ArticleNature immunology2006
Remodeling of the lectin-EGF-like domain interface in P- and L-selectin increases adhesiveness and shear resistance under hydrodynamic force.
Article in Nature immunology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 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
58 citing papers in PubMed, 106 citations in OpenAlex.
- Theory and Examples of Catch Bonds.The journal of physical chemistry. B · 2024Article
- Molecular mechanisms of catch bonds and their implications for platelet hemostasis.Biophysical reviews · 2023Review
- Neutralizing Antibodies Against Allosteric Proteins: Insights From a Bacterial Adhesin.Journal of molecular biology · 2022Review
- Identification of New Toxicity Mechanisms in Drug-Induced Liver Injury through Systems Pharmacology.Genes · 2022Article
- Sphingosine 1-phosphate modulation and immune cell trafficking in inflammatory bowel disease.Nature reviews. Gastroenterology & hepatology · 2022Review
- Low-affinity integrin states have faster ligand-binding kinetics than the high-affinity state.eLife · 2021Article
- Stabilization of the Hinge Region of Human E-selectin Enhances Binding Affinity to Ligands Under Force.Cellular and molecular bioengineering · 2021Article
- Functional binding of E-selectin to its ligands is enhanced by structural features beyond its lectin domain.The Journal of biological chemistry · 2020Article
- Article
- Article
- High integrin αProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Conformational switch of the bacterial adhesin FimH in the absence of the regulatory domain: Engineering a minimalistic allosteric system.The Journal of biological chemistry · 2018Article
- Glycan Bound to the Selectin Low Affinity State Engages Glu-88 to Stabilize the High Affinity State under Force.The Journal of biological chemistry · 2017Article
- Phenomenological and microscopic theories for catch bonds.Journal of structural biology · 2017Article
- Article
- Comparison of human and mouse E-selectin binding to Sialyl-Lewis(x).BMC structural biology · 2016Article
- E-selectin ligand complexes adopt an extended high-affinity conformation.Journal of molecular cell biology · 2016Article
- Quantitative Characterization of E-selectin Interaction with Native CD44 and P-selectin Glycoprotein Ligand-1 (PSGL-1) Using a Real Time Immunoprecipitation-based Binding Assay.The Journal of biological chemistry · 2015Article
- Inactive conformation enhances binding function in physiological conditions.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Inhibition and Reversal of Microbial Attachment by an Antibody with Parasteric Activity against the FimH Adhesin of Uropathogenic E. coli.PLoS pathogens · 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
3 authors at 1 institution in 1 country.
Funding
Abstract
Crystal structures of the lectin and epidermal growth factor (EGF)-like domains of P-selectin show 'bent' and 'extended' conformations. An extended conformation would be 'favored' by forces exerted on a selectin bound at one end to a ligand and at the other end to a cell experiencing hydrodynamic drag forces. To determine whether the extended conformation has higher affinity for ligand, we introduced an N-glycosylation site to 'wedge open' the interface between the lectin and EGF-like domains of P-selectin. This alteration increased the affinity of P-selectin for its ligand P-selectin glycoprotein 1 (PSGL-1) and thereby the strength of P-selectin-mediated rolling adhesion. Similarly, an asparagine-to-glycine substitution in the lectin-EGF-like domain interface of L-selectin enhanced rolling adhesion under shear flow. Our results demonstrate that force, by 'favoring' an extended selectin conformation, can strengthen selectin-ligand bonds.
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.