ReviewPlant molecular biology2002
Protein-protein interactions in the secretory pathway, a growing demand for experimental approaches in vivo.
Review in Plant molecular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
3 citing papers in PubMed.
- Coupled transport of Arabidopsis p24 proteins at the ER-Golgi interface.Journal of experimental botany · 2012Article
- Golgi-mediated vacuolar sorting of the endoplasmic reticulum chaperone BiP may play an active role in quality control within the secretory pathway.The Plant cell · 2006Article
- Fluorescent proteins as tools to aid protein production.Microbial cell factories · 2005Article
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.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The function of the secretory pathway is dependent on multiple protein-protein interactions at various stages. Currently, such interactions are mainly studied using physical methods that document direct contact or affinity in vitro. The development of vital fluorescence imaging as well as quantitative protein transport assays opens up the implementation of in vivo approaches which can be used to verify models based on in vitro work. The purpose of this review is to provide an overview of the various approaches involving living cells to resolve interactions between proteins that control complex mechanisms. In particular, it is illustrated how combinations of several methods can establish whether postulated interactions are of biological relevance or due to artefacts inherent to the experimental set-up.
Indexed as
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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.