The DOI matches its Crossref record; 88 of the 88 references it cites were found in a registry or an index.
N-glycan structure dictates extension of protein folding or onset of disposal
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Citations
Cites
Yoshida, H., Matsui, T., Yamamoto, A., Okada, T., & Mori, K. (2001) · Cell · doi:10.1016/s0092-8674(01)00611-0 · Cited by 4,039
THE MAMMALIAN UNFOLDED PROTEIN RESPONSE
Schröder, M., & Kaufman, R. J. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074134 · Cited by 3,026
Özcan, U., Yilmaz, E., Özcan, L., Furuhashi, M., Vaillancourt, E., Smith, R. O., Görgün, C. Z., & Hotamisligil, G. S. (2006) · Science · doi:10.1126/science.1128294 · Cited by 2,413
Roles of N-Linked Glycans in the Endoplasmic Reticulum
Helenius, A., & Aebi, M. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073752 · Cited by 2,037
Decay of Endoplasmic Reticulum-Localized mRNAs During the Unfolded Protein Response
Hollien, J., & Weissman, J. S. (2006) · Science · doi:10.1126/science.1129631 · Cited by 1,317
ERAD: the long road to destruction
Meusser, B., Hirsch, C., Jarosch, E., & Sommer, T. (2005) · Nature Cell Biology · doi:10.1038/ncb0805-766 · Cited by 1,220
Setting the Standards: Quality Control in the Secretory Pathway
Ellgaard, L., Molinari, M., & Helenius, A. (1999) · Science · doi:10.1126/science.286.5446.1882 · Cited by 1,192
Self-citationLee, K., Tirasophon, W., Shen, X., Michalak, M., Prywes, R., Okada, T., Yoshida, H., Mori, K., & Kaufman, R. J. (2002) · Genes & Development · doi:10.1101/gad.964702 · Cited by 1,054
Therapeutic approaches to protein-misfolding diseases
Cohen, F. E., & Kelly, J. W. (2003) · Nature · doi:10.1038/nature02265 · Cited by 800
A Time-Dependent Phase Shift in the Mammalian Unfolded Protein Response
Yoshida, H., Matsui, T., Hosokawa, N., Kaufman, R. J., Nagata, K., & Mori, K. (2003) · Developmental Cell · doi:10.1016/s1534-5807(03)00022-4 · Cited by 675
Cited by
Bassil, E., Coku, A., & Blumwald, E. (2012) · Journal of Experimental Botany · doi:10.1093/jxb/ers250 · Cited by 310
Solís, D., Bovin, N. V., Davis, A. P., Jiménez-Barbero, J., Romero, A., Roy, R., Smetana, K., & Gabius, H.-J. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.03.016 · Cited by 222
Protein Native-State Stabilization by Placing Aromatic Side Chains in N-Glycosylated Reverse Turns
Culyba, E. K., Price, J. L., Hanson, S. R., Dhar, A., Wong, C.-H., Gruebele, M., Powers, E. T., & Kelly, J. W. (2011) · Science · doi:10.1126/science.1198461 · Cited by 171
The unfolded protein response and its relevance to connective tissue diseases
Boot-Handford, R. P., & Briggs, M. D. (2010) · Cell and Tissue Research · doi:10.1007/s00441-009-0877-8 · Cited by 143
The role of MRH domain-containing lectins in ERAD
Hosokawa, N., Kamiya, Y., & Kato, K. (2010) · Glycobiology · doi:10.1093/glycob/cwq013 · Cited by 71
Metadata
- Authors
- Molinari, M.
- Venue
- Nature Chemical Biology
- Published
- 2007-05-17
- Volume
- 3
- Issue
- 6
- Pages
- 313-320
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- OpenAlex
- W2070112408
- Cited by
- 300
- References
- 88
- FWCI
- 9.34
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: N-glycan structure dictates extension of protein folding or onset of disposal. https://app.cochat.ai/papers/10.1038/nchembio880
- The paper
- Molinari, M. (2007). N-glycan structure dictates extension of protein folding or onset of disposal. Nature Chemical Biology. https://doi.org/10.1038/nchembio880
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.