The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
Structural and Functional Analysis of the Mitotic Rotamase Pin1 Suggests Substrate Recognition Is Phosphorylation Dependent
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Cites
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Overcoming the challenges in administering biopharmaceuticals: Formulation and delivery strategies
Mitragotri, S., Burke, P. A., & Langer, R. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4363 · Cited by 1,702
The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein
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Self-citationThe prolyl isomerase PIN1: a pivotal new twist in phosphorylation signalling and disease
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Protein Allostery and Conformational Dynamics
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Metadata
- Authors
- Ranganathan, R., Lu, K. P., Hunter, T., & Noel, J. P.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1997-06
- Volume
- 89
- Issue
- 6
- Pages
- 875-886
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2113675798
- Cited by
- 699
- References
- 47
- FWCI
- 7.42
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Structural and Functional Analysis of the Mitotic Rotamase Pin1 Suggests Substrate Recognition Is Phosphorylation Dependent. https://app.cochat.ai/papers/10.1016/s0092-8674(00)80273-1
- The paper
- Ranganathan, R., Lu, K. P., Hunter, T., & Noel, J. P. (1997). Structural and Functional Analysis of the Mitotic Rotamase Pin1 Suggests Substrate Recognition Is Phosphorylation Dependent. Cell. https://doi.org/10.1016/s0092-8674(00)80273-1
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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.
