| Year |
Citation |
Score |
| 1999 |
Lennon JJ, Walsh KA. Locating and identifying posttranslational modifications by in-source decay during MALDI-TOF mass spectrometry Protein Science. 8: 2487-2493. PMID 10595553 DOI: 10.1110/Ps.8.11.2487 |
0.314 |
|
| 1997 |
Lennon JJ, Walsh KA. Direct sequence analysis of proteins by in-source fragmentation during delayed ion extraction Protein Science. 6: 2446-2453. PMID 9385647 DOI: 10.1002/Pro.5560061118 |
0.343 |
|
| 1996 |
Kowalak JA, Walsh KA. β-Methylthio-aspartic acid: Identification of a novel posttranslational modification in ribosomal protein S12 from Escherichia coli Protein Science. 5: 1625-1632. PMID 8844851 DOI: 10.1002/Pro.5560050816 |
0.362 |
|
| 1996 |
Smith JA, Francis SH, Walsh KA, Kumar S, Corbin JD. Autophosphorylation of type Iβ cGMP-dependent protein kinase increases basal catalytic activity and enhances allosteric activation by cGMP or cAMP Journal of Biological Chemistry. 271: 20756-20762. PMID 8702828 DOI: 10.1074/Jbc.271.34.20756 |
0.315 |
|
| 1996 |
Francist SH, Smith JA, Colbran JL, Grimes K, Walsh KA, Kumar S, Corbin JD. Arginine 75 in the pseudosubstrate sequence of type Iβ cGMP-dependent protein kinase is critical for autoinhibition, although autophosphorylated serine 63 is outside this sequence Journal of Biological Chemistry. 271: 20748-20755. PMID 8702827 DOI: 10.1074/Jbc.271.34.20748 |
0.442 |
|
| 1996 |
Ohguro H, Rudnicka-Nawrot M, Buczyłko J, Zhao X, Taylor JA, Walsh KA, Palczewski K. Structural and enzymatic aspects of rhodopsin phosphorylation. The Journal of Biological Chemistry. 271: 5215-24. PMID 8617805 DOI: 10.1074/Jbc.271.9.5215 |
0.302 |
|
| 1995 |
Resing KA, Johnson RS, Walsh KA. Mass spectrometric analysis of 21 phosphorylation sites in the internal repeat of rat profilaggrin, precursor of an intermediate filament associated protein. Biochemistry. 34: 9477-87. PMID 7626618 DOI: 10.1021/Bi00029A024 |
0.354 |
|
| 1995 |
Thulin CD, Walsh KA. Identification of the amino terminus of human filaggrin using differential LC/MS techniques: implications for profilaggrin processing. Biochemistry. 34: 8687-92. PMID 7612609 DOI: 10.1021/Bi00027A018 |
0.395 |
|
| 1995 |
Thulin CD, Walsh KA. Identification of the amino terminal peptide of N-terminally blocked proteins by differential deutero-acetylation using LC/MS techniques Techniques in Protein Chemistry. 6: 55-62. DOI: 10.1016/S1080-8914(06)80010-4 |
0.413 |
|
| 1994 |
Ohguro H, Johnson RS, Ericsson LH, Walsh KA, Palczewski K. Control of rhodopsin multiple phosphorylation Biochemistry. 33: 1023-1028. PMID 8305429 DOI: 10.1021/Bi00170A022 |
0.302 |
|
| 1994 |
Florio VA, Sonnenburg WK, Johnson R, Kwak KS, Jensen GS, Walsh KA, Beavo JA. Phosphorylation of the 61-kDa calmodulin-stimulated cyclic nucleotide phosphodiesterase at serine 120 reduces its affinity for calmodulin. Biochemistry. 33: 8948-54. PMID 8043581 DOI: 10.1021/Bi00196A012 |
0.576 |
|
| 1994 |
Palczewski K, Buczylko J, Ohguro H, Annan RS, Carr SA, Crabb JW, Kaplan MW, Johnson RS, Walsh KA. Characterization of a truncated form of arrestin isolated from bovine rod outer segments Protein Science. 3: 314-324. PMID 8003967 DOI: 10.1002/Pro.5560030215 |
0.382 |
|
| 1994 |
Ohguro H, Palczewski K, Walsh KA, Johnson RS. Topographic study of arrestin using differential chemical modifications and hydrogen/deuterium exchange Protein Science. 3: 2428-2434. PMID 7756996 DOI: 10.1002/Pro.5560031226 |
0.344 |
|
| 1994 |
Johnson RS, Walsh KA. Mass spectrometric measurement of protein amide hydrogen exchange rates of apo- and holo-myoglobin Protein Science. 3: 2411-2418. PMID 7756994 DOI: 10.1002/Pro.5560031224 |
0.323 |
|
| 1994 |
Palczewski K, Subbaraya I, Gorczyca WA, Helekar BS, Ruiz CC, Ohguro H, Huang J, Zhao X, Crabb JW, Johnson RS, Walsh KA, Gray-Keller MP, Detwiler PB, Baehr W. Molecular cloning and characterization of retinal photoreceptor guanylyl cyclase-activating protein Neuron. 13: 395-404. PMID 7520254 DOI: 10.1016/0896-6273(94)90355-7 |
0.349 |
|
| 1993 |
Ohguro H, Palczewski K, Ericsson LH, Walsh KA, Johnson RS. Sequential phosphorylation of rhodopsin at multiple sites Biochemistry. 32: 5718-5724. PMID 8504090 DOI: 10.1021/Bi00072A030 |
0.327 |
|
| 1993 |
Stover DR, Walsh KA. A Novel Method of Identifying Phosphorylation Sites Using a Thiophosphorylated Peptide and ESI-MS Techniques in Protein Chemistry. 193-200. DOI: 10.1016/B978-0-12-058757-5.50027-5 |
0.325 |
|
| 1992 |
Isom LL, De Jongh KS, Patton DE, Reber BF, Offord J, Charbonneau H, Walsh K, Goldin AL, Catterall WA. Primary structure and functional expression of the beta 1 subunit of the rat brain sodium channel. Science (New York, N.Y.). 256: 839-42. PMID 1375395 DOI: 10.1126/Science.1375395 |
0.585 |
|
| 1992 |
Johnson RS, Walsh KA. Sequence analysis of peptide mixtures by automated integration of Edman and mass spectrometric data Protein Science. 1: 1083-1091. PMID 1304388 DOI: 10.1002/Pro.5560010902 |
0.366 |
|
| 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 |
0.628 |
|
| 1991 |
Stover DR, Charbonneau H, Tonks NK, Walsh KA. Protein-tyrosine-phosphatase CD45 is phosphorylated transiently on tyrosine upon activation of Jurkat T cells Proceedings of the National Academy of Sciences of the United States of America. 88: 7704-7707. PMID 1652760 DOI: 10.1073/Pnas.88.17.7704 |
0.582 |
|
| 1991 |
Novack JP, Charbonneau H, Bentley JK, Walsh KA, Beavo JA. Sequence comparison of the 63-, 61-, and 59-kDa calmodulin-dependent cyclic nucleotide phosphodiesterases. Biochemistry. 30: 7940-7. PMID 1651112 DOI: 10.1021/bi00246a010 |
0.731 |
|
| 1991 |
Charbonneau H, Kumar S, Novack JP, Blumenthal DK, Griffin PR, Shabanowitz J, Hunt DF, Beavo JA, Walsh KA. Evidence for domain organization within the 61-kDa calmodulin-dependent cyclic nucleotide phosphodiesterase from bovine brain. Biochemistry. 30: 7931-40. PMID 1651111 DOI: 10.1021/Bi00246A009 |
0.761 |
|
| 1990 |
Trong HL, Beier N, Sonnenburg WK, Stroop SD, Walsh KA, Beavo JA, Charbonneau H. Amino acid sequence of the cyclic GMP stimulated cyclic nucleotide phosphodiesterase from bovine heart. Biochemistry. 29: 10280-8. PMID 2176866 DOI: 10.1021/Bi00496A018 |
0.751 |
|
| 1990 |
Lozeman FJ, Litchfield DW, Piening C, Takio K, Walsh KA, Krebs EG. Isolation and characterization of human cDNA clones encoding the alpha and the alpha' subunits of casein kinase II. Biochemistry. 29: 8436-47. PMID 2174700 DOI: 10.1021/Bi00488A034 |
0.337 |
|
| 1990 |
Charbonneau H, Prusti RK, LeTrong H, Sonnenburg WK, Mullaney PJ, Walsh KA, Beavo JA. Identification of a noncatalytic cGMP-binding domain conserved in both the cGMP-stimulated and photoreceptor cyclic nucleotide phosphodiesterases. Proceedings of the National Academy of Sciences of the United States of America. 87: 288-92. PMID 2153290 DOI: 10.1073/Pnas.87.1.288 |
0.734 |
|
| 1990 |
Apel ED, Byford MF, Au D, Walsh KA, Storm DR. Identification of the protein kinase C phosphorylation site in neuromodulin. Biochemistry. 29: 2330-5. PMID 2140056 DOI: 10.1021/Bi00461A017 |
0.355 |
|
| 1990 |
Kumar S, Harrylock M, Walsh KA, Cormier MJ, Charbonneau H. Amino acid sequence of the Ca2+-triggered luciferin binding protein of Renilla reniformis Febs Letters. 268: 287-290. PMID 1974522 DOI: 10.1016/0014-5793(90)81029-N |
0.754 |
|
| 1990 |
Fischer EH, Tonks NK, Charbonneau H, Cicirelli MF, Cool DE, Diltz CD, Krebs EG, Walsh KA. Protein tyrosine phosphatases: a novel family of enzymes involved in transmembrane signalling. Advances in Second Messenger and Phosphoprotein Research. 24: 273-9. PMID 1698407 |
0.571 |
|
| 1989 |
Griffin PR, Kumar S, Shabanowitz J, Charbonneau H, Namkung PC, Walsh KA, Hunt DF, Petra PH. The amino acid sequence of the sex steroid-binding protein of rabbit serum Journal of Biological Chemistry. 264: 19066-19075. PMID 2808412 |
0.659 |
|
| 1989 |
Novack JP, Charbonneau H, Blumenthal DK, Walsh KA, Beavo JA. The domain structure of the calmodulin-dependent phosphodiesterase isozymes Advances in Experimental Medicine and Biology. 255: 387-395. PMID 2618869 DOI: 10.1007/978-1-4684-5679-0_42 |
0.744 |
|
| 1989 |
Cool DE, Tonks NK, Charbonneau H, Walsh KA, Fischer EH, Krebs EG. cDNA isolated from a human T-cell library encodes a member of the protein-tyrosine-phosphatase family. Proceedings of the National Academy of Sciences of the United States of America. 86: 5257-61. PMID 2546150 DOI: 10.1073/Pnas.86.14.5257 |
0.664 |
|
| 1989 |
Charbonneau H, Tonks NK, Kumar S, Diltz CD, Harrylock M, Cool DE, Krebs EG, Fischer EH, Walsh KA. Human placenta protein-tyrosine-phosphatase: amino acid sequence and relationship to a family of receptor-like proteins. Proceedings of the National Academy of Sciences of the United States of America. 86: 5252-6. PMID 2546149 DOI: 10.1073/Pnas.86.14.5252 |
0.687 |
|
| 1988 |
Petra PH, Que BG, Namkung PC, Ross JBA, Charbonneau H, Walsh KA, Griffin PR, Shabanowitz J, Hunt DF. Affinity labeling, molecular cloning, and comparative amino acid sequence analyses of sex steroid-binding protein of plasma. A multidisciplinary approach for understanding steroid-protein interaction and its physiological role Annals of the New York Academy of Sciences. 538: 10-24. PMID 3190079 DOI: 10.1111/J.1749-6632.1988.Tb48844.X |
0.656 |
|
| 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 |
0.643 |
|
| 1988 |
Titani K, Walsh KA. Human von Willebrand factor: The molecular glue of platelet plugs Trends in Biochemical Sciences. 13: 94-97. PMID 3072708 DOI: 10.1016/0968-0004(88)90048-5 |
0.376 |
|
| 1988 |
Tonks NK, Charbonneau H, Diltz CD, Fischer EH, Walsh KA. Demonstration that the leukocyte common antigen CD45 is a protein tyrosine phosphatase. Biochemistry. 27: 8695-701. PMID 2853967 DOI: 10.1021/Bi00424A001 |
0.595 |
|
| 1988 |
Charbonneau H, Tonks NK, Walsh KA, Fischer EH. The leukocyte common antigen (CD45): a putative receptor-linked protein tyrosine phosphatase. Proceedings of the National Academy of Sciences of the United States of America. 85: 7182-6. PMID 2845400 DOI: 10.1073/Pnas.85.19.7182 |
0.659 |
|
| 1987 |
Eyre DR, Apon S, Wu JJ, Ericsson LH, Walsh KA. Collagen type IX: Evidence for covalent linkages to type II collagen in cartilage Febs Letters. 220: 337-341. PMID 3609327 DOI: 10.1016/0014-5793(87)80842-6 |
0.359 |
|
| 1987 |
Marti T, Takio K, Walsh KA, Terzi G, Truman JW. Microanalysis of the amino acid sequence of the eclosion hormone from the tobacco hornworm Manduca sexta. Febs Letters. 219: 415-8. PMID 3609300 DOI: 10.1016/0014-5793(87)80263-6 |
0.452 |
|
| 1987 |
Cover WH, Ryan JP, Bassford PJ, Walsh KA, Bollinger J, Randall LL. Suppression of a signal sequence mutation by an amino acid substitution in the mature portion of the maltose-binding protein. Journal of Bacteriology. 169: 1794-800. PMID 3553148 DOI: 10.1128/Jb.169.5.1794-1800.1987 |
0.339 |
|
| 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 |
0.654 |
|
| 1987 |
Marti T, Rösselet SJ, Titani K, Walsh KA. Identification of disulfide-bridged substructures within human von Willebrand factor Biochemistry. 26: 8099-8109. PMID 3502076 DOI: 10.1021/Bi00399A013 |
0.4 |
|
| 1987 |
Takio K, Kuenzel EA, Walsh KA, Krebs EG. Amino acid sequence of the beta subunit of bovine lung casein kinase II. Proceedings of the National Academy of Sciences of the United States of America. 84: 4851-5. PMID 3299375 DOI: 10.1073/Pnas.84.14.4851 |
0.409 |
|
| 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 |
0.621 |
|
| 1987 |
Ericsson LH, Eriksen N, Walsh KA, Benditt EP. Primary structure of duck amyloid protein A The form deposited in tissues may be identical to its serum precursor Febs Letters. 218: 11-16. PMID 3109944 DOI: 10.1016/0014-5793(87)81008-6 |
0.374 |
|
| 1987 |
Wakim BT, Alexander KA, Masure HR, Cimler BM, Storm DR, Walsh KA. Amino acid sequence of P-57, a neurospecific calmodulin-binding protein. Biochemistry. 26: 7466-70. PMID 2962637 DOI: 10.1021/Bi00397A040 |
0.465 |
|
| 1987 |
Metrione RM, Schweitz H, Walsh KA. The amino acid sequence of toxin RpIII from the sea anemone, Radianthus paumotensis Febs Letters. 218: 59-62. PMID 2885222 DOI: 10.1016/0014-5793(87)81018-9 |
0.45 |
|
| 1987 |
Charbonneau H, Novack JP, MacFarland RT, Walsh KA, Beavo JA. Structure And Function Of Calmodulin-Dependent Phosphodiesterase Isozymes Calcium-Binding Proteins in Health and Disease. 505-517. DOI: 10.1016/B978-0-12-521040-9.50092-9 |
0.687 |
|
| 1986 |
Hormel S, Walsh KA, Prickril BC, Titani K, LeGall J, Sieker LC. Amino acid sequence of rubredoxin from Desulfovibrio desulfuricans strain 27774 Febs Letters. 201: 147-150. PMID 3709804 DOI: 10.1016/0014-5793(86)80588-9 |
0.422 |
|
| 1986 |
Takio K, Blumenthal DK, Walsh KA, Titani K, Krebs EG. Amino acid sequence of rabbit skeletal muscle myosin light chain kinase. Biochemistry. 25: 8049-57. PMID 3542042 DOI: 10.1021/Bi00372A038 |
0.464 |
|
| 1986 |
Walsh KA, Titani K, Takio K, Kumar S, Hayes R, Petra PH. Amino acid sequence of the sex steroid binding protein of human blood plasma Biochemistry. 25: 7584-7590. PMID 3542030 DOI: 10.1021/Bi00371A048 |
0.487 |
|
| 1986 |
Titani K, Kumar S, Takio K, Ericsson LH, Wade RD, Ashida K, Walsh KA, Chopek MW, Sadler JE, Fujikawa K. Amino acid sequence of human von Willebrand factor Biochemistry. 25: 3171-3184. PMID 3524673 DOI: 10.1021/Bi00359A015 |
0.473 |
|
| 1986 |
Hormel S, Adman E, Walsh KA, Beppu T, Titani K. The amino acid sequence of the blue copper protein of Alcaligenes faecalis Febs Letters. 197: 301-304. PMID 3512305 DOI: 10.1016/0014-5793(86)80346-5 |
0.407 |
|
| 1986 |
Charbonneau H, Beier N, Walsh KA, Beavo JA. Identification of a conserved domain among cyclic nucleotide phosphodiesterases from diverse species Proceedings of the National Academy of Sciences of the United States of America. 83: 9308-9312. PMID 3025833 DOI: 10.1073/Pnas.83.24.9308 |
0.744 |
|
| 1985 |
Resing KA, Dale BA, Walsh KA. Multiple copies of phosphorylated filaggrin in epidermal profilaggrin demonstrated by analysis of tryptic peptides Biochemistry. 24: 4167-4175. PMID 4052387 DOI: 10.1021/Bi00336A053 |
0.392 |
|
| 1985 |
Edelman AM, Takio K, Blumenthal DK, Hansen RS, Walsh KA, Titani K, Krebs EG. Characterization of the calmodulin-binding and catalytic domains in skeletal muscle myosin light chain kinase. The Journal of Biological Chemistry. 260: 11275-85. PMID 3897230 |
0.323 |
|
| 1985 |
Resing K, Green JD, Walsh KA. A 53,000-Da esterase in Strongylocentrotus purpuratus semen is derived from phagocytic cells, not sperm Developmental Biology. 107: 87-93. PMID 3880713 DOI: 10.1016/0012-1606(85)90378-1 |
0.316 |
|
| 1985 |
Blumenthal DK, Takio K, Edelman AM, Charbonneau H, Titani K, Walsh KA, Krebs EG. Identification of the calmodulin-binding domain of skeletal muscle myosin light chain kinase. Proceedings of the National Academy of Sciences of the United States of America. 82: 3187-91. PMID 3858814 DOI: 10.1073/Pnas.82.10.3187 |
0.667 |
|
| 1985 |
Takio K, Blumenthal DK, Edelman AM, Walsh KA, Krebs EG, Titani K. Amino acid sequence of an active fragment of rabbit skeletal muscle myosin light chain kinase. Biochemistry. 24: 6028-37. PMID 3841288 DOI: 10.1021/Bi00343A002 |
0.461 |
|
| 1985 |
Charbonneau H, Walsh KA, McCann RO, Prendergast FG, Cormier MJ, Vanaman TC. Amino acid sequence of the calcium-dependent photoprotein aequorin Biochemistry. 24: 6762-6771. PMID 2866797 DOI: 10.1021/Bi00345A006 |
0.824 |
|
| 1984 |
Hoffman JS, Ericsson LH, Eriksen N, Walsh KA, Benditt EP. Murine tissue amyloid protein AA. NH2-terminal sequence identity with only one of two serum amyloid protein (ApoSAA) gene products. The Journal of Experimental Medicine. 159: 641-6. PMID 6693836 DOI: 10.1084/Jem.159.2.641 |
0.416 |
|
| 1984 |
Marchildon GA, Casnellie JE, Walsh KA, Krebs EG. Covalently bound myristate in a lymphoma tyrosine protein kinase. Proceedings of the National Academy of Sciences of the United States of America. 81: 7679-82. PMID 6595656 DOI: 10.1073/Pnas.81.24.7679 |
0.355 |
|
| 1984 |
Reimann EM, Titani K, Ericsson LH, Wade RD, Fischer EH, Walsh KA. Homology of the gamma subunit of phosphorylase b kinase with cAMP-dependent protein kinase. Biochemistry. 23: 4185-92. PMID 6541504 DOI: 10.1021/Bi00313A027 |
0.417 |
|
| 1984 |
Karplus PA, Walsh KA, Herriott JR. Amino acid sequence of spinach ferredoxin:NADP+ oxidoreductase Biochemistry. 23: 6576-6583. PMID 6529571 DOI: 10.1021/Bi00321A046 |
0.824 |
|
| 1984 |
Titani K, Sasagawa T, Ericsson LH, Kumar S, Smith SB, Krebs EG, Walsh KA. Amino acid sequence of the regulatory subunit of bovine type I adenosine cyclic 3',5'-phosphate dependent protein kinase. Biochemistry. 23: 4193-9. PMID 6487597 DOI: 10.1021/Bi00313A028 |
0.414 |
|
| 1984 |
Resing KA, Walsh KA, Dale BA. Identification of two intermediates during processing of profilaggrin to filaggrin in neonatal mouse epidermis Journal of Cell Biology. 99: 1372-1378. PMID 6480697 DOI: 10.1083/Jcb.99.4.1372 |
0.349 |
|
| 1984 |
Takio K, Smith SB, Krebs EG, Walsh KA, Titani K. Amino acid sequence of the regulatory subunit of bovine type II adenosine cyclic 3',5'-phosphate dependent protein kinase. Biochemistry. 23: 4200-6. PMID 6386045 DOI: 10.1021/bi00313a029 |
0.375 |
|
| 1984 |
Takio K, Wade RD, Smith SB, Krebs EG, Walsh KA, Titani K. Guanosine cyclic 3',5'-phosphate dependent protein kinase, a chimeric protein homologous with two separate protein families. Biochemistry. 23: 4207-18. PMID 6091741 DOI: 10.1021/Bi00313A030 |
0.411 |
|
| 1984 |
Walsh KA, Sasagawa T. [3] High-performance liquid chromatography probes for posttranslationally modified amino acids Methods in Enzymology. 106: 22-29. DOI: 10.1016/0076-6879(84)06005-5 |
0.412 |
|
| 1983 |
Walsh KA, Daniel RM, Morgan HW. A soluble NADH dehydrogenase (NADH: ferricyanide oxidoreductase) from Thermus aquaticus strain T351 Biochemical Journal. 209: 427-433. PMID 6847628 DOI: 10.1042/Bj2090427 |
0.304 |
|
| 1983 |
Sasagawa T, Titani K, Walsh KA. Selective isolation of tryptophan-containing peptides by hydrophobicity modulation Analytical Biochemistry. 134: 224-229. PMID 6660492 DOI: 10.1016/0003-2697(83)90288-9 |
0.311 |
|
| 1983 |
Shoji S, Ericsson LH, Walsh KA, Fischer EH, Titani K. Amino acid sequence of the catalytic subunit of bovine type II adenosine cyclic 3',5'-phosphate dependent protein kinase. Biochemistry. 22: 3702-9. PMID 6311252 DOI: 10.1021/Bi00284A025 |
0.466 |
|
| 1983 |
Sasagawa T, Titani K, Walsh KA. Selective isolation of methionine-containing peptides by hydrophobicity modulation Analytical Biochemistry. 128: 371-376. PMID 6303157 DOI: 10.1016/0003-2697(83)90388-3 |
0.307 |
|
| 1982 |
Titani K, Sasagawa T, Resing K, Walsh KA. A simple and rapid purification of commercial trypsin and chymotrypsin by reverse-phase high-performance liquid chromatography Analytical Biochemistry. 123: 408-412. PMID 7125214 DOI: 10.1016/0003-2697(82)90465-1 |
0.34 |
|
| 1982 |
Parmelee DC, Titani K, Ericsson LH, Eriksen N, Benditt EP, Walsh KA. Amino acid sequence of amyloid-related apoprotein (apoSAA1) from human high-density lipoprotein. Biochemistry. 21: 3298-303. PMID 7115671 DOI: 10.1021/Bi00257A008 |
0.371 |
|
| 1982 |
Bloxham DP, Parmelee DC, Kumar S, Walsh KA, Titani K. Complete amino acid sequence of porcine heart citrate synthase Biochemistry. 21: 2028-2036. PMID 7093227 DOI: 10.1021/Bi00538A009 |
0.481 |
|
| 1982 |
Sasagawa T, Ericsson LH, Walsh KA, Schreiber WE, Fischer EH, Titani K. Complete amino acid sequence of human brain calmodulin. Biochemistry. 21: 2565-9. PMID 7093203 DOI: 10.1021/Bi00539A041 |
0.474 |
|
| 1982 |
Takio K, Smith SB, Krebs EG, Walsh KA, Titani K. Primary structure of the regulatory subunit of type II cAMP-dependent protein kinase from bovine cardiac muscle. Proceedings of the National Academy of Sciences of the United States of America. 79: 2544-8. PMID 6283532 DOI: 10.1073/Pnas.79.8.2544 |
0.445 |
|
| 1982 |
Soderling TR, Walsh K. Selective modification and purification of phosphopeptides for automated sequence analysis Journal of Chromatography A. 253: 243-251. DOI: 10.1016/S0021-9673(01)88382-5 |
0.357 |
|
| 1981 |
Walsh KA, Ericsson LH, Parmelee DC, Titani K. Advances in protein sequencing Annual Review of Biochemistry. 50: 261-284. PMID 7023360 DOI: 10.1146/Annurev.Bi.50.070181.001401 |
0.38 |
|
| 1981 |
Bradshaw RA, Cancedda F, Ericsson LH, Neumann PA, Piccoli SP, Schlesinger MJ, Shriefer K, Walsh KA. Amino acid sequence of Escherichia coli alkaline phosphatase. Proceedings of the National Academy of Sciences of the United States of America. 78: 3473-7. PMID 7022451 DOI: 10.1073/Pnas.78.6.3473 |
0.481 |
|
| 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 |
0.622 |
|
| 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 |
0.649 |
|
| 1980 |
Thibodeau SN, Walsh KA. Processing of precursor proteins by preparations of oviduct microsomes Annals of the New York Academy of Sciences. 343: 180-191. PMID 6930850 DOI: 10.1111/J.1749-6632.1980.Tb47251.X |
0.319 |
|
| 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 |
0.6 |
|
| 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 |
0.619 |
|
| 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 |
0.593 |
|
| 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 |
0.553 |
|
| 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 |
0.629 |
|
| 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 |
0.638 |
|
| 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 |
0.6 |
|
| 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 |
0.622 |
|
| 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 |
0.571 |
|
| 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 |
0.542 |
|
| 1978 |
Palmiter RD, Gagnon J, Walsh KA. Ovalbumin: A secreted protein without a transient hydrophobic leader sequence Proceedings of the National Academy of Sciences of the United States of America. 75: 94-98. PMID 272676 DOI: 10.1073/Pnas.75.1.94 |
0.426 |
|
| 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 |
0.588 |
|
| 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 |
0.602 |
|
| 1977 |
Fujikawa K, Walsh KA, Davie EW. Isolation and characterization of bovine factor XII (hageman factor) Biochemistry. 16: 2270-2278. PMID 861210 DOI: 10.1021/Bi00629A036 |
0.465 |
|
| 1977 |
Bitar KG, Blankenship DT, Walsh KA, Dunlap RB, Reddy AV, Freisheim JH. Amino acid sequence of dihydrofolate reductase from an amethopterin-resistant strain of Lactobacillus casei. Febs Letters. 80: 119-22. PMID 408191 DOI: 10.1016/0014-5793(77)80420-1 |
0.369 |
|
| 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 |
0.623 |
|
| 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 |
0.566 |
|
| 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 |
0.469 |
|
| 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 |
0.524 |
|
| 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 |
0.559 |
|
| 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 |
0.555 |
|
| 1975 |
Fodor EJB, Ako H, Walsh KA. Isolation of a protease from sea urchin eggs before and after fertilization. Biochemistry. 14: 4923-4927. PMID 1182129 DOI: 10.1021/Bi00693A022 |
0.317 |
|
| 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 |
0.574 |
|
| 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 |
0.665 |
|
| 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 |
0.621 |
|
| 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 |
0.622 |
|
| 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 |
0.618 |
|
| 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 |
0.628 |
|
| 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 |
0.497 |
|
| 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 |
0.509 |
|
| 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 |
0.556 |
|
| 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 |
0.559 |
|
| 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 |
0.462 |
|
| 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 |
0.537 |
|
| 1974 |
Walsh KA, Burstein Y, Pangburn MK. [50] Thermolysin and other neutral metalloendopeptidases Methods in Enzymology. 34: 435-440. PMID 4217421 DOI: 10.1016/S0076-6879(74)34053-0 |
0.388 |
|
| 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 |
0.453 |
|
| 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 |
0.617 |
|
| 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 |
0.496 |
|
| 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 |
0.564 |
|
| 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 |
0.512 |
|
| 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 |
0.504 |
|
| 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 |
0.6 |
|
| 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 |
0.619 |
|
| 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 |
0.502 |
|
| 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 |
0.609 |
|
| 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 |
0.574 |
|
| 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 |
0.493 |
|
| 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 |
0.749 |
|
| 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 |
0.511 |
|
| 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 |
0.757 |
|
| 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 |
0.536 |
|
| 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 |
0.673 |
|
| 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 |
0.554 |
|
| 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 |
0.598 |
|
| 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 |
0.562 |
|
| 1970 |
Neurath H, Walsh KA, Bradshaw RA. Enzymes in crystals. Nature. 225: 881. PMID 16056793 DOI: 10.1038/225881B0 |
0.487 |
|
| 1970 |
Sanders MM, Walsh KA, Arnon R. Immunological cross-reaction between trypsin and chymotrypsin as a guide to structural homology Biochemistry. 9: 2356-2363. PMID 5463758 DOI: 10.1021/Bi00813A020 |
0.372 |
|
| 1970 |
Houston LL, Walsh KA. The transient inactivation of trypsin by mild acetylation with N-acetylimidazole Biochemistry. 9: 156-166. PMID 5460783 DOI: 10.1021/Bi00803A020 |
0.307 |
|
| 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 |
0.624 |
|
| 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 |
0.48 |
|
| 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 |
0.526 |
|
| 1969 |
Granberg RR, Walsh KA, Bradshaw RA. Increased output and accelerated analysis time with the automatic amino acid analyzer Analytical Biochemistry. 30: 454-464. PMID 5821306 DOI: 10.1016/0003-2697(69)90141-9 |
0.364 |
|
| 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 |
0.589 |
|
| 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 |
0.538 |
|
| 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 |
0.55 |
|
| 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 |
0.536 |
|
| 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 |
0.604 |
|
| 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 |
0.627 |
|
| 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 |
0.522 |
|
| 1968 |
Winter WP, Walsh KA, Neurath H. Homology as applied to proteins Science. 162: 1433. PMID 5700064 DOI: 10.1126/Science.162.3861.1433 |
0.52 |
|
| 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 |
0.415 |
|
| 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 |
0.521 |
|
| 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 |
0.539 |
|
| 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 |
0.485 |
|
| 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 |
0.554 |
|
| 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 |
0.504 |
|
| 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 |
0.642 |
|
| 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 |
0.511 |
|
| 1964 |
Kumar KSVS, Walsh KA, Neurath H. Chemical characterization of bovine carboxypeptidase A isolated from a single pancreas Biochemistry. 3: 1726-1727. PMID 14235338 |
0.444 |
|
| 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 |
0.524 |
|
| 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 |
0.487 |
|
| 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 |
0.49 |
|
| 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 |
0.559 |
|
| 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 |
0.422 |
|
| 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 |
0.56 |
|
| 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 |
0.485 |
|
| 1962 |
Walsh KA, Kauffman DL, Neurath H. The amino terminal sequence of bovine trypsinogen Biochemistry. 1: 893-898. PMID 13998642 DOI: 10.1021/Bi00911A023 |
0.624 |
|
| 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 |
0.519 |
|
| 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 |
0.492 |
|
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