ArticleThe Journal of biological chemistry2011
Novel p65 binding glucocorticoid-induced leucine zipper peptide suppresses experimental autoimmune encephalomyelitis.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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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
31 citing papers in PubMed, 61 citations in OpenAlex.
- Disruption of Epithelial Barrier Integrity via Altered GILZ/c-Rel/RACK1 Signaling in Inflammatory Bowel Disease.Journal of Crohn's & colitis · 2025Article
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- Review
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- Glucocorticoid Therapy in Inflammatory Bowel Disease: Mechanisms and Clinical Practice.Frontiers in immunology · 2021Review
- Glucocorticoid-Induced Leucine Zipper: A Promising Marker for Monitoring and Treating Sepsis.Frontiers in immunology · 2020Review
- Nuclear Factor κB (NF-κB)-Mediated Inflammation in Multiple Sclerosis.Frontiers in immunology · 2020Review
- A Glance at the Use of Glucocorticoids in Rare Inflammatory and Autoimmune Diseases: Still an Indispensable Pharmacological Tool?Frontiers in immunology · 2020Review
- Glucocorticoid-induced leucine zipper "quantifies" stressors and increases male susceptibility to PTSD.Translational psychiatry · 2019Article
- Could GILZ Be the Answer to Glucocorticoid Toxicity in Lupus?Frontiers in immunology · 2019Review
- Glucocorticoids and Glucocorticoid-Induced-Leucine-Zipper (GILZ) in Psoriasis.Frontiers in immunology · 2019Review
- Implicating the Role of GILZ in Glucocorticoid Modulation of T-Cell Activation.Frontiers in immunology · 2019Review
- Glucocorticoid-Induced Leucine Zipper: A Novel Anti-inflammatory Molecule.Frontiers in pharmacology · 2019Review
- Mechanisms of NF-κB p65 and strategies for therapeutic manipulation.Journal of inflammation research · 2018Review
- Nuclear factor-kappa B: Glucocorticoid-induced leucine zipper interface analogs suppress pathology in an Alzheimer's disease model.Alzheimer's & dementia (New York, N. Y.) · 2018Article
- Glucocorticoid Induced Leucine Zipper in Lipopolysaccharide Induced Neuroinflammation.Frontiers in aging neuroscience · 2018Article
- Glucocorticoid-Induced Leucine Zipper in Central Nervous System Health and Disease.Molecular neurobiology · 2017Review
- Non-canonical Glucocorticoid Receptor Transactivation ofFrontiers in immunology · 2017Article
- Overexpression of Glucocorticoid-induced Leucine Zipper (GILZ) increases susceptibility to Imiquimod-induced psoriasis and involves cutaneous activation of TGF-β1.Scientific reports · 2016Article
- Low expression of the GILZ may contribute to adipose inflammation and altered adipokine production in human obesity.Journal of lipid research · 2016Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Multiple sclerosis (MS) is a neurological disease characterized by inflammatory demyelination in the brain and spinal cord. The immune-mediated inflammation involves well orchestrated intermolecular interactions that exhibit rapid binding kinetics. The binding interfaces of transient interactions frequently include proline residues that favor an extended conformation for molecular recognition. Linear interface peptides are excellent lead inhibitors of specific protein-protein interactions because only small segments of the interface contribute to the binding. Glucocorticoid-induced leucine zipper (GILZ), a recently identified molecule exhibits potent anti-inflammatory properties. Mechanistically, a proline-rich segment in the carboxyl terminus of GILZ physically binds the p65 subunit of nuclear factor-κB and inhibits the transactivation of inflammatory cytokines. Integrating knowledge derived from the mechanism of action of GILZ with in silico structure prediction identified an immunomodulatory peptide, the GILZ-P. Treatment with GILZ-P exhibited therapeutic efficacy in experimental autoimmune encephalomyelitis, a model for human MS.
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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.