ArticlemSphere2022
Defining the HIV Capsid Binding Site of Nucleoporin 153.
Article in mSphere, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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.
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Who cites it
8 citing papers in PubMed, 7 citations in OpenAlex.
- Analysis and design of disordered polypeptides with optimized sequence patterning properties.PLoS computational biology · 2026Article
- Analysis and design of disordered polypeptides with optimized sequence patterning properties.bioRxiv : the preprint server for biology · 2026Article
- Impact of HIV-1 capsid polymorphisms on viral infectivity and susceptibility to lenacapavir.mBio · 2025Article
- The identification of a novel interaction site for the human immunodeficiency virus capsid on nucleoporin 153.The Journal of general virology · 2025Article
- Structural insights into HIV-2 CA lattice formation and FG-pocket binding revealed by single-particle cryo-EM.Cell reports · 2025Article
- Review
- Statistical modeling to quantify the uncertainty of FoldX-predicted protein folding and binding stability.BMC bioinformatics · 2023Article
- Discovery and Mechanistic Investigation of Piperazinone Phenylalanine Derivatives with Terminal Indole or Benzene Ring as Novel HIV-1 Capsid Modulators.Molecules (Basel, Switzerland) · 2022Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
The interaction between the HIV-1 capsid and human nucleoporin 153 (NUP153) is vital for delivering the HIV-1 preintegration complex into the nucleus via the nuclear pore complex. The interaction with the capsid requires a phenylalanine/glycine-containing motif in the C-terminus of NUP153 (NUP153C). This study used molecular modeling and biochemical assays to comprehensively determine the amino acids in NUP153 that are important for capsid interaction. Molecular dynamics, FoldX, and PyRosetta simulations delineated the minimal capsid binding motif of NUP153 based on the known structure of NUP153 bound to the HIV-1 capsid hexamer. Computational predictions were experimentally validated by testing the interaction of NUP153 with capsid using an
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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.