ArticleThe Journal of biological chemistry2010
Modulation of integrin activation by an entropic spring in the {beta}-knee.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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
28 citing papers in PubMed, 35 citations in OpenAlex.
- Contributions of the individual domains of αCytoskeleton (Hoboken, N.J.) · 2024Article
- Intact Transition Epitope Mapping-Force Interferences by Variable Extensions (ITEM-FIVE).Biomolecules · 2024Article
- Family-wide analysis of integrin structures predicted by AlphaFold2.bioRxiv : the preprint server for biology · 2023Article
- Family-wide analysis of integrin structures predicted by AlphaFold2.Computational and structural biotechnology journal · 2023Article
- Review
- Structure of an extended βBlood · 2018Article
- Cryo-EM structure of the αvβ8 integrin reveals a mechanism for stabilizing integrin extension.Nature structural & molecular biology · 2018Article
- Human long intrinsically disordered protein regions are frequent targets of positive selection.Genome research · 2018Article
- In silico analysis of structural modifications in and around the integrin αIIb genu caused by ITGA2B variants in human platelets with emphasis on Glanzmann thrombasthenia.Molecular genetics & genomic medicine · 2018Article
- Low-affinity binding inMolecular biology of the cell · 2017Article
- Conformational equilibria and intrinsic affinities define integrin activation.The EMBO journal · 2017Article
- Structural flexibility at a major conserved antibody target on hepatitis C virus E2 antigen.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Protein stability: a crystallographer's perspective.Acta crystallographica. Section F, Structural biology communications · 2016Review
- Computational approaches for inferring the functions of intrinsically disordered proteins.Frontiers in molecular biosciences · 2015Review
- Multi-scale ensemble modeling of modular proteins with intrinsically disordered linker regions: application to p53.Biophysical journal · 2014Article
- Selective targeting of TGF-β activation to treat fibroinflammatory airway disease.Science translational medicine · 2014Article
- From sequence and forces to structure, function, and evolution of intrinsically disordered proteins.Structure (London, England : 1993) · 2013Article
- Complete integrin headpiece opening in eight steps.The Journal of cell biology · 2013Article
- Article
- Immunoregulation through membrane proteins modified by reducing conditions induced by immune reactions.European journal of immunology · 2013Review
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 3 institutions in 1 country.
Funding
Abstract
We show that the length of a loop in the β-knee, between the first and second cysteines (C1-C2) in integrin EGF-like (I-EGF) domain 2, modulates integrin activation. Three independent sets of mutants, including swaps among different integrin β-subunits, show that C1-C2 loop lengths of 12 and longer favor the low affinity state and masking of ligand-induced binding site (LIBS) epitopes. Shortening length from 12 to 4 residues progressively increases ligand binding and LIBS epitope exposure. Compared with length, the loop sequence had a smaller effect, which was ascribable to stabilizing loop conformation, and not interactions with the α-subunit. The data together with structural calculations support the concept that the C1-C2 loop is an entropic spring and an emerging theme that disordered regions can regulate allostery. Diversity in the length of this loop may have evolved among integrin β-subunits to adjust the equilibrium between the bent and extended conformations at different set points.
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.