ArticleACS nano2014
Probing the effect of force on HIV-1 receptor CD4.
Article in ACS nano, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.
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
14 citing papers in PubMed, 1 synthesis or guideline pooled it, 27 citations in OpenAlex.
- Adjuvant roles of interleukin-7 in enhancing T cell recovery during antiretroviral therapy for individuals with HIV: a systematic review and meta-analysis.Annals of medicine · 2025Pooled it
- Generation and characterization of humanized CD4 knock-in mice expressing chimeric mouse/human CD4 protein.Lab animal · 2026Article
- The strongest protein binder is surprisingly labile.Protein science : a publication of the Protein Society · 2024Article
- High-throughput virtual search of small molecules for controlling the mechanical stability of human CD4.The Journal of biological chemistry · 2024Article
- Protein nanomechanics in biological context.Biophysical reviews · 2021Review
- Extracellular vesicles regulate gap junction-mediated intercellular communication and HIV-1 infection of human neural progenitor cells.Neurobiology of disease · 2021Article
- A biophysical perspective on receptor-mediated virus entry with a focus on HIV.Biochimica et biophysica acta. Biomembranes · 2020Review
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- Mechanical architecture and folding of E. coli type 1 pilus domains.Nature communications · 2018Article
- The influence of disulfide bonds on the mechanical stability of proteins is context dependent.The Journal of biological chemistry · 2017Article
- Engineering broadly neutralizing antibodies for HIV prevention and therapy.Advanced drug delivery reviews · 2016Review
- A simple two-state protein unfolds mechanically via multiple heterogeneous pathways at single-molecule resolution.Nature communications · 2016Article
- Lighting Up the Force: Investigating Mechanisms of Mechanotransduction Using Fluorescent Tension Probes.Molecular and cellular biology · 2015Review
- Force-induced remodelling of proteins and their complexes.Current opinion in structural biology · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Cell-surface proteins are central for the interaction of cells with their surroundings and are also associated with numerous diseases. These molecules are exposed to mechanical forces, but the exact relation between force and the functions and pathologies associated with cell-surface proteins is unclear. An important cell-surface protein is CD4, the primary receptor of HIV-1. Here we show that mechanical force activates conformational and chemical changes on CD4 that may be important during viral attachment. We have used single-molecule force spectroscopy and analysis on HIV-1 infectivity to demonstrate that the mechanical extension of CD4 occurs in a time-dependent manner and correlates with HIV-1 infectivity. We show that Ibalizumab, a monoclonal antibody that blocks HIV-1, prevents the mechanical extension of CD4 domains 1 and 2. Furthermore, we demonstrate that thiol/disulfide exchange in CD4 requires force for exposure of cryptic disulfide bonds. This mechanical perspective provides unprecedented information that can change our understanding on how viruses interact with their hosts.
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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.