ArticleBiochemistry2006
Importance of force linkage in mechanochemistry of adhesion receptors.
Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
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
71 citing papers in PubMed, 139 citations in OpenAlex.
- Review
- Mesenchymal cell contractility regulates villus morphogenesis and intestinal architecture.Developmental biology · 2025Article
- Whole-genome resequencing reveals new mutations in candidate genes for Beichuan-white goat prolificacya.Animal biotechnology · 2024Article
- Topology of molecular deformations induces triphasic catch bonding in selectin-ligand bonds.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Novel bioengineering strategies for drug delivery systems.Applied materials today · 2023Article
- Machine learning/molecular dynamic protein structure prediction approach to investigate the protein conformational ensemble.Scientific reports · 2022Article
- Mechanically active integrins target lytic secretion at the immune synapse to facilitate cellular cytotoxicity.Nature communications · 2022Article
- Chemo- and mechanosensing by dendritic cells facilitate antigen surveillance in the spleen.Immunological reviews · 2022Review
- The MIDAS domain of AAA mechanoenzyme Mdn1 forms catch bonds with two different substrates.eLife · 2022Article
- Single-molecule imaging of von Willebrand factor reveals tension-dependent self-association.Blood · 2021Article
- Low-affinity integrin states have faster ligand-binding kinetics than the high-affinity state.eLife · 2021Article
- Integrin-based mechanosensing through conformational deformation.Biophysical journal · 2021Article
- The principles of directed cell migration.Nature reviews. Molecular cell biology · 2021Review
- Exosomal regulation of lymphocyte homing to the gut.Blood advances · 2019Article
- Ligand- and cation-induced structural alterations of the leukocyte integrin LFA-1.The Journal of biological chemistry · 2018Article
- Self-regulation in chemical and bio-engineering materials for intelligent systems.CAAI Transactions on Intelligence Technology · 2018Article
- Direction of actin flow dictates integrin LFA-1 orientation during leukocyte migration.Nature communications · 2017Article
- Cellular fluid shear stress on implant surfaces-establishment of a novel experimental set up.International journal of implant dentistry · 2017Article
- Mechanical forces in the immune system.Nature reviews. Immunology · 2017Review
- Integrin extension enables ultrasensitive regulation by cytoskeletal force.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
11 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The alpha subunit-inserted (I) domain of integrin alphaLbeta2 [lymphocyte function-associated antigen-1 (LFA-1)] binds to intercellular adhesion molecule-1 (ICAM-1). The C- and N-termini of the alpha I domain are near one another on the "lower" face, opposite the metal ion-dependent adhesion site (MIDAS) on the "upper face". In conversion to the open alpha I domain conformation, a 7 A downward, axial displacement of C-terminal helix alpha7 is allosterically linked to rearrangement of the MIDAS into its high-affinity conformation. Here, we test the hypothesis that when an applied force is appropriately linked to conformational change, the conformational change can stabilize adhesive interactions that resist the applied force. Integrin alpha I domains were anchored to the cell surface through their C- or N-termini using type I or II transmembrane domains, respectively. C-terminal but not N-terminal anchorage robustly supported cell rolling on ICAM-1 substrates in shear flow. In contrast, when the alphaL I domain was mutationally stabilized in the open conformation with a disulfide bond, it mediated comparable levels of firm adhesion with type I and type II membrane anchors. To exclude other effects as the source of differential adhesion, these results were replicated using alpha I domains conjugated through the N- or C-terminus to polystyrene microspheres. Our results demonstrate a mechanical feedback system for regulating the strength of an adhesive bond. A review of crystal structures of integrin alpha and beta subunit I domains and selectins in high- and low-affinity conformations demonstrates a common mechanochemical design in which biologically applied tensile force stabilizes the more extended, high-affinity conformation.
Indexed as
Identifiers
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.