ArticleTrends in cell biology2012
Alternative nuclear transport for cellular protein quality control.
Article in Trends in cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
34 citing papers in PubMed, 54 citations in OpenAlex.
- ER protein CLCC1 promotes nuclear envelope fusion in herpesviral and host processes.Nature communications · 2025Article
- A nuclear protein quality control system for elimination of nucleolus-related inclusions.The EMBO journal · 2025Article
- Nuclear envelope budding and its cellular functions.Nucleus (Austin, Tex.) · 2023Article
- Centralspindlin proteins Pavarotti and Tumbleweed along with WASH regulate nuclear envelope budding.The Journal of cell biology · 2023Article
- Quality control mechanisms that protect nuclear envelope identity and function.The Journal of cell biology · 2022Review
- Review
- Atg39 selectively captures inner nuclear membrane into lumenal vesicles for delivery to the autophagosome.The Journal of cell biology · 2021Article
- Article
- Nuclear envelope budding is a response to cellular stress.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- Article
- Methodologies to monitor protein turnover at the inner nuclear membrane.Methods in enzymology · 2019Article
- Fantastic nuclear envelope herniations and where to find them.Biochemical Society transactions · 2018Review
- Article
- Article
- A model for coordinating nuclear mechanics and membrane remodeling to support nuclear integrity.Current opinion in cell biology · 2016Review
- This bud's for you: mechanisms of cellular nucleocytoplasmic trafficking via nuclear envelope budding.Current opinion in cell biology · 2016Review
- The Lamin B receptor is essential for cholesterol synthesis and perturbed by disease-causing mutations.eLife · 2016Article
- The ESCRT machinery: new roles at new holes.Current opinion in cell biology · 2016Review
- Pelger-Huët anomaly and Greenberg skeletal dysplasia: LBR-associated diseases of cholesterol metabolism.Rare diseases (Austin, Tex.) · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Herpesvirus capsids traverse the nuclear envelope (NE) by utilizing an unusual export pathway termed nuclear egress. In this process, the viral capsid is delivered into the perinuclear space (PNS), producing a vesicular intermediate after fission. After fusion with the outer nuclear membrane (ONM), the naked capsid is released into the cytosol. A recent study now suggests that this pathway might be an endogenous cellular pathway, co-opted by viruses, that serves to transport cellular cargo exceeding the size limit imposed by the nuclear pore complex (NPC). We propose that one function of this pathway is to transport nuclear protein aggregates to the cytosolic autophagy machinery. Our model has implications for our understanding of laminopathies and related diseases affecting proteins residing at the inner nuclear membrane (INM) and nuclear lamina.
Indexed as
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.