The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Prolyl Oligopeptidase
Open accessAbstract
Abstract Prolyl oligopeptidase is a large cytosolic enzyme that belongs to a new class of serine peptidases. The enzyme is involved in the maturation and degradation of peptide hormones and neuropeptides, which relate to the induction of amnesia. The 1.4 A resolution crystal structure is presented here. The enzyme contains a peptidase domain with an α/β hydrolase fold, and its catalytic triad (Ser554, His680, Asp641) is covered by the central tunnel of an unusual β propeller. This domain makes prolyl oligopeptidase an oligopeptidase by excluding large structured peptides from the active site. In this way, the propeller protects larger peptides and proteins from proteolysis in the cytosol. The structure is also obtained with a transition state inhibitor, which may facilitate drug design to treat memory disorders.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
Cited by
Lambeir, A.-M., Durinx, C., Scharpé, S., & De Meester, I. (2003) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/713609354 · Cited by 955
α/β Hydrolase fold enzymes: the family keeps growing
Nardini, M., & Dijkstra, B. W. (1999) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)00037-8 · Cited by 829
Towler, P., Staker, B., Prasad, S. G., Menon, S., Tang, J., Parsons, T., Ryan, D., Fisher, M., Williams, D., Dales, N. A., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311191200 · Cited by 696
Protein Repeats: Structures, Functions, and Evolution
Andrade, M. A., Perez-Iratxeta, C., & Ponting, C. P. (2001) · Journal of Structural Biology · doi:10.1006/jsbi.2001.4392 · Cited by 615
CD26, let it cut or cut it down
De Meester, I., Korom, S., Van Damme, J., & Scharpé, S. (1999) · Immunology Today · doi:10.1016/s0167-5699(99)01486-3 · Cited by 451
Metadata
- Authors
- Fülöp, V., Böcskei, Z., & Polgár, L.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1998-07
- Volume
- 94
- Issue
- 2
- Pages
- 161-170
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W1764151989
- Cited by
- 496
- References
- 1
- FWCI
- 7.31
- Type
- journal article
- Language
- en
- Open access
- bronze
About these checks
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Prolyl Oligopeptidase. https://app.cochat.ai/papers/10.1016/s0092-8674(00)81416-6
- The paper
- Fülöp, V., Böcskei, Z., & Polgár, L. (1998). Prolyl Oligopeptidase. Cell. https://doi.org/10.1016/s0092-8674(00)81416-6
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.