The structural aspects of limited proteolysis of native proteins.
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[1] W. Kabsch,et al. Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features , 1983, Biopolymers.
[2] K. Bennett,et al. Monitoring papain digestion of a monoclonal antibody by electrospray ionization mass spectrometry. , 1997, Analytical biochemistry.
[3] S. Anderson,et al. Binding of amino acid side-chains to S1 cavities of serine proteinases. , 1997, Journal of molecular biology.
[4] S. Hubbard,et al. Limited proteolysis of native proteins: The interaction between avidin and proteinase K , 1995, Protein science : a publication of the Protein Society.
[5] H. Neurath,et al. Role of proteolytic enzymes in biological regulation (a review). , 1976, Proceedings of the National Academy of Sciences of the United States of America.
[6] V. De Filippis,et al. Limited proteolysis of lysozyme in trifluoroethanol. Isolation and characterization of a partially active enzyme derivative. , 1995, European journal of biochemistry.
[7] V. De Filippis,et al. Limited proteolysis of cytochrome c in trifluoroethanol , 1995, FEBS letters.
[8] P E Wright,et al. Structural characterization of a partly folded apomyoglobin intermediate. , 1990, Science.
[9] P E Wright,et al. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. , 1993, Science.
[10] M Bolognesi,et al. Grafting of a calcium-binding loop of thermolysin to Bacillus subtilis neutral protease. , 1991, Biochemistry.
[11] J. Katzenellenbogen,et al. Analysis of the structural core of the human estrogen receptor ligand binding domain by selective proteolysis/mass spectrometric analysis. , 1995, Biochemistry.
[12] C. Tsou,et al. Inactivation during denaturation of ribonuclease A by guanidinium chloride is accompanied by unfolding at the active site. , 1995, The Biochemical journal.
[13] K. Linderstrøm-Lang,et al. Structure and enzymatic break-down of proteins. , 1950 .
[14] A. Fersht,et al. Engineering a novel specificity in subtilisin BPN'. , 1993, Biochemistry.
[15] J M Thornton,et al. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. , 1995, Protein engineering.
[16] W. L. Jorgensen,et al. Molecular dynamics simulations of the unfolding of apomyoglobin in water. , 1993, Biochemistry.
[17] C. López-Otín,et al. β‐Turns as structural motifs for the proteolytic processing of seed proteins , 1990, FEBS letters.
[18] H. Neurath. Protein science in 1996 , 1997 .
[19] P. Kraulis. A program to produce both detailed and schematic plots of protein structures , 1991 .
[20] V. De Filippis,et al. Probing the structure of hirudin from Hirudinaria manillensis by limited proteolysis. Isolation, characterization and thrombin-inhibitory properties of N-terminal fragments. , 1994, European journal of biochemistry.
[21] T. Vajda,et al. Comparison of the effect of calcium(II) and manganese(II) ions on trypsin autolysis. , 1981, Journal of inorganic biochemistry.
[22] I. Taylor,et al. Probing the domain structure of the type IC DNA methyltransferase M.EcoR124I by limited proteolysis. , 1995, Journal of molecular biology.
[23] William R. Taylor,et al. An ellipsoidal approximation of protein shape , 1983 .
[24] H. Scheraga,et al. STRUCTURAL STUDIES OF RIBONUCLEASE. VIII. TRYPTIC HYDROLYSIS OF RIBONUCLEASE A AT ELEVATED TEMPERATURES. , 1963, Biochemistry.
[25] V. De Filippis,et al. Probing the molten globule state of alpha-lactalbumin by limited proteolysis. , 1995, Biochemistry.
[26] M. A. Shea,et al. Quantitative endoproteinase GluC footprinting of cooperative Ca2+ binding to calmodulin: proteolytic susceptibility of E31 and E87 indicates interdomain interactions. , 1995, Biochemistry.
[27] F. Schmid,et al. Use of a trypsin-pulse method to study the refolding pathway of ribonuclease. , 1986, European journal of biochemistry.
[28] A. English,et al. LOCAL STABILITIES OF HORSE CYTOCHROME C METALLODERIVATIVES AS PROBED BY TRYPTIC DIGESTION AND ELECTROSPRAY MASS SPECTROMETRY , 1996 .
[29] R. Beynon,et al. Proteolysis and physiological regulation. , 1987, Molecular aspects of medicine.
[30] J M Yon,et al. The folding of pancreatic elastase: independent domain refolding and inter-domain interaction. , 1978, Biochemical and biophysical research communications.
[31] D. Lomas,et al. Probing serpin reactive-loop conformations by proteolytic cleavage. , 1996, The Biochemical journal.
[32] B. Kerfelec,et al. Uncoupling of catalysis and colipase binding in pancreatic lipase by limited proteolysis. , 1992, Protein engineering.
[33] B. Lee,et al. The interpretation of protein structures: estimation of static accessibility. , 1971, Journal of molecular biology.
[34] B. van den Burg,et al. Identification of autodigestion target sites in Bacillus subtilis neutral proteinase. , 1990, The Biochemical journal.
[35] C. Vita,et al. Limited proteolysis of thermolysin by subtilisin: isolation and characterization of a partially active enzyme derivative. , 1985, Biochemistry.
[36] E. Bek,et al. Prohormonal cleavage sites are associated with omega loops. , 1990, Biochemistry.
[37] M. Meldal,et al. Extensive comparison of the substrate preferences of two subtilisins as determined with peptide substrates which are based on the principle of intramolecular quenching. , 1992, Biochemistry.
[38] R. Bruccoleri,et al. Correlation among sites of limited proteolysis, enzyme accessibility and segmental mobility , 1987, FEBS letters.
[39] J. Sussman,et al. The structure of the complex between avidin and the dye, 2‐(4'‐hydroxyazobenzene) benzoic acid (HABA) , 1993, FEBS letters.
[40] U. Arnold,et al. Thermal unfolding and proteolytic susceptibility of ribonuclease A. , 1996, European journal of biochemistry.
[41] A. Leslie,et al. Crystal structure of ovalbumin as a model for the reactive centre of serpins , 1990, Nature.
[42] T. Nishino,et al. The Structure of Chicken Liver Xanthine Dehydrogenase , 1995, The Journal of Biological Chemistry.
[43] R. Huber,et al. Natural protein proteinase inhibitors and their interaction with proteinases. , 1992, European journal of biochemistry.
[44] David M. Blow,et al. Structure and mechanism of chymotrypsin , 1976 .
[45] V. De Filippis,et al. Probing the conformational state of apomyoglobin by limited proteolysis. , 1997, Journal of molecular biology.
[46] R. Sauer,et al. The structural stability of a protein is an important determinant of its proteolytic susceptibility in Escherichia coli. , 1989, The Journal of biological chemistry.
[47] M. Zamai,et al. Correlation between sites of limited proteolysis and segmental mobility in thermolysin. , 1986, Biochemistry.
[48] M. Ottesen. Induction of biological activity by limited proteolysis. , 1967, Annual review of biochemistry.
[49] J M Thornton,et al. Molecular recognition. Conformational analysis of limited proteolytic sites and serine proteinase protein inhibitors. , 1991, Journal of molecular biology.
[50] J. Enghild,et al. Conformation of the reactive site loop of alpha 1-proteinase inhibitor probed by limited proteolysis. , 1992, Biochemistry.
[51] C. Dobson,et al. A partially folded state of hen egg white lysozyme in trifluoroethanol: structural characterization and implications for protein folding. , 1993, Biochemistry.
[52] R. Huber,et al. Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Crystal structure determination and stereochemistry of the contact region. , 1973, Journal of molecular biology.
[53] A. Berger,et al. On the size of the active site in proteases. I. Papain. , 1967, Biochemical and biophysical research communications.
[54] G J Williams,et al. The Protein Data Bank: a computer-based archival file for macromolecular structures. , 1977, Journal of molecular biology.
[55] W. Bode,et al. Human leukocyte and porcine pancreatic elastase: X-ray crystal structures, mechanism, substrate specificity, and mechanism-based inhibitors. , 1989, Biochemistry.
[56] M. Newcomer,et al. Cellular retinoid-binding proteins: limited proteolysis reveals a conformational change upon ligand binding. , 1994, Biochemistry.
[57] V. Eijsink,et al. Structural determinants of the stability of thermolysin-like proteinases , 1995, Nature Structural Biology.
[58] C. Gwizdek,et al. Proteolytic mapping and substrate protection of the Escherichia coli melibiose permease. , 1997, Biochemistry.
[59] J. Kraut. Serine proteases: structure and mechanism of catalysis. , 1977, Annual review of biochemistry.
[60] V. De Filippis,et al. Probing the partly folded states of proteins by limited proteolysis. , 1997, Folding & design.
[61] F. Richards,et al. The preparation of subtilisn-modified ribonuclease and the separation of the peptide and protein components. , 1959, The Journal of biological chemistry.
[62] W R Taylor,et al. Location of ‘continuous’ antigenic determinants in the protruding regions of proteins. , 1986, The EMBO journal.
[63] G Vriend,et al. Protein stabilization by hydrophobic interactions at the surface. , 1994, European journal of biochemistry.
[64] C. Anfinsen,et al. Nuclease-T: an active derivative of staphylococcal nuclease composed of two noncovalently bonded peptide fragments. , 1967, Proceedings of the National Academy of Sciences of the United States of America.
[65] J. Thornton,et al. Substrate recognition by proteinases. , 1992, Faraday discussions.
[66] K. Nishikawa,et al. Radial locations of amino acid residues in a globular protein: correlation with the sequence. , 1986, Journal of biochemistry.
[67] K. Kuwajima. The molten globule state of α‐lactalbumin , 1996, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[68] O. Ptitsyn. Structures of folding intermediates. , 1995, Current opinion in structural biology.
[69] B. Dijkstra,et al. Topological characterization and modeling of the 3D structure of lipase from Pseudomonas aeruginosa , 1993, FEBS letters.
[70] C. Anfinsen,et al. Steps in the formation of active derivatives of staphylococcal nuclease during trypsin digestion. , 1968, The Journal of biological chemistry.
[71] J M Thornton,et al. Modeling studies of the change in conformation required for cleavage of limited proteolytic sites , 1994, Protein science : a publication of the Protein Society.