ArticlePlant physiology1997
Importin alpha from Arabidopsis thaliana is a nuclear import receptor that recognizes three classes of import signals.
Article in Plant physiology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 91 citations in OpenAlex.
- Engineered NLS-PBase system boosts stability and productivity in recombinant cell lines.Bioresources and bioprocessing · 2026Article
- Nuclear dynamics: Formation of bodies and trafficking in plant nuclei.Frontiers in plant science · 2022Review
- Evaluations of Genomic Prediction and Identification of New Loci for Resistance to Stripe Rust Disease in Wheat (Frontiers in genetics · 2021Article
- Nuclear import of LIKE HETEROCHROMATIN PROTEIN1 is redundantly mediated by importins α-1, α-2 and α-3.The Plant journal : for cell and molecular biology · 2020Article
- Identification of Domains and Factors Involved in MINIYO Nuclear Import.Frontiers in plant science · 2019Article
- Functional insights of nucleocytoplasmic transport in plants.Frontiers in plant science · 2014Review
- The distribution of different classes of nuclear localization signals (NLSs) in diverse organisms and the utilization of the minor NLS-binding site inplantnuclear import factor importin-α.Plant signaling & behavior · 2013Article
- Crystal structure of rice importin-α and structural basis of its interaction with plant-specific nuclear localization signals.The Plant cell · 2012Article
- Nucleo-cytoplasmic transport of proteins and RNA in plants.Plant cell reports · 2011Review
- Inositol 1,4,5-trisphosphate and Ran expression during simulated and real microgravity.Protoplasma · 2006Article
- Nucleo-cytoplasmic partitioning of proteins in plants: implications for the regulation of environmental and developmental signalling.Current genetics · 2003Review
- Signal- and importin-dependent nuclear targeting of the kidney anion exchanger 1-binding protein kanadaptin.The Biochemical journal · 2002Article
- Import of Agrobacterium T-DNA into plant nuclei: two distinct functions of VirD2 and VirE2 proteins.The Plant cell · 2001Article
- Viruses, microorganisms and scientists meet the nuclear pore. Leysin, VD, Switzerland, February 26-March 1, 1998.The EMBO journal · 1999Review
- Nuclear localization signal receptor importin alpha associates with the cytoskeleton.The Plant cell · 1998Article
- The nuclear pore complex.Plant molecular biology · 1998Review
- Two birds with one stone: genes that encode products targeted to two or more compartments.Plant molecular biology · 1998Review
- Interaction of the DNA modifying proteins VirD1 and VirD2 of Agrobacterium tumefaciens: analysis by subcellular localization in mammalian cells.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- A glycoprotein modified with terminal N-acetylglucosamine and localized at the nuclear rim shows sequence similarity to aldose-1-epimerases.The Plant cell · 1998Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein import into the nucleus is a two-step process. In vitro import systems from vertebrate cell extracts have shown several soluble factors are required. One of these factors is the receptor importin alpha, which binds to nuclear localization signals (NLS) in vitro. We previously cloned an importin alpha homolog from Arabidopsis thaliana (At-IMP alpha) and demonstrated that this protein was not depleted from tobacco (Nicotiana tabacum) protoplasts after permeabilization of the plasma membrane, (Hicks et al., 1996). To determine if At-IMP alpha is functional, we used an in vitro NLS-binding assay. We found that At-IMP alpha is specific, and the receptor is able to recognize three classes of NLS identified in plants. Purified antibodies to At-IMP alpha were used to determine the in vivo location of importin alpha in tobacco protoplasts. Importin alpha is found in the cytoplasm and nucleus, and it is most highly concentrated at the nuclear envelope. The biochemical properties of nuclear importin alpha and localization studies using purified nuclei demonstrate that importin alpha is tightly associated with the plant nucleus. Moreover, these results suggest that a fraction of nuclear importin alpha interacts with the nuclear pore complex.
Indexed as
Identifiers
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.