The DOI matches its Crossref record; 103 of the 103 references it cites were found in a registry or an index.
Serine peptidases: Classification, structure and function
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Cites
The Structure of the Potassium Channel: Molecular Basis of K + Conduction and Selectivity
Doyle, D. A., Cabral, J. M., Pfuetzner, R. A., Kuo, A., Gulbis, J. M., Cohen, S. L., Chait, B. T., & MacKinnon, R. (1998) · Science · doi:10.1126/science.280.5360.69 · Cited by 6,807
The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction
Glickman, M. H., & Ciechanover, A. (2002) · Physiological Reviews · doi:10.1152/physrev.00027.2001 · Cited by 4,237
Mutations in PCSK9 cause autosomal dominant hypercholesterolemia
Abifadel, M., Varret, M., Rabès, J.-P., Allard, D., Ouguerram, K., Devillers, M., Cruaud, C., Benjannet, S., Wickham, L., Erlich, D., et al. (2003) · Nature Genetics · doi:10.1038/ng1161 · Cited by 2,985
PERUTZ, M. F. (1970) · Nature · doi:10.1038/228726a0 · Cited by 2,926
Sussman, J. L., Harel, M., Frolow, F., Oefner, C., Goldman, A., Toker, L., & Silman, I. (1991) · Science · doi:10.1126/science.1678899 · Cited by 2,707
Serine Protease Mechanism and Specificity
Hedstrom, L. (2002) · Chemical Reviews · doi:10.1021/cr000033x · Cited by 1,827
Acetylcholinesterase — new roles for an old actor
Soreq, H., & Seidman, S. (2001) · Nature Reviews Neuroscience · doi:10.1038/35067589 · Cited by 1,390
The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex
Xu, Z., Horwich, A. L., & Sigler, P. B. (1997) · Nature · doi:10.1038/41944 · Cited by 1,239
Molecular and cellular biology of cholinesterases
Massoulié, J., Pezzementi, L., Bon, S., Krejci, E., & Vallette, F.-M. (1993) · Progress in Neurobiology · doi:10.1016/0301-0082(93)90040-y · Cited by 1,214
A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood
Brown, M. S., & Goldstein, J. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11041 · Cited by 1,134
Cited by
Ruiz-Perez, F., & Nataro, J. P. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1355-8 · Cited by 149
Synergistic strategies of predominant toxins in snake venoms
Xiong, S., & Huang, C. (2018) · Toxicology Letters · doi:10.1016/j.toxlet.2018.02.004 · Cited by 78
Metadata
- Authors
- Page, M. J., & Di Cera, E.
- Venue
- Cellular and Molecular Life Sciences
- Published
- 2008-02-09
- Volume
- 65
- Issue
- 7-8
- Pages
- 1220-1236
- ISSN
- 1420-682X (ISSN-L)
- 1420-9071
- OpenAlex
- W2094079380
- Cited by
- 438
- References
- 103
- FWCI
- 6.57
- Type
- journal article
- Language
- en
- Open access
- green
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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.
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- Page, M. J., & Di Cera, E. (2008). Serine peptidases: Classification, structure and function. Cellular and Molecular Life Sciences. https://doi.org/10.1007/s00018-008-7565-9
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.
