ArticleThe Journal of cell biology1990
Targeting of a cytosolic protein to the nuclear periphery.
Article in The Journal of cell biology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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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.
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Who cites it
12 citing papers in PubMed, 32 citations in OpenAlex.
- Possibility of cytoplasmic pre-tRNA splicing: the yeast tRNA splicing endonuclease mainly localizes on the mitochondria.Molecular biology of the cell · 2003Article
- Nic96p is required for nuclear pore formation and functionally interacts with a novel nucleoporin, Nup188p.The Journal of cell biology · 1996Article
- A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p.The Journal of cell biology · 1995Article
- Functional interaction of Nic96p with a core nucleoporin complex consisting of Nsp1p, Nup49p and a novel protein Nup57p.The EMBO journal · 1995Article
- nup1 mutants exhibit pleiotropic defects in nuclear pore complex function.The Journal of cell biology · 1994Article
- Interactions and three-dimensional localization of a group of nuclear pore complex proteins.The Journal of cell biology · 1994Article
- NUP2, a novel yeast nucleoporin, has functional overlap with other proteins of the nuclear pore complex.Molecular biology of the cell · 1993Article
- A new subclass of nucleoporins that functionally interact with nuclear pore protein NSP1.The EMBO journal · 1992Article
- A new family of yeast nuclear pore complex proteins.The Journal of cell biology · 1992Article
- Nuclear transport and nuclear pores in yeast.Antonie van Leeuwenhoek · 1992Review
- Across the nuclear pores with the help of nucleoporins.Chromosoma · 1991Review
- A complex of nuclear pore proteins required for pore function.The Journal of cell biology · 1991Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The yeast nuclear envelope protein NSP1 is located at the nuclear pores and mediates its essential function via the carboxy-terminal domain. The passenger protein, cytosolic dihydrofolate reductase from mouse, was fused to the 220 residue long NSP1 carboxy-terminal domain. When expressed in yeast, this chimeric protein was tightly associated with nuclear structures and was localized at the nuclear periphery very similar to authentic NSP1. Furthermore, the DHFR-C-NSP1 fusion protein was able to complement a yeast mutant lacking a functional NSP1 gene showing that DHFR-C-NSP1 fulfils the same basic function as compared to the endogenous NSP1 protein. These data also show that the NSP1 protein is composed of separate functional moieties: a carboxy-terminal domain that is sufficient to mediate the association with the nuclear periphery and an amino-terminal and middle repetitive domain with an as yet unknown function. It is suggested that heptad repeats found in the NSP1 carboxy-terminal domain, which are similar to those found in intermediate filament proteins, are crucial for mediating the association with the nuclear pores.
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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.