The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
[11] Diamide: An oxidant probe for thiols
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Citations
Cites
Ellman, G. L. (1959) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(59)90090-6 · Cited by 26,311
Oxidized Redox State of Glutathione in the Endoplasmic Reticulum
Hwang, C., Sinskey, A. J., & Lodish, H. F. (1992) · Science · doi:10.1126/science.1523409 · Cited by 1,968
The Glutathione Status of Cells
Kosower, N. S., & Kosower, E. M. (1978) · International Review of Cytology · doi:10.1016/s0074-7696(08)60166-7 · Cited by 1,211
Self-citationDiamide, a new reagent for the intracellular oxidation of glutathione to the disulfide
Kosower, N. S., Kosower, E. M., Wertheim, B., & Correa, W. S. (1969) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(69)90850-x · Cited by 525
Self-citationNewton, G. L., Dorian, R., & Fahey, R. C. (1981) · Analytical Biochemistry · doi:10.1016/0003-2697(81)90498-x · Cited by 451
Oliver, J. M., Albertini, D. F., & Berlin, R. D. (1976) · The Journal of cell biology · doi:10.1083/jcb.71.3.921 · Cited by 219
The physiological consequences of glutathione variations
Uhlig, S., & Wendel, A. (1992) · Life Sciences · doi:10.1016/0024-3205(92)90509-n · Cited by 196
The modification and assembly of proteins in the endoplasmic reticulum
Gaut, J. R., & Hendershot, L. M. (1993) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(93)90127-c · Cited by 159
Glutathione VII. Differentiation among substrates by the thiol-oxidizing agent, diamide
Kosower, E. M., Correa, W. S., Kinon, B. J., et al. (1972) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(72)90114-6 · Cited by 124
Self-citationKosower, N. S., Zipser, Y., & Faltin, Z. (1982) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(82)90424-2 · Cited by 60
Self-citation
Cited by
Glutathione and its role in cellular functions
Sies, H. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00177-x · Cited by 1,735
ATM Activation by Oxidative Stress
Guo, Z., Kozlov, S., Lavin, M. F., Person, M. D., & Paull, T. T. (2010) · Science · doi:10.1126/science.1192912 · Cited by 1,079
The ERO1 Gene of Yeast Is Required for Oxidation of Protein Dithiols in the Endoplasmic Reticulum
Frand, A. R., & Kaiser, C. A. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80017-9 · Cited by 494
Protein Disulfide Bond Formation in the Cytoplasm during Oxidative Stress
Cumming, R. C., Andon, N. L., Haynes, P. A., Park, M., Fischer, W. H., & Schubert, D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312267200 · Cited by 462
Thorpe, G. W., Fong, C. S., Alic, N., Higgins, V. J., & Dawes, I. W. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0305888101 · Cited by 450
Metadata
- Authors
- Kosower, N. S., & Kosower, E. M.
- Venue
- Methods in Enzymology
- Publisher
- Elsevier
- Published
- 1995
- Volume
- 251
- Pages
- 123-133
- ISSN
- 0076-6879 (ISSN-L)
- OpenAlex
- W1563653502
- Cited by
- 340
- References
- 20
- FWCI
- 21.37
- Type
- book chapter
- Language
- en
- Open access
- closed
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- The paper
- Kosower, N. S., & Kosower, E. M. (1995). [11] Diamide: An oxidant probe for thiols. Methods in Enzymology. https://doi.org/10.1016/0076-6879(95)51116-4
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.