The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Glycoform-dependent conformational alteration of the Fc region of human immunoglobulin G1 as revealed by NMR spectroscopy
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Cites
Shields, R. L., Lai, J., Keck, R., O'Connell, L. Y., Hong, K., Meng, Y. G., Weikert, S. H. A., & Presta, L. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202069200 · Cited by 1,835
Shinkawa, T., Nakamura, K., Yamane, N., Shoji-Hosaka, E., Kanda, Y., Sakurada, M., Uchida, K., Anazawa, H., Satoh, M., Yamasaki, M., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210665200 · Cited by 1,413
Self-citationAgalactosyl glycoforms of IgG autoantibodies are pathogenic
Rademacher, T. W., Williams, P., & Dwek, R. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.13.6123 · Cited by 253
Role of Oligosaccharide Residues of IgG1-Fc in FcγRIIb Binding
Mimura, Y., Sondermann, P., Ghirlando, R., Lund, J., Young, S. P., Goodall, M., & Jefferis, R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107478200 · Cited by 236
The biological activity of human monoclonal IgG anti-D is reduced by β-galactosidase treatment
Kumpel, B. M., Wang, Y., Griffiths, H. L., Hadley, A. G., & Rook, G. A. W. (1995) · Human Antibodies · doi:10.3233/hab-1995-6301 · Cited by 68
Cited by
The impact of glycosylation on monoclonal antibody conformation and stability
Zheng, K., Bantog, C., & Bayer, R. (2011) · mAbs · doi:10.4161/mabs.3.6.17922 · Cited by 342
Conceptual Approaches to Modulating Antibody Effector Functions and Circulation Half-Life
Saunders, K. O. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01296 · Cited by 316
Huhn, C., Selman, M. H. J., Ruhaak, L. R., Deelder, A. M., & Wuhrer, M. (2009) · PROTEOMICS · doi:10.1002/pmic.200800715 · Cited by 301
Structural Comparison of Fucosylated and Nonfucosylated Fc Fragments of Human Immunoglobulin G1
Matsumiya, S., Yamaguchi, Y., Saito, J.-I., Nagano, M., Sasakawa, H., Otaki, S., Satoh, M., Shitara, K., & Kato, K. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.02.034 · Cited by 278
Self-citationGlycosylation of immunoglobulin G determines osteoclast differentiation and bone loss
Harre, U., Lang, S. C., Pfeifle, R., Rombouts, Y., Frühbeißer, S., Amara, K., Bang, H., Lux, A., Koeleman, C. A., Baum, W., et al. (2015) · Nature Communications · doi:10.1038/ncomms7651 · Cited by 261
Metadata
- Authors
- Yamaguchi, Y., Nishimura, M., Nagano, M., Yagi, H., Sasakawa, H., Uchida, K., Shitara, K., & Kato, K.
- Venue
- Biochimica et Biophysica Acta (BBA) - General Subjects
- Publisher
- Elsevier BV
- Published
- 2006-04
- Volume
- 1760
- Issue
- 4
- Pages
- 693-700
- ISSN
- 0304-4165 (ISSN-L)
- OpenAlex
- W2004919864
- Cited by
- 204
- References
- 5
- FWCI
- 1.96
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Glycoform-dependent conformational alteration of the Fc region of human immunoglobulin G1 as revealed by NMR spectroscopy. https://app.cochat.ai/papers/10.1016/j.bbagen.2005.10.002
- The paper
- Yamaguchi, Y., Nishimura, M., Nagano, M., Yagi, H., Sasakawa, H., Uchida, K., Shitara, K., & Kato, K. (2006). Glycoform-dependent conformational alteration of the Fc region of human immunoglobulin G1 as revealed by NMR spectroscopy. Biochimica et Biophysica Acta (BBA) - General Subjects. https://doi.org/10.1016/j.bbagen.2005.10.002
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.