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A Small Ubiquitin-Related Polypeptide Involved in Targeting RanGAP1 to Nuclear Pore Complex Protein RanBP2
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Cites
Distinct functions for the two importin subunits in nuclear protein import
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Lysine acetylation targets protein complexes and co-regulates major cellular functions
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Apg10p, a novel protein‐conjugating enzyme essential for autophagy in yeast
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Sumoylation increases HIF-1α stability and its transcriptional activity
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DNA repair factor XPC is modified by SUMO-1 and ubiquitin following UV irradiation.
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The Nup358-RanGAP Complex Is Required for Efficient Importin α/β-dependent Nuclear Import
Hutten, S., Flotho, A., Melchior, F., & Kehlenbach, R. H. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-12-1279 · Cited by 140
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Hirano, Y., Murata, S., Tanaka, K., Shimizu, M., & Sato, R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212448200 · Cited by 110
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Nicotine coregulates multiple pathways involved in protein modification/degradation in rat brain
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The Role of Sumoylation in the Response to Hypoxia: An Overview
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Fasting‐sensitive SUMO‐switch on Prox1 controls hepatic cholesterol metabolism
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Self-citationSUMOylation regulates the homologous to E6-AP carboxyl terminus (HECT) ubiquitin ligase Rsp5p
Novoselova, T. V., Rose, R.-S., Marks, H. M., & Sullivan, J. A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.424234 · Cited by 9
Nemo-like kinase disrupts nuclear import and drives TDP43 mislocalization in ALS
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“RanGAP1 sumoylation is critical for nuclear envelope localization and its interaction with RanBP2 (Figure 5C) (35–37).”
Metadata
- Authors
- Mahajan, R., Delphin, C., Guan, T., Gerace, L., & Melchior, F.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1997-01
- Volume
- 88
- Issue
- 1
- Pages
- 97-107
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W1981243923
- Cited by
- 1,256
- References
- 1
- FWCI
- 28.80
- Type
- journal article
- Language
- en
- Open access
- bronze
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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.