The DOI matches its Crossref record; 112 of the 116 references it cites were found in a registry or an index.
Structure, function, and biology of SHIP proteins
Abstract
One of the “simple” curiosities of life, at least for a biological scientist, is how the growth and development of a complete organism from a single cell is controlled. Part of the answer includes growth factor receptors and their respective ligands, which transduce signals across cell membranes and into the nucleus for transcriptional readout. The molecular nature of these intracellular signals determines the type of signals, the pathways involved, subsequent regulatory interactions, and eventual transcription factor activation/repression. Hematopoietic cell development has been a fruitful system for the
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In the citing paper
“This lipid dephosphorylation reaction prevents receptor activation, mitigating signal transduction through the phosphatidylinositol-3-kinase/mammalian target of rapamycin (PI3K/mTOR) pathway.10”
From Microglial INPP5D limits plaque formation and glial reactivity in the PSAPP mouse model of Alzheimer's disease (2023) · cites this paper as [10]
In the citing paper
“SHIP1 negatively regulates targets such as immune cell surface receptors by catalyzing the conversion of phosphatidylinositol (3,4,5)-trisphosphate (PI[3,4,5]P3) to phosphatidylinositol (3,4)-bisphosphate (PI[3,4]P2).”
From Microglial INPP5D limits plaque formation and glial reactivity in the PSAPP mouse model of Alzheimer's disease (2023) · cites this paper as [10]
In the citing paper
“The inositol polyphosphate-5-phosphatase D (INPP5D) gene encodes a dual-specificity phosphatase that can dephosphorylate both phospholipids and phosphoproteins.”
From Microglial INPP5D limits plaque formation and glial reactivity in the PSAPP mouse model of Alzheimer's disease (2023) · cites this paper as [10]
In the citing paper
“SHIP1 was originally observed in hematopoietic cells after a variety of cytokines and growth factors induced the tyrosine phosphorylation of this 145-kDa protein [98–104].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [104]
Citations
Cites
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SH2 domains recognize specific phosphopeptide sequences
Songyang, Z. (1993) · Cell · doi:10.1016/0092-8674(93)90404-e · Cited by 2,620
Signal Transduction through MAP Kinase Cascades
Lewis, T. S., Shapiro, P. S., & Ahn, N. G. (1998) · Advances in cancer research · doi:10.1016/s0065-230x(08)60765-4 · Cited by 1,759
Targeted Disruption of the Mouse Stat1 Gene Results in Compromised Innate Immunity to Viral Disease
Durbin, J. E., Hackenmiller, R., Simon, M. C., & Levy, D. E. (1996) · Cell · doi:10.1016/s0092-8674(00)81289-1 · Cited by 1,539
Pten is essential for embryonic development and tumour suppression
Cristofano, A. D., Pesce, B., Cordon‐Cardo, C., & Pandolfi, P. P. (1998) · Nature Genetics · doi:10.1038/1235 · Cited by 1,518
Stephens, L., Anderson, K. E., Stokoe, D., Erdjument‐Bromage, H., Painter, G. F., Holmes, A. B., Gaffney, P. R. J., Reese, C. B., McCormick, F. P., Tempst, P., et al. (1998) · Science · doi:10.1126/science.279.5351.710 · Cited by 1,061
Specific Inhibition of Stat3 Signal Transduction by PIAS3
Chung, C. D., Liao, J., Liu, B., Rao, X., Jay, P., Berta, P., & Shuai, K. (1997) · Science · doi:10.1126/science.278.5344.1803 · Cited by 980
Rozakis-Adcock, M., McGlade, J. C., Mbamalu, G., Pelicci, G., Daly, R. J., Li, W., Batzer, A., Thomas, S. Μ., Brugge, J. S., Pelicci, P. G., et al. (1992) · Nature · doi:10.1038/360689a0 · Cited by 973
Mutation of Pten/Mmac1 in mice causes neoplasia in multiple organ systems
Podsypanina, K., Ellenson, L. H., Nemes, A., Gu, J., Tamura, M., Yamada, K. M., Cordon‐Cardo, C., Cattoretti, G., Fisher, P. E., & Parsons, R. E. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.4.1563 · Cited by 947
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Genetic regulation of osteoclast development and function
Teitelbaum, S. L., & Ross, F. P. (2003) · Nature Reviews Genetics · doi:10.1038/nrg1122 · Cited by 1,720
The protein kinase B/Akt signalling pathway in human malignancy
Nicholson, K. M., & Anderson, N. G. (2002) · Cellular Signalling · doi:10.1016/s0898-6568(01)00271-6 · Cited by 1,665
Phosphoinositides: Tiny Lipids With Giant Impact on Cell Regulation
Balla, T. (2013) · Physiological Reviews · doi:10.1152/physrev.00028.2012 · Cited by 1,638
Synthesis and Function of 3-Phosphorylated Inositol Lipids
Vanhaesebroeck, B., Leevers, S. J., Ahmadi, K., Timms, J., Katso, R., Driscoll, P. C., Woscholski, R., Parker, P. J., & Waterfield, M. D. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.535 · Cited by 1,535
Ravetch, J. V., & Lanier, L. L. (2000) · Science · doi:10.1126/science.290.5489.84 · Cited by 1,278
Metadata
- Authors
- Rohrschneider, L. R., Fuller, J. F., Wolf, I., Liu, Y., & Lucas, D. M.
- Affiliations
- Fred Hutch Cancer Center (US)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2000-03-01
- Volume
- 14
- Issue
- 5
- Pages
- 505-520
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2162332365
- Cited by
- 294
- References
- 116
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 3 · 2023: 7 · 2022: 4 · 2021: 3 · 2020: 6 · 2019: 3 · 2018: 5 · 2017: 5 · 2016: 3 · 2015: 6 · 2014: 9 · 2013: 11 · 2012: 16
- Type
- posted content
- Language
- en
- Open access
- closed
- Locations
- Genes & Development (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Fred Hutchinson Cancer Research Center
- National Institutes of Health (5r01ca020551-21, 1f32dk009774-01)
- National Cancer Institute (CA20551, CA4987)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK09774)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
- Keywords
- hematopoietic cell development, growth factor receptors, signal transduction, transcriptional regulation, transcription factor activation, protein structure-function relationship
- MeSH terms
- Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases, Animals, B-Lymphocytes, Humans, Phosphoric Monoester Hydrolases, src Homology Domains, Protein Isoforms
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