Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans.
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C. Chothia | M. Bycroft | J. Clarke | M. Proctor | S. Freund | S. J. Hamill | G. Benian | S. Fong | S. Hamill | C. Chothia | Jane Clarke | Mark R. Proctor | Sun Fong | Stefan M.V. Freund
[1] C. Chothia,et al. Members of the immunoglobulin superfamily in bacteria , 1996, Protein science : a publication of the Protein Society.
[2] V. Berezin,et al. The three-dimensional structure of the first domain of neural cell adhesion molecule , 1996, Nature Structural Biology.
[3] A. Fersht,et al. Active barnase variants with completely random hydrophobic cores. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[4] K. R. Weiss,et al. Ca2+ /S100 regulation of giant protein kinases , 1996, Nature.
[5] A. Pastore,et al. Immunoglobulin-like modules from titin I-band: extensible components of muscle elasticity. , 1996, Structure.
[6] A. Pastore,et al. The elastic I-band region of titin is assembled in a "modular" fashion by weakly interacting Ig-like domains. , 1996, Journal of molecular biology.
[7] Siegfried Labeit,et al. Titins: Giant Proteins in Charge of Muscle Ultrastructure and Elasticity , 1995, Science.
[8] K. R. Weiss,et al. Phosphorylation of myosin regulatory light chains by the molluscan twitchin kinase. , 1995, European journal of biochemistry.
[9] A. Pastore,et al. Tertiary structure of an immunoglobulin-like domain from the giant muscle protein titin: a new member of the I set. , 1995, Structure.
[10] R. Sauer,et al. Critical side-chain interactions at a subunit interface in the Arc repressor dimer. , 1995, Biochemistry.
[11] D. I. Stuart,et al. Crystal structure of an integrin-binding fragment of vascular cell adhesion molecule-1 at 1.8 Å resolution , 1995, Nature.
[12] H. Erickson,et al. Reversible unfolding of fibronectin type III and immunoglobulin domains provides the structural basis for stretch and elasticity of titin and fibronectin. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[13] P Bork,et al. The immunoglobulin fold. Structural classification, sequence patterns and common core. , 1994, Journal of molecular biology.
[14] A. Pastore,et al. Immunoglobulin‐type domains of titin are stabilized by amino‐terminal extension , 1994, FEBS letters.
[15] K. R. Weiss,et al. cAMP-dependent phosphorylation of Aplysia twitchin may mediate modulation of muscle contractions by neuropeptide cotransmitters. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[16] T. Chambers,et al. Protein kinase domain of twitchin has protein kinase activity and an autoinhibitory region. , 1994, The Journal of biological chemistry.
[17] A. Fersht,et al. Three-dimensional solution structure and 13C assignments of barstar using nuclear magnetic resonance spectroscopy. , 1994, Biochemistry.
[18] B. Kemp,et al. Insights into autoregulation from the crystal structure of twitchin kinase , 1994, Nature.
[19] C Chothia,et al. Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains. , 1994, Journal of molecular biology.
[20] A. Pastore,et al. Immunoglobulin-type domains of titin: same fold, different stability? , 1994, Biochemistry.
[21] L. Kay,et al. A gradient 13C NOESY-HSQC experiment for recording NOESY spectra of 13C-labeled proteins dissolved in H2O , 1993 .
[22] F. E. Weber,et al. The major myosin-binding domain of skeletal muscle MyBP-C (C protein) resides in the COOH-terminal, immunoglobulin C2 motif , 1993, The Journal of cell biology.
[23] A. Vorotnikov,et al. A kinase-related protein stabilizes unphosphorylated smooth muscle myosin minifilaments in the presence of ATP. , 1993, The Journal of biological chemistry.
[24] S. L'Hernault,et al. Additional sequence complexity in the muscle gene, unc-22, and its encoded protein, twitchin, of Caenorhabditis elegans. , 1993, Genetics.
[25] A. Fersht,et al. Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation. , 1993, Biochemistry.
[26] Paul A. Keifer,et al. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity , 1992 .
[27] H M Holden,et al. X-ray structure determination of telokin, the C-terminal domain of myosin light chain kinase, at 2.8 A resolution. , 1992, Journal of molecular biology.
[28] K. Wüthrich,et al. Support of1H NMR assignments in proteins by biosynthetically directed fractional13C-labeling , 1992 .
[29] Ad Bax,et al. Correlating Backbone Amide and Side-Chain Resonances in Larger Proteins By Multiple Relayed Triple Resonance NMR , 1992 .
[30] S. Labeit,et al. Towards a molecular understanding of titin. , 1992, The EMBO journal.
[31] L Serrano,et al. The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. , 1992, Journal of molecular biology.
[32] S. Grzesiek,et al. Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein , 1992 .
[33] B. Matthews,et al. Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. , 1992, Science.
[34] P. Kraulis. A program to produce both detailed and schematic plots of protein structures , 1991 .
[35] W. Lim,et al. The role of internal packing interactions in determining the structure and stability of a protein. , 1991, Journal of molecular biology.
[36] G. Marius Clore,et al. 1H1H correlation via isotropic mixing of 13C magnetization, a new three-dimensional approach for assigning 1H and 13C spectra of 13C-enriched proteins , 1990 .
[37] A. Lesk,et al. Conformations of immunoglobulin hypervariable regions , 1989, Nature.
[38] R. Waterston,et al. Sequence of an unusually large protein implicated in regulation of myosin activity in C. elegans , 1989, Nature.
[39] B. Matthews,et al. Hydrophobic packing in T4 lysozyme probed by cavity-filling mutants. , 1989, Proceedings of the National Academy of Sciences of the United States of America.
[40] L. Kay,et al. Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin 1 beta. , 1989, Biochemistry.
[41] A. Fersht,et al. Contribution of hydrophobic interactions to protein stability , 1988, Nature.
[42] K. Wüthrich. NMR of proteins and nucleic acids , 1988 .
[43] A. Lesk,et al. Canonical structures for the hypervariable regions of immunoglobulins. , 1987, Journal of molecular biology.
[44] Ad Bax,et al. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy , 1985 .
[45] A M Lesk,et al. Evolution of proteins formed by beta-sheets. II. The core of the immunoglobulin domains. , 1982, Journal of molecular biology.
[46] J. Keeler,et al. A convenient and accurate method for the measurement of the values of spin-spin coupling constants , 1995 .
[47] A. F. Williams,et al. The immunoglobulin superfamily--domains for cell surface recognition. , 1988, Annual review of immunology.
[48] G. Bodenhausen,et al. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy , 1980 .