ReviewPlant signaling & behavior2015
Biological significance and topological basis of aquaporin-partnering protein-protein interactions.
Review in Plant signaling & behavior, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Overexpression ofPlant signaling & behavior · 2025Article
- Effectiveness of Fuling () and its extracts against spleen deficiency in rats tonifying spleen.Journal of traditional Chinese medicine = Chung i tsa chih ying wen pan · 2023Article
- Rice aquaporin OsPIP2;2 is a water-transporting facilitator in relevance to drought-tolerant responses.Plant direct · 2021Article
- Three Proteins (Hpa2, HrpF and XopN) Are Concomitant Type III Translocators in Bacterial Blight Pathogen of Rice.Frontiers in microbiology · 2020Article
- Real-time monitoring of translocation of selected type-III effectors fromJournal of biosciences · 2019Article
- Rice aquaporin PIP1;3 and harpin Hpa1 of bacterial blight pathogen cooperate in a type III effector translocation.Journal of experimental botany · 2019Article
- Plant Aquaporins in Infection by and Immunity Against Pathogens - A Critical Review.Frontiers in plant science · 2019Article
- Plant Aquaporin AtPIP1;4 Links Apoplastic H2O2 Induction to Disease Immunity Pathways.Plant physiology · 2016Article
- Mutual Interactions between Aquaporins and Membrane Components.Frontiers in plant science · 2016Review
- Harpin Hpa1 Interacts with Aquaporin PIP1;4 to Promote the Substrate Transport and Photosynthesis in Arabidopsis.Scientific reports · 2015Article
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 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aquaporins (AQPs) are intramolecular channels essential for transport of H2O, CO2, and other small substrates across membranes. Through this function, AQPs can modulate CO2 uptake and assimilation in plants and regulate water relations and many other physiological processes in all living organisms. To execute their physiological roles, AQPs may experience 3 types of hetero-molecular interaction, between AQPs and their kinases; between AQP isoforms; and between AQPs and other proteins that are neither AQPs nor kinases. Interacting with non-AQP non-kinase proteins may enable AQPs to extend their functions beyond substrate transport, and most fascinatingly, to serve as a gateway control for translocation of virulence effectors from pathogenic bacteria into the cytosol of eukaryotic cells. In this mini review, we will summarize the latter 2 types of interaction and discuss the physiological and/or pathological significance. We will also discuss a research angle to elucidate the structural basis of AQP-partnering protein interactions.
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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.