| Year |
Citation |
Score |
| 2010 |
Neurath H. Structural Relations among Proteolytic Enzymes. Science (New York, N.Y.). 148: 666-7. PMID 17801948 DOI: 10.1126/Science.148.3670.666-B |
0.315 |
|
| 2010 |
Neurath H. Active Sites of Enzyme Precursors. Science (New York, N.Y.). 136: 328. PMID 17745931 DOI: 10.1126/Science.136.3513.328 |
0.321 |
|
| 2000 |
NEURATH H. Some considerations of the multiple specificity of proteolytic enzymes. Annals of the New York Academy of Sciences. 68: 11-23; discussion 23. PMID 13479016 DOI: 10.1111/J.1749-6632.1957.Tb42608.X |
0.308 |
|
| 1991 |
Cole KR, Kumar S, Trong HL, Woodbury RG, Walsh KA, Neurath H. Rat mast cell carboxypeptidase: amino acid sequence and evidence of enzyme activity within mast cell granules. Biochemistry. 30: 648-55. PMID 1988052 DOI: 10.1021/Bi00217A009 |
0.55 |
|
| 1989 |
Trong HL, Newlands GF, Miller HR, Charbonneau H, Neurath H, Woodbury RG. Amino acid sequence of a mouse mucosal mast cell protease. Biochemistry. 28: 391-5. PMID 2706264 |
0.59 |
|
| 1988 |
Remington SJ, Woodbury RG, Reynolds RA, Matthews BW, Neurath H. The structure of rat mast cell protease II at 1.9-A resolution. Biochemistry. 27: 8097-105. PMID 3233198 DOI: 10.1021/Bi00421A019 |
0.301 |
|
| 1988 |
Wade RD, Hass GM, Kumar S, Walsh KA, Neurath H. The amino acid sequence of the activation peptide of bovine pro-carboxypeptidase A. Biochimie. 70: 1137-42. PMID 3147705 DOI: 10.1016/0300-9084(88)90178-2 |
0.55 |
|
| 1987 |
Titani K, Torff HJ, Hormel S, Kumar S, Walsh KA, Rödl J, Neurath H, Zwilling R. Amino acid sequence of a unique protease from the crayfish Astacus fluviatilis. Biochemistry. 26: 222-6. PMID 3548817 DOI: 10.1021/Bi00375A029 |
0.547 |
|
| 1987 |
Le Trong H, Neurath H, Woodbury RG. Substrate specificity of the chymotrypsin-like protease in secretory granules isolated from rat mast cells. Proceedings of the National Academy of Sciences of the United States of America. 84: 364-7. PMID 3540962 DOI: 10.1073/Pnas.84.2.364 |
0.369 |
|
| 1987 |
Le Trong H, Parmelee DC, Walsh KA, Neurath H, Woodbury RG. Amino acid sequence of rat mast cell protease I (chymase). Biochemistry. 26: 6988-94. PMID 3122823 DOI: 10.1021/Bi00396A020 |
0.541 |
|
| 1987 |
WOODBURY RG, TRONG HL, NEURATH H. Structure and function of mast cell proteases. Acta Histochemica Et Cytochemica. 20: 261-269. DOI: 10.1267/Ahc.20.261 |
0.315 |
|
| 1986 |
Neurath H. The versatility of proteolytic enzymes. Journal of Cellular Biochemistry. 32: 35-49. PMID 3533969 DOI: 10.1002/Jcb.240320105 |
0.319 |
|
| 1985 |
Powers JC, Tanaka T, Harper JW, Minematsu Y, Barker L, Lincoln D, Crumley KV, Fraki JE, Schechter NM, Lazarus GG, Nakajima K, Nakashino K, Neurath H, Woodbury RG. Mammalian chymotrypsin-like enzymes. Comparative reactivities of rat mast cell proteases, human and dog skin chymases, and human cathepsin G with peptide 4-nitroanilide substrates and with peptide chloromethyl ketone and sulfonyl fluoride inhibitors Biochemistry. 24: 2048-2058. PMID 3893542 DOI: 10.1021/Bi00329A037 |
0.366 |
|
| 1984 |
Neurath H. Evolution of proteolytic enzymes. Science (New York, N.Y.). 224: 350-7. PMID 6369538 DOI: 10.1126/Science.6369538 |
0.383 |
|
| 1984 |
Titani K, Ericsson LH, Kumar S, Jakob F, Neurath H, Zwilling R. Amino acid sequence of crayfish (Astacus fluviatilis) carboxypeptidase B Biochemistry. 23: 1245-1250. DOI: 10.1021/Bi00301A035 |
0.341 |
|
| 1983 |
Titani K, Sasagawa T, Woodbury RG, Ericsson LH, Dörsam H, Kraemer M, Neurath H, Zwilling R. Amino acid sequence of crayfish (Astacus fluviatilis) trypsin If. Biochemistry. 22: 1459-65. PMID 6838862 DOI: 10.1021/Bi00275A021 |
0.417 |
|
| 1983 |
Neurath H. Editorial - Documentation of Sequence Analysis of Proteins Biochemistry. 22: 2595-2595. DOI: 10.1021/Bi00280A600 |
0.305 |
|
| 1981 |
Woodbury RG, Everitt MT, Neurath H. Mast cell proteases. Methods in Enzymology. 80: 588-609. PMID 7043202 DOI: 10.1016/S0076-6879(81)80047-X |
0.303 |
|
| 1981 |
Bloxham DP, Parmelee DC, Kumar S, Wade RD, Ericsson LH, Neurath H, Walsh KA, Titani K. Primary structure of porcine heart citrate synthase. Proceedings of the National Academy of Sciences of the United States of America. 78: 5381-5. PMID 6795632 DOI: 10.1073/Pnas.78.9.5381 |
0.538 |
|
| 1981 |
Shoji S, Parmelee DC, Wade RD, Kumar S, Ericsson LH, Walsh KA, Neurath H, Long GL, Demaille JG, Fischer EH, Titani K. Complete amino acid sequence of the catalytic subunit of bovine cardiac muscle cyclic AMP-dependent protein kinase. Proceedings of the National Academy of Sciences of the United States of America. 78: 848-51. PMID 6262777 DOI: 10.1073/Pnas.78.2.848 |
0.539 |
|
| 1981 |
Woodbury RG, Neurath H. Mast Cell Proteases Methods in Enzymology. 145-158. DOI: 10.1007/978-3-642-68211-7_14 |
0.334 |
|
| 1980 |
Bloxham DP, Ericsson LH, Titani K, Walsh KA, Neurath H. Limited proteolysis of pig heart citrate synthase by subtilisin, chymotrypsin, and trypsin. Biochemistry. 19: 3979-85. PMID 6773558 DOI: 10.1021/Bi00558A014 |
0.531 |
|
| 1980 |
Enfield DL, Ericsson LH, Fujikawa K, Walsh KA, Neurath H, Titani K. Amino acid sequence of the light chain of bovine factor X1 (Stuart factor). Biochemistry. 19: 659-67. PMID 6766735 DOI: 10.1021/Bi00545A009 |
0.518 |
|
| 1980 |
Takio K, Walsh KA, Neurath H, Smith SB, Krebs EG, Titani K. The amino acid sequence of a hinge region in the regulatory subunit of bovine cardiac muscle cyclic AMP-dependent protein kinase II. Febs Letters. 114: 83-8. PMID 6247212 DOI: 10.1016/0014-5793(80)80865-9 |
0.49 |
|
| 1979 |
Londsdale-Eccles JD, Kerr MA, Walsh KA, Neurath H. Catalysis by zymogens: increased reactivity at high ionic strength. Febs Letters. 100: 157-60. PMID 571353 DOI: 10.1016/0014-5793(79)81154-0 |
0.501 |
|
| 1979 |
Everitt MT, Neurath H. Purification and partial characterization of an alpha-chymotrypsin-like protease of rat peritoneal mast cells. Biochimie. 61: 653-62. PMID 497254 DOI: 10.1016/S0300-9084(79)80163-7 |
0.345 |
|
| 1979 |
Leary TR, Grahn DT, Neurath H, Hass GM. Structure of potato carboxypeptidase inhibitor: disulfide pairing and exposure of aromatic residues. Biochemistry. 18: 2252-6. PMID 444453 DOI: 10.1021/Bi00578A018 |
0.36 |
|
| 1979 |
Zwilling R, Jakob F, Bauer H, Neurath H, Enfield DL. Crayfish carboxypeptidase. Affinity chromatography, characterization and amino-terminal sequence. European Journal of Biochemistry / Febs. 94: 223-9. PMID 436840 DOI: 10.1111/J.1432-1033.1979.Tb12889.X |
0.41 |
|
| 1979 |
Katayama K, Ericsson LH, Enfield DL, Walsh KA, Neurath H, Davie EW, Titani K. Comparison of amino acid sequence of bovine coagulation Factor IX (Christmas Factor) with that of other vitamin K-dependent plasma proteins. Proceedings of the National Academy of Sciences of the United States of America. 76: 4990-4. PMID 291916 DOI: 10.1073/Pnas.76.10.4990 |
0.528 |
|
| 1978 |
Titani K, Koide A, Ericsson LH, Kumar S, Hermann J, Wade RD, Walsh KA, Neurath H, Fischer EH. Sequence of the carboxyl-terminal 492 residues of rabbit muscle glycogen phosphorylase including the pyridoxal 5'-phosphate binding site. Biochemistry. 17: 5680-93. PMID 728426 DOI: 10.1021/Bi00619A014 |
0.539 |
|
| 1978 |
Hermann J, Titani K, Ericsson LH, Wade RD, Neurath H, Walsh KA. Amino acid sequence of two cyanogen bromide fragments of glycogen phosphorylase. Biochemistry. 17: 5672-9. PMID 728425 DOI: 10.1021/Bi00619A013 |
0.507 |
|
| 1978 |
Koide A, Titani K, Ericsson LH, Kumar S, Neurath H, Walsh KA. Sequence of the amino-terminal 349 residues of rabbit muscle glycogen phosphorylase including the sites of covalent and allosteric control. Biochemistry. 17: 5657-72. PMID 728424 DOI: 10.1021/Bi00619A012 |
0.525 |
|
| 1978 |
Lonsdale-Eccles JD, Neurath H, Walsh KA. Probes of the mechanism of zymogen catalysis. Biochemistry. 17: 2805-9. PMID 687564 DOI: 10.1021/Bi00607A016 |
0.494 |
|
| 1978 |
Kerr MA, Grahn DT, Walsh KA, Neurath H. Activation of bovine factor X (Stuart factor)--analogy with pancreatic zymogen-enzyme systems. Biochemistry. 17: 2645-8. PMID 678535 DOI: 10.1021/Bi00606A029 |
0.499 |
|
| 1978 |
Woodbury RG, Katunuma N, Kobayashi K, Titani K, Neurath H, Anderson WF, Matthews BW. Covalent structure of a group-specific protease from rat small intestine. Appendix: crystallographic data for a group specific protease from rat intestine. Biochemistry. 17: 811-9. PMID 629933 DOI: 10.1021/Bi00598A010 |
0.366 |
|
| 1978 |
Woodbury RG, Everitt M, Sanada Y, Katunuma N, Lagunoff D, Neurath H. A major serine protease in rat skeletal muscle: evidence for its mast cell origin. Proceedings of the National Academy of Sciences of the United States of America. 75: 5311-3. PMID 103093 DOI: 10.1073/Pnas.75.11.5311 |
0.349 |
|
| 1977 |
de Haën C, Walsh KA, Neurath H. Isolation and amino-terminal sequence analysis of a new pancreatic trypsinogen of the African lungfish Protopterus aethiopicus. Biochemistry. 16: 4421-5. PMID 911766 |
0.48 |
|
| 1977 |
Anderson LE, Walsh KA, Neurath H. Bovine enterokinase. Purification, specificity, and some molecular properties. Biochemistry. 16: 3354-60. PMID 889800 DOI: 10.1021/Bi00634A011 |
0.542 |
|
| 1977 |
Alter GM, Leussing DL, Neurath H, Vallee BL. Kinetic properties of carboxypeptidase B in solutions and crystals. Biochemistry. 16: 3663-8. PMID 560863 DOI: 10.1021/Bi00635A024 |
0.308 |
|
| 1977 |
Titani K, Koide A, Hermann J, Ericsson LH, Kumar S, Wade RD, Walsh KA, Neurath H, Fischer EH. Complete amino acid sequence of rabbit muscle glycogen phosphorylase. Proceedings of the National Academy of Sciences of the United States of America. 74: 4762-6. PMID 270711 DOI: 10.1073/Pnas.74.11.4762 |
0.527 |
|
| 1976 |
Hass GM, Ako H, Grahn DT, Neurath H. Carboxypeptidase inhibitor from potatoes. The effects of chemical modifications on inhibitory activity. Biochemistry. 15: 93-100. PMID 1247515 DOI: 10.1021/Bi00646A015 |
0.371 |
|
| 1976 |
Neurath H, Walsh KA. Role of proteolytic enzymes in biological regulation (a review). Proceedings of the National Academy of Sciences of the United States of America. 73: 3825-32. PMID 1069267 DOI: 10.1073/Pnas.73.11.3825 |
0.532 |
|
| 1976 |
Kerr MA, Walsh KA, Neurath H. A proposal for the mechanism of chymotrypsinogen activation. Biochemistry. 15: 5566-70. PMID 999829 DOI: 10.1021/Bi00670A022 |
0.43 |
|
| 1976 |
Pangburn MK, Levy PL, Walsh KA, Neurath H. Thermal stability of homologous neutral metalloendopeptidases in thermophilic and mesophilic bacteria: structural considerations. Experientia. Supplementum. 26: 19-30. PMID 820564 |
0.443 |
|
| 1976 |
Kuhn RW, Walsh KA, Neurath H. Reaction of yeast carboxypeptidase C1 with group-specific reagents. Biochemistry. 15: 4881-5. PMID 10962 DOI: 10.1021/Bi00667A020 |
0.519 |
|
| 1975 |
Kerr MA, Walsh KA, Neurath H. Catalysis by serine proteases and their zymogens. A study of acyl intermediates by circular dichroism. Biochemistry. 14: 5088-94. PMID 1238107 DOI: 10.1021/Bi00694A010 |
0.507 |
|
| 1975 |
Zwilling R, Neurath H, Ericsoon LH, Enfield DL. The amino-terminal sequence of an invertebrate trypsin (crayfish Astacus leptodactylus): homology with other serine proteases. Febs Letters. 60: 247-9. PMID 1227963 DOI: 10.1016/0014-5793(75)80723-X |
0.364 |
|
| 1975 |
de Haën C, Neurath H, Teller DC. The phylogeny of trypsin-related serine proteases and their zymogens. New methods for the investigation of distant evolutionary relationships. Journal of Molecular Biology. 92: 225-59. PMID 1142424 DOI: 10.1016/0022-2836(75)90225-9 |
0.384 |
|
| 1975 |
Titani K, Cohen P, Walsh KA, Neurath H. Amino-terminal sequence of rabbit muscle phosphorylase. Febs Letters. 55: 120-3. PMID 1140412 DOI: 10.1016/0014-5793(75)80974-4 |
0.477 |
|
| 1975 |
Titani K, Ericsson LH, Neurath H, Walsh KA. Amino acid sequence of dogfish trypsin. Biochemistry. 14: 1358-66. PMID 1092332 DOI: 10.1021/Bi00678A003 |
0.57 |
|
| 1975 |
Titani K, Fujikawa K, Enfield DL, Ericsson LH, Walsh KA, Neurath H. Bovine factor X1 (Stuart factor): amino-acid sequence of heavey chain. Proceedings of the National Academy of Sciences of the United States of America. 72: 3082-6. PMID 1059093 DOI: 10.1073/Pnas.72.8.3082 |
0.538 |
|
| 1975 |
Titani K, Ericsson LH, Walsh KA, Neurath H. Amino-acid sequence of bovine carboxypeptidase B. Proceedings of the National Academy of Sciences of the United States of America. 72: 1666-70. PMID 1057162 DOI: 10.1073/Pnas.72.5.1666 |
0.546 |
|
| 1975 |
Enfield DL, Ericsson LH, Blum HE, Fischer EH, Neurath H. Amino-acid sequence of parvalbumin from rabbit skeletal muscle. Proceedings of the National Academy of Sciences of the United States of America. 72: 1309-13. PMID 1055405 DOI: 10.1073/Pnas.72.4.1309 |
0.359 |
|
| 1975 |
Enfield DL, Ericsson LH, Walsh KA, Neurath H, Titani K. Bovine factor X1 (Stuart factor). Primary structure of the light chain. Proceedings of the National Academy of Sciences of the United States of America. 72: 16-9. PMID 1054492 DOI: 10.1073/Pnas.72.1.16 |
0.518 |
|
| 1975 |
Levy PL, Pangburn MK, Burstein Y, Ericsson LH, Neurath H, Walsh KA. Evidence of homologous relationship between thermolysin and neutral protease A of Bacillus subtilis. Proceedings of the National Academy of Sciences of the United States of America. 72: 4341-5. PMID 812093 DOI: 10.1073/Pnas.72.11.4341 |
0.557 |
|
| 1975 |
Gertler A, Walsh K, Neurath H. Corrections - Catalysis by Chymotrypsinogen. Demonstration of an Acyl-Zymogen Intermediate Biochemistry. 14: 196-196. DOI: 10.1021/Bi00672A602 |
0.454 |
|
| 1974 |
Gertler A, Walsh KA, Neurath H. Catalysis by chymotrypsinogen. Demonstration of an acyl-zymogen intermediate. Biochemistry. 13: 1302-10. PMID 4856029 DOI: 10.1021/Bi00703A038 |
0.474 |
|
| 1974 |
Burstein Y, Walsh KA, Neurath H. Evidence of an essential histidine residue in thermolysin. Biochemistry. 13: 205-10. PMID 4808703 DOI: 10.1021/Bi00698A030 |
0.471 |
|
| 1974 |
Kuhn RW, Walsh KA, Neurath H. Isolation and partial characterization of an acid carboxypeptidase from yeast. Biochemistry. 13: 3871-7. PMID 4606695 DOI: 10.1021/Bi00716A008 |
0.485 |
|
| 1974 |
Enfield DL, Ericsson LH, Fujikawa K, Titani K, Walsh KA, Neurath H. Bovine factor IX (Christmas factor). Further evidence of homology with factor X (Stuart factor) and prothrombin. Febs Letters. 47: 132-5. PMID 4473377 DOI: 10.1016/0014-5793(74)80442-4 |
0.403 |
|
| 1974 |
Morgan PH, Walsh KA, Neurath H. Inactivation of trypsinogen by methane sulfonyl fluoride. Febs Letters. 41: 108-10. PMID 4368804 DOI: 10.1016/0014-5793(74)80965-8 |
0.511 |
|
| 1974 |
Gertler A, Walsh KA, Neurath H. Catalysis by chymotrypsinogen: Increased reactivity due to oxidation of methionine 192 Febs Letters. 38: 157-160. DOI: 10.1016/0014-5793(74)80103-1 |
0.402 |
|
| 1973 |
Hermodson MA, Ericsson LH, Neurath H, Walsh KA. Determination of the amino acid sequence of porcine trypsin by sequenator aalysis. Biochemistry. 12: 3146-53. PMID 4738933 DOI: 10.1021/Bi00741A002 |
0.517 |
|
| 1973 |
Robinson NC, Neurath H, Walsh KA. Preparation and characterization of guanidinated trypsinogen and -guanidinated trypsin. Biochemistry. 12: 414-20. PMID 4734231 DOI: 10.1021/Bi00727A009 |
0.453 |
|
| 1973 |
Robinson NC, Neurath H, Walsh KA. The relation of the -amino group of trypsin to enzyme function and zymogen activation. Biochemistry. 12: 420-6. PMID 4683488 DOI: 10.1021/Bi00727A010 |
0.517 |
|
| 1973 |
Pangburn MK, Burstein Y, Morgan PH, Walsh KA, Neurath H. Affinity chromatography of thermolysin and of neutral proteases from B. subtilis. Biochemical and Biophysical Research Communications. 54: 371-9. PMID 4200397 DOI: 10.1016/0006-291X(73)90932-7 |
0.456 |
|
| 1972 |
Matthews BW, Colman PM, Jansonius JN, Titani K, Walsh KA, Neurath H. Structure of thermolysin. Nature: New Biology. 238: 41-3. PMID 18663850 DOI: 10.1038/Newbio238041A0 |
0.444 |
|
| 1972 |
Titani K, Hermodson MA, Ericsson LH, Walsh KA, Neurath H. Amino-acid sequence of thermolysin. Nature: New Biology. 238: 35-7. PMID 18663848 DOI: 10.1038/Newbio238035A0 |
0.512 |
|
| 1972 |
Reeck GR, Neurath H. Isolation and characterization of pancreatic procarboxypeptidase B and carboxypeptidase B of the African lungfish. Biochemistry. 11: 3947-55. PMID 5079891 DOI: 10.1021/Bi00771A018 |
0.576 |
|
| 1972 |
Titani K, Hermodson MA, Ericsson LH, Walsh KA, Neurath H. Amino acid sequence of thermolysin. Isolation and characterization of the fragments obtained by cleavage with cyanogen bromide. Biochemistry. 11: 2427-35. PMID 5040648 DOI: 10.1021/Bi00763A007 |
0.525 |
|
| 1972 |
Reeck GR, Neurath H. Pancreatic trypsinogen from the African lungfish. Biochemistry. 11: 503-10. PMID 5011961 DOI: 10.1021/Bi00754A004 |
0.563 |
|
| 1972 |
Hermodson MA, Ericsson LH, Titani K, Neurath H, Walsh KA. Application of sequenator analyses to the study of proteins. Biochemistry. 11: 4493-502. PMID 4675874 DOI: 10.1021/Bi00774A011 |
0.436 |
|
| 1972 |
Hermodson MA, Kuhn RW, Walsh KA, Neurath H, Eriksen N, Benditt EP. Amino acid sequence of monkey amyloid protein A. Biochemistry. 11: 2934-8. PMID 4625315 DOI: 10.1021/Bi00766A002 |
0.512 |
|
| 1972 |
Morgan PH, Robinson NC, Walsh KA, Neurath H. Inactivation of bovine trypsinogen and chymotrypsinogen by diisopropylphosphorofluoridate. Proceedings of the National Academy of Sciences of the United States of America. 69: 3312-6. PMID 4508324 DOI: 10.1073/Pnas.69.11.3312 |
0.529 |
|
| 1972 |
Titani K, Hermodson MA, Fujikawa K, Ericsson LH, Walsh KA, Neurath H, Davie EW. Bovine factor X 1a (activated Stuart factor). Evidence of homology with mammalian serine proteases. Biochemistry. 11: 4899-903. PMID 4264286 DOI: 10.1021/Bi00776A004 |
0.437 |
|
| 1971 |
Hermodson MA, Tye RW, Reeck GR, Neurath H, Walsh KA. Comparison of the amino terminal sequences of bovine, dogfish, and lungfish trypsinogens. Febs Letters. 14: 222-224. PMID 11945763 DOI: 10.1016/0014-5793(71)80622-1 |
0.689 |
|
| 1971 |
Robinson NC, Tye RW, Neurath H, Walsh KA. Isolation of trypsins by affinity chromatography Biochemistry. 10: 2743-2747. PMID 5558697 DOI: 10.1021/Bi00790A014 |
0.446 |
|
| 1971 |
Reeck GR, Walsh KA, Hermodson MA, Neurath H. New forms of bovine carboxypeptidase B and their homologous relationships to carboxypeptidase A Proceedings of the National Academy of Sciences of the United States of America. 68: 1226-1230. PMID 5288370 DOI: 10.1073/Pnas.68.6.1226 |
0.717 |
|
| 1971 |
P?tra PH, Hermodson MA, Walsh KA, Neurath H. Characterization of bovine carboxypeptidase A (Allan). Biochemistry. 10: 4023-5. PMID 5143102 DOI: 10.1021/Bi00798A600 |
0.478 |
|
| 1971 |
Reeck GR, Walsh KA, Neurath H. Isolation and characterization of carboxypeptidases A and B from activated pancreatic juice. Biochemistry. 10: 4690-8. PMID 5140186 DOI: 10.1021/Bi00801A015 |
0.663 |
|
| 1971 |
Bradshaw RA, Walsh KA, Neurath H. Amino acid sequence of bovine carboxypeptidase A. Isolation and characterization of the thermolytic peptides of the cyanogen bromide fragment F-I. Biochemistry. 10: 951-61. PMID 5102490 |
0.597 |
|
| 1971 |
Bradshaw RA, Walsh KA, Neurath H. Amino acid sequence of bovine carboxypeptidase A. Tryptic and chymotryptic peptides of the cyanogen bromide fragment F-I. Biochemistry. 10: 938-50. PMID 5102489 DOI: 10.1021/Bi00782A004 |
0.627 |
|
| 1971 |
Bradshaw RA, Walsh KA, Neurath H. Amino acid sequence of bovine carboxypeptidase A. Isolation and characterization of selected peptic and nagarse peptides and the complete sequence of fragment F-I. Biochemistry. 10: 961-72. PMID 4927805 |
0.598 |
|
| 1971 |
Hermodson MA, Tye RW, Reeck GR, Neurath H, Walsh KA. Comparison of the amino terminal sequences of bovine, dogfish, and lungfish trypsinogens Febs Letters. 14: 222-224. DOI: 10.1016/0014-5793(71)80622-1 |
0.602 |
|
| 1970 |
Neurath H, Walsh KA, Bradshaw RA. Enzymes in crystals. Nature. 225: 881. PMID 16056793 DOI: 10.1038/225881B0 |
0.586 |
|
| 1970 |
Radhakrishnan TM, Bradshaw RA, Deranleau DA, Neurath H. The solution conformation of bovine carboxypeptidase a: Reaction with 2-hydroxy-5-nitrobenzyl bromide and N-methylnicotinamide chloride. Febs Letters. 7: 72-76. PMID 11947434 DOI: 10.1016/0014-5793(70)80621-4 |
0.685 |
|
| 1970 |
Reeck GR, Winter WP, Neurath H. Pancreatic enzymes of the African lungfish protopterus aethiopicus Biochemistry. 9: 1398-1403. PMID 5418375 DOI: 10.1021/Bi00808A014 |
0.606 |
|
| 1970 |
Arnon R, Neurath H. Immunochemical studies on bovine trypsin and trypsinogen derivatives Immunochemistry. 7: 241-248,IN1-IN2,249-. PMID 4986003 DOI: 10.1016/0019-2791(70)90161-8 |
0.344 |
|
| 1970 |
Bradshaw RA, Neurath H, Tye RW, Walsh KA, Winter WP. Comparison of the partial amino-acid sequence of dogfish trypsinogen with bovine trypsinogen. Nature. 226: 237-9. PMID 4908582 DOI: 10.1038/226237A0 |
0.647 |
|
| 1970 |
Walsh KA, Ericsson LH, Bradshaw RA, Neurath H. Chemical evidence of a disulfide bond in bovine carboxypeptidase A. Biochemistry. 9: 219-25. PMID 4904866 DOI: 10.1021/Bi00804A005 |
0.57 |
|
| 1970 |
Neurath H, Bradshaw RA, Pétra PH, Walsh KA. 3. Carboxypeptidase. Bovine carboxypeptidase A--activation, chemical structure and molecular heterogeneity. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 257: 159-76. PMID 4399044 DOI: 10.1098/Rstb.1970.0019 |
0.619 |
|
| 1969 |
Pétra PH, Bradshaw RA, Walsh KA, Neurath H. Identification of the amino acid replacements characterizing the allotypic forms of bovine carboxypeptidase A. Biochemistry. 8: 2762-8. PMID 5817619 DOI: 10.1021/Bi00835A011 |
0.627 |
|
| 1969 |
Nomoto M, Srinivasan NG, Bradshaw RA, Wade RD, Neurath H. The amino acid sequence of bovine carboxypeptidase A. I. Preparation and properties of the fragments obtained by cyanogen bromide cleavage. Biochemistry. 8: 2755-62. PMID 5817618 DOI: 10.1021/Bi00835A010 |
0.561 |
|
| 1969 |
Radhakrishnan TM, Russo SF, Walsh KA, Neurath H. The inhibition of trypsinogen activation by low concentrations of urea Archives of Biochemistry and Biophysics. 130: 326-331. PMID 5778649 DOI: 10.1016/0003-9861(69)90040-X |
0.498 |
|
| 1969 |
Radhakrishnan TM, Walsh KA, Neurath H. The promotion of activation of bovine trypsinogen by specific modification of aspartyl residues Biochemistry. 8: 4020-4027. PMID 5388145 DOI: 10.1021/Bi00838A019 |
0.497 |
|
| 1969 |
Bradshaw RA, Babin DR, Nomoto M, Srinivasin NG, Ericsson LH, Walsh KA, Neurath H. The amino acid sequence of bovine carboxypeptidase A. II. Tryptic and chymotryptic peptides of the cyanogen bromide fragment F-III. Biochemistry. 8: 3859-71. PMID 5387531 |
0.585 |
|
| 1969 |
Arnon R, Neurath H. An immunological approach to the study of evolution of trypsins Proceedings of the National Academy of Sciences of the United States of America. 64: 1323-1328. PMID 5271755 DOI: 10.1073/Pnas.64.4.1323 |
0.328 |
|
| 1969 |
Bradshaw RA, Ericsson LH, Walsh KA, Neurath H. The amino acid sequence of bovine carboxypeptidase A. Proceedings of the National Academy of Sciences of the United States of America. 63: 1389-94. PMID 5260942 DOI: 10.1073/Pnas.63.4.1389 |
0.633 |
|
| 1969 |
Bradshaw RA, Neurath H, Walsh KA. Considerations of the concept of structural homology as applied to bovine carboxypeptidases A and B. Proceedings of the National Academy of Sciences of the United States of America. 63: 406-11. PMID 5257130 DOI: 10.1073/Pnas.63.2.406 |
0.651 |
|
| 1968 |
Kenner RA, Walsh KA, Neurath H. The reaction of tyrosyl residues of bovine trypsin and trypsinogen with tetranitromethane Biochemical and Biophysical Research Communications. 33: 353-360. PMID 5749171 DOI: 10.1016/0006-291X(68)90577-9 |
0.486 |
|
| 1968 |
Winter WP, Walsh KA, Neurath H. Homology as applied to proteins Science. 162: 1433. PMID 5700064 DOI: 10.1126/Science.162.3861.1433 |
0.447 |
|
| 1968 |
Neurath H, Bradshaw RA, Ericsson LH, Babin DR, Petra PH, Walsh KA. Current status of the chemical structure of bovine pancreatic carboxypeptidase A. Brookhaven Symposia in Biology. 21: 1-23. PMID 4891792 |
0.541 |
|
| 1967 |
Freisheim JH, Walsh KA, Neurath H. The activation of bovine procarboxypeptidase A. II. Mechanism of activation of the succinylated enzyme precursor Biochemistry. 6: 3020-3028. PMID 6069858 DOI: 10.1021/Bi00862A008 |
0.492 |
|
| 1967 |
Freisheim JH, Walsh KA, Neurath H. The activation of bovine procarboxypeptidase A. I. Isolation and properties of the succinylated enzyme precursor Biochemistry. 6: 3010-3019. PMID 6069857 DOI: 10.1021/Bi00862A007 |
0.51 |
|
| 1967 |
Radhakrishnan TM, Walsh KA, Neurath H. Relief by modification of carboxylate groups of the calcium requirement for the activation of trypsinogen [8] Journal of the American Chemical Society. 89: 3059-3061. PMID 6043820 DOI: 10.1021/Ja00988A052 |
0.435 |
|
| 1967 |
Neurath H, Walsh KA, Winter WP. Evolution of structure and function of proteases Science. 158: 1638-1644. PMID 4862530 DOI: 10.1126/Science.158.3809.1638 |
0.508 |
|
| 1966 |
Prahl JW, Neurath H. Pancreatic enzymes of the spiny pacific dogfish. I. Cationic chymotrypsinogen and chymotrypsin Biochemistry. 5: 2131-2146. PMID 5963456 DOI: 10.1021/Bi00870A047 |
0.304 |
|
| 1966 |
McClure WO, Neurath H. The reaction of carboxypeptidase A with chromophoric substrates. Biochemistry. 5: 1425-38. PMID 5958218 DOI: 10.1021/Bi00868A041 |
0.593 |
|
| 1966 |
Deranleau DA, Neurath H. The combination of chymotrypsin and chymotrypsinogen with fluorescent substrates and inhibitors for chymotrypsin Biochemistry. 5: 1413-1425. PMID 5958217 DOI: 10.1021/Bi00868A040 |
0.616 |
|
| 1966 |
Walsh KA, Ericsson LH, Neurath H. Bovine carboxypeptidase A variants resulting from allelomorphism Proceedings of the National Academy of Sciences of the United States of America. 56: 1339-1344. PMID 5230156 DOI: 10.1073/Pnas.56.4.1339 |
0.44 |
|
| 1966 |
Prahl J, Neurath H. CORRECTION-Pancreatic Enzymes The Spiny Pacific Dogfish I. Cationic Chymotrypsinogen and Chymotrypsin Biochemistry. 5: 2483-2483. DOI: 10.1021/Bi00871A045 |
0.302 |
|
| 1964 |
MCCLURE WO, NEURATH H, WALSH KA. THE REACTION OF CARBOXYPEPTIDASE A WITH HIPPURYL-DL-BETA-PHENYLLACTATE. Biochemistry. 3: 1897-901. PMID 14269307 DOI: 10.1021/Bi00900A019 |
0.63 |
|
| 1964 |
BARGETZI JP, THOMPSON EO, SAMPATHKUMAR KS, WALSH KA, NEURATH H. THE AMINO- AND CARBOXYL-TERMINAL RESIDUES AND THE SELF-DIGESTION OF The Journal of Biological Chemistry. 239: 3767-3774. PMID 14257605 |
0.404 |
|
| 1964 |
Kumar KSVS, Walsh KA, Neurath H. Chemical characterization of bovine carboxypeptidase A isolated from a single pancreas Biochemistry. 3: 1726-1727. PMID 14235338 |
0.38 |
|
| 1964 |
WALSH KA, NEURATH H. TRYPSINOGEN AND CHYMOTRYPSINOGEN AS HOMOLOGOUS PROTEINS Proceedings of the National Academy of Sciences of the United States Of. 52: 884-889. PMID 14224394 DOI: 10.1073/Pnas.52.4.884 |
0.451 |
|
| 1964 |
WALSH KA, KAUFFMAN DL, KUMAR KS, NEURATH H. ON THE STRUCTURE AND FUNCTION OF BOVINE TRYPSINOGEN AND TRYPSIN Proceedings of the National Academy of Sciences of the United States Of. 51: 301-308. PMID 14124328 DOI: 10.1073/Pnas.51.2.301 |
0.44 |
|
| 1964 |
Cox DJ, Bovard FC, Bargetzi JP, Walsh KA, Neurath H. Procedures for the isolation of crystalline bovine pancreatic carboxypeptidase A. II. Isolation of carboxypeptidase Aα from procarboxypeptidase A Biochemistry. 3: 44-47. PMID 14114502 DOI: 10.1021/Bi00889A008 |
0.442 |
|
| 1964 |
Bargetzi J, Sampath Kumar KS, Cox D, Walsh K, Neurath H. Corrections - The Amino Acid Composition of Bovine Pancreatic Carboxypeptidase A. Biochemistry. 3: 469-469. DOI: 10.1021/Bi00891A605 |
0.489 |
|
| 1963 |
Kumar KSVS, Walsh KA, Bargetzi JP, Neurath H. Chemical relationships among various forms of bovine pancreatic carboxypeptidase A Biochemistry. 2: 1475-1479. PMID 14093929 |
0.375 |
|
| 1963 |
Bargetzi JP, Kumar KSVS, Cox DJ, Walsh KA, Neurath H. The amino acid composition of bovine pancreatic carboxypeptidase A Biochemistry. 2: 1468-1474. PMID 14093928 DOI: 10.1021/Bi00906A046 |
0.491 |
|
| 1962 |
WALSH KA, SAMPATH KUMAR KS, BARGETZI JP, NEURATH H. Approaches to the selective chemical labeling of the active site of carboxypepticase A Proceedings of the National Academy of Sciences of the United States of America. 48: 1443-1449. PMID 14004737 DOI: 10.1073/Pnas.48.8.1443 |
0.436 |
|
| 1962 |
Walsh KA, Kauffman DL, Neurath H. The amino terminal sequence of bovine trypsinogen Biochemistry. 1: 893-898. PMID 13998642 DOI: 10.1021/Bi00911A023 |
0.514 |
|
| 1962 |
Walsh KA, Kauffman DL, Neurath H. Peptides isolated from tryptic and chymotrypic hydrolysates of S-sulfo-trypsinogen Bba - Biochimica Et Biophysica Acta. 65: 540-543. PMID 13998641 DOI: 10.1016/0006-3002(62)90468-7 |
0.45 |
|
| 1961 |
BROWN JR, COX DJ, GREENSHIELDS RN, WALSH KA, YAMASAKI M, NEURATH H. The chemical structure and enzymatic functions of bovine procarboxypeptidase A Proceedings of the National Academy of Sciences of the United States of America. 47: 1554-1560. PMID 13873678 DOI: 10.1073/Pnas.47.10.1554 |
0.451 |
|
| 1959 |
NEURATH H, HARTLEY BS. The hydrolysis of peptide and ester bonds by proteolytic enzymes. Journal of Cellular and Comparative Physiology. 54: 179-202. PMID 14426720 DOI: 10.1002/Jcp.1030540414 |
0.315 |
|
| 1959 |
Neurath H. Protein structure and enzyme action Reviews of Modern Physics. 31: 185-190. DOI: 10.1103/Revmodphys.31.185 |
0.327 |
|
| 1958 |
Dixon GH, Kauffman DL, Neurath H. AMINO ACID SEQUENCE IN THE REGION OF DIISOPROPYL PHOSPHORYL BINDING IN DIP-TRYPSIN Journal of the American Chemical Society. 80: 1260-1261. DOI: 10.1021/Ja01538A059 |
0.33 |
|
| 1957 |
Neurath H. The Activation of Zymogens Advances in Protein Chemistry. 12: 319-386. DOI: 10.1016/S0065-3233(08)60119-9 |
0.344 |
|
| 1956 |
DREYER WJ, NEURATH H, RUPLEY JA. Structural changes in the activation of chymotrypsinogen and trypsinogen; effect of urea on chymotrypsinogen and delta-chymotrypsin. Archives of Biochemistry and Biophysics. 65: 243-59. PMID 13373422 DOI: 10.1016/0003-9861(56)90191-6 |
0.565 |
|
| 1956 |
Dixon GH, Dreyer WJ, Neurath H. THE REACTION OF p-NITROPHENYL ACETATE WITH CHYMOTRYPSIN1 Journal of the American Chemical Society. 78: 4810-4810. DOI: 10.1021/Ja01599A071 |
0.517 |
|
| 1955 |
DREYER WJ, NEURATH H. The activation of chymotrypsinogen; isolation and identification of a peptide liberated during activation. The Journal of Biological Chemistry. 217: 527-39. PMID 13271414 |
0.51 |
|
| 1955 |
DREYER WJ, WADE RD, NEURATH H. Observations on the electrophoretic and ultracentrifugal changes accompanying the activation of chymotrypsinogen. Archives of Biochemistry and Biophysics. 59: 145-56. PMID 13269165 DOI: 10.1016/0003-9861(55)90471-9 |
0.554 |
|
| 1955 |
RUPLEY JA, DREYER WJ, NEURATH H. Structural changes in the activation of chymotrypsinogen. Biochimica Et Biophysica Acta. 18: 162-3. PMID 13260271 DOI: 10.1016/0006-3002(55)90036-6 |
0.533 |
|
| 1955 |
Neurath H, Dreyer WJ. Mechanism of activation of trypsinogen and chymotrypsinogen Discussions of the Faraday Society. 20: 32-43. DOI: 10.1039/Df9552000032 |
0.532 |
|
| 1955 |
Dreyer WJ, Neurath H. THE ACTIVATION OF CHYMOTRYPSINOGEN Journal of the American Chemical Society. 77: 814-815. DOI: 10.1021/Ja01608A097 |
0.537 |
|
| 1951 |
Neurath H. Amino acids and proteins, Cold Spring Harbor symposia on quantitative biology. Vol. 14 Archives of Biochemistry and Biophysics. 31: 465. DOI: 10.1016/0003-9861(51)90171-3 |
0.328 |
|
| 1949 |
KAUFMAN S, NEURATH H. The effect of methanol on the hydrolysis of acetyl-L-tyrosinamide by chymotrypsin. The Journal of Biological Chemistry. 180: 181-7. PMID 18133384 |
0.412 |
|
| 1949 |
KAUFMAN S, NEURATH H. Structural requirements of specific substrates for chymotrypsin; an analysis of the contribution of the structural components to enzymatic hydrolysis. Archives of Biochemistry. 21: 437-53. PMID 18126330 |
0.464 |
|
| 1949 |
KAUFMAN S, NEURATH H. Inhibition of chymotrypsin by structural analogs of specific substrates. Archives of Biochemistry. 21: 245. PMID 18124510 |
0.466 |
|
| 1949 |
KAUFMAN S, NEURATH H, SCHWERT GW. The specific peptidase and esterase activities of chymotrypsin. The Journal of Biological Chemistry. 177: 793-814. PMID 18110457 |
0.475 |
|
| 1949 |
KAUFMAN S, NEURATH H. Structural requirements of specific inhibitors for alpha-chymotrypsin. The Journal of Biological Chemistry. 181: 623-33. PMID 15393781 |
0.424 |
|
| 1948 |
KAUFMAN S, SCHWERT GW, NEURATH H. The specific peptidase and esterase activities of chymotrypsin. Archives of Biochemistry. 17: 203-5. PMID 18910698 |
0.475 |
|
| 1947 |
NEURATH H, VOLKIN E. Biologic false positive reactions in serologic tests for syphilis; preparation and properties of serologically active serum globulin fractions obtained by fractional precipitation with ammonium sulfate. American Journal of Syphilis, Gonorrhea, and Venereal Diseases. 31: 347-73. PMID 20344061 |
0.612 |
|
| 1947 |
NEURATH H, VOLKIN E, CRAIG HW. A preliminary survey analysis with the euglobulin-inhibition method for the serologic diagnosis of syphilis. Federation Proceedings. 6: 431. PMID 20343915 |
0.565 |
|
| 1947 |
NEURATH H, VOLKIN E. Biologic false positive reactions in serologic tests for syphilis; a preliminary survey analysis with the euglobulin-inhibition method for the serologic differentiation between true and biologic false positive reactions. American Journal of Syphilis, Gonorrhea, and Venereal Diseases. 31: 436-56. PMID 20253130 |
0.592 |
|
| 1947 |
VOLKIN E, NEURATH H, CRAIG HW. Biologic false positive reactions in serologic tests for syphilis; quantitative aspects of the inhibition phenomenon. American Journal of Syphilis, Gonorrhea, and Venereal Diseases. 31: 413-35. PMID 20253129 |
0.59 |
|
| 1947 |
VOLKIN E, NEURATH H. Biologic false positive reactions in serologic tests for syphilis; preparation and properties of serum protein fractions which inhibit biologic false positive reactions. American Journal of Syphilis, Gonorrhea, and Venereal Diseases. 31: 397-412. PMID 20253128 |
0.608 |
|
| 1947 |
NEURATH H, VOLKIN E. Biologic false positive reactions in serologic tests for syphilis. American Journal of Syphilis, Gonorrhea, and Venereal Diseases. 31: 347-468. PMID 20253126 |
0.584 |
|
| 1946 |
NEURATH H, VOLKIN E, CRAIG HW. False positive reactions in serologic tests for syphilis; nature and mechanism of selective inhibition by a heat-stable serum component. Federation Proceedings. 5: 250. PMID 21064606 |
0.582 |
|
| 1946 |
PUTNAM FW, NEURATH H. Chemical and enzymatic properties of crystalline carboxypeptidase. The Journal of Biological Chemistry. 166: 603-19. PMID 20276175 |
0.401 |
|
| 1945 |
NEURATH H, PUTNAM FW. Interaction between proteins and synthetic detergents; molecular-kinetic studies of serum albumin-sodium dodecyl sulfate mixtures. The Journal of Biological Chemistry. 160: 397-408. PMID 21004547 |
0.418 |
|
| 1945 |
Neurath H, Volkin E, Erickson JO, Putnam FW, Craig HW, Cooper GR, Sharp DG, Taylor AR, Beard JW. THE SEROLOGICAL DIAGNOSIS OF SYPHILIS. Science (New York, N.Y.). 101: 68-9. PMID 17840923 DOI: 10.1126/Science.101.2612.68 |
0.655 |
|
| 1944 |
Putnam FW, Neurath H. STOICHIOMETRIC COMPLEXES OF SERUM ALBUMIN AND SODIUM DODECYL SULFATE Journal of the American Chemical Society. 66: 1992-1992. DOI: 10.1021/Ja01239A514 |
0.446 |
|
| 1944 |
Putnam FW, Neurath H. The Precipitation of Proteins by Synthetic Detergents1a Journal of the American Chemical Society. 66: 692-697. DOI: 10.1021/Ja01233A009 |
0.471 |
|
| 1944 |
Neurath H, Greenstein JP, Putnam FW, Erickson JO. The chemistry of protein denaturation Chemical Reviews. 34: 157-265. DOI: 10.1021/Cr60108A003 |
0.477 |
|
| 1943 |
Martin DS, Erickson JO, Putnam FW, Neurath H. NATIVE AND REGENERATED BOVINE ALBUMIN : II. IMMUNOLOGICAL PROPERTIES. The Journal of General Physiology. 26: 533-9. PMID 19873365 |
0.426 |
|
| 1943 |
Putnam FW, Erickson JO, Volkin E, Neurath H. NATIVE AND REGENERATED BOVINE ALBUMIN : I. PREPARATION AND PHYSICOCHEMICAL PROPERTIES. The Journal of General Physiology. 26: 513-31. PMID 19873364 DOI: 10.1085/Jgp.26.6.513 |
0.667 |
|
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