ArticleJournal of plant research2005
Occurrence and characterization of PEND proteins in angiosperms.
Article in Journal of plant research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed, 14 citations in OpenAlex.
- Genome communication in plants mediated by organelle-n-ucleus-located proteins.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020Review
- Identification, Gene Structure, and Expression ofFrontiers in plant science · 2020Article
- Dynamic composition, shaping and organization of plastid nucleoids.Frontiers in plant science · 2014Review
- Review
- Nucleoid-enriched proteomes in developing plastids and chloroplasts from maize leaves: a new conceptual framework for nucleoid functions.Plant physiology · 2012Article
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 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The PEND protein is a DNA-binding protein in the inner envelope membrane of the developing chloroplast. It consists of a short pre-sequence, an N-terminal DNA-binding domain (cbZIP), a central repeat domain, and a C-terminal transmembrane domain. PEND homologs have been detected in various angiosperms, including Arabidopsis thaliana, Brassica napus, Medicago truncatula, cucumber and cherry. Monocot homologs have also been detected in barley and rice, but sequence conservation was low in monocots. PEND-related sequences have not been detected in non-flowering plants and algae. Green fluorescent protein fusions consisting of the N-terminal as well as full-length PEND homologs in A. thaliana and B. napus were targeted to chloroplasts, and localized to nucleoids and chloroplast periphery, respectively. Immunoblot analysis suggested that crucifer homologs were present in chloroplasts probably as a dimer, as in the case of pea. These results suggest that PEND protein is present in angiosperms, and the homologs in crucifers are functionally analogous to the PEND protein in pea.
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.