
    • T.L. Religa, R. Sprangers, and L.E. Kay Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR Science 328 2010 98 102
    • (2010) Science , vol.328 , pp. 98-102
    • Religa, T.L.1    Sprangers, R.2    Kay, L.E.3
  • 40
    • 77957970501 scopus 로고    scopus 로고
    • The proteasome antechamber maintains substrates in an unfolded state
    • A.M. Ruschak, T.L. Religa, S. Breuer, S. Witt, and L.E. Kay The proteasome antechamber maintains substrates in an unfolded state Nature 467 2010 868 871
    • (2010) Nature , vol.467 , pp. 868-871
    • Ruschak, A.M.1    Religa, T.L.2    Breuer, S.3    Witt, S.4    Kay, L.E.5
  • 41
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • DOI 10.1038/nature02263
    • A.L. Goldberg Protein degradation and protection against misfolded or damaged proteins Nature 426 2003 895 899 (Pubitemid 38056882)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 895-899
    • Goldberg, A.L.1
  • 42
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • DOI 10.1016/S0092-8674(00)80929-0
    • W. Baumeister, J. Walz, F. Zuhl, and E. Seemuller The proteasome: paradigm of a self-compartmentalizing protease Cell 92 1998 367 380 (Pubitemid 28093014)
    • (1998) Cell , vol.92 , Issue.3 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zuhl, F.3    Seemuller, E.4
  • 43
    • 33847066706 scopus 로고    scopus 로고
    • Functions of the proteasome: From protein degradation and immune surveillance to cancer therapy
    • A.L. Goldberg Functions of the proteasome: from protein degradation and immune surveillance to cancer therapy Biochem. Soc. Trans. 35 2007 12 17
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 12-17
    • Goldberg, A.L.1
  • 44
    • 0032991161 scopus 로고    scopus 로고
    • Analysis of deuterium relaxation-derived methyl axis order parameters and correlation with local structure
    • DOI 10.1023/A:1008387715167
    • A. Mittermaier, L.E. Kay, and J.D. Forman-Kay Analysis of deuterium relaxation-derived methyl axis order parameters and correlation with local structure J. Biomol. NMR 13 1999 181 185 (Pubitemid 29089228)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.2 , pp. 181-185
    • Mittermaier, A.1    Kay, L.E.2    Forman-Kay, J.D.3
  • 46
    • 19444387760 scopus 로고    scopus 로고
    • The 1.9 A structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions
    • DOI 10.1016/j.molcel.2005.04.016, PII S1097276505012797
    • A. Forster, E.I. Masters, F.G. Whitby, H. Robinson, and C.P. Hill The 1.9 A structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions Mol. Cell 18 2005 589 599 (Pubitemid 40726235)
    • (2005) Molecular Cell , vol.18 , Issue.5 , pp. 589-599
    • Forster, A.1    Masters, E.I.2    Whitby, F.G.3    Robinson, H.4    Hill, C.P.5
  • 48
    • 0001149934 scopus 로고
    • Methyl group dynamics from relaxation of double quantum filtered NMR signals-application to deoxycholate
    • L.E. Kay, and J.H. Prestegard Methyl group dynamics from relaxation of double quantum filtered NMR signals-application to deoxycholate J. Am. Chem. Soc. 109 1987 3829 3835
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 3829-3835
    • Kay, L.E.1    Prestegard, J.H.2
  • 49
    • 0000631220 scopus 로고
    • Relaxation-induced violations of coherence transfer selection rules in nuclear magnetic resonance
    • N. Muller, G. Bodenhausen, and R.R. Ernst Relaxation-induced violations of coherence transfer selection rules in nuclear magnetic resonance J. Magn. Reson. 75 1987 297 334
    • (1987) J. Magn. Reson. , vol.75 , pp. 297-334
    • Muller, N.1    Bodenhausen, G.2    Ernst, R.R.3
  • 51
    • 33846998346 scopus 로고    scopus 로고
    • Probing side-chain dynamics in the proteasome by relaxation violated coherence transfer NMR spectroscopy
    • V. Tugarinov, R. Sprangers, and L.E. Kay Probing side-chain dynamics in the proteasome by relaxation violated coherence transfer NMR spectroscopy J. Am. Chem. Soc. 129 2007 1743 1750
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 1743-1750
    • Tugarinov, V.1    Sprangers, R.2    Kay, L.E.3
  • 52
    • 77955567725 scopus 로고    scopus 로고
    • (13)CHD(2) methyl group probes of millisecond time scale exchange in proteins by (1)H relaxation dispersion: An application to proteasome gating residue dynamics
    • A.J. Baldwin, T.L. Religa, D.F. Hansen, G. Bouvignies, and L.E. Kay (13)CHD(2) methyl group probes of millisecond time scale exchange in proteins by (1)H relaxation dispersion: an application to proteasome gating residue dynamics J. Am. Chem. Soc. 132 2010 10992 10995
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 10992-10995
    • Baldwin, A.J.1    Religa, T.L.2    Hansen, D.F.3    Bouvignies, G.4    Kay, L.E.5
  • 53
    • 0034919305 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for quantifying microsecond-to- millisecond motions in biological macromolecules
    • DOI 10.1016/S0076-6879(01)39315-1
    • A.G. Palmer, C.D. Kroenke, and J.P. Loria NMR methods for quantifying microsecond-to-millisecond motions in biological macromolecules Methods Enzymol. 339 2001 204 238 (Pubitemid 32666562)
    • (2001) Methods in Enzymology , vol.339 , pp. 204-238
    • Palmer III, A.G.1    Kroenke, C.D.2    Loria, J.P.3
  • 54
    • 24644445756 scopus 로고    scopus 로고
    • 1H CPMG-based relaxation dispersion experiments: Complications and a simple solution
    • DOI 10.1007/s10858-005-2468-7
    • D.M. Korzhnev, A.K. Mittermaier, and L.E. Kay Cross-correlated spin relaxation effects in methyl 1H CPMG-based relaxation dispersion experiments: complications and a simple solution J. Biomol. NMR 31 2005 337 342 (Pubitemid 41348909)
    • (2005) Journal of Biomolecular NMR , vol.31 , Issue.4 , pp. 337-342
    • Korzhnev, D.M.1    Mittermaier, A.K.2    Kay, L.E.3
  • 55
    • 24744447629 scopus 로고    scopus 로고
    • Methyl groups as probes of structure and dynamics in NMR studies of high-molecular-weight proteins
    • DOI 10.1002/cbic.200500110
    • V. Tugarinov, and L.E. Kay Methyl groups as probes of structure and dynamics in NMR studies of high-molecular-weight proteins ChemBioChem 6 2005 1567 1577 (Pubitemid 41296962)
    • (2005) ChemBioChem , vol.6 , Issue.9 , pp. 1567-1577
    • Tugarinov, V.1    Kay, L.E.2
  • 56
    • 50149085281 scopus 로고    scopus 로고
    • Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy
    • P. Vallurupalli, D.F. Hansen, and L.E. Kay Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy Proc. Natl. Acad. Sci. USA 105 2008 11766 11771
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 11766-11771
    • Vallurupalli, P.1    Hansen, D.F.2    Kay, L.E.3
  • 57
    • 77956501272 scopus 로고    scopus 로고
    • A transient and low-populated protein-folding intermediate at atomic resolution
    • D.M. Korzhnev, T.L. Religa, W. Banachewicz, A.R. Fersht, and L.E. Kay A transient and low-populated protein-folding intermediate at atomic resolution Science 329 2010 1312 1316
    • (2010) Science , vol.329 , pp. 1312-1316
    • Korzhnev, D.M.1    Religa, T.L.2    Banachewicz, W.3    Fersht, A.R.4    Kay, L.E.5
  • 58
    • 33646910002 scopus 로고    scopus 로고
    • 20S proteasomes have the potential to keep substrates in store for continual degradation
    • DOI 10.1074/jbc.M511951200
    • M. Sharon, S. Witt, K. Felderer, B. Rockel, W. Baumeister, and C.V. Robinson 20S proteasomes have the potential to keep substrates in store for continual degradation J. Biol. Chem. 281 2006 9569 9575 (Pubitemid 43864675)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.14 , pp. 9569-9575
    • Sharon, M.1    Witt, S.2    Felderer, K.3    Rockel, B.4    Baumeister, W.5    Robinson, C.V.6
  • 60
    • 4344612865 scopus 로고    scopus 로고
    • Monitoring the transition from the T to the R state in E. coli aspartate transcarbamoylase by X-ray crystallography: Crystal structures of the E50A mutant enzyme in four distinct allosteric states
    • DOI 10.1016/j.jmb.2004.06.002, PII S0022283604006357
    • K. Stieglitz, B. Stec, D.P. Baker, and E.R. Kantrowitz Monitoring the transition from the T to the R state in E. coli aspartate transcarbamoylase by X-ray crystallography: crystal structures of the E50A mutant enzyme in four distinct allosteric states J. Mol. Biol. 341 2004 853 868 (Pubitemid 39118415)
    • (2004) Journal of Molecular Biology , vol.341 , Issue.3 , pp. 853-868
    • Stieglitz, K.1    Stec, B.2    Baker, D.P.3    Kantrowitz, E.R.4
  • 61
    • 0030691115 scopus 로고    scopus 로고
    • The structure of ClpP at 2.3 A resolution suggests a model for ATP- dependent proteolysis
    • J. Wang, J.A. Harting, and J.M. Flanagan The structure of ClpP at 2.3 resolution suggests a model for ATP-dependent proteolysis Cell 91 1997 447 456 (Pubitemid 27508234)
    • (1997) Cell , vol.91 , Issue.4 , pp. 447-456
    • Wang, J.1    Hartling, J.A.2    Flanagan, J.M.3
  • 62
    • 34548304719 scopus 로고    scopus 로고
    • Solution NMR of supramolecular complexes: Providing new insights into function
    • DOI 10.1038/nmeth1080, PII NMETH1080
    • R. Sprangers, A. Velyvis, and L.E. Kay Solution NMR of supramolecular complexes: providing new insights into function Nat. Methods 4 2007 697 703 (Pubitemid 47338161)
    • (2007) Nature Methods , vol.4 , Issue.9 , pp. 697-703
    • Sprangers, R.1    Velyvis, A.2    Kay, L.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.