The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
Self-hydrolyzing maleimides improve the stability and pharmacological properties of antibody-drug conjugates
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Citations
Cites
Effects of Drug Loading on the Antitumor Activity of a Monoclonal Antibody Drug Conjugate
Hamblett, K. J., Senter, P. D., Chace, D. F., Sun, M. M. C., Lenox, J., Cerveny, C. G., Kissler, K. M., Bernhardt, S. X., Kopcha, A. K., Zabinski, R. F., et al. (2004) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-04-0789 · Cited by 1,247
Self-citationDevelopment of potent monoclonal antibody auristatin conjugates for cancer therapy
Doronina, S. O., Toki, B. E., Torgov, M. Y., Mendelsohn, B. A., Cerveny, C. G., Chace, D. F., DeBlanc, R. L., Gearing, R. P., Bovee, T. D., Siegall, C. B., et al. (2003) · Nature Biotechnology · doi:10.1038/nbt832 · Cited by 1,206
Self-citationShen, B.-Q., Xu, K., Liu, L., Raab, H., Bhakta, S., Kenrick, M., Parsons-Reponte, K. L., Tien, J., Yu, S.-F., Mai, E., et al. (2012) · Nature Biotechnology · doi:10.1038/nbt.2108 · Cited by 1,008
Francisco, J. A., Cerveny, C. G., Meyer, D. L., Mixan, B. J., Klussman, K., Chace, D. F., Rejniak, S. X., Gordon, K. A., DeBlanc, R., Toki, B. E., et al. (2003) · Blood · doi:10.1182/blood-2003-01-0039 · Cited by 931
Self-citationAntibody–Drug Conjugates: An Emerging Concept in Cancer Therapy
Chari, R. V. J., Miller, M. L., & Widdison, W. C. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201307628 · Cited by 930
Antibody-Drug Conjugates in Cancer Therapy
Sievers, E. L., & Senter, P. D. (2013) · Annual Review of Medicine · doi:10.1146/annurev-med-050311-201823 · Cited by 770
Self-citationSenter, P. D., & Sievers, E. L. (2012) · Nature Biotechnology · doi:10.1038/nbt.2289 · Cited by 763
Self-citationDubowchik, G. M., Firestone, R. A., Padilla, L., Willner, D., Hofstead, S. J., Mosure, K., Knipe, J. O., Lasch, S. J., & Trail, P. A. (2002) · Bioconjugate Chemistry · doi:10.1021/bc025536j · Cited by 555
Strop, P., Liu, S.-H., Dorywalska, M., Delaria, K., Dushin, R. G., Tran, T.-T., Ho, W.-H., Farias, S., Casas, M. G., Abdiche, Y., et al. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.01.010 · Cited by 505
Contribution of Linker Stability to the Activities of Anticancer Immunoconjugates
Alley, S. C., Benjamin, D. R., Jeffrey, S. C., Okeley, N. M., Meyer, D. L., Sanderson, R. J., & Senter, P. D. (2008) · Bioconjugate Chemistry · doi:10.1021/bc7004329 · Cited by 479
Self-citation
Cited by
Engineering precision nanoparticles for drug delivery
Mitchell, M. J., Billingsley, M. M., Haley, R. M., Wechsler, M. E., Peppas, N. A., & Langer, R. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-020-0090-8 · Cited by 7,933
Strategies and challenges for the next generation of antibody–drug conjugates
Beck, A., Goetsch, L., Dumontet, C., & Corvaïa, N. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.268 · Cited by 2,271
Agarwal, P., & Bertozzi, C. R. (2015) · Bioconjugate Chemistry · doi:10.1021/bc5004982 · Cited by 605
Site-selective protein-modification chemistry for basic biology and drug development
Krall, N., da Cruz, F. P., Boutureira, O., & Bernardes, G. J. L. (2016) · Nature Chemistry · doi:10.1038/nchem.2393 · Cited by 583
Residue-Specific Peptide Modification: A Chemist’s Guide
deGruyter, J. N., Malins, L. R., & Baran, P. S. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00536 · Cited by 573
Metadata
- Authors
- Lyon, R. P., Setter, J. R., Bovee, T. D., Doronina, S. O., Hunter, J. H., Anderson, M. E., Balasubramanian, C. L., Duniho, S. M., Leiske, C. I., Li, F., & Senter, P. D.
- Venue
- Nature Biotechnology
- Published
- 2014-09-07
- Volume
- 32
- Issue
- 10
- Pages
- 1059-1062
- ISSN
- 0733-222X (ISSN-L)
- 1087-0156
- 1546-1696
- OpenAlex
- W2010363872
- Cited by
- 461
- References
- 28
- FWCI
- 29.58
- Type
- journal article
- Language
- en
- Open access
- closed
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Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Self-hydrolyzing maleimides improve the stability and pharmacological properties of antibody-drug conjugates. https://app.cochat.ai/papers/10.1038/nbt.2968
- The paper
- Lyon, R. P., Setter, J. R., Bovee, T. D., Doronina, S. O., Hunter, J. H., Anderson, M. E., Balasubramanian, C. L., Duniho, S. M., Leiske, C. I., Li, F., & Senter, P. D. (2014). Self-hydrolyzing maleimides improve the stability and pharmacological properties of antibody-drug conjugates. Nature Biotechnology. https://doi.org/10.1038/nbt.2968
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.
