The DOI matches its Crossref record; 132 of the 132 references it cites were found in a registry or an index.
Arginase: an old enzyme with new tricks
Open accessAbstract
Arginase has roots in early life forms. It converts L-arginine to urea and ornithine. The former provides protection against NH3; the later serves to stimulate cell growth and other physiological functions. Excessive arginase activity in mammals has been associated with cardiovascular and nervous system dysfunction and diseases. Two relevant aspects of this elevated activity may be involved in these disease states. First, excessive arginase activity reduces the supply of L-arginine needed by nitric oxide (NO) synthase to produce NO. Second, excessive production of ornithine leads to vascular structural problems and neural toxicity. Recent research has identified inflammatory agents and reactive oxygen species (ROS) as drivers of this pathologic elevation of arginase activity and expression. Here we review involvement of arginase in cardiovascular and nervous system dysfunction and discuss potential therapeutic interventions targeting excess arginase.
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
Nitric Oxide and Peroxynitrite in Health and Disease
Pacher, P., Beckman, J. S., & Liaudet, L. (2007) · Physiological Reviews · doi:10.1152/physrev.00029.2006 · Cited by 6,390
Nitric oxide synthases: regulation and function
Forstermann, U., & Sessa, W. C. (2012) · European Heart Journal · doi:10.1093/eurheartj/ehr304 · Cited by 4,409
Nitric oxide: an endogenous modulator of leukocyte adhesion.
Kubes, P., Suzuki, M., & Granger, D. N. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.11.4651 · Cited by 3,029
Arginine metabolism: nitric oxide and beyond
WU, G., & MORRIS, S. M. (1998) · Biochemical Journal · doi:10.1042/bj3360001 · Cited by 2,811
Endothelium‐derived relaxing and contracting factors
Furchgott, R. F., & Vanhoutte, P. M. (1989) · The FASEB Journal · doi:10.1096/fasebj.3.9.2545495 · Cited by 1,993
De Caterina, R., Libby, P., Peng, H. B., Thannickal, V. J., Rajavashisth, T. B., Gimbrone, M. A., Shin, W. S., & Liao, J. K. (1995) · Journal of Clinical Investigation · doi:10.1172/jci118074 · Cited by 1,782
ENDOGENOUS NITRIC OXIDE INHIBITS HUMAN PLATELET ADHESION TO VASCULAR ENDOTHELIUM
Radomski, M. W., Palmer, R. M. J., & Moncada, S. (1987) · The Lancet · doi:10.1016/s0140-6736(87)91481-4 · Cited by 1,437
(2005) · doi:10.1016/j.ucl.2005.08.007 · Cited by 759
Arginase: an emerging key player in the mammalian immune system
Munder, M. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00291.x · Cited by 694
Macrophage plasticity in experimental atherosclerosis
Khallou-Laschet, J., Varthaman, A., Fornasa, G., Compain, C., Gaston, A.-T., Clement, M., Dussiot, M., Levillain, O., Graff-Dubois, S., Nicoletti, A., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008852 · Cited by 517
Cited by
MiRNA-124 induces neuroprotection and functional improvement after focal cerebral ischemia
Hamzei Taj, S., Kho, W., Riou, A., Wiedermann, D., & Hoehn, M. (2016) · Biomaterials · doi:10.1016/j.biomaterials.2016.03.025 · Cited by 175
Metadata
- Authors
- Caldwell, R. B., Toque, H. A., Narayanan, S. P., & Caldwell, R. W.
- Venue
- Trends in Pharmacological Sciences
- Publisher
- Elsevier BV
- Published
- 2015-06
- Volume
- 36
- Issue
- 6
- Pages
- 395-405
- ISSN
- 0165-6147 (ISSN-L)
- OpenAlex
- W2067510355
- Cited by
- 332
- References
- 132
- FWCI
- 3.51
- Type
- journal article
- Language
- en
- Open access
- green
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: Arginase: an old enzyme with new tricks. https://app.cochat.ai/papers/10.1016/j.tips.2015.03.006
- The paper
- Caldwell, R. B., Toque, H. A., Narayanan, S. P., & Caldwell, R. W. (2015). Arginase: an old enzyme with new tricks. Trends in Pharmacological Sciences. https://doi.org/10.1016/j.tips.2015.03.006
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.
