ArticleBiophysical journal2008
Interleukin-22 forms dimers that are recognized by two interleukin-22R1 receptor chains.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed, 52 citations in OpenAlex.
- Cytokine multimerization: when more is more and sometimes less.Nature reviews. Immunology · 2026Review
- Exploring the Potentiality of a Plant Platform for Monoclonal Antibody Production in Veterinary Medicine.Vaccines · 2024Article
- Amelioration of DSS-Induced Acute Colitis in Mice by Recombinant Monomeric Human Interleukin-22.Immune network · 2022Article
- Interleukin-22 in Renal Protection and Its Pathological Role in Kidney Diseases.Frontiers in immunology · 2022Review
- Interleukin-22: a potential therapeutic target in atherosclerosis.Molecular medicine (Cambridge, Mass.) · 2021Review
- Systemic overexpression of interleukin-22 induces the negative immune-regulator SOCS3 and potently reduces experimental arthritis in mice.Rheumatology (Oxford, England) · 2021Article
- Interleukin-22 Deficiency Contributes to Dextran Sulfate Sodium-Induced Inflammation in Japanese Medaka,Frontiers in immunology · 2021Article
- IL-22 Binding Protein (IL-22BP) in the Regulation of IL-22 Biology.Frontiers in immunology · 2021Review
- Article
- Interleukin-37 monomer is the active form for reducing innate immunity.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Modulation of Interleukin-12 activity in the presence of heparin.Scientific reports · 2017Article
- Interleukin 22 attenuated angiotensin II induced acute lung injury through inhibiting the apoptosis of pulmonary microvascular endothelial cells.Scientific reports · 2017Article
- Inflammatory and Anti-Inflammatory Equilibrium, Proliferative and Antiproliferative Balance: The Role of Cytokines in Multiple Myeloma.Mediators of inflammation · 2017Review
- Increased frequency of circulating Th22 cells in patients with B-cell non-Hodgkin's lymphoma.Oncotarget · 2016Article
- Biological and pathological activities of interleukin-22.Journal of molecular medicine (Berlin, Germany) · 2016Review
- IL-22: a promising candidate to inhibit viral-induced liver disease progression and hepatocellular carcinoma.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016Review
- Interleukin-22: immunobiology and pathology.Annual review of immunology · 2015Review
- Therapeutic opportunities of the IL-22-IL-22R1 system.Nature reviews. Drug discovery · 2014Review
- Interleukin 22 signaling promotes cell growth in mantle cell lymphoma.Translational oncology · 2011Article
- Evolutionary divergence and functions of the human interleukin (IL) gene family.Human genomics · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Interleukin-22 (IL-22) is a class 2 cytokine whose primary structure is similar to that of interleukin 10 (IL-10) and interferon-gamma (IFN-gamma). IL-22 induction during acute phase immune response indicates its involvement in mechanisms of inflammation. Structurally different from IL-10 and a number of other members of IL-10 family, which form intertwined inseparable V-shaped dimers of two identical polypeptide chains, a single polypeptide chain of IL-22 folds on itself in a relatively globular structure. Here we present evidence, based on native gel electrophoresis, glutaraldehyde cross-linking, dynamic light scattering, and small angle x-ray scattering experiments, that human IL-22 forms dimers and tetramers in solution under protein concentrations assessable by these experiments. Unexpectedly, low-resolution molecular shape of IL-22 dimers is strikingly similar to that of IL-10 and other intertwined cytokine dimeric forms. Furthermore, we determine an ab initio molecular shape of the IL-22/IL-22R1 complex which reveals the V-shaped IL-22 dimer interacting with two cognate IL-22R1 molecules. Based on this collective evidence, we argue that dimerization might be a common mechanism of all class 2 cytokines for the molecular recognition with their respective membrane receptor. We also speculate that the IL-22 tetramer formation could represent a way to store the cytokine in nonactive form at high concentrations that could be readily converted into functionally active monomers and dimers upon interaction with the cognate cellular receptors.
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.