The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.
Antioxidant enzymes in the digestive gland of the common mussel Mytilus edulis
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 317,331
(1975) · Journal of AOAC INTERNATIONAL · doi:10.1093/jaoac/58.5.1085 · Cited by 19,795
McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63504-5 · Cited by 12,952
Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase.
Paglia, D. E., & Valentine, W. N. (1967) · PubMed · Cited by 10,889
Glutathione peroxidase activity in selenium-deficient rat liver
Lawrence, R. A., & Burk, R. F. (1976) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(76)90747-6 · Cited by 3,528
Wendel, A. (1981) · Methods in Enzymology · doi:10.1016/s0076-6879(81)77046-0 · Cited by 3,009
Assaying for superoxide dismutase activity: Some large consequences of minor changes in conditions
Beyer, W. F., & Fridovich, I. (1987) · Analytical Biochemistry · doi:10.1016/0003-2697(87)90489-1 · Cited by 2,915
Oxygen free radicals and iron in relation to biology and medicine: Some problems and concepts
Halliwell, B., & Gutteridge, J. M. C. (1986) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(86)90305-x · Cited by 2,038
Prooxidant and antioxidant mechanisms in aquatic organisms
Winston, G. W., & Di Giulio, R. T. (1991) · Aquatic Toxicology · doi:10.1016/0166-445x(91)90033-6 · Cited by 1,353
Handbook Methods For Oxygen Radical Research: 0
(2018) · CRC Press eBooks · doi:10.1201/9781351072922 · Cited by 737
The antioxidant action of taurine, hypotaurine and their metabolic precursors
Aruoma, O. I., Halliwell, B., Hoey, B. M., & Butler, J. (1988) · Biochemical Journal · doi:10.1042/bj2560251 · Cited by 580
Biochemical responses in aquatic animals: A review of determinants of oxidative stress
Di Giulio, R. T., Washburn, P. C., Wenning, R. J., Winston, G. W., & Jewell, C. S. (1989) · Environmental Toxicology and Chemistry · doi:10.1002/etc.5620081203 · Cited by 550
Klug, D., Rabani, J., & Fridovich, I. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)44987-9 · Cited by 495
BIOCHEMICAL RESPONSES IN AQUATIC ANIMALS: A REVIEW OF DETERMINANTS OF OXIDATIVE STRESS
Di Giulio, R. T., Washburn, P. C., Wenning, R. J., Winston, G. W., & Jewell, C. S. (1989) · Environmental Toxicology and Chemistry · doi:10.1897/1552-8618(1989)8[1103:briaaa]2.0.co;2 · Cited by 490
Livingstone, D. R., Martinez, P. G., Michel, X., Narbonne, J. F., O'Hara, S., Ribera, D., & Winston, G. W. (1990) · Functional Ecology · doi:10.2307/2389604 · Cited by 437
Self-citationOxygen Radicals, Hydrogen Peroxide, and Oxygen Toxicity
Fridovich, I. (1976) · Free Radicals in Biology · doi:10.1016/b978-0-12-566501-8.50013-4 · Cited by 430
Takahashi, K., Avissar, N., Whitin, J., & Cohen, H. (1987) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(87)90624-2 · Cited by 411
The role of selenium peroxidases in the protection against oxidative damage of membranes
Ursini, F., & Bindoli, A. (1987) · Chemistry and Physics of Lipids · doi:10.1016/0009-3084(87)90053-3 · Cited by 392
Purification and properties of human erythrocyte glutathione peroxidase.
Awasthi, Y. C., Beutler, E., & Srivastava, S. K. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41289-1 · Cited by 357
Fielden, E. M., Roberts, P. B., Bray, R. C., Lowe, D. J., Mautner, G. N., Rotilio, G., & Calabrese, L. (1974) · Biochemical Journal · doi:10.1042/bj1390049 · Cited by 351
Organic Xenobiotic Metabolism in Marine Invertebrates
Livingstone, D. R. (1991) · Advances in Comparative and Environmental Physiology · doi:10.1007/978-3-642-75897-3_2 · Cited by 339
Self-citationOxidants and antioxidants in aquatic animals
Winston, G. W. (1991) · Comparative Biochemistry and Physiology Part C: Comparative Pharmacology · doi:10.1016/0742-8413(91)90148-m · Cited by 283
Glutathione Peroxidase Brought into Focus
Flohé, L. (1982) · Free Radicals in Biology · doi:10.1016/b978-0-12-566505-6.50014-4 · Cited by 268
Reduced oxygen species, mutation, induction and cancer initiation
Vuillaume, M. (1987) · Mutation Research/Reviews in Genetic Toxicology · doi:10.1016/0165-1110(87)90014-5 · Cited by 259
Oxygen toxicity and reactive oxygen metabolites in mammals
Jamieson, D. (1989) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(89)90103-2 · Cited by 227
Cand, F., & Verdetti, J. (1989) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(89)90101-9 · Cited by 209
The Toxicology of Molecular Oxygen
Diguiseppi, J., Fridovich, I., & McCord, J. M. (1984) · CRC Critical Reviews in Toxicology · doi:10.3109/10408448409044213 · Cited by 205
Isolation and characterization of a manganese-containing superoxide dismutase from yeast.
Ravindranath, S. D., & Fridovich, I. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41165-4 · Cited by 182
Hypoxia, reactive oxygen, and cell injury
de Groot, H., & Littauer, A. (1989) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(89)90047-6 · Cited by 174
LIVINGSTONE, D., & Farrar, S. V. (1984) · The Science of The Total Environment · doi:10.1016/0048-9697(84)90080-9 · Cited by 172
Self-citationBorg, D. C., & Schaich, K. M. (1984) · Israel Journal of Chemistry · doi:10.1002/ijch.198400007 · Cited by 167
Cytochrome P-450 and oxidative metabolism in molluscs
Livingstone, D. R., Kirchin, M. A., & Wiseman, A. (1989) · Xenobiotica · doi:10.3109/00498258909043161 · Cited by 150
Self-citationMunday, R., & Winterbourn, C. C. (1989) · Biochemical Pharmacology · doi:10.1016/0006-2952(89)90641-2 · Cited by 141
Angerm�ller, S., & Fahimi, H. D. (1981) · Histochemistry and Cell Biology · doi:10.1007/bf00592568 · Cited by 127
Ovothiol Replaces Glutathione Peroxidase as a Hydrogen Peroxide Scavenger in Sea Urchin Eggs
Turner, E. E., Hager, L. J., & Shapiro, B. M. (1988) · Science · doi:10.1126/science.3187533 · Cited by 108
Michiels, C., & Remacle, J. (1988) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1988.tb14392.x · Cited by 101
Oxygen dependence of oxidative stress
Tribble, D. L., & Jones, D. P. (1990) · Biochemical Pharmacology · doi:10.1016/0006-2952(90)90152-b · Cited by 99
Biological role of superoxide ion-radical
Byczkowski, J. Z., & Gessner, T. (1988) · International Journal of Biochemistry · doi:10.1016/0020-711x(88)90095-x · Cited by 97
A critical reevaluation of some assay methods for superoxide dismutase activity
Goldstein, S., Michel, C., Bors, W., Sarán, M., & Czapski, G. (1988) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(88)90050-0 · Cited by 93
Isolation and characterization of a manganese-containing superoxide dismutase from rat liver
Salin, M. L., Day, E. D., & Crapo, J. D. (1978) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(78)90027-9 · Cited by 89
Cadenas, E., Mira, D., Brunmark, A. B., et al. (1988) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(88)90032-9 · Cited by 86
Oxidation of reduced cytochrome c by hydrogen peroxide: Implications for Superoxide assays
Vandewalle, P. L., & Petersen, N. O. (1987) · FEBS Letters · doi:10.1016/0014-5793(87)81336-4 · Cited by 74
Livingstone, D. R., Martinez, P. G., & Winston, G. W. (1989) · Aquatic Toxicology · doi:10.1016/0166-445x(89)90037-4 · Cited by 64
Self-citationSignificance of alterations in hepatic antioxidant enzymes. Primacy of glutathione peroxidase
Simmons, T. W., & Jamall, I. S. (1988) · Biochemical Journal · doi:10.1042/bj2510913 · Cited by 58
de GROOT, H., & Noll, T. (1987) · Chemistry and Physics of Lipids · doi:10.1016/0009-3084(87)90051-x · Cited by 57
Purification and Properties of a Peroxidase from Halobacterium halobium L-33
Fukumori, Y., Fujiwara, T., OKADA-TAKAHASHI, Y., et al. (1985) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a135352 · Cited by 48
Wenming, R. J., & Giulio, R. T. D. (1988) · Comparative Biochemistry and Physiology Part C Comparative Pharmacology · doi:10.1016/0742-8413(88)90092-8 · Cited by 44
Three different types of catalases in Klebsiella pneumoniae
Goldberg, I., & Hochman, A. (1989) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(89)90572-9 · Cited by 41
Beloqui, Ó., & Cederbaum, A. I. (1986) · Biochemical Pharmacology · doi:10.1016/0006-2952(86)90172-3 · Cited by 36
A study of the pH dependence of the activity of porcine Cu,Zn superoxide dismutase
Argese, E., Rigo, A., Viglino, P., Orsega, E. F., Marmocchi, F., Cocco, D., & Rotilio, G. (1984) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(84)90309-1 · Cited by 24
Cited by
Valavanidis, A., Vlahogianni, T., Dassenakis, M., & Scoullos, M. (2006) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2005.03.013 · Cited by 1,795
Abele, D., Heise, K., Pörtner, H. O., & Puntarulo, S. (2002) · Journal of Experimental Biology · doi:10.1242/jeb.205.13.1831 · Cited by 487
Metadata
- Authors
- Livingstone, D. R., Lips, F., Martinez, P. G., & Pipe, R. K.
- Venue
- Marine Biology
- Published
- 1992-06
- Volume
- 112
- Issue
- 2
- Pages
- 265-276
- ISSN
- 0025-3162 (ISSN-L)
- 1432-1793
- OpenAlex
- W1994193889
- Cited by
- 342
- References
- 51
- FWCI
- 1.78
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.