Isolation and spectroscopic analyses of S-100 proteins and their interactions with metal ions.

[1]  H. Vogel,et al.  Structural differences in the two calcium binding sites of the porcine intestinal calcium binding protein: a multinuclear NMR study. , 1985, Biochemistry.

[2]  C. Kay,et al.  A fluorimetry study of N‐(1‐pyrenyl)iodoacetamide‐labelled bovine brain S‐100a protein , 1985 .

[3]  J. Kuo,et al.  S‐100 Modulates Ca2+‐Independent Phosphorylation of an Endogenous Protein (Mr= 19K) in Brain , 1984, Journal of neurochemistry.

[4]  C. Kay,et al.  Hydrodynamic properties of bovine brain S‐100 proteins , 1984, FEBS letters.

[5]  Y. Ohtsuki,et al.  Immunohistochemical study on the distribution of α and β subunits of S-100 protein in human neoplasm and normal tissues , 1984 .

[6]  H. Hidaka,et al.  A rapid separation of bovine brain S-100a and S-100b proteins and related conformation studies. , 1983, Archives of biochemistry and biophysics.

[7]  L. Berliner,et al.  Manganese (II) electron spin resonance and cadmium-113 nuclear magnetic resonance evidence for the nature of the calcium binding site in alpha-lactalbumins. , 1983, Biochemistry.

[8]  R. Donato Effect of S‐100 protein on assembly of brain microtubule proteins in vitro , 1983, FEBS letters.

[9]  H. Hidaka,et al.  Effect of S‐100 protein on microtubule assembly—disassembly , 1983, FEBS letters.

[10]  K. Haglid,et al.  Zinc ion binding to human brain calcium binding proteins, calmodulin and S100b protein. , 1983, Biochemical and biophysical research communications.

[11]  C. Kay,et al.  Isolation and spectral studies on the calcium binding properties of bovine brain S-100a protein. , 1983, Biochemistry.

[12]  J. Baudier,et al.  Ions binding to S100 proteins: structural changes induced by calcium and zinc on S100a and S100b proteins. , 1983, Biochemistry.

[13]  D. Jacobowitz,et al.  S‐100‐Mediated Inhibition of Brain Protein Phosphorylation , 1983, Journal of neurochemistry.

[14]  B. Sykes,et al.  Spectral studies on the calcium binding properties of bovine brain S-100b protein. , 1983, Biochemistry.

[15]  Alexander Marks,et al.  Role of antibody to S100 protein in diagnostic pathology. , 1983, American journal of clinical pathology.

[16]  T. Nakajima,et al.  An immunoperoxidase study of S-100 protein distribution in normal and neoplastic tissues , 1982, The American journal of surgical pathology.

[17]  J. Baudier,et al.  Zinc‐dependent affinity chromatography of the S100b protein on phenyl—Sepharose , 1982, FEBS letters.

[18]  H. Hidaka,et al.  S-100 antigen in human T lymphocytes. , 1982, Biochemical and biophysical research communications.

[19]  K. Haglid,et al.  Effect of S‐100 proteins and calmodulin on Ca2+‐induced disassembly of brain microtubule proteins in vitro , 1982, FEBS letters.

[20]  C. Kay,et al.  Physicochemical and optical studies on calcium- and potassium-induced conformational changes in bovine brain S-100b protein. , 1982, Biochemistry.

[21]  R. Wollmann,et al.  S-100 protein in human chondrocytes , 1982, Nature.

[22]  T. Isobe,et al.  Structural relation of two S-100 proteins in bovine brain; subunit composition of S-100a protein. , 2005, European journal of biochemistry.

[23]  F. Michetti,et al.  Immunochemical and immunocytochemical localization of S-100 antigen in normal human skin , 1981, Nature.

[24]  B. Sykes,et al.  Hydrogen-1 nuclear magnetic resonance investigation on bovine cardiac troponin C. Comparison of tyrosyl assignments and calcium-induced structural changes to those of two homologous proteins, rabbit skeletal troponin C and bovine brain calmodulin. , 1981, Biochemistry.

[25]  T. Isobe,et al.  The Amino-Acid Sequence of the α Subunit in Bovine Brain S-100a Protein , 1981 .

[26]  K. Seamon Calcium- and magnesium-dependent conformational states of calmodulin as determined by nuclear magnetic resonance. , 1980, Biochemistry.

[27]  T. Isobe,et al.  The amino-acid sequence of S-100 protein (PAP I-b protein) and its relation to the calcium-binding proteins. , 1978, European journal of biochemistry.

[28]  J. Thornton,et al.  Calcium binding by troponin-C. A proton magnetic resonance study. , 1977, Journal of molecular biology.

[29]  T. Isobe,et al.  Reinvestigation of extremely acidic proteins in bovine brain. , 1977, Biochimica et biophysica acta.

[30]  T. Vanaman,et al.  Structural similarities between the Ca2+-dependent regulatory proteins of 3':5'-cyclic nucleotide phosphodiesterase and actomyosin ATPase. , 1976, The Journal of biological chemistry.

[31]  R. Kretsinger,et al.  Troponin and parvalbumin calcium binding regions predicted in myosin light chain and T4 lysozyme. , 1975, Science.

[32]  C. Kay,et al.  Physicochemical studies on the complexes troponin C with troponin T, and reconstituted troponin, and their interaction with calcium ions. , 1974, Biochemistry.

[33]  R. Martin,et al.  Conformations of carp muscle calcium binding parvalbumin. , 1974, Biochemistry.

[34]  B. Moore A soluble protein characteristic of the nervous system. , 1965, Biochemical and biophysical research communications.

[35]  F. Teale,et al.  The ultraviolet fluorescence of proteins in neutral solution. , 1960, The Biochemical journal.

[36]  G. Weber,et al.  Ultraviolet fluorescence of the aromatic amino acids. , 1957, The Biochemical journal.