Publications from the Walsh / Neurath Groups 1952 - 1979
sorted by year : author
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1952 - 1979     1980 - present 
1979   ___________________________________________________   1979
Everitt, M. T., and Neurath, H. (1979). Purification and partial characterization of an alpha-chymotrypsin-like protease of rat peritoneal mast cells. Biochimie 61, 653-62.

Katayama, K., Ericsson, L. H., Enfield, D. L., Walsh, K. A., Neurath, H., Davie, E. W., and Titani, K. (1979). Comparison of amino acid sequence of bovine coagulation Factor IX (Christmas Factor) with that of other vitamin K-dependent plasma proteins. Proc. Natl. Acad. Sci. USA 76, 4990-4. [Medline]

Leary, T. R., Grahn, D. T., Neurath, H., and Hass, G. M. (1979). Structure of potato carboxypeptidase inhibitor: disulfide pairing and exposure of aromatic residues. Biochemistry 18, 2252-6.

Levine, A. E., and Walsh, K. A. (1979). Involvement of an acrosin-like enzyme in the acrosome reaction of sea urchin sperm. Dev. Biol. 72, 126-37. [Medline]

Londsdale Eccles, J. D., Kerr, M. A., Walsh, K. A., and Neurath, H. (1979). Catalysis by zymogens: increased reactivity at high ionic strength. FEBS Lett. 100, 157-60.

Maloy, W. L., Bowien, B. U., Zwolinski, G. K., Kumar, K. G., Wood, H. G., Ericsson, L. H., and Walsh, K. A. (1979). Amino acid sequence of the biotinyl subunit from transcarboxylase. J. Biol. Chem. 254, 11615-22. [Medline]

Neurath, H. (1979). Limited proteolysis--an overview. pp. 1-3. In: Cohen GN, Holzer H, ed. Limited proteolysis in microorganisms. Bethesda, DHEW/NIH.

Neurath, H., and Garson, L. (1979). Computer system for Biochemistry. Biochemistry 18, 5035-7.

Soderling, T. R., Sheorain, V. S., and Ericsson, L. H. (1979). Phosphorylation of glycogen synthase by phosphorylase kinase: stoichiometry, specificity and site of phosphorylation. FEBS Lett. 106, 181-4.

Zwilling, R., Jakob, F., Bauer, H., Neurath, H., and Enfield, D. L. (1979). Crayfish carboxypeptidase. Affinity chromatography, characterization and amino-terminal sequence. European Journal Of Biochemistry 94, 223-9. 

1978   ___________________________________________________   1978
Gagnon, J., Palmiter, R. D., and Walsh, K. A. (1978). Comparison of the NH2-terminal sequence of ovalbumin as synthesized in vitro and in vivo. J. Biol. Chem. 253, 7464-8.

Hermann, J., Titani, K., Ericsson, L. H., Wade, R. D., Neurath, H., and Walsh, K. A. (1978). Amino acid sequence of two cyanogen bromide fragments of glycogen phosphorylase. Biochemistry 17, 5672-9.

Holcenberg, J. S., Ericsson, L., and Roberts, J. (1978). Amino acid sequence of the diazooxonorleucine binding site of Acinetobacter and Pseudomonas 7A glutaminase--asparaginase enzymes. Biochemistry 17, 411-7.

Kerr, M. A., Grahn, D. T., Walsh, K. A., and Neurath, H. (1978). Activation of bovine factor X (Stuart factor)--analogy with pancreatic zymogen-enzyme systems. Biochemistry 17, 2645-8.

Koide, A., Titani, K., Ericsson, L. H., Kumar, S., Neurath, H., and Walsh, K. A. (1978). Sequence of the amino-terminal 349 residues of rabbit muscle glycogen phosphorylase including the sites of covalent and allosteric control. Biochemistry 17, 5657-72.

Levine, A. E., Walsh, K. A., and Fodor, E. J. (1978). Evidence of an acrosin-like enzyme in sea urchin sperm. Developmental Biology 63, 299-306.

Lonsdale Eccles, J. D., Neurath, H., and Walsh, K. A. (1978). Probes of the mechanism of zymogen catalysis. Biochemistry 17, 2805-9.

Palmiter, R. D., Gagnon, J., and Walsh, K. A. (1978). Ovalbumin: a secreted protein without a transient hydrophobic leader sequence. Proc. Natl. Acad. Sci. USA 75, 94-8.

Thibodeau, S. N., Palmiter, R. D., and Walsh, K. A. (1978). Precursor of egg white ovomucoid. Amino acid sequence of an NH2-terminal extension. J. Biol. Chem. 253, 9018-23.

Titani, K., Koide, A., Ericsson, L. H., Kumar, S., Hermann, J., Wade, R. D., Walsh, K. A., Neurath, H., and Fischer, E. H. (1978). Sequence of the carboxyl-terminal 492 residues of rabbit muscle glycogen phosphorylase including the pyridoxal 5'-phosphate binding site. Biochemistry 17, 5680-93.

Walsh, K. A., Ericsson, L. H., and Titani, K. in Versatility of Proteins (C. H. Li, Ed.), Academic Press, 1978, 39.

Woodbury, R. G., Everitt, M., Sanada, Y., Katunuma, N., Lagunoff, D., and Neurath, H. (1978). A major serine protease in rat skeletal muscle: evidence for its mast cell origin. Proc. Natl. Acad. Sci. USA 75, 5311-3.

Woodbury, R. G., Katunuma, N., Kobayashi, K., Titani, K., Neurath, H., Anderson, W. F., and Matthews, B. W. (1978). 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.

Woodbury, R. G., and Neurath, H. (1978). Purification of an atypical mast cell protease and its levels in developing rats. Biochemistry 17, 4298-304. 

1977   ___________________________________________________   1977
Alter, G. M., Leussing, D. L., Neurath, H., and Vallee, B. L. (1977). Kinetic properties of carboxypeptidase B in solutions and crystals. Biochemistry 16, 3663-8.

Anderson, L. E., Walsh, K. A., and Neurath, H. (1977). Bovine enterokinase. Purification, specificity, and some molecular properties. Biochemistry 16, 3354-60.

Bitar, K. G., Blankenship, D. T., Walsh, K. A., Dunlap, R. B., Reddy, A. V., and Freisheim, J. H. (1977). Amino acid sequence of dihydrofolate reductase from an amethopterin-resistant strain of Lactobacillus casei. FEBS Lett. 80, 119-22.

de Haen, C., Walsh, K. A., and Neurath, H. (1977). Isolation and amino-terminal sequence analysis of a new pancreatic trypsinogen of the African lungfish Protopterus aethiopicus. Biochemistry 16, 4421-5.

Ericsson, L. H., Wade, R. D., Gagnon, J., McDonald, R. M., Granberg, R., and Walsh, K. A. (1977). High performance liquid chromatography of Pth-amino acids using a Durrum D-500 analyzer. In INSERM Symposium Number 5, A. Previero and M. A. Coletti-Previero, eds.: North Holland Publ. Co., Amsterdam), pp. 137.

Freisheim, J. H., Ericsson, L. H., Bitar, K. G., Dunlap, R. B., and Reddy, A. V. (1977). An active center tryptophan residue in dihydrofolate reductase: chemical modification, sequence surrounding the critical residue, and structural homology considerations. Archives Of Biochemistry and Biophysics 180, 310-7.

Fujikawa, K., Walsh, K. A., and Davie, E. W. (1977). Isolation and characterization of bovine factor XII (Hageman factor). Biochemistry 16, 2270-8.

Kisiel, W., Canfield, W. M., Ericsson, L. H., and Davie, E. W. (1977). Anticoagulant properties of bovine plasma protein C following activation by thrombin. Biochemistry 16, 5824-31.

Neurath, H., and Walsh, K. A. (1977). The role of proteases in physiological regulation: an overview. In FEBS 11th Meeting, S. Magnusson, ed., pp. 1.

Palmiter, R. D., Gagnon, J., Ericsson, L. H., and Walsh, K. A. (1977). Precursor of egg white lysozyme. Amino acid sequence of an NH2-terminal extension. J. Biol. Chem. 252, 6386-93.

Palmiter, R. D., Thibodeau, S. N., Gagnon, J., and Walsh, K. A. (1977). Role of proteases in the secretion of lysozyme, ovomucoid, canalbumin, and ovalbumin from the chick oviduct. In FEBS 11th Meeting, S. Magnusson, ed., pp. 89.

Thompson, A. R., Enfield, D. L., Ericsson, L. H., Legaz, M. E., and Fenton, J. W. I. I. (1977). Human thrombin: partial primary structure. Archives Of Biochemistry and Biophysics 178, 356-67.

Titani, K., Koide, A., Hermann, J., Ericsson, L. H., Kumar, S., Wade, R. D., Walsh, K. A., Neurath, H., and Fischer, E. H. (1977). Complete amino acid sequence of rabbit muscle glycogen phosphorylase. Proc. Natl. Acad. Sci. USA 74, 4762-6. 

1976   ___________________________________________________   1976
Ako, H., Hass, G. M., Grahn, D. T., and Neurath, H. (1976). Carboxypeptidase inhibitor from potatoes. Interaction with derivatives of carboxypeptidase A. Biochemistry 15, 2573-8.

Eriksen, N., Ericsson, L. H., Pearsall, N., Lagunoff, D., and Benditt, E. P. (1976). Mouse amyloid protein AA: Homology with nonimmunoglobulin protein of human and monkey amyloid substance. Proc. Natl. Acad. Sci. USA 73, 964-7.

Hass, G. M., Ako, H., Grahn, D. T., and Neurath, H. (1976). Carboxypeptidase inhibitor from potatoes. The effects of chemical modifications on inhibitory activity. Biochemistry 15, 93-100.

Kerr, M. A., Walsh, K. A., and Neurath, H. (1976). A proposal for the mechanism of chymotrypsinogen activation. Biochemistry 15, 5566-70.

Kisiel, W., Ericsson, L. H., and Davie, E. W. (1976). Proteolytic activation of protein C from bovine plasma. Biochemistry 15, 4893-900.

Kuhn, R. W., Walsh, K. A., and Neurath, H. (1976). Reaction of yeast carboxypeptidase C1 with group-specific reagents. Biochemistry 15, 4881-5.

Neurath, H., and Walsh, K. A. (1976). The role of proteases in biological regulation. pp. 29-42. In: Ribbons DW, Brew K, ed. Proteolysis and physiological regulation. New York, Academic Press.

Neurath, H., and Walsh, K. A. (1976). Role of proteolytic enzymes in biological regulation (a review). Proc. Natl. Acad. Sci. USA 73, 3825-32.

Pangburn, M. K., Levy, P. L., Walsh, K. A., and Neurath, H. (1976). Thermal stability of homologous neutral metalloendopeptidases in thermophilic and mesophilic bacteria: structural considerations. Experientia, 19-30. 

1975   ___________________________________________________   1975
De Haen, C., Neurath, H., and Teller, D. C. (1975). 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.

Enfield, D. L., Ericsson, L. H., Blum, H. E., Fischer, E. H., and Neurath, H. (1975). Amino-acid sequence of parvalbumin from rabbit skeletal muscle. Proc. Natl. Acad. Sci. USA 72, 1309-13.

Enfield, D. L., Ericsson, L. H., Walsh, K. A., Neurath, H., and Titani, K. (1975). Bovine factor X1 (Stuart factor). Primary structure of the light chain. Proc. Natl. Acad. Sci. USA 72, 16-9.

Fodor, E. J., Ako, H., and Walsh, K. A. (1975). Isolation of a protease from sea urchin eggs before and after fertilization. Biochemistry 14, 4923-7.

Hass, G. M., Nau, H., Biemann, K., Grahn, D. T., Ericsson, L. H., and Neurath, H. (1975). The amino acid sequence of a carboxypeptidase inhibitor from potatoes. Biochemistry 14, 1334-42.

Kerr, M. A., Walsh, K. A., and Neurath, H. (1975). Catalysis by serine proteases and their zymogens. A study of acyl intermediates by circular dichroism. Biochemistry 14, 5088-94.

Levy, P. L., Pangburn, M. K., Burstein, Y., Ericsson, L. H., Neurath, H., and Walsh, K. A. (1975). Evidence of homologous relationship between thermolysin and neutral protease A of Bacillus subtilis. Proc. Natl. Acad. Sci. USA 72, 4341-5.

Neurath, H. (1975). Limited proteolysis and zymogen activation. pp. 51-64. In: Reich E, et al., ed. Proteases and biological control. Cold Spring Harbor, Cold Spring Harbor Laboratory.

Pangburn, M. K., and Walsh, K. A. (1975). Thermolysin and neutral protease: mechanistic considerations. Biochemistry 14, 4050.

Titani, K., Cohen, P., Walsh, K. A., and Neurath, H. (1975). Amino-terminal sequence of rabbit muscle phosphorylase. FEBS Lett. 55, 120-3.

Titani, K., Ericsson, L. H., Neurath, H., and Walsh, K. A. (1975). Amino acid sequence of dogfish trypsin. Biochemistry 14, 1358-66.

Titani, K., Ericsson, L. H., Walsh, K. A., and Neurath, H. (1975). Amino-acid sequence of bovine carboxypeptidase B. Proc. Natl. Acad. Sci. USA 72, 1666-70.

Titani, K., Fujikawa, K., Enfield, D. L., Ericsson, L. H., Walsh, K. A., and Neurath, H. (1975). Bovine factor X1 (Stuart factor): amino-acid sequence of heavey chain. Proc. Natl. Acad. Sci. USA 72, 3082-6.

Walsh, K. A. (1975). Unifying concepts among proteases. pp. 1-11. In: Reich E, et al., ed. Proteases and biological control. Cold Spring Harbor, Cold Spring Harbor Laboratory.

Zwilling, R., Neurath, H., Ericsoon, L. H., and Enfield, D. L. (1975). The amino-terminal sequence of an invertebrate trypsin (crayfish Astacus leptodactylus): homology with other serine proteases. FEBS Lett. 60, 247-9. 

1974   ___________________________________________________   1974
Burstein, Y., Walsh, K. A., and Neurath, H. (1974). Evidence of an essential histidine residue in thermolysin. Biochemistry 13, 205-10.

Enfield, D. L., Ericsson, L. H., Fujikawa, K., Titani, K., Walsh, K. A., and Neurath, H. (1974). Bovine factor IX (Christmas factor). Further evidence of homology with factor X (Stuart factor) and prothrombin. FEBS Lett. 47, 132-5.

Enfield, D. L., Ericsson, L. H., Walsh, K. A., Neurath, H., and Titani, K. (1974). Bovine Factor X1 (Stuart factor). Primary structure of the light chain. Proc. Natl. Acad. Sci. USA 72, 16.

Fujikawa, K., Coan, M. H., Enfield, D. L., Titani, K., Ericsson, L. H., and Davie, E. W. (1974). A comparison of bovine prothrombin, factor IX (Christmas factor), and factor X (Stuart factor). Proc. Natl. Acad. Sci. USA 71, 427-30.

Gertler, A., Walsh, K. A., and Neurath, H. (1974). Catalysis by chymotrypsinogen: increased reactivity due to oxidation of Met 192. FEBS Lett. 8, 157.

Gertler, A., Walsh, K. A., and Neurath, H. (1974). Catalysis by chymotrypsinogen. Demonstration of an acyl-zymogen intermediate. Biochemistry 13, 1302-10.

Hass, G. M., Plikaytis, B., and Neurath, H. (1974). Modification of the acetyl and nitro derivatives of carboxypeptidase A by N-bromoacetyl-N-methyl-L-phenylalanine. FEBS Lett. 46, 162-5.

Jur'asek, L., Carpenter, M. R., Smillie, L. B., Gertler, A., Levy, S., and Ericsson, L. H. (1974). Amino acid sequence of Streptomyces griseus protease B, A MAJOR COMPONENT OF Pronase. Biochem. Biophys. Res. Comm. 61, 1095-100.

Kuhn, R. W., Walsh, K. A., and Neurath, H. (1974). Isolation and partial characterization of an acid carboxypeptidase from yeast. Biochemistry 13, 3871-7.

Morgan, P. H., Walsh, K. A., and Neurath, H. (1974). Inactivation of trypsinogen by methane sulfonyl fluoride. FEBS Lett. 41, 108-10.

Uren, J. R., and Neurath, H. (1974). Intrinsic enzymatic activity of bovine procarboxypeptidase A S5. Biochemistry 13, 3512-20.

Walsh, K. A., Burstein, Y., and Pangburn, M. K. (1974). Affinity chromatography of thermolysin and other neutral metalloendopeptidases. Methods Enzymol 34, 435-40. 

1973   ___________________________________________________   1973
Hermodson, M. A., Ericsson, L. H., Neurath, H., and Walsh, K. A. (1973). Determination of the amino acid sequence of porcine trypsin by sequenator aalysis. Biochemistry 12, 3146-53.

Neurath, H., Walsh, K. A., and Gertler, A. (1973). Initiation of physiological functions by limited proteolysis. In 3rd International Symposium on Metabolic Interconversion of Enzymes (Seattle, WA), pp. 301.

Pangburn, M. K., Burstein, Y., Morgan, P. H., Walsh, K. A., and Neurath, H. (1973). Affinity chromatography of thermolysin and of neutral proteases from B. subtilis. Biochem. Biophys. Res. Comm. 54, 371-9.

Robinson, N. C., Neurath, H., and Walsh, K. A. (1973). Preparation and characterization of guanidinated trypsinogen and -guanidinated trypsin. Biochemistry 12, 414-20.

Robinson, N. C., Neurath, H., and Walsh, K. A. (1973). The relation of the a-amino group of trypsin to enzyme function and zymogen activation. Biochemistry 12, 420-6.

Stoll, E., Ericsson, L. H., and Zuber, H. (1973). The function of the two subunits of thermophilic aminopeptidase I. Proc. Natl. Acad. Sci. USA 70, 3781-4. 

1972   ___________________________________________________   1972
Hass, G. M., Govier, M. A., Grahn, D. T., and Neurath, H. (1972). Modification of bovine carboxypeptidase B with N-bromoacetyl-N-methyl-L-phenylalanine. Biochemistry 11, 3787-92.

Hermodson, M. A., Ericsson, L. H., Titani, K., Neurath, H., and Walsh, K. A. (1972). Application of sequenator analyses to the study of proteins. Biochemistry 11, 4493-502.

Hermodson, M. A., Kuhn, R. W., Walsh, K. A., Neurath, H., Eriksen, N., and Benditt, E. P. (1972). Amino acid sequence of monkey amyloid protein A. Biochemistry 11, 2934-8.

Morgan, P. H., Robinson, N. C., Walsh, K. A., and Neurath, H. (1972). Inactivation of bovine trypsinogen and chymotrypsinogen by diisopropylphosphorofluoridate. Proc. Natl. Acad. Sci. USA 69, 3312-6.

Reeck, G. R., and Neurath, H. (1972). Isolation and characterization of pancreatic procarboxypeptidase B and carboxypeptidase B of the African lungfish. Biochemistry 11, 3947-55.

Reeck, G. R., and Neurath, H. (1972). Pancreatic trypsinogen from the African lungfish. Biochemistry 11, 503-10.

Stoll, E., Hermodson, M. A., Ericsson, L. H., and Zuber, H. (1972). Subunit structure of the thermophilic aminopeptidase I from Bacillus stearothermophilus. Biochemistry 11, 4731-5.

Titani, K., Hermodson, M. A., Ericsson, L. H., Walsh, K. A., and Neurath, H. (1972). Amino acid sequence of thermolysin. Isolation and characterization of the fragments obtained by cleavage with cyanogen bromide. Biochemistry 11, 2427-35.

Titani, K., Hermodson, M. A., Ericsson, L. H., Walsh, K. A., and Neurath, H. (1972). Amino-acid sequence of thermolysin. Nature New Biology 238, 35-37.

Titani, K., Hermodson, M. A., Fujikawa, K., Ericsson, L. H., Walsh, K. A., Neurath, H., and Davie, E. W. (1972). Bovine factor X 1a (activated Stuart factor). Evidence of homology with mammalian serine proteases. Biochemistry 11, 4899-903.

Uren, J. R., and Neurath, H. (1972). Mechanism of activation of bovine procarboxypeptidase A S 5 . Alterations in primary and quaternary structure. Biochemistry 11, 4483-92.

Walsh, K. A. (1972). Probing biological function and tracing molecular evolution by automated sequence analysis. In Fractions (Beckman Instruments, Inc.), pp. 1. 

1971   ___________________________________________________   1971
Angeletti, R. H., Bradshaw, R. A., and Wade, R. D. (1971). Subunit structure and amino acid composition of mouse submaxillary gland nerve growth factor. Biochemistry 10, 463-9.

Benditt, E. P., Eriksen, N., Hermodson, M. A., and Ericsson, L. H. (1971). The major proteins of human and monkey amyloid substance: common properties including unusual N-terminal amino acid sequences. FEBS Letters 19, 169-173.

Bradshaw, R. A., Walsh, K. A., and Neurath, H. (1971). Amino acid sequence of bovine carboxypeptidase A. Tryptic and chymotryptic peptides of the cyanogen bromide fragment F-I. Biochemistry 10, 938-50.

Bradshaw, R. A., Walsh, K. A., and Neurath, H. (1971). 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.

Bradshaw, R. A., Walsh, K. A., and Neurath, H. (1971). 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.

Hass, G. M., and Neurath, H. (1971). Affinity labeling of bovine carboxypeptidase A Leu by N-bromoacetyl-N-methyl-L-phenylalanine. II. Sites of modification. Biochemistry 10, 3541-6.

Hass, G. M., and Neurath, H. (1971). Affinity labeling of bovine carboxypeptidase A Leu by N-bromoacetyl-N-methyl-L-phenylalanine. I. Kinetics of inactivation. Biochemistry 10, 3535-40.

Hermodson, M. A., Tye, R. W., Reeck, G. R., Neurath, H., and Walsh, K. A. (1971). Comparison of the amino terminal sequences of bovine, dogfish and lungfish trypsinogens. FEBS Lett. 14, 222.

Kenner, R. A., and Neurath, H. (1971). Activity and fluorescent derivatives of aminotyrosyl trypsin and trypsinogen. Biochemistry 10, 551-7.

Neurath, H., Fischer, E. H., and Singer, S. J. (1971). Enzyme control and macromolecular assembly. Science 172, 185-9.

P'Etra, P. H., and Neurath, H. (1971). Modification of carboxyl groups in bovine carboxypeptidase A. II. Chemical identification of a functional glutamic acid residue and other reactive groups. Biochemistry 10, 3171-7.

Petra, P. H., Hermodson, M. A., Walsh, K. A., and Neurath, H. (1971). Characterization of bovine carboxypeptidase A (Allan). Biochemistry 10, 4023-5.

Reeck, G. R., Walsh, K. A., Hermodson, M. A., and Neurath, H. (1971). New forms of bovine carboxypeptidase B and their homologous relationships to carboxypeptidase A. Proc. Natl. Acad. Sci. USA 68, 1226-30.

Reeck, G. R., Walsh, K. A., and Neurath, H. (1971). Isolation and characterization of carboxypeptidases A and B from activated pancreatic juice. Biochemistry 10, 4690-8.

Robinson, N. C., Tye, R. W., Neurath, H., and Walsh, K. A. (1971). Isolation of trypsins by affinity chromatography. Biochemistry 10, 2743-7. 

1970   ___________________________________________________   1970
Arnon, R., and Neurath, H. (1970). Immunochemical studies on bovine trypsin and trypsinogen derivatives. Immunochemistry 7, 241-50.

Behnke, W. D., Teller, D. C., Wade, R. D., and Neurath, H. (1970). Hybrid formation of carboxypeptidase A and fraction II of procarboxypeptidase A. Biochemistry 9, 4189-200.

Behnke, W. D., Wade, R. D., and Neurath, H. (1970). Interactions of the endopeptidase subunit of bovine procarboxypeptidase A-S6. Biochemistry 9, 4179-88.

Bradshaw, R. A., Neurath, H., Tye, R. W., Walsh, K. A., and Winter, W. P. (1970). Comparison of the partial amino-acid sequence of dogfish trypsinogen with bovine trypsinogen. Nature 226, 237-9.

Houston, L. L., and Walsh, K. A. (1970). The transient inactivation of trypsin by mild acetylation with N-acetylimidazole. Biochemistry 9, 156-66.

Lacko, A. G., and Neurath, H. (1970). Studies on procarboxypeptidase A and carboxypeptidase A of the spiny pacific dogfish (Squalus acanthias). Biochemistry 9, 4680-90.

Neurath, H., Bradshaw, R. A., Petra, P. H., and Walsh, K. A. (1970). 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.

Reeck, G. R., Winter, W. P., and Neurath, H. (1970). Pancreatic enzymes of the African lungfish Protopterus aethiopicus. Biochemistry 9, 1398-403.

Sanders, M. M., Walsh, K. A., and Arnon, R. (1970). Immunological cross-reaction between trypsin and chymotrypsin as a guide to structural homology. Biochemistry 9, 2356-63.

Walsh, K. A. in Methods in Enzymology ,Vol. XIX, (Perlman and Lorand, Eds.), Academic Press, New York, 1970, 41.

Walsh, K. A., Ericsson, L. H., Bradshaw, R. A., and Neurath, H. (1970). Chemical evidence of a disulfide bond in bovine carboxypeptidase A. Biochemistry 9, 219-25.

Walsh, K. A., Houston, L. L., and Kenner, R. A. in Structure-Function Relationship of Proteolytic Enzymes (P. Desnuelle, H. Neurath and M. Ottesen, Eds.), Munksgaard, Copenhagen, Denmark, 1970, 56.

Walsh, K. A., McDonald, R. M., and Bradshaw, R. A. (1970). Automatic systems for detecting cystine and cystinyl peptides during column chromatography. Anal. Biochem. 35, 193-202.

Walsh, K. A., and Wilcox, P. E. in Methods in Enzymology ,Vol. XIX, (Perlman and Lorand, Eds.), Academic Press, New York, 1970, 31.

Winter, W. P., and Neurath, H. (1970). Purification and properties of a trypsin-like enzyme from the starfish Evasterias trochelii. Biochemistry 9, 4673-9. 

1969   ___________________________________________________   1969
Arnon, R., and Neurath, H. (1969). An immunological approach to the study of evolution of trypsins. Proc. Natl. Acad. Sci. USA 64, 1323-8.

Bradshaw, R. A., Babin, D. R., Nomoto, M., Srinivasin, N. G., Ericsson, L. H., Walsh, K. A., and Neurath, H. (1969). The amino acid sequence of bovine carboxypeptidase A. II. Tryptic and chymotryptic peptides of the cyanogen bromide fragment F-III. Biochemistry 8, 3859-71.

Bradshaw, R. A., Ericsson, L. H., Walsh, K. A., and Neurath, H. (1969). The amino acid sequence of bovine carboxypeptidase A. Proc. Natl. Acad. Sci. USA 63, 1389-94.

Bradshaw, R. A., Neurath, H., and Walsh, K. A. (1969). Considerations of the concept of structural homology as applied to bovine carboxypeptidases A and B. Proc. Natl. Acad. Sci. USA 63, 406-11. [Medline]

Granberg, R. R., Walsh, K. A., and Bradshaw, R. A. (1969). Increased output and accelerated analysis time with the automatic amino acid analyzer. Anal. Biochem. 30, 454-64.

Haynes, R., and Walsh, K. A. (1969). Enzyme envelopes on colloidal particles. Biochem. Biophys. Res. Comm. 36, 235-42. [Medline]

Nomoto, M., Srinivasan, N. G., Bradshaw, R. A., Wade, R. D., and Neurath, H. (1969). The amino acid sequence of bovine carboxypeptidase A. I. Preparation and properties of the fragments obtained by cyanogen bromide cleavage. Biochemistry 8, 2755-62.

P'Etra, P. H., and Neurath, H. (1969). The heterogeneity of bovine carboxypeptidase A. I. The chromatographic purification of carboxypeptidase A (Anson). Biochemistry 8, 2466-75.

P'Etra, P. H., and Neurath, H. (1969). Heterogeneity of bovine carboxypeptidase A. II. Chromatographic purification of carboxypeptidase A (Cox). Biochemistry 8, 5029-36.

Petra, P. H., Bradshaw, R. A., Walsh, K. A., and Neurath, H. (1969). Identification of the amino acid replacements characterizing the allotypic forms of bovine carboxypeptidase A. Biochemistry 8, 2762-8. [Medline]

Radhakrishnan, T. M., Russo, S. F., Walsh, K. A., and Neurath, H. (1969). The inhibition of trypsinogen activation by low concentrations of urea. Archives Of Biochemistry and Biophysics 130, 326-31. [Medline]

Radhakrishnan, T. M., Walsh, K. A., and Neurath, H. (1969). The promotion of activation of bovine trypsinogen by specific modification of aspartyl residues. Biochemistry 8, 4020-7. 

1968   ___________________________________________________   1968
Beeley, J. G., and Neurath, H. (1968). The reaction of trypsin with bromoacetone. Biochemistry 7, 1239-51.

Kenner, R. A., Walsh, K. A., and Neurath, H. (1968). The reaction of tyrosyl residues of bovine trypsin and trypsinogen with tetranitromethane. Biochem. Biophys. Res. Comm. 33, 353-60. [Medline]

Neurath, H., Bradshaw, R. A., Ericsson, L. H., Babin, D. R., Petra, P. H., and Walsh, K. A. (1968). Current status of the chemical structure of bovine pancreatic carboxypeptidase A. Brookhaven Symposia In Biology 21, 1-23. [Medline]

Winter, W. P., Walsh, K. A., and Neurath, H. (1968). Homology as applied to proteins. Science 162, 1433. [Medline] 

1967   ___________________________________________________   1967
Freisheim, J. H., Walsh, K. A., and Neurath, H. (1967). The activation of bovine procarboxypeptidase A. I. Isolation and properties of the succinylated enzyme precursor. Biochemistry 6, 3010-9. [Medline]

Freisheim, J. H., Walsh, K. A., and Neurath, H. (1967). The activation of bovine procarboxypeptidase A. II. Mechanism of activation of the succinylated enzyme precursor. Biochemistry 6, 3020-8. [Medline]

Lacko, A. G., and Neurath, H. (1967). A monomeric form of procarboxypeptidase A from the spiny pacific dogfish. Biochem. Biophys. Res. Comm. 26, 272-7.

Neurath, H., Walsh, K. A., and Winter, W. P. (1967). Evolution of structure and function of proteases. Science 158, 1638-44. [Medline]

Radhakrishnan, T. M., Walsh, K. A., and Neurath, H. (1967). Relief by modification of carboxylate groups of the calcium requirement for the activation of trypsinogen. Journal Of the American Chemical Society 89, 3059-61. 

1966   ___________________________________________________   1966
Deranleau, D. A., and Neurath, H. (1966). The combination of chymotrypsin and chymotrypsinogen with fluorescent substrates and inhibitors for chymotrypsin. Biochemistry 5, 1413-25.

Houston, L. L., and Walsh, K. A. (1966). A partially active trypsin induced by limited acetylation. Biochem. Biophys. Res. Comm. 25, 175-80. [Medline]

McClure, W. O., and Neurath, H. (1966). The reaction of carboxypeptidase A with chromophoric substrates. Biochemistry 5, 1425-38. [Medline]

Prahl, J. W., and Neurath, H. (1966). Pancreatic enzymes of the spiny Pacific dogfish. I. Cationic chymotrypsinogen and chymotrypsin. Biochemistry 5, 2131-46. [Medline]

Walsh, K. A., Ericsson, L. H., and Neurath, H. (1966). Bovine carboxypeptidase A variants resulting from allelomorphism. Proc. Natl. Acad. Sci. USA 56, 1339-44. [Medline] 

1965   ___________________________________________________   1965
Wintersberger, E., Neurath, H., Coombs, T. L., and Wallee, B. L. (1965). A zinc-binding thiol group in the active center of bovine carboxypeptidase B. Biochemistry 4, 1526-32. [Medline] 

1964   ___________________________________________________   1964
Bargetzi, J.-P., Thompson, E. O. P., Kumar, K. S. V. S., Walsh, K. A., and Neurath, H. (1964). Amino and carboxyl terminal residues and the self digestion of bovine pancreatic carboxypeptidase A. J. Biol. Chem. 239, 3767.

Cox, D. J., Bovard, F. C., Bargetzi, J.-P., Walsh, K. A., and Neurath, H. (1964). Procedures for the isolation of crystalline bovine pancreatic carboxypeptidase A. II. Isolation of carboxypeptidase Aa from procarboxypeptidase A. Biochemistry 3, 44.

Kumar, K. S. V. S., Clegg, J., and Walsh, K. A. (1964). The N-terminal sequence of bovine carboxypeptidase A and its relation to zymogen activation. Biochemistry 3, 1728.

Kumar, K. S. V. S., Walsh, K. A., Bargetzi, J.-P., and Neurath, H. (1964). Chemical relationships among various forms of bovine pancreatic carboxypeptidase A. Biochemistry 2, 1475.

Kumar, K. S. V. S., Walsh, K. A., and Neurath, H. (1964). Characterization of bovine carboxypeptidase A isolated from a single pancreas. Biochemistry 3, 1726.

McClure, W., Neurath, H., and Walsh, K. A. (1964). The reaction of carboxypeptidase with Hippuryl-DL-ß-Phenyllacetate. Biochemistry 3, 1907.

Walsh, K. A., Kauffman, D. L., Kumar, K. S. V. S., and Neurath, H. (1964). On the structure and function of bovine trypsinogen and trypsin. Proc. Natl. Acad. Sci. USA 51, 301.

Walsh, K. A., and Neurath, H. (1964). Trypsinogen and chymotrypsinogen as homologous proteins. Proc. Natl. Acad. Sci. USA 52, 884. 

1963   ___________________________________________________   1963
Bargetzi, J.-P., Walsh, K. A., Cox, D. J., Kumar, K. S. V. S., and Neurath, H. (1963). Amino acid composition of bovine carboxypeptidase A. Biochemistry 2, 1468.

Kumar, K. S. V. S., Walsh, K. A., Bargetzi, J.-P., and Neurath, H. in Aspects of Protein Structure (G. M. Ramachandran, Ed.), Academic Press, London, 1963, 319-335. 

1962   ___________________________________________________   1962
Walsh, K. A., and Brown, J. R. (1962). Internal standards for amino acid analyses. Biochem. Biophys. Acta 58, 596.

Walsh, K. A., Dauffman, D., and Neurath, H. (1962). The amino terminal sequence of trypsinogen. Biochemistry 1, 893.

Walsh, K. A., Kauffman, D. L., and Neurath, H. (1962). Peptides isolated from tryptic and chymotryptic hydrolysates of S-sulfo-trypsinogen. Biochem. Biophys. Acta 65, 540.

Walsh, K. A., Kumar, K. S. V. S., Bargetzi, J.-P., and Neurath, H. (1962). Approaches to the selective chemical labeling of the active site of carboxypeptidase A. Proc. Natl. Acad. Sci. USA 48, 1443. 

1961   ___________________________________________________   1961
Brown, J. R., Cox, D. J., Greenshields, R. M., Walsh, K. A., Yamasaki, M., and Neurath, H. (1961). The chemical structure and enzymatic functions of bovine procarboxypeptidase A. Proc. Natl. Acad. Sci. USA 47, 1554. 

1957   ___________________________________________________   1957
Dixon, G. H., and Neurath, H. (1957). Acylation of the enzymatic site of d-chymotrypsin by esters, acid anhydrides, and acid chlorides. J. Biol. Chem. 225, 1049.

Wilcox, P. E., Kraut, J., Wade, R. D., and Neurath, H. (1957). The molecualr weight of a-chymotrypsinogen. Biochem. Biophys. Acta 24, 72. 

1956   ___________________________________________________   1956
Dixon, G. H., Dreyer, W. J., and Neurath, H. (1956a). The reaction of p-nitrophenyl acetate with chymotrypsin. J. Am. Chem. Soc. 78, 4810.

Dixon, G. H., Go, S., and Neurath, H. (1956b). Peptides combined with 14C- diisoprophyl phosphoryl following degradation of 14C-dip-trypsin with a-chymotrypsin. Biochem. Biophys. Acta 19, 193.

Dixon, G. H., and Neurath, H. (1956). The reaction of DFP with trypsin. Biochem. Biophys. Acta 20, 572.

Holter, H., and Neurath, H. (1956). 60th birthday anniversary dedication for Prof Kaj U. Linderstrom-Land. Arch. Biochem. Biophys. 65, 1.

Keller, P. J., Cohen, E., and Neurath, H. (1956a). Procarboxy-peptidase. Fed. Proc. 15.

Keller, P. J., Cohen, E., and Neurath, H. (1956b). Purification and properties of procarboxypeptidase. J. Biol. Chem. 223, 457.

Neurath, H., Rupley, J. A., and Dreyer, W. J. (1956). Structural changes in the activation of chymotrypsinogen and trypsinogen effect of urea on chymotrypsinogen and delta-chymotrypsin. Arch. Biochem. Biophys. 65, 243. 

1955   ___________________________________________________   1955
Bettelheim, F. R., and Neurath, H. (1955a). Amino terminal groups in chymotrypsinogen. J. Biol. Chem. 212, 235.

Bettelheim, F. R., and Neurath, H. (1955b). The rapid activation of chymotrypsin. J. Biol. Chem. 212, 241.

Davie, E. W., and Neurath, H. (1955a). Identification of a peptide released during autocatalytic activation of trypsinogen. J. Biol. Chem. 212, 515.

Davie, E. W., and Neurath, H. (1955b). The terminal groups of the soy bean trypsin inhibitor. J. Biol. Chem. 212, 407.

Dreyer, W. J., and Neurath, H. (1955a). The activation of chymotrypsinogen. J. Am. Chem. Soc. 77, 814.

Dreyer, W. J., and Neurath, H. (1955b). The activation of chymotrypsinogen, isolation and identification of a peptide liberated during activation. J. Biol. Chem. 217, 527.

Dreyer, W. J., Wade, R. D., and Neurath, H. (1955). Observations on the electrophoretic and ultracentrifugal changes accompanying the activation of chymotrypsinogen. Arch. Biochem. Biophys. 59, 145.

Halsey, Y. D., and Neurath, H. (1955a). The reaction of methyl mercury nitrate with the sulfhydryl groups of yeast glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 214, 589.

Halsey, Y. D., and Neurath, H. (1955b). The terminal carboxyl groups of denatured yeast triosephosphate dehydrogenase. J. Biol. Chem. 217, 247.

Neurath, H. (1955). The activation of trypsinogen and chymotrypsinogen. In 3rd Int. Cong. Biochem., Brussels.

Neurath, H., and Dreyer, W. J. (1955a). Activaiton of chymotrypsinogen. Fed. Proc. 14, 1.

Neurath, H., and Dreyer, W. J. (1955b). Mechanism of activation of trypsinogen and chymotrypsinogen. Disc. Faraday Soc. 1.

Rupley, J. A., Dreyer, W. J., and Neurath, H. (1955). Structural changes in the activaiton of chymotrypsinogen. Biochem. Biophys. Acta 18.

Vallee, B. L., and Neurath, H. (1955). Carboxypeptidase, a zinc metalloenzyme. J. Biol. Chem. 217, 253. 

1954   ___________________________________________________   1954
Bettelheim, F. R., and Neurath, H. (1954). Tyrosine-O-sulfate in a peptide from fibrinogen. J. Am. Chem. Soc. 76, 2838.

Cunningham, L. W., Jr., and Neurath, H. (1954a). Molecular-kinetic properties of crystalline diisopropylphosphoryl trypsin. J. Biol. Chem. 211, 13.

Cunningham, L. W., Jr., and Neurath, H. (1954b). Reaction of diethyl p-nitrophenyl phosphate-inhibited a-chymotrypsin by hydroxylamine. J. Biol. Chem. 207, 4431.

Gladner, J. A., and Neurath, H. (1954). Carboxyl terminal groups of proteolytic enzymes. II. Chymotrypsins. J. Biol. Chem. 206, 911.

Neurath, H., and Davie, E. W. (1954). Terminal groups of components of the trypsin system. Fed. Proc. 13, 1.

Neurath, H., Gladner, J. A., and Davie, E. W. (1954) in "The Mechanism of Enzyme Action" (W. D. McElroy and B. Glass, Eds.), Johns Hopkins Press, Baltimore, MD.

Vallee, B. L., and Neurath, H. (1954). Carboxypeptidase, a zinc metalloprotein. J. Am. Chem. Soc. 76, 5006. 

1953   ___________________________________________________   1953
Cunningham, L. W., Jr., and Neurath, H. (1953). Reactivation of a-chymotrypsin inhibited by organic phosphates. Biochim. Biophys. Acta. 11, 310.

Cunningham, L. W., Jr., Tietze, F., Green, N. M., and Neurath, H. (1953). Molecular kinetic properties of trypsin and related proteins. Faraday Soc. Discussion 13.

Davie, E. W., and Neurath, H. (1953). C-terminal groups of trypsinogen, D.F.P.-trypsin and carboxypeptidase. J. Am. Chem. Soc. 74, 6305.

Davie, E. W., and Neurath, H. (1953). Identification of the peptide split from trypsinogen during autocatalytic activation. Biochim. Biophys. Acta. 11, 442.

Gladner, J. A., and Neurath, H. (1953). Carboxyl terminal groups of proteolytic enzymes. I. the activation of chymotrypsinogen to a-chymotrypsin. J. Biol. Chem. 205, 345.

Green, N. M., and Neurath, H. (1953). Competition among trypsin inhibitors. J. Biol. Chem. 205, 535.

Green, N. M., and Neurath, H. (1953). The effects of divalent cations on trypsin. J. Biol. Chem. 204, 379.

Morrison, W. L., and Neurath, H. (1953). Proteolytic enzymes of the formed elements of human blood. J. Biol. Chem. 200.

Neurath, H. (1953). Advances in enzymology and related subjects of biochemistry. J. Am. Chem. Soc. 75, 2536.

Neurath, H., and Gladner, J. A. (1953). Effects of carboxypeptidase on the chymotrypsin system. Fed. Proc. 12, 827.

Tietze, F., and Neurath, H. (1953). Molecular-kinetic properties of crystalline trypsinogen. J. Biol. Chem. 204, 1.

Tietze, F., and Neurath, H. (1953). The sedimentation constant of insulin in acid solution: a re-examination. J. Am. Chem. Soc. 75, 1753. 

1952   ___________________________________________________   1952
Gladner, J. A., and Neurath, H. (1952). C-terminal groups in chymotrypsinogen and DFP-a-chymotrypsin in relation to the activation process. Biochem. Biophys. Acta 9, 335.

Green, N. M., Gladner, J. A., Cunningham, L. W., Jr., and Neurath, H. (1952). The effects of divalent cations on the enzymatic activities of trypsin and of a-chymotrypsin. J. Am. Chem. Soc. 74, 2122.

Neurath, H., Cunningham, L. W., Jr., Tietze, F., and Green, N. M. (1952). Reaction of the trypsin system with diisopropylfluorophosphate (DFP). Fed. Proc. 11, 1.

1952 - 1979 (current page)     1980 - present
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