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Sensitive substrates for human leukocyte and porcine pancreatic elastase: A study of the merits of various chromophoric and fluorogenic leaving groups in assays for serine proteases
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“The KM for MeOSuc-AAPV-pNA was found to be 0.152 mM compared to a previously published value of 0.14 mM [29].”
From Discrimination of Methionine Sulfoxide and Sulfone by Human Neutrophil Elastase (2021) · cites this paper as [29]
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Cites
Ellman, G. L. (1959) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(59)90090-6 · Cited by 26,824
The preparation and properties of two new chromogenic substrates of trypsin
Erlanger, B. F., Kokowsky, N., & Cohen, W. (1961) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(61)90145-x · Cited by 3,346
Determination of sulfhydryl groups with 2,2′- or 4,4′-dithiodipyridine
Grassetti, D. R., & Murray, J. F. (1967) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(67)90426-2 · Cited by 988
The synthesis and analytical use of a highly sensitive and convenient substrate of elastase
Bieth, J. G., Spiess, B., & Wermuth, C. G. (1974) · Biochemical Medicine · doi:10.1016/0006-2944(74)90134-3 · Cited by 732
Nakajima, K., Powers, J. C., Ashe, B. M., & Zimmerman, M. D. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)50690-6 · Cited by 595
Self-citationNew Fluorogenic Substrates for α-Thrombin, Factor Xa, Kallikreins, and Urokinase1
Morita, T., Kato, H., Iwanaga, S., Takada, K., Kimura, T., & Sakakibara, S. (1977) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a131840 · Cited by 382
Sensitive assays for trypsin, elastase, and chymotrypsin using new fluorogenic substrates
Zimmerman, M. D., Ashe, B. M., Yurewicz, E. C., & Patel, G. F. (1977) · Analytical Biochemistry · doi:10.1016/0003-2697(77)90006-9 · Cited by 264
Self-citationPowers, J. C., Gupton, B. F., Harley, A. D., Nishino, N., & Whitley, R. J. (1977) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(77)90203-0 · Cited by 223
Self-citationA new fluorogenic substrate for chymotrypsin
Zimmerman, M., Yurewicz, E. C., & Patel, G. F. (1976) · Analytical Biochemistry · doi:10.1016/s0003-2697(76)80066-8 · Cited by 187
Self-citationMcDonald, J. K., & Ellis, S. (1975) · Life Sciences · doi:10.1016/0024-3205(75)90137-x · Cited by 165
Research works printed but not linked: 8
- Hance, 1975, Amer. Rev. Resp. Dis, 112, 656
- Zimmerman, 1977, 75, 750
- Yurewicz, 1975, 34, 234
- Powers, 1977, Vol. 46, 208
- Lehninger, 1957, Vol. 3, 886
- Palgar, 1972, Acta Biochim. Biophys. Acad. Sci. Hung, 7, 319
- Hirohara, 1974, 71, 1643
- Geneste, 1969, 64, 683
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Wewers, M. D., Casolaro, M. A., Sellers, S. E., Swayze, S. C., McPhaul, K. M., Wittes, J. T., & Crystal, R. G. (1987) · New England Journal of Medicine · doi:10.1056/nejm198704233161704 · Cited by 631
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Campbell, E. J., Senior, R. M., McDonald, J. A., Cox, D. L., Greco, J. M., & Landis, J. A. (1982) · Journal of Clinical Investigation · doi:10.1172/jci110681 · Cited by 243
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Ogushi, F., Fells, G. A., Hubbard, R. C., Straus, S. D., & Crystal, R. G. (1987) · Journal of Clinical Investigation · doi:10.1172/jci113214 · Cited by 215
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Wachtfogel, Y. T., Kucich, U., James, H. L., Scott, C. F., Schapira, M., Zimmerman, M. D., Cohen, A. B., & Colman, R. W. (1983) · Journal of Clinical Investigation · doi:10.1172/jci111126 · Cited by 211
Self-citationThe major neutral proteinase of Entamoeba histolytica.
Keene, W. E., Petitt, M., Allen, S., & McKerrow, J. H. (1986) · The Journal of Experimental Medicine · doi:10.1084/jem.163.3.536 · Cited by 196
Neutrophil-mediated epithelial injury during transmigration: role of elastase
Ginzberg, H. H., Cherapanov, V., Dong, Q., Cantin, A. M., McCulloch, C. A., Shannon, P. T., & Downey, G. P. (2001) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.2001.281.3.g705 · Cited by 194
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Powers, J. C., Tanaka, T., Harper, J. W., Minematsu, Y., Barker, L. N., Lincoln, D., Crumley, K. V., Fräki, J. E., & Schechter, N. M. (1985) · Biochemistry · doi:10.1021/bi00329a037 · Cited by 175
Self-citationNeutral endopeptidase 24.11 in human neutrophils: cleavage of chemotactic peptide.
Connelly, J. C., Skidgel, R. A., Schulz, W., Johnson, A. R., & Erdös, E. G. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.24.8737 · Cited by 172
Rhodamine-based compounds as fluorogenic substrates for serine proteinases
Leytus, S. P., Melhado, L. L., & Mangel, W. F. (1983) · Biochemical Journal · doi:10.1042/bj2090299 · Cited by 166
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Giannopoulou, C., & Cimasoni, G. (1996) · Journal of Dental Research · doi:10.1177/00220345960750030601 · Cited by 156
McKerrow, J. H., Pino-Heiss, S., Lindquist, R. N., & Werb, Z. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)83680-3 · Cited by 151
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Dunwiddie, C. T., Thornberry, N. A., Bull, H. G., Sardana, M. K., Friedman, P. A., Jacobs, J., & Simpson, E. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84761-0 · Cited by 151
Yöder, M. C., Chua, R., & Tepper, R. S. (1991) · American Review of Respiratory Disease · doi:10.1164/ajrccm/143.5_pt_1.1044 · Cited by 137
Wewers, M. D., Herzyk, D. J., & Gadek, J. E. (1988) · Journal of Clinical Investigation · doi:10.1172/jci113724 · Cited by 131
Barrett, A. J. (1981) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(81)80046-8 · Cited by 127
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Senior, R. M., Campbell, E. J., Landis, J. A., Cox, F. R., Kuhn, C., & Koren, H. S. (1982) · Journal of Clinical Investigation · doi:10.1172/jci110462 · Cited by 125
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Waxman, L., & Darke, P. L. (2000) · Antiviral chemistry & chemotherapy · doi:10.1177/095632020001100101 · Cited by 122
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Idell, S., Kucich, U., Fein, A. M., Kueppers, F., James, H. L., Walsh, P. N., Weinbaum, G., Colman, R. W., & Cohen, A. B. (1985) · PubMed · doi:10.1164/arrd.1985.132.5.1098 · Cited by 110
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Asahi, M., Lindquist, R. N., Fukuyama, K., Apodaca, G., Epstein, W. L., & McKerrow, J. H. (1985) · Biochemical Journal · doi:10.1042/bj2320139 · Cited by 106
Sklar, L. A., McNeil, V. M., Jesaitis, A. J., Painter, R. G., & Cochrane, C. G. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)83801-2 · Cited by 105
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McRae, B. J., Kurachi, K., Heimark, R. L., Fujikawa, K., Davie, E. W., & Powers, J. C. (1981) · Biochemistry · doi:10.1021/bi00528a022 · Cited by 92
Self-citationHarper, J. W., Cook, R. R., Roberts, C. J., McLaughlin, B. H., & Powers, J. C. (1984) · Biochemistry · doi:10.1021/bi00308a023 · Cited by 91
Self-citationCathepsin-G and leukocyte elastase inactivate human tumor necrosis factor and lymphotoxin
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Secretion of a proteolytic anticoagulant by Ancylostoma hookworms.
Hotez, P. J., & Cerami, A. (1983) · The Journal of Experimental Medicine · doi:10.1084/jem.157.5.1594 · Cited by 89
Plagnat, D., Giannopoulou, C., Carrel, A., Bernard, J., Mombelli, A., & Belser, U. C. (2002) · Clinical Oral Implants Research · doi:10.1034/j.1600-0501.2002.130301.x · Cited by 88
Teshima, T., Griffin, J., & Powers, J. C. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34638-6 · Cited by 88
Self-citationGiannopoulou, C., Andersen, E., Demeurisse, C., & Cimasoni, G. (1992) · Journal of Dental Research · doi:10.1177/00220345920710020301 · Cited by 88
Smith, C. E., & Johnson, D. A. (1985) · Biochemical Journal · doi:10.1042/bj2250463 · Cited by 87
Trifilieff, A., Walker, C., Keller, T. H., Kottirsch, G., & Neumann, U. (2002) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0704616 · Cited by 86
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Schrijver, G., Schalkwijk, J., Robben, J. C. M., Assmann, K. J. M., & Koene, R. A. P. (1989) · The Journal of Experimental Medicine · doi:10.1084/jem.169.4.1435 · Cited by 85
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Bieth, J. G. (1981) · Elsevier eBooks · doi:10.1016/b978-0-08-027379-2.50020-x · Cited by 84
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Kramps, J. A., Twisk, C. V., & Derlinden, A. C. V. (1983) · Scandinavian Journal of Clinical and Laboratory Investigation · doi:10.1080/00365518309168282 · Cited by 83
Chang, M., Kistler, E. B., & Schmid‐Schönbein, G. W. (2011) · Shock · doi:10.1097/shk.0b013e318240b59b · Cited by 82
Motegi, Y., & Kita, H. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.161.8.4340 · Cited by 80
Harper, J. W., & Powers, J. C. (1985) · Biochemistry · doi:10.1021/bi00346a028 · Cited by 80
Self-citationZhang, X., Wu, H., Li, P., Qu, Z., Tan, M., & Han, K. (2016) · Chemical Communications · doi:10.1039/c6cc04373a · Cited by 79
Assmann, K. J. M., van Son, J. P., Dijkman, H. B. P. M., & Koene, R. A. P. (1992) · The Journal of Experimental Medicine · doi:10.1084/jem.175.3.623 · Cited by 79
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Saugstad, O. D., Hallman, M., Abraham, J. L., Epstein, B. L., Cochrane, C. G., & Gluck, L. (1984) · Pediatric Research · doi:10.1203/00006450-198406000-00002 · Cited by 74
Tchoupé, J. R., Moreau, T., Gauthier, F., & Bieth, J. G. (1991) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(91)90232-o · Cited by 71
Wewers, M. D., Casolaro, M. A., & Crystal, R. G. (1987) · PubMed · doi:10.1164/arrd.1987.135.3.539 · Cited by 70
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Yoshioka, A., Betsuyaku, T., Nishimura, M., Miyamoto, K., Kondo, T., & Kawakami, Y. (1995) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.152.6.8520785 · Cited by 69
Hasmann, A., Geweßler, U., Hulla, E., Schneider, K. P., Binder, B., Francesko, A., Tzanov, T., Schintler, M., van der Palen, J. A. M., Guebitz, G. M., et al. (2011) · Experimental Dermatology · doi:10.1111/j.1600-0625.2011.01256.x · Cited by 70
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Kam, C. M., McRae, B. J., Harper, J. W., Niemann, M. A., Volanakis, J. E., & Powers, J. C. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61371-7 · Cited by 68
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Tani, K., Yasuoka, S., Ogushi, F., Asada, K., Fujisawa, K., Ozaki, T., Sano, N., & Ogura, T. (1991) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb/5.1.34 · Cited by 66
Sadowska, A. M., van Overveld, F. J., Górecka, D., Zdral, A., Filewska, M., Demkow, U. A., Luyten, C., Saenen, E., Zielinski, J., & Backer, W. A. D. (2004) · Respiratory Medicine · doi:10.1016/j.rmed.2004.07.005 · Cited by 65
Takeuchi, K., Wood, H., & Swank, R. T. (1986) · The Journal of Experimental Medicine · doi:10.1084/jem.163.3.665 · Cited by 64
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Strickland, D. K., Bhattacharya, P., & Olson, S. T. (1984) · Biochemistry · doi:10.1021/bi00309a002 · Cited by 61
Hu, J., den Steen, P. E. V., Dillen, C., & Opdenakker, G. (2005) · Biochemical Pharmacology · doi:10.1016/j.bcp.2005.04.047 · Cited by 55
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Cho, K., Tanaka, T., Cook, R. R., Kisiel, W., Fujikawa, K., Kurachi, K., & Powers, J. C. (1984) · Biochemistry · doi:10.1021/bi00299a009 · Cited by 55
Self-citationNeutrophils Mediate Acute Lung Injury in Rabbits: Role of Neutrophil Elastase
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Schalkwijk, J., van den Berg, W. B., van de Putte, L. B., & Joosten, L. A. B. (1987) · PubMed Central · Cited by 54
Mahajan, A., Grüneboom, A., Hasíková, L., Podolska, M. J., Kling, L., Maueröder, C., Dahms, F., Christiansen, S. H., Lochnit, G., Krenn, V., et al. (2019) · Journal of Leukocyte Biology · doi:10.1002/jlb.hi0718-249rr · Cited by 53
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Isaacs, W. B., & Coffey, D. S. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)90893-8 · Cited by 52
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Self-citationBrower, M. S., Walz, D. A., Garry, K., & Fenton, J. W. (1987) · PubMed · doi:10.1182/blood.v69.3.813.813 · Cited by 48
Poe, M., Bennett, C. D., Biddison, W. E., Blake, J. T., Norton, G. P., Rodkey, J. A., SIGAL, N. H., Turner, R. V., Wu, J. K., & Zweerink, H. J. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37694-4 · Cited by 47
Backer, W. A. D., Amsel, B. J., Jorens, P. G., Bossaert, L. L., Hiemstra, P. S., van Noort, P., & van Overveld, F. J. (1996) · Intensive Care Medicine · doi:10.1007/bf02044114 · Cited by 47
樋口, 和., Kajiki, A., Nakamura, M., Harada, S., Pula, P. J., Scott, A. L., & Dannenberg, A. M. (1988) · Inflammation · doi:10.1007/bf00915768 · Cited by 47
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Resnick, S., Pappagianis, D., & McKerrow, J. H. (1987) · Infection and Immunity · doi:10.1128/iai.55.11.2807-2815.1987 · Cited by 47
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Yoshimura, T., Barker, L. N., & Powers, J. C. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34637-4 · Cited by 46
Self-citationCantin, A., Bilodeau, G., & Bégin, R. (1989) · Pediatric Pulmonology · doi:10.1002/ppul.1950070105 · Cited by 54
Edelstein, C., Italia, J. A., & Scanu, A. M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.17.11079 · Cited by 45
Lungarella, G., Menegazzi, R., Gardi, C., Spessotto, P., Santi, M. M. D., Bertoncin, P., Patriarca, P., Calzoni, P., & Zabucchi, G. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90060-a · Cited by 44
Lowe, F. C., & Isaacs, J. T. (1984) · PubMed · Cited by 44
Honda, M. (2023) · Food Chemistry · doi:10.1016/j.foodchem.2023.135954 · Cited by 43
Metadata
- Authors
- Castillo, M. J., Nakajima, K., Zimmerman, M., & Powers, J. C.
- Affiliations
- Georgia Institute of Technology (US)
- Merck & Co., Inc., Rahway, NJ, USA (United States) (US)
- Corresponding author
- Powers, James C.
- Venue
- Analytical Biochemistry
- Publisher
- Elsevier BV
- Published
- 1979-10
- Volume
- 99
- Issue
- 1
- Pages
- 53-64
- ISSN
- 0003-2697 (ISSN-L)
- OpenAlex
- W2059777229
- Cited by
- 268
- References
- 28
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 3 · 2023: 4 · 2022: 3 · 2021: 4 · 2020: 2 · 2019: 2 · 2018: 4 · 2017: 6 · 2016: 3 · 2015: 1 · 2014: 4 · 2013: 3 · 2012: 3
- FWCI
- 5.55
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Analytical Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Peptidase Inhibition and Analysis
- Keywords
- elastase, neutrophil elastase, porcine pancreatic elastase, fluorogenic substrates, chromogenic substrates, 4-methylcoumarin, Ellman's reagent, 4,4'-dithiodipyridine, enzyme kinetics, substrate sensitivity
- MeSH terms
- Amino Acid Sequence, Animals, Humans, Indicators and Reagents, Kinetics, Leukocytes, Oligopeptides, Pancreas, Pancreatic Elastase, Peptide Hydrolases, Serine, Spectrometry, Fluorescence, Substrate Specificity, Swine
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