ArticlePlant molecular biology2004
Remorins form a novel family of coiled coil-forming oligomeric and filamentous proteins associated with apical, vascular and embryonic tissues in plants.
Article in Plant molecular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 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
38 citing papers in PubMed, 81 citations in OpenAlex.
- Article
- Mechanisms controlling the plasma membrane targeting and the nanodomain organization of the plant SPFH protein HIR2.The Plant journal : for cell and molecular biology · 2026Article
- Genome-wide identification of the Remorin genes in Adiantum nelumboides and their responses to diverse abiotic stresses.BMC plant biology · 2025Article
- Dynamic pre-structuration of lipid nanodomain-segregating remorin proteins.Communications biology · 2024Article
- Genome-Wide Identification of theLife (Basel, Switzerland) · 2024Article
- Genome-wide characterization of Remorin gene family and their responsive expression to abiotic stresses and plant hormone in Brassica napus.Plant cell reports · 2024Article
- Plasmodesmata-associated Flotillin positively regulates broad-spectrum virus cell-to-cell trafficking.Plant biotechnology journal · 2024Article
- Stabilization of membrane topologies by proteinaceous remorin scaffolds.Nature communications · 2023Article
- Molecular characterization and expression analysis of theFrontiers in plant science · 2023Article
- How salt stress-responsive proteins regulate plant adaptation to saline conditions.Plant molecular biology · 2022Review
- Membrane nanodomains modulate formin condensation for actin remodeling in Arabidopsis innate immune responses.The Plant cell · 2022Article
- Genome-wide association mapping of seed oligosaccharides in chickpea.Frontiers in plant science · 2022Article
- Membrane nanodomains and transport functions in plant.Plant physiology · 2021Review
- Connecting the dots: from nanodomains to physiological functions of REMORINs.Plant physiology · 2021Review
- The Nanoscale Organization of the Plasma Membrane and Its Importance in Signaling: A Proteolipid Perspective.Plant physiology · 2020Review
- Deviating from the Beaten Track: New Twists in Brassinosteroid Receptor Function.International journal of molecular sciences · 2020Review
- Genome-Wide Identification and Characterization of the Wheat Remorin (The plant genome · 2019Article
- Nanodomain Clustering of the Plant Protein Remorin by Solid-State NMR.Frontiers in molecular biosciences · 2019Article
- Altered Subcellular Localization of a Tobacco Membrane Raft-Associated Remorin Protein by Tobamovirus Infection and Transient Expression of Viral Replication and Movement Proteins.Frontiers in plant science · 2018Article
- Comparative Physiological and Proteomic Analysis Reveal Distinct Regulation of Peach Skin Quality Traits by Altitude.Frontiers in plant science · 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
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Remorins form a superfamily of plant-specific plasma membrane/lipid-raft-associated proteins of unknown structure and function. Using specific antibodies, we localized tomato remorin 1 to apical tissues, leaf primordia and vascular traces. The deduced remorin protein sequence contains a predicted coiled coil-domain, suggesting its participation in protein-protein interactions. Circular dichroism revealed that recombinant potato remorin contains an alpha-helical region that forms a functional coiled-coil domain. Electron microscopy of purified preparations of four different recombinant remorins, one from potato, two divergent isologs from tomato, and one from Arabidopsis thaliana , demonstrated that the proteins form highly similar filamentous structures. The diameters of the negatively-stained filaments ranged from 4.6-7.4 nm for potato remorin 1, 4.3-6.2 nm for tomato remorin 1, 5.7-7.5 nm for tomato remorin 2, and 5.7-8.0 nm for Arabidopsis Dbp. Highly polymerized remorin 1 was detected in glutaraldehyde-crosslinked tomato plasma membrane preparations and a population of the protein was immunolocalized in tomato root tips to structures associated with discrete regions of the plasma membrane.
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.