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Dynamics of the dihydrofolate reductase - Folate complex: Catalytic sites and regions known to undergo conformational change exhibit diverse dynamical features
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0029639625
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Solution structure of (Cd2+)1-calbindin D9k reveals details of the stepwise structural changes along the Apo→(Ca2+)II1→(Ca2+)I,II2 binding pathway
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0029135419
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Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state
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0029564421
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Nuclear magnetic resonance evidence for Ca(2+)-induced extrusion of the myristoyl group of recoverin
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of special interest. An interesting example of the coupling between calcium binding and the activation of membrane-binding activity. This study demonstrates the role of calcium in facilitating the exclusion of the myristoyl group from the protein making it solvent accessible and therefore membrane accessible (see also [54]).
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Calcium-induced conformational transition revealed by the solution structure of apocalmodulin
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of special interest. Clarification of the linkage between calcium binding and the binding of target protein domains by calmodulin. This study showed the absence of a solvent-exposed hydrophobic surface in apocalmodulin which is used to bind target domains in the calcium-saturated state (see also [57]).
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Zhang M, Tanaka T, Ikura M. Calcium-induced conformational transition revealed by the solution structure of apocalmodulin. of special interest Nat Struct Biol. 2:1995;758-767 Clarification of the linkage between calcium binding and the binding of target protein domains by calmodulin. This study showed the absence of a solvent-exposed hydrophobic surface in apocalmodulin which is used to bind target domains in the calcium-saturated state (see also [57]).
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Nat Struct Biol
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Zhang, M.1
Tanaka, T.2
Ikura, M.3
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57
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0029159794
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Solution structure of calcium-free calmodulin
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of special interest. See annotation [56].
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Kuboniwa H, Tjandra N, Grzesiek S, Ren H, Klee CB, Bax A. Solution structure of calcium-free calmodulin. of special interest Nat Struct Biol. 2:1995;769-776 See annotation [56].
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Nat Struct Biol
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Kuboniwa, H.1
Tjandra, N.2
Grzesiek, S.3
Ren, H.4
Klee, C.B.5
Bax, A.6
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58
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Structural analysis of a novel interaction by calmodulin: High-affinity binding of a peptide in the absence of calcium
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Urbauer JL, Short JH, Dow LK, Wand AJ. Structural analysis of a novel interaction by calmodulin: high-affinity binding of a peptide in the absence of calcium. Biochemistry. 34:1995;8099-8109.
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Biochemistry
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Urbauer, J.L.1
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Dow, L.K.3
Wand, A.J.4
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Structural water in oxidized and reduced horse heart cytochrome c
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Qi PX, Urbauer JL, Fuentes EJ, Leopold MF, Wand AJ. Structural water in oxidized and reduced horse heart cytochrome c. Nat Struct Biol. 1:1994;378-382.
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Qi, P.X.1
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Fuentes, E.J.3
Leopold, M.F.4
Wand, A.J.5
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60
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0028921374
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Detection of long-lived bound water molecules in complexes of human dihydrofolate reductase with methotrexate and NADPH
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of special interest. A good example of the use of NMR to probe the role of water in the complexation of proteins with small ligands.
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Meiering EM, Wagner G. Detection of long-lived bound water molecules in complexes of human dihydrofolate reductase with methotrexate and NADPH. of special interest J Mol Biol. 247:1995;294-308 A good example of the use of NMR to probe the role of water in the complexation of proteins with small ligands.
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J Mol Biol
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Meiering, E.M.1
Wagner, G.2
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61
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0028103855
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Homeodomain - DNA recognition
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Gehring WJ, Qian YQ, Billeter M, Furukubo-Tokunaga K, Schier AF, Resendez-Perez D, Affolter M, Otting G, Wüthrich K. Homeodomain - DNA recognition. Cell. 78:1994;211-223.
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Cell
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Gehring, W.J.1
Qian, Y.Q.2
Billeter, M.3
Furukubo-Tokunaga, K.4
Schier, A.F.5
Resendez-Perez, D.6
Affolter, M.7
Otting, G.8
Wüthrich, K.9
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62
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0028773080
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Localization of bound water in the solution structure of a complex of the erythroid transcription factor GATA-1 with DNA
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Clore GM, Bax A, Omichinski JG, Gronenborn AM. Localization of bound water in the solution structure of a complex of the erythroid transcription factor GATA-1 with DNA. Structure. 2:1994;89-94.
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Structure
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Clore, G.M.1
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Gronenborn, A.M.4
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63
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0028921999
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Demonstration of positionally disordered water within a protein hydrophobic cavity by NMR
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of special interest. A somewhat controversial demonstration of positionally disordered water within an apparently empty cavity (see [64, 65] for an exchange of interpretations).
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Ernst JA, Clubb RT, Zhou HX, Gronenborn AM, Clore GM. Demonstration of positionally disordered water within a protein hydrophobic cavity by NMR. of special interest Science. 267:1995;1813-1817 A somewhat controversial demonstration of positionally disordered water within an apparently empty cavity (see [64, 65] for an exchange of interpretations).
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Science
, vol.267
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Ernst, J.A.1
Clubb, R.T.2
Zhou, H.X.3
Gronenborn, A.M.4
Clore, G.M.5
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64
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0029561720
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Use of NMR to detect water within nonpolar protein cavities
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Matthews BW, Morton AG, Dahlquist FW. Use of NMR to detect water within nonpolar protein cavities. Science. 270:1995;1847-1849.
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Science
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Matthews, B.W.1
Morton, A.G.2
Dahlquist, F.W.3
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65
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0029561720
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Technical comments: Response to use of NMR to detect water within nonpolar cavities
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Ernst JA, Clubb RT, Zhou HX, Gronenborn AM, Clore GM. Technical comments: response to use of NMR to detect water within nonpolar cavities. Science. 270:1995;1848-1849.
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Science
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Ernst, J.A.1
Clubb, R.T.2
Zhou, H.X.3
Gronenborn, A.M.4
Clore, G.M.5
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67
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0026536335
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Solution structure of a calmodulin-target peptide complex by multidimensional NMR
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Ikura M, Clore GM, Gronenborn AM, Zhu G, Klee CB, Bax A. Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science. 256:1992;632-638.
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Science
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Ikura, M.1
Clore, G.M.2
Gronenborn, A.M.3
Zhu, G.4
Klee, C.B.5
Bax, A.6
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68
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0029121483
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Solution structure of the Shc SH2 domain complexed with a tyrosine-phosphorylated peptide from the T-cell receptor
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Zhou MM, Meadows RP, Logan TM, Yoon HS, Wade WS, Ravichandran KS, Burakoff SJ, Fesik SW. Solution structure of the Shc SH2 domain complexed with a tyrosine-phosphorylated peptide from the T-cell receptor. Proc Natl Acad Sci USA. 92:1995;7784-7788.
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Zhou, M.M.1
Meadows, R.P.2
Logan, T.M.3
Yoon, H.S.4
Wade, W.S.5
Ravichandran, K.S.6
Burakoff, S.J.7
Fesik, S.W.8
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69
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0028354446
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Nuclear magnetic resonance structure of an SH2 domain of phospholipase C - Gamma 1 complexed with a high affinity binding peptide
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Pascal SM, Singer AU, Gish G, Yamazaki T, Shoelson SE, Pawson T, Kay LE, Forman-Kay JD. Nuclear magnetic resonance structure of an SH2 domain of phospholipase C - gamma 1 complexed with a high affinity binding peptide. Cell. 77:1994;461-472.
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Pascal, S.M.1
Singer, A.U.2
Gish, G.3
Yamazaki, T.4
Shoelson, S.E.5
Pawson, T.6
Kay, L.E.7
Forman-Kay, J.D.8
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70
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0029644240
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Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B
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Qin J, Clore GM, Kennedy WM, Huth JR, Gronenborn AM. Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B. Structure. 3:1995;289-297.
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Qin, J.1
Clore, G.M.2
Kennedy, W.M.3
Huth, J.R.4
Gronenborn, A.M.5
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71
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0030042698
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Correlation between dynamics and high affinity binding in an SH2 domain interaction
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of special interest. A good example of the use of NMR relaxation techniques to probe the perturbation of the dynamics of a protein by the binding of ligand. This is one of the first applications of a recently developed technique [30] allowing the use of deuterium relaxation in the context of high-resolution solution NMR of proteins.
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Kay LE, Muhandiram DR, Farrow NA, Aubin Y, Forman-Kay JD. Correlation between dynamics and high affinity binding in an SH2 domain interaction. of special interest Biochemistry. 35:1996;361-368 A good example of the use of NMR relaxation techniques to probe the perturbation of the dynamics of a protein by the binding of ligand. This is one of the first applications of a recently developed technique [30] allowing the use of deuterium relaxation in the context of high-resolution solution NMR of proteins.
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Biochemistry
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Kay, L.E.1
Muhandiram, D.R.2
Farrow, N.A.3
Aubin, Y.4
Forman-Kay, J.D.5
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72
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15N NMR relaxation
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15N NMR relaxation. Biochemistry. 33:1994;5984-6003.
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Biochemistry
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Farrow, N.A.1
Muhandiram, R.2
Singer, A.U.3
Pascal, S.M.4
Kay, C.M.5
Gish, G.6
Shoelson, S.E.7
Pawson, T.8
Forman-Kay, J.D.9
Kay, L.E.10
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73
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84970061891
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Solution structure of the tetrameric minimum transforming domain of p53
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Lee W, Harvey TS, Yin Y, Yau P, Litchfield D, Arrowsmith CH. Solution structure of the tetrameric minimum transforming domain of p53. Nat Struct Biol. 1:1994;877-890.
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Lee, W.1
Harvey, T.S.2
Yin, Y.3
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Litchfield, D.5
Arrowsmith, C.H.6
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74
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0028939079
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Interhelical angles in the solution structure of oligomerization domain of p53: Correction
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Clore GM, Omichinski JG, Sakaguchi K, Zambrano N, Sakamoto H, Appella E, Gronenborn AM. Interhelical angles in the solution structure of oligomerization domain of p53: correction. Science. 267:1995;1515-1516.
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Science
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Clore, G.M.1
Omichinski, J.G.2
Sakaguchi, K.3
Zambrano, N.4
Sakamoto, H.5
Appella, E.6
Gronenborn, A.M.7
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75
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0028965832
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Refined solution structure of the oligomerization domain of the tumour suppressor p53
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Clore GM, Ernst J, Clubb R, Omichinski JG, Kennedy WM, Sakaguchi K, Appella E, Gronenborn AM. Refined solution structure of the oligomerization domain of the tumour suppressor p53. Nat Struct Biol. 2:1995;321-333.
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Nat Struct Biol
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Clore, G.M.1
Ernst, J.2
Clubb, R.3
Omichinski, J.G.4
Kennedy, W.M.5
Sakaguchi, K.6
Appella, E.7
Gronenborn, A.M.8
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76
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0027787519
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Determination of the nuclear magnetic resonance solution structure of an Antennapedia homeodomain - DNA complex
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Billeter, M.1
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Wüthrich, K.6
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77
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0024997404
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Protein - DNA contacts in the structure of a homeodomain - DNA complex determined by nuclear magnetic resonance spectroscopy in solution
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Otting G, Qian YQ, Billeter M, Muller M, Affolter M, Gehring WJ, Wüthrich K. Protein - DNA contacts in the structure of a homeodomain - DNA complex determined by nuclear magnetic resonance spectroscopy in solution. EMBO J. 9:1990;3085-3092.
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Otting, G.1
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Muller, M.4
Affolter, M.5
Gehring, W.J.6
Wüthrich, K.7
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78
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0029078107
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Solution structure of the C-terminal single-stranded DNA-binding domain of Escherichia coli topoisomerase I
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Yu L, Zhu CX, Tse-Dinh YC, Fesik SW. Solution structure of the C-terminal single-stranded DNA-binding domain of Escherichia coli topoisomerase I. Biochemistry. 34:1995;7622-7628.
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Biochemistry
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Yu, L.1
Zhu, C.X.2
Tse-Dinh, Y.C.3
Fesik, S.W.4
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79
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0028676257
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Solution structure of the Ets domain of Fli-1 when bound to DNA
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Liang H, Mao X, Olejniczak ET, Nettesheim DG, Yu L, Meadows RP, Thompson CB, Fesik SW. Solution structure of the Ets domain of Fli-1 when bound to DNA. Nat Struct Biol. 1:1994;871-875.
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Nat Struct Biol
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Liang, H.1
Mao, X.2
Olejniczak, E.T.3
Nettesheim, D.G.4
Yu, L.5
Meadows, R.P.6
Thompson, C.B.7
Fesik, S.W.8
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80
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0028874393
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Modulation of transcription factor Ets-1 DNA binding: DNA-induced unfolding of an alpha helix
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Petersen JM, Skalicky JJ, Donaldson LW, McIntosh LP, Alber T, Graves BJ. Modulation of transcription factor Ets-1 DNA binding: DNA-induced unfolding of an alpha helix. Science. 269:1995;1866-1869.
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Science
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Petersen, J.M.1
Skalicky, J.J.2
Donaldson, L.W.3
McIntosh, L.P.4
Alber, T.5
Graves, B.J.6
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81
-
-
0029131298
-
Structural basis for DNA bending by the architectural transcription factor LEF-1
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of special interest. A particularly nice example of the use of NMR to study protein - DNA complexes (see also [83,84] for a related system).
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Love JJ, Li X, Case DA, Giese K, Grosschedl R, Wright PE. Structural basis for DNA bending by the architectural transcription factor LEF-1. of special interest Nature. 376:1995;791-795 A particularly nice example of the use of NMR to study protein - DNA complexes (see also [83,84] for a related system).
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(1995)
Nature
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, pp. 791-795
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Love, J.J.1
Li, X.2
Case, D.A.3
Giese, K.4
Grosschedl, R.5
Wright, P.E.6
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82
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0027284167
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NMR structure of a specific DNA complex of Zn-containing DNA binding domain of GATA-1
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Omichinski JG, Clore GM, Schaad O, Felsenfeld G, Trainor C, Appella E, Stahl SJ, Gronenborn AM. NMR structure of a specific DNA complex of Zn-containing DNA binding domain of GATA-1. Science. 261:1993;438-446.
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Science
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Omichinski, J.G.1
Clore, G.M.2
Schaad, O.3
Felsenfeld, G.4
Trainor, C.5
Appella, E.6
Stahl, S.J.7
Gronenborn, A.M.8
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83
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0029075461
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Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex
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Werner MH, Huth JR, Gronenborn AM, Clore GM. Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex. Cell. 81:1995;705-714.
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(1995)
Cell
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Werner, M.H.1
Huth, J.R.2
Gronenborn, A.M.3
Clore, G.M.4
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84
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0029096665
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NMR spectroscopic analysis of the DNA conformation induced by the human tests determining factor SRY
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Werner MH, Bianchi ME, Gronenborn AM, Clore GM. NMR spectroscopic analysis of the DNA conformation induced by the human tests determining factor SRY. Biochemistry. 34:1995;11998-12004.
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Biochemistry
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Werner, M.H.1
Bianchi, M.E.2
Gronenborn, A.M.3
Clore, G.M.4
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85
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0028885514
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Multidimensional heteronuclear NMR experiments for structure determination of isotopically labeled RNA
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of special interest. An important review of methods for the isotopic enrichment of RNA and the application of triple resonance strategies to the assignment problem.
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Pardi A. Multidimensional heteronuclear NMR experiments for structure determination of isotopically labeled RNA. of special interest Methods Enzymol. 261:1995;350-380 An important review of methods for the isotopic enrichment of RNA and the application of triple resonance strategies to the assignment problem.
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Methods Enzymol
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Pardi, A.1
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86
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0028803380
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Preparation of isotopically enriched RNAs for heteronuclear NMR
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Batey RT, Battiste JL, Williamson JR. Preparation of isotopically enriched RNAs for heteronuclear NMR. Methods Enzymol. 261:1995;300-322.
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Methods Enzymol
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Batey, R.T.1
Battiste, J.L.2
Williamson, J.R.3
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87
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0028858599
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Solution structure of a bovine immunodeficiency virus Tat-TAR peptide - RNA complex
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of special interest. An important success for the comprehensive study of the structure of RNA - protein complexes by NMR methods.
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Puglisi JD, Chen L, Blanchard S, Frankel AD. Solution structure of a bovine immunodeficiency virus Tat-TAR peptide - RNA complex. of special interest Science. 270:1995;1200-1203 An important success for the comprehensive study of the structure of RNA - protein complexes by NMR methods.
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Science
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Puglisi, J.D.1
Chen, L.2
Blanchard, S.3
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13C-labeled polysaccharide from Streptococcus mitis J22
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13C-labeled polysaccharide from Streptococcus mitis J22. Biopolymers. 34:1994;1327-1338.
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Biopolymers
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Gitti, R.1
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One dimensional inverse-detected methods of measurement of long-range proton - Carbon coupling constants. Application to saccharides
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Uhrin D, Mele A, Kover KE, Boyd J, Dwek RA. One dimensional inverse-detected methods of measurement of long-range proton - carbon coupling constants. Application to saccharides. J Magn Reson Ser A. 108:1994;160-170.
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J Magn Reson Ser A
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Uhrin, D.1
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NMR developments in structural studies of carbohydrates and their complexes
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Van Halbeek H. NMR developments in structural studies of carbohydrates and their complexes. Curr Opin Struct Biol. 4:1994;697-709.
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Conformation of beta-methylmelibiose bound to the ricin B-chain as determined from transferred nuclear Overhauser effects
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Bevilacqua, V.L.1
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The conformation of the sialyl Lewis X ligand changes upon binding to E-selectin
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Cooke RM, Hale RS, Lister SG, Shah G, Weir MP. The conformation of the sialyl Lewis X ligand changes upon binding to E-selectin. Biochemistry. 33:1994;10591-10596.
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Biochemistry
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Cooke, R.M.1
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95
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0028300617
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Solution structure of a trisaccharide - Antibody complex: Comparison to NMR measurements with a crystal structure
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Bundle DR, Baumann H, Brisson J-R, Gagné SM, Zdanov A, Cygler M. Solution structure of a trisaccharide - antibody complex: comparison to NMR measurements with a crystal structure. Biochemistry. 33:1994;5183-5192.
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Biochemistry
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Bundle, D.R.1
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Brisson J-R3
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96
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0029000758
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Solution structure of a cellulose-binding domain from Cellulomonas fimi by nuclear magnetic resonance spectroscopy
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Xu GY, Ong E, Gilkes NR, Kilburn DG, Muhandiram DR, Harris-Brandts M, Carver JP, Kay LE, Harvey TS. Solution structure of a cellulose-binding domain from Cellulomonas fimi by nuclear magnetic resonance spectroscopy. Biochemistry. 34:1995;6993-7009.
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Biochemistry
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Xu, G.Y.1
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Harris-Brandts, M.6
Carver, J.P.7
Kay, L.E.8
Harvey, T.S.9
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97
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0028824423
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NMR identification of calcineurin B residues affected by binding of a calcineurin A peptide
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of special interest. An interesting case in which the binding of a target peptide removes the need for detergent solubilization of the receptor protein.
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Anglister J, Ren H, Klee CB, Bax A. NMR identification of calcineurin B residues affected by binding of a calcineurin A peptide. of special interest FEBS Lett. 375:1995;108-112 An interesting case in which the binding of a target peptide removes the need for detergent solubilization of the receptor protein.
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FEBS Lett
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Anglister, J.1
Ren, H.2
Klee, C.B.3
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0029077792
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NMR structures of phospholipase A2 reveal conformational changes during interfacial activation
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Van den Berg B, Tessari M, Boelens R, Dijkman R, De Haas GH, Kaptein R, Verheij HM. NMR structures of phospholipase A2 reveal conformational changes during interfacial activation. Nat Struct Biol. 2:1995;402-406.
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Nat Struct Biol
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Van den Berg, B.1
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Verheij, H.M.7
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99
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0028947465
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Reconstitution of membrane proteins into lipid-rich bilayered mixed micelles for NMR studies
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of special interest. A survey of the physical behavior of bicelles in the presence of various proteins. This study sets the stage for potentially rapid progress in the use of high resolution solution NMR to membrane protein systems (see also [100]).
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Sanders CR, Landis GC. Reconstitution of membrane proteins into lipid-rich bilayered mixed micelles for NMR studies. of special interest Biochemistry. 34:1995;4030-4040 A survey of the physical behavior of bicelles in the presence of various proteins. This study sets the stage for potentially rapid progress in the use of high resolution solution NMR to membrane protein systems (see also [100]).
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(1995)
Biochemistry
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, pp. 4030-4040
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Sanders, C.R.1
Landis, G.C.2
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100
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0028970550
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Small angle X-ray scattering studies of magnetically oriented lipid bilayers
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of special interest. An examination of the physical character of bicelles. This study helps sets the stage for potentially rapid progress in the application of high resolution solution NMR to membrane protein systems (see also [99]).
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Hare BJ, Prestegard JH, Engleman DM. Small angle X-ray scattering studies of magnetically oriented lipid bilayers. of special interest Biophys J. 69:1995;1891-1896 An examination of the physical character of bicelles. This study helps sets the stage for potentially rapid progress in the application of high resolution solution NMR to membrane protein systems (see also [99]).
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(1995)
Biophys J
, vol.69
, pp. 1891-1896
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Hare, B.J.1
Prestegard, J.H.2
Engleman, D.M.3
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