The structural aspects of limited proteolysis of native proteins.

[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.