The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
Asparagine synthetase: Function, structure, and role in disease
Open accessAbstract
Asparagine synthetase (ASNS) converts aspartate and glutamine to asparagine and glutamate in an ATP-dependent reaction. ASNS is present in most, if not all, mammalian organs, but varies widely in basal expression. Human ASNS activity is highly responsive to cellular stress, primarily by increased transcription from a single gene located on chromosome 7. Elevated ASNS protein expression is associated with resistance to asparaginase therapy in childhood acute lymphoblastic leukemia. There is evidence that ASNS expression levels may also be inversely correlated with asparaginase efficacy in certain solid tumors as well. Children with mutations in the ASNS gene exhibit developmental delays, intellectual disability, microcephaly, intractable seizures, and progressive brain atrophy. Thus far, 15 unique mutations in the ASNS gene have been clinically associated with asparagine synthetase deficiency (ASD). Molecular modeling using the Escherichia coli ASNS-B structure has revealed that most of the reported ASD substitutions are located near catalytic sites or within highly conserved regions of the protein. For some ASD patients, fibroblast cell culture studies have eliminated protein and mRNA synthesis or stability as the basis for decreased proliferation.
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Kilberg, M. S., Shan, J., & Su, N. (2009) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2009.05.008 · Cited by 591
Self-citationL‐asparaginase treatment in acute lymphoblastic leukemia: A focus on Erwinia asparaginase
Pieters, R., Hunger, S. P., Boos, J., Rizzari, C., Silverman, L., Baruchel, A., Goekbuget, N., Schrappe, M., & Pui, C. (2011) · Cancer · doi:10.1002/cncr.25489 · Cited by 569
Eukaryotic Initiation Factor 2 Phosphorylation and Translational Control in Metabolism
Baird, T. D., & Wek, R. C. (2012) · Advances in Nutrition · doi:10.3945/an.112.002113 · Cited by 469
Structure of the Blood–Brain Barrier and Its Role in the Transport of Amino Acids
Hawkins, R. A., O’Kane, R. L., Simpson, I. A., & Viña, J. R. (2006) · The Journal of Nutrition · doi:10.1093/jn/136.1.218s · Cited by 453
Asparagine Synthetase Chemotherapy
Richards, N. G. J., & Kilberg, M. S. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142520 · Cited by 244
Self-citationAsparagine synthetase: regulation by cell stress and involvement in tumor biology
Balasubramanian, M. N., Butterworth, E. A., & Kilberg, M. S. (2013) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00015.2013 · Cited by 241
Self-citationAslanian, A. M., Fletcher, B. S., & Kilberg, M. S. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3570321 · Cited by 167
Self-citationRuzzo, E. K., Capo-Chichi, J.-M., Ben-Zeev, B., Chitayat, D., Mao, H., Pappas, A. L., Hitomi, Y., Lu, Y.-F., Yao, X., Hamdan, F. F., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.08.013 · Cited by 164
The Transcription Factor Network Associated With the Amino Acid Response in Mammalian Cells
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Li, X., & Zhang, H. (2024) · The FEBS Journal · doi:10.1111/febs.16803 · Cited by 90
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Tan, M. M. X., Lawton, M. A., Pollard, M. I., Brown, E., Real, R., Carrasco, A. M., Bekadar, S., Jabbari, E., Reynolds, R. H., Iwaki, H., et al. (2024) · npj Parkinson's Disease · doi:10.1038/s41531-024-00729-8 · Cited by 17
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Metadata
- Authors
- Lomelino, C. L., Andring, J. T., McKenna, R., & Kilberg, M. S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2017-12
- Volume
- 292
- Issue
- 49
- Pages
- 19952-19958
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2766142559
- Cited by
- 308
- References
- 26
- FWCI
- 7.34
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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