ReviewThe Biochemical journal2001
The Phox homology (PX) domain, a new player in phosphoinositide signalling.
Review in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 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
42 citing papers in PubMed, 125 citations in OpenAlex.
- In Silico Identification and Analysis of Proteins Containing the Phox Homology Phosphoinositide-Binding Domain in Kinetoplastea Protists: Evolutionary Conservation and Uniqueness of Phox-Homology-Domain-Containing Protein Architectures.International journal of molecular sciences · 2023Article
- Review
- Article
- ImitateDB: A database for domain and motif mimicry incorporating host and pathogen protein interactions.Amino acids · 2022Article
- Article
- Identification of Specific Lysines and Arginines That Mediate Angiomotin Membrane Association.ACS omega · 2019Article
- Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Phospholipase D1 Signaling: Essential Roles in Neural Stem Cell Differentiation.Journal of molecular neuroscience : MN · 2018Review
- Using the Predicted Structure of the Amot Coiled Coil Homology Domain to Understand Lipid Binding.Indiana University journal of undergraduate research · 2018Article
- Sorting nexin-4 regulates β-amyloid production by modulating β-site-activating cleavage enzyme-1.Alzheimer's research & therapy · 2017Article
- Characteristics of a Regulator of G-Protein Signaling (RGS)Frontiers in microbiology · 2017Article
- Rab5-family guanine nucleotide exchange factors bind retromer and promote its recruitment to endosomes.Molecular biology of the cell · 2015Article
- Lupus risk variants in the PXK locus alter B-cell receptor internalization.Frontiers in genetics · 2014Article
- Topical application of phosphatidyl-inositol-3,5-bisphosphate for acute lung injury in neonatal swine.Journal of cellular and molecular medicine · 2012Article
- SNX5 is essential for efficient macropinocytosis and antigen processing in primary macrophages.Biology open · 2012Article
- A structure-based protocol for learning the family-specific mechanisms of membrane-binding domains.Bioinformatics (Oxford, England) · 2012Article
- Sorting nexin 12 interacts with BACE1 and regulates BACE1-mediated APP processing.Molecular neurodegeneration · 2012Article
- Atypical membrane-embedded phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2)-binding site on p47(phox) Phox homology (PX) domain revealed by NMR.The Journal of biological chemistry · 2012Article
- Sorting nexin 19 regulates the number of dense core vesicles in pancreatic β-cells.Journal of diabetes investigation · 2012Article
- SNX3 controls Wingless/Wnt secretion through regulating retromer-dependent recycling of Wntless.Cell research · 2011Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphoinositides are key regulators of diverse cellular processes. The pleckstrin homology (PH) domain mediates the action of PtdIns(3,4)P(2), PtdIns(4,5)P(2) and PtdIns(3,4,5)P(3), while the FYVE domain relays the pulse of PtdIns3P. The recent establishment that the Phox homology (PX) domain interacts with PtdIns3P and other phosphoinositides suggests another mechanism by which phosphoinositides can regulate/integrate multiple cellular events via a spectrum of PX domain-containing proteins. Together with the recent discovery that the epsin N-terminal homologue (ENTH) domain interacts with PtdIns(4,5)P(2), it is becoming clear that phosphoinositides regulate diverse cellular events through interactions with several distinct structural motifs present in many different proteins.
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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.