The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Proline and hydroxyproline metabolism: implications for animal and human nutrition
Open accessAbstract
Proline plays important roles in protein synthesis and structure, metabolism (particularly the synthesis of arginine, polyamines, and glutamate via pyrroline-5-carboxylate), and nutrition, as well as wound healing, antioxidative reactions, and immune responses. On a per-gram basis, proline plus hydroxyproline are most abundant in collagen and milk proteins, and requirements of proline for whole-body protein synthesis are the greatest among all amino acids. Therefore, physiological needs for proline are particularly high during the life cycle. While most mammals (including humans and pigs) can synthesize proline from arginine and glutamine/glutamate, rates of endogenous synthesis are inadequate for neonates, birds, and fish. Thus, work with young pigs (a widely used animal model for studying infant nutrition) has shown that supplementing 0.0, 0.35, 0.7, 1.05, 1.4, and 2.1% proline to a proline-free chemically defined diet containing 0.48% arginine and 2% glutamate dose dependently improved daily growth rate and feed efficiency while reducing concentrations of urea in plasma. Additionally, maximal growth performance of chickens depended on at least 0.8% proline in the diet. Likewise, dietary supplementation with 0.07, 0.14, and 0.28% hydroxyproline (a metabolite of proline) to a plant protein-based diet enhanced weight gains of salmon. Based on its regulatory roles in cellular biochemistry, proline can be considered as a functional amino acid for mammalian, avian, and aquatic species. Further research is warranted to develop effective strategies of dietary supplementation with proline or hydroxyproline to benefit health, growth, and development of animals and humans.
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
Arginine metabolism: nitric oxide and beyond
WU, G., & MORRIS, S. M. (1998) · Biochemical Journal · doi:10.1042/bj3360001 · Cited by 2,811
Self-citationMaternal Nutrition and Fetal Development
Bazer, F. W., Spencer, T. E., Wu, G., Cudd, T. A., & Meininger, C. J. (2004) · The Journal of Nutrition · doi:10.1093/jn/134.9.2169 · Cited by 1,019
Self-citationThe metabolism of proline, a stress substrate, modulates carcinogenic pathways
Phang, J. M., Donald, S. P., Pandhare, J., & Liu, Y. (2008) · Amino Acids · doi:10.1007/s00726-008-0063-4 · Cited by 252
Utilization of amino acids by bacteria from the pig small intestine
Dai, Z.-L., Zhang, J., Wu, G., & Zhu, W.-Y. (2010) · Amino Acids · doi:10.1007/s00726-010-0556-9 · Cited by 246
Self-citationIntestinal nitrogen recycling and utilization in health and disease
Bergen, W. G., & Wu, G. (2009) · The Journal of Nutrition · doi:10.3945/jn.109.104497 · Cited by 183
Self-citation
Cited by
Differential Roles of M1 and M2 Microglia in Neurodegenerative Diseases
Tang, Y., & Le, W. (2016) · Molecular Neurobiology · doi:10.1007/s12035-014-9070-5 · Cited by 2,190
Glycine metabolism in animals and humans: implications for nutrition and health
Wang, W., Wu, Z., Dai, Z., Yang, Y., Wang, J., & Wu, G. (2013) · Amino Acids · doi:10.1007/s00726-013-1493-1 · Cited by 766
Self-citationProline-dependent regulation of collagen metabolism
Karna, E., Szoka, L., Huynh, T. Y. L., & Palka, J. A. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03363-3 · Cited by 221
Ashraf, S. A., Adnan, M., Patel, M., Siddiqui, A. J., Sachidanandan, M., Snoussi, M., & Hadi, S. (2020) · Marine Drugs · doi:10.3390/md18050265 · Cited by 136
Metadata
- Authors
- Wu, G., Bazer, F. W., Burghardt, R. C., Johnson, G. A., Kim, S. W., Knabe, D. A., Li, P., Li, X., McKnight, J. R., Satterfield, M. C., & Spencer, T. E.
- Venue
- Amino Acids
- Published
- 2010-08-10
- Volume
- 40
- Issue
- 4
- Pages
- 1053-1063
- ISSN
- 0939-4451 (ISSN-L)
- 1438-2199
- OpenAlex
- W2090436419
- Cited by
- 686
- References
- 5
- FWCI
- 36.13
- 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
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.