The DOI matches its Crossref record; 178 of the 178 references it cites were found in a registry or an index.
The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine
Open accessAbstract
The enzymes of O-GlcNAc cycling couple the nutrient-dependent synthesis of UDP-GlcNAc to O-GlcNAc modification of Ser/Thr residues of key nuclear and cytoplasmic targets. This series of reactions culminating in O-GlcNAcylation of targets has been termed the Hexosamine Signaling Pathway (HSP). The evolutionarily ancient enzymes of O-GlcNAc cycling have co-evolved with other signaling effecter molecules; they are recruited to their targets by many of the same mechanisms used to organize canonic kinase-dependent signaling pathways. This co-recruitment of the enzymes of O-GlcNAc cycling drives a binary switch impacting pathways of anabolism and growth (nutrient uptake) and catabolic pathways (nutrient sparing and salvage). The Hexosamine Signaling Pathway (HSP) has thus emerged as a versatile cellular regulator modulating numerous cellular signaling cascades influencing growth, metabolism, cellular stress, circadian rhythm, and host-pathogen interactions. In mammals, the nutrient-sensing HSP has been harnessed to regulate such cell-specific functions as neutrophil migration, and activation of B-cells and T-cells. This review summarizes the diverse approaches being used to examine O-GlcNAc cycling. It will emphasize the impact O-GlcNAcylation has upon signaling pathways that may be become deregulated in diseases of the immune system, diabetes mellitus, cancer, cardiovascular disease, and neurodegenerative diseases.
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2 retracted
GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis
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Cited by
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Schulte, M. L., Fu, A., Zhao, P., Li, J., Geng, L., Smith, S. T., Kondo, J., Coffey, R. J., Johnson, M. O., Rathmell, J. C., et al. (2018) · Nature Medicine · doi:10.1038/nm.4464 · Cited by 494
Lysosome biogenesis: Regulation and functions
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Metadata
- Authors
- Hanover, J. A., Krause, M. W., & Love, D. C.
- Venue
- Biochimica et Biophysica Acta (BBA) - General Subjects
- Publisher
- Elsevier BV
- Published
- 2010-02
- Volume
- 1800
- Issue
- 2
- Pages
- 80-95
- ISSN
- 0304-4165 (ISSN-L)
- OpenAlex
- W2061011762
- Cited by
- 342
- References
- 178
- FWCI
- 9.84
- Type
- journal article
- Language
- en
- Open access
- green
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