The spectrin repeat folds into a three‐helix bundle in solution
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A. Pastore | G. Rivas | M. Saraste | J. Pascual | M. Pfuhl
[1] J. Sambrook,et al. Molecular Cloning: A Laboratory Manual , 2001 .
[2] M. Saraste,et al. Does Vav bind to F‐actin through a CH domain? , 1995, FEBS letters.
[3] A. Pastore,et al. Molecular mechanism of the calcium‐induced conformational change in the spectrin EF‐hands. , 1995, The EMBO journal.
[4] Eric Oldfield,et al. 1H, 13C and 15N chemical shift referencing in biomolecular NMR , 1995, Journal of biomolecular NMR.
[5] A. Palmer,et al. Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme. , 1995, Journal of molecular biology.
[6] R. Yu,et al. The first human alpha-spectrin structural domain begins with serine. , 1994, The Journal of biological chemistry.
[7] Michael Nilges,et al. Structure of the pleckstrin homology domain from β-spectrin , 1994, Nature.
[8] J. Keeler,et al. Minimizing Sensitivity Losses in Gradient-Selected 15N-1H HSQC Spectra of Proteins , 1994 .
[9] D. Wishart,et al. The 13C Chemical-Shift Index: A simple method for the identification of protein secondary structure using 13C chemical-shift data , 1994, Journal of biomolecular NMR.
[10] D. Branton,et al. Crystal structure of the repetitive segments of spectrin. , 1993, Science.
[11] E. Zuiderweg,et al. Improved 13C-Resolved HSQC-NOESY Spectra in H2O, Using Pulsed Field Gradients , 1993 .
[12] Vladimir Sklenar,et al. Gradient-Tailored Water Suppression for 1H-15N HSQC Experiments Optimized to Retain Full Sensitivity , 1993 .
[13] R A Smith,et al. Loop mobility in a four-helix-bundle protein: 15N NMR relaxation measurements on human interleukin-4. , 1992, Biochemistry.
[14] V. Saudek,et al. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions , 1992, Journal of biomolecular NMR.
[15] Andrea Musacchio,et al. Crystal structure of a Src-homology 3 (SH3) domain , 1992, Nature.
[16] M Ikura,et al. Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible. , 1992, Biochemistry.
[17] D A Parry,et al. Analysis of the three-alpha-helix motif in the spectrin superfamily of proteins. , 1992, Biophysical journal.
[18] L. Kay,et al. Pulse sequences for removal of the effects of cross correlation between dipolar and chemical-shift anisotropy relaxation mechanisms on the measurement of heteronuclear T1 and T2 values in proteins , 1992 .
[19] G. Wagner,et al. A constant-time three-dimensional triple-resonance pulse scheme to correlate intraresidue 1HN, 15N, and 13C′ chemical shifts in 15N13C-labelled proteins , 1992 .
[20] F. Richards,et al. The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. , 1992, Biochemistry.
[21] S. Grzesiek,et al. Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein , 1992 .
[22] D. Branton,et al. Phasing the conformational unit of spectrin. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[23] A. Lupas,et al. Predicting coiled coils from protein sequences , 1991, Science.
[24] A. Pastore,et al. The relationship between chemical shift and secondary structure in proteins , 1990 .
[25] F. Costa,et al. Point mutation in the beta-spectrin gene associated with alpha I/74 hereditary elliptocytosis. Implications for the mechanism of spectrin dimer self-association. , 1990, The Journal of clinical investigation.
[26] Paul C. Driscoll,et al. Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins , 1990 .
[27] L. Kay,et al. Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. , 1989, Biochemistry.
[28] Ad Bax,et al. Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins , 1989 .
[29] P. V. von Hippel,et al. Calculation of protein extinction coefficients from amino acid sequence data. , 1989, Analytical biochemistry.
[30] M. Saraste,et al. Primary structure of the brain alpha-spectrin [published erratum appears in J Cell Biol 1989 Mar;108(3):following 1175] , 1989, The Journal of cell biology.
[31] K. Wüthrich. NMR of proteins and nucleic acids , 1988 .
[32] D. Branton,et al. The molecular basis of erythrocyte shape. , 1986, Science.
[33] K Wüthrich,et al. Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances. , 1984, Journal of molecular biology.
[34] Vincent T. Marchesi,et al. Erythrocyte spectrin is comprised of many homologous triple helical segments , 1984, Nature.
[35] W. Kabsch,et al. Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features , 1983, Biopolymers.
[36] A. Szabó,et al. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity , 1982 .
[37] A. Szabó,et al. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results , 1982 .
[38] U. K. Laemmli,et al. Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.
[39] A. Pastore,et al. The C-terminal domain of alpha-spectrin is structurally related to calmodulin. , 1995, European journal of biochemistry.
[40] T. Laue,et al. Modern Analytical Ultracentrifugation , 1994, Emerging Biochemical and Biophysical Techniques.
[41] A. Minton. Conservation of Signal: A New Algorithm for the Elimination of the Reference Concentration as an Independently Variable Parameter in the Analysis of Sedimentation Equilibrium , 1994 .
[42] D. Gilligan,et al. The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane. , 1993, Annual review of cell biology.
[43] Arthur J. Rowe,et al. Analytical ultracentrifugation in biochemistry and polymer science , 1992 .
[44] F. Studier,et al. Use of T7 RNA polymerase to direct expression of cloned genes. , 1990, Methods in enzymology.
[45] L. Kay,et al. New methods for the measurement of NHCαH coupling constants in 15N-labeled proteins , 1990 .