Affinage

CIDEA

Lipid transferase CIDEA · UniProt O60543

Length
219 aa
Mass
24.7 kDa
Annotated
2026-06-09
64 papers in source corpus 34 papers cited in narrative 33 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

CIDEA is a CIDE-domain protein that governs cellular triglyceride storage by acting at lipid droplets while doubling as a nuclear transcriptional regulator of lipid and thermogenic gene programs (PMID:18509062, PMID:20810722, PMID:31563853). At lipid droplets, where it colocalizes with perilipin, its C-terminal ~104 residues are necessary and sufficient for droplet targeting and for shielding stored triglyceride from lipolysis, whereas the N-terminal CIDE domain drives the formation of enlarged droplets (PMID:18509062, PMID:20810722); mechanistically, CIDEA enlarges droplets by promoting lipid-droplet fusion through an amphipathic helix that embeds in the phospholipid monolayer and binds phosphatidic acid, forming trans-complexes at droplet-droplet contacts that permit directional lipid transfer (PMID:26609809). CIDEA also shuttles between droplets and the nucleus: during adipocyte browning a bipartite nuclear localization signal drives concentration-dependent nuclear entry, where CIDEA relieves LXRα-mediated repression and strengthens PPARγ binding at the UCP1 enhancer to drive UCP1 transcription (PMID:31563853, PMID:21315073), and in mammary epithelium it acts as a transcriptional coactivator of C/EBPβ, displacing HDAC1 to induce XOR expression required for milk lipid secretion (PMID:22245780). In brown fat CIDEA suppresses thermogenesis: knockout mice have elevated UCP1-dependent metabolic rate and resist diet-induced obesity, and CIDEA inhibits UCP1 activity indirectly without altering UCP1 protein levels (PMID:12910269, PMID:27923808, PMID:26118629), in part by complexing with the AMPK-β subunit in the ER and driving its ubiquitin-dependent degradation (PMID:18480843). CIDEA expression is integrated by lipogenic and nuclear-receptor signaling — induced by PPARα/γ, by SREBP-1c downstream of insulin and saturated fatty acids, and by ERRα/PGC-1α/SENP2 — and repressed by TNF-α via NF-κB/JNK and by DNMT3B-mediated promoter methylation (PMID:17462989, PMID:20575761, PMID:22278400, PMID:37748256, PMID:18607384, PMID:37703946), while CIDEA protein is itself turned over by proteasomal degradation following polyubiquitination at K23 (PMID:17711404). Independently of its lipid roles, CIDEA promotes apoptosis: its C-terminal region induces DNA fragmentation inhibitable by DFF45, and it functions as a pro-apoptotic effector in adipocytes, β-cells, and cochlear hair cells (PMID:9564035, PMID:20154362, PMID:41262044).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 1998 High

    Established CIDEA's first molecular activity by showing it could trigger programmed cell death, defining a two-domain architecture in which the C-terminus kills and the N-terminal CIDE domain confers DFF45 regulation.

    Evidence Ectopic expression in 293T cells with DNA fragmentation assays, domain deletion mutants, and DFF45 co-expression

    PMID:9564035

    Open questions at the time
    • Did not establish the physiological context of apoptotic activity
    • No endogenous substrate or partner of the C-terminal killing domain identified
  2. 2003 High

    Connected CIDEA to whole-body energy metabolism by showing it restrains UCP1-dependent thermogenesis, recasting the apoptotic gene as a metabolic regulator.

    Evidence Cidea-null mouse with metabolic rate, cold tolerance, lipolysis measurements and direct UCP1 activity assay

    PMID:12910269

    Open questions at the time
    • Mechanism by which CIDEA suppresses UCP1 not resolved
    • Did not address subcellular site of action
  3. 2007 High

    Defined how CIDEA protein abundance is controlled and how its transcription is wired to lipid-sensing nuclear receptors.

    Evidence CHX chase and ubiquitination assays with lysine mutagenesis (K23); EMSA/ChIP/reporter for PPARα/γ PPRE

    PMID:17462989 PMID:17711404

    Open questions at the time
    • E3 ligase responsible for K23 ubiquitination not identified
    • Tissue specificity of PPRE usage not resolved
  4. 2008 High

    Relocated CIDEA's primary site of action to lipid droplets and revealed two distinct metabolic mechanisms: suppression of lipolysis at droplets and ER-based degradation of AMPK-β.

    Evidence Perilipin colocalization, Cidea-GFP overexpression and RNAi lipolysis assays; reciprocal Co-IP and ubiquitination assays with AMPK subunits plus Cidea-null cells

    PMID:18480843 PMID:18509062

    Open questions at the time
    • Reconciliation of earlier mitochondrial localization claims incomplete
    • How CIDEA enlarges droplets mechanistically unresolved at this stage
  5. 2008 Medium

    Mapped upstream transcriptional and signaling control of CIDEA, including PGC-1α/ERRα activation, RIP140 corepression, and TNF-α suppression via NF-κB and JNK.

    Evidence Promoter reporter/EMSA assays, RIP140-PGC-1α interaction, RNAi with lipolysis and cytokine readouts, JNK inhibitor experiments in human adipocytes

    PMID:15919794 PMID:18607384 PMID:18794372

    Open questions at the time
    • Single-lab promoter studies
    • Post-transcriptional component of TNF-α effect not molecularly defined
  6. 2008 Medium

    Documented apoptosis-associated nuclear redistribution of CIDEA, linking its localization to cell-death function.

    Evidence Immunocytochemistry and subcellular fractionation under apoptotic stimuli in HeLa cells

    PMID:18645223

    Open questions at the time
    • Mechanism and signal driving translocation not defined
    • Single-lab localization study
  7. 2010 High

    Dissected CIDEA's domain logic at lipid droplets, separating C-terminal targeting/triglyceride shielding from N-terminal droplet enlargement, and tied hepatic CIDEA induction to the SREBP-1c/insulin axis.

    Evidence Deletion constructs with LD morphology and triglyceride/glycerol assays; EMSA/ChIP/reporter plus SREBP-1c-null hepatocytes; insulin-PI3K/Akt apoptosis studies

    PMID:20154362 PMID:20575761 PMID:20810722

    Open questions at the time
    • Structural basis of N-terminal-mediated enlargement not yet shown
    • How insulin coordinately controls CIDEA in liver vs adipose not unified
  8. 2011 Medium

    Expanded CIDEA's regulatory inputs (FoxO1, Akt1/2) and revealed direct interaction with LXRs, foreshadowing a nuclear-receptor coactivator role.

    Evidence siRNA epistasis and pathway inhibitors in adipocytes and β-cells; protein-binding and transactivation assays with cell fractionation for LXR

    PMID:21315073 PMID:21636835 PMID:21945815

    Open questions at the time
    • LXR interaction surface and direct binding not structurally mapped
    • Single-lab interaction assays
  9. 2012 High

    Demonstrated a bona fide nuclear transcriptional-coactivator function by showing CIDEA drives C/EBPβ-dependent XOR expression for milk lipid secretion.

    Evidence Nuclear Co-IP, ChIP for C/EBPβ and HDAC1 at Xdh promoter, Cidea-null mammary phenotype, and rescue

    PMID:22245780

    Open questions at the time
    • How CIDEA partitions between droplet and nuclear pools not defined here
    • Generality of coactivator role across tissues unknown
  10. 2015 High

    Provided the biophysical mechanism of CIDEA-driven droplet enlargement and clarified that brown-fat UCP1 suppression is indirect rather than via mitochondrial CIDEA.

    Evidence Amphipathic-helix mutagenesis, PA-binding and LD fusion reconstitution with live imaging; aP2-hCidea transgenic mice with isolated-mitochondria UCP1 activity assays

    PMID:26118629 PMID:26609809 PMID:27923808

    Open questions at the time
    • Molecular intermediary linking CIDEA to UCP1 activity inhibition still unidentified
    • Regulation of trans-complex assembly in vivo not defined
  11. 2019 High

    Resolved the droplet-to-nucleus shuttling mechanism and showed nuclear CIDEA promotes thermogenesis by remodeling LXRα/PPARγ occupancy at the UCP1 enhancer, an apparent counterpoint to its BAT UCP1-suppressing role.

    Evidence CRISPR knockout with rescue in primary human adipocytes, live-cell NLS imaging, and ChIP at the UCP1 enhancer

    PMID:31563853

    Open questions at the time
    • Reconciliation of pro- and anti-thermogenic roles across depots not settled
    • Signals controlling concentration-dependent shuttling not defined
  12. 2023 Medium

    Layered additional transcriptional and epigenetic control (SENP2/ERRα/PGC-1α, Egr-1 circadian coupling, DNMT3B methylation) onto CIDEA regulation in metabolic tissues.

    Evidence SENP2/ERRα knockdown in adipocytes, Egr-1 knockout circadian liver profiling, DNMT3B manipulation with bisulfite sequencing and rescue

    PMID:36964140 PMID:37703946 PMID:37748256

    Open questions at the time
    • Mostly single-lab studies
    • Integration of multiple inputs at a single promoter not modeled
  13. 2025 Medium

    Extended CIDEA's pro-apoptotic function to a new physiological context, showing it mediates damage-induced hair-cell death and that its editing protects against ototoxic loss.

    Evidence Cidea-null mice with neomycin/noise exposure and AAV-delivered CRISPR editing in cochlea

    PMID:41262044

    Open questions at the time
    • Molecular pathway from CIDEA to hair-cell apoptosis not defined
    • Single study

Open questions

Synthesis pass · forward-looking unresolved questions
  • The central unresolved question is how CIDEA reconciles its opposing roles—lipid-droplet fusion/storage, depot-specific pro- and anti-thermogenic transcriptional effects, and pro-apoptotic activity—through a unified control of its localization, abundance, and partner choice.
  • No structural model unifying droplet-binding and nuclear coactivator surfaces
  • Signals dictating droplet-vs-nucleus partitioning unknown
  • Direct effector linking CIDEA to UCP1 activity inhibition unidentified

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140110 transcription regulator activity 2 GO:0140313 molecular sequestering activity 2 GO:0008289 lipid binding 1
Localization
GO:0005634 nucleus 3 GO:0005811 lipid droplet 3 GO:0005783 endoplasmic reticulum 1
Pathway
R-HSA-1430728 Metabolism 3 R-HSA-5357801 Programmed Cell Death 3 R-HSA-74160 Gene expression (Transcription) 2
Partners
CEBPBCIDECDFFALXRAPPARGPRKAB1

Evidence

Reading pass · 33 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1998 CIDEA activates apoptosis in mammalian cells and induces DNA fragmentation; this activity is inhibited by DFF45/ICAD. Mutant analysis showed the C-terminal region of CIDEA is necessary and sufficient for killing, while the N-terminal CIDE domain (homologous to DFF45) is required for DFF45-mediated inhibition of CIDEA. Ectopic expression in 293T cells, DNA fragmentation assay, domain deletion/mutant analysis, co-expression with DFF45 The EMBO journal High 9564035
2003 Cidea directly suppresses UCP1 activity in brown adipose tissue mitochondria, thereby regulating thermogenesis and lipolysis; Cidea-null mice have higher UCP1-dependent metabolic rate and are resistant to diet-induced obesity. Cidea-null mouse model (genetic knockout), metabolic rate measurements, cold tolerance assay, in vivo lipolysis, direct UCP1 activity assay Nature genetics High 12910269
2007 CIDEA protein stability is regulated by ubiquitin-mediated proteasomal degradation. CIDEA is polyubiquitinated primarily at K23 in its N-terminal region; mutation of N-terminal lysine residues (N-5KA mutant) dramatically stabilizes the protein. Cycloheximide chase assay, proteasome inhibitor treatment, ubiquitination assay, site-directed mutagenesis of individual lysine residues The Biochemical journal High 17711404
2007 PPARα and PPARγ transcriptionally regulate Cidea expression in mouse liver through a shared proximal PPRE element (Cidea-PPRE1 at -680/-668) in the Cidea gene promoter. Transactivation assay, gel-shift (EMSA), chromatin immunoprecipitation (ChIP), luciferase reporter assay The Journal of biological chemistry High 17462989
2008 Cidea colocalizes with lipid droplets (not mitochondria as previously thought), co-localizing with perilipin. Cidea-GFP expression greatly enhances lipid droplet size in preadipocytes and COS cells, and RNAi depletion of Cidea elevates lipolysis in human adipocytes. Fluorescence microscopy/colocalization with perilipin, ectopic Cidea-GFP expression in preadipocytes and COS cells, RNAi knockdown with lipolysis assay Proceedings of the National Academy of Sciences of the United States of America High 18509062
2008 Cidea forms a complex with the β subunit (but not α or γ subunit) of AMPK in the endoplasmic reticulum and promotes ubiquitin-dependent proteasomal degradation of the AMPK-β subunit, reducing AMPK protein levels and enzymatic activity in brown adipose tissue. Co-immunoprecipitation in vivo, subcellular colocalization, co-expression with AMPK subunits and stability assay, ubiquitination assay, Cidea-null adipocyte differentiation from MEFs/preadipocytes The EMBO journal High 18480843
2008 The corepressor RIP140 directly interacts with PGC-1α and suppresses its activity, which in turn represses CIDEA expression; conversely, PGC-1α induces CIDEA expression via estrogen-related receptor α (ERRα) and NRF-1 binding sites on the CIDEA promoter. Luciferase reporter/promoter assay, ectopic expression of RIP140 and PGC-1α, protein-protein interaction assay (direct interaction between RIP140 and PGC-1α), adipocyte lipid droplet imaging Molecular and cellular biology Medium 18794372
2008 CIDEa redistributes from mitochondria to the nucleus during apoptosis induction in HeLa cells, as shown by immunocytochemistry and subcellular fractionation, suggesting mitochondrial sequestration of CIDEa with nuclear translocation promoting apoptosis. Immunocytochemistry, subcellular fractionation/Western blot, tetracycline-inducible expression system, camptothecin and valinomycin treatments General physiology and biophysics Medium 18645223
2008 TNF-α decreases CIDEA expression in human adipocytes via the JNK (c-Jun N-terminal kinase) MAP kinase pathway, and CIDEA depletion by RNAi stimulates lipolysis and increases TNF-α secretion by a post-transcriptional mechanism. RNAi knockdown in human adipocytes, lipolysis assay (glycerol release), TNF-α treatment with JNK pathway inhibitor, TNF-α secretion measurement Diabetes Medium 15919794
2008 TNF-α negatively regulates transcription of the human CIDEA gene through an NF-κB binding site at position -163/-151 in the CIDEA promoter; basal transcriptional activity is confined to the 97 bp immediately upstream of the TSS. Luciferase reporter assay with deletion constructs, EMSA, mutational analysis of NF-κB site, human adipocyte and 3T3-L1 transfection International journal of obesity Medium 18607384
2009 Acute cold exposure down-regulates CIDEA mRNA and protein in rat interscapular BAT via sympathetically activated β3-adrenoreceptors, as demonstrated by pharmacological blockade with propranolol and SR59230A. Cold exposure in vivo, pharmacological blockade (propranolol, SR59230A), norepinephrine turnover measurement, quantitative RT-PCR and Western blot Biochemical and biophysical research communications Medium 19577538
2009 The FSP27/CIDEC CIDE-C domain directly interacts with CIDEA; FSP27 protein levels are reduced by co-expression of CIDEA. Interaction assay (co-immunoprecipitation/pulldown), co-expression and Western blot, domain deletion constructs American journal of physiology. Endocrinology and metabolism Medium 19843876
2010 The carboxy-terminal 104 amino acids of human Cidea are necessary and sufficient for lipid droplet targeting and triglyceride shielding (inhibition of lipolysis), while the N-terminal domain is required for the formation of enlarged lipid droplets (not just clustering of small droplets). Expression of deletion constructs in 3T3-L1 and COS-1 cells, lipid droplet morphology imaging, triglyceride quantification, basal glycerol release assay Journal of lipid research High 20810722
2010 SREBP-1c directly mediates insulin-induced Cidea expression in hepatocytes by binding to a sterol-regulatory element (SRE) in the Cidea gene promoter; Cidea in turn mediates SREBP-1c-dependent lipid accumulation. Luciferase reporter assay, EMSA, ChIP, adenovirus-mediated SREBP-1c overexpression, hepatocytes from SREBP-1c-null mice, Cidea knockdown The Biochemical journal High 20575761
2010 Insulin decreases CIDEA expression in human adipocytes via a PI3K/Akt1/2-dependent pathway; CIDEA depletion by siRNA inhibits starvation-induced apoptosis similarly to insulin, identifying CIDEA as a pro-apoptotic effector downstream of Akt signaling in adipocytes. PI3K/Akt inhibitors, siRNA knockdown, apoptosis assay, adipocyte number quantification Journal of lipid research Medium 20154362
2011 Insulin regulates CIDEA expression via the PI3K/Akt1/2 pathway; specific knockdown of Akt1/2 (but not JNK or ERK) prevented insulin-induced downregulation of CIDEA and inhibition of apoptosis in human adipocytes. PI3K inhibitors (wortmannin, PI-103), Akt inhibitor (API-2), JNK inhibitor (SP600125), siRNA knockdown of Akt1/2, apoptosis assay Journal of lipid research Medium 21636835
2011 CIDEA physically interacts with liver X receptors (LXRs) in human white adipocytes and modulates their transcriptional activity; CIDEA localizes to both cytoplasm and nucleus in these cells. Bioinformatic identification of nuclear receptor binding motifs, protein-protein binding assay, transactivation assay, cell fractionation FEBS letters Medium 21315073
2011 FoxO1 mediates palmitic acid-induced upregulation of Cidea in pancreatic β-cells; suppression of FoxO1 inhibits palmitate-induced Cidea expression and apoptosis, identifying a FoxO1→Cidea pro-apoptotic axis in β-cells. FoxO1 siRNA knockdown, Cidea siRNA knockdown, palmitic acid treatment, apoptosis assay in β-cells Molecular and cellular endocrinology Medium 21945815
2012 Cidea functions as a transcriptional coactivator of C/EBPβ in mammary epithelial cells; it physically interacts with C/EBPβ in the nucleus, promotes C/EBPβ binding to the Xdh (XOR) promoter, displaces HDAC1 from the promoter, and thereby induces XOR expression required for milk lipid secretion. Nuclear fractionation, co-immunoprecipitation of Cidea with C/EBPβ, ChIP for C/EBPβ and HDAC1 at Xdh promoter, Cidea-null mouse mammary gland phenotype, ectopic Cidea expression Nature medicine High 22245780
2012 Overexpression of Cidea in mouse liver increases hepatic lipid accumulation and large lipid droplet formation; Cidea deficiency reduces lipid accumulation in diet-induced obese and ob/ob mice. Cidea expression in hepatocytes is specifically induced by saturated fatty acids via SREBP1c. Adenovirus-mediated Cidea overexpression in mouse liver, Cidea-null mice on HFD and ob/ob background, Cidea knockdown in ob/ob livers, saturated FA treatment of hepatocytes, SREBP1c knockdown/overexpression Hepatology High 22278400
2014 Cidea is required for lipid storage and sebum secretion in sebaceous glands; Cidea deficiency leads to smaller lipid droplets in sebocytes, reduced skin surface lipids (TAG and wax diesters), and impaired water repulsion/thermoregulation. Cidea overexpression in human SZ95 sebocytes increases lipid storage and large lipid droplet formation. Cidea-null mouse phenotyping, skin lipid analysis, sebocyte lipid droplet imaging, CIDEA overexpression in SZ95 cells Molecular and cellular biology Medium 24636991
2015 CIDEA promotes lipid droplet (LD) fusion via an amphipathic helix that embeds in the LD phospholipid monolayer and binds phosphatidic acid (PA). CIDEA forms trans-complexes at LD-LD contact sites through contributions of the N-terminal CIDE domain and a C-terminal dimerization region, and these complexes interact with cone-shaped PA to increase phospholipid barrier permeability and enable lipid transfer between droplets. Amphipathic helix mutagenesis, PA-binding assay (lipid overlay/liposome pulldown), LD fusion assay, live-cell imaging of LD-LD contacts, domain deletion constructs, reconstitution of fusion in cells eLife High 26609809
2015 Cidea overexpression in adipose tissues (aP2-hCidea transgenic mice) mechanistically promotes adipose tissue expandability and increases lipid droplet size in white fat; UCP1 activity is markedly suppressed in brown-fat mitochondria from these mice despite unchanged UCP1 protein levels, indicating Cidea indirectly inhibits UCP1 activity (not by reducing its expression), and the effect is not due to mitochondrial localization of Cidea. Transgenic mouse model (aP2-hCidea), isolated brown-fat mitochondria UCP1 activity assay, UCP1 protein quantification, adipose tissue histology, metabolic phenotyping American journal of physiology. Endocrinology and metabolism High 26118629 27923808
2018 CIDEA promotes hepatic lipid accumulation via SREBP1c-mediated transcriptional induction; acetaldehyde specifically induces Cidea expression through activation of the SRE element in the Cidea promoter, which is abolished by SREBP1c knockdown. Dual-luciferase reporter gene assay (SRE element), SREBP1c knockdown (siRNA), acetaldehyde treatment of AML12 cells Scientific reports Medium 29352167
2019 During adipocyte britening, CIDEA shuttles from lipid droplets to the nucleus via a bipartite nuclear localization signal in a concentration-dependent manner. In the nucleus, CIDEA specifically inhibits LXRα-mediated repression of the UCP1 enhancer and strengthens PPARγ binding to the UCP1 enhancer, thereby driving UCP1 transcription. CRISPR-Cas9nD10A knockout of CIDEA in primary human adipocytes, CIDEA re-expression rescue, live-cell nuclear localization imaging, ChIP for LXRα and PPARγ at UCP1 enhancer, transcriptome analysis iScience High 31563853
2021 ER stress increases Cidea mRNA levels (maintained partly by increased mRNA stability) and stabilizes CIDE-A protein (normally sensitive to proteasomal degradation); this is negatively regulated by ATF6. Elevated CIDE-A expression under ER stress accompanies increased cell death. Induction of acute ER stress in PCCL3 thyrocytes, mRNA stability assay, proteasome inhibitor treatment, ATF6 manipulation, comparison with chronic ER stress-adapted cells JCI insight Medium 33661766
2021 CIDEA overexpression in esophageal squamous cell carcinoma cells triggers G1-phase arrest and caspase-dependent mitochondrial apoptosis through the JNK-p21/Bad pathway; JNK activation by CIDEA induces actin cytoskeletal disruption, IL-6 release, and decreased STAT3 phosphorylation, while CIDEA-mediated apoptotic cell death and p53 acetylation are JNK-independent. CIDEA ectopic expression in ESCC cells, in vivo tumorigenesis in nude mice, caspase assay, JNK pathway inhibition, flow cytometry cell cycle analysis Frontiers in oncology Medium 33614508
2022 METTL16 upregulates CIDEA expression at the translational level in an m6A-dependent manner in hepatocytes; METTL16 overexpression increases CIDEA expression and lipogenic gene expression in HepG2 cells. m6A high-throughput sequencing, METTL16 overexpression and knockdown in HepG2 cells, qRT-PCR and Western blot PeerJ Low 36518278
2022 CIDEA inhibits AMPK activity in bovine mammary epithelial cells by suppressing AMPK phosphorylation, which enhances PPARγ expression and nuclear translocation of SREBP1, thereby increasing fatty acid and triglyceride synthesis. CIDEA overexpression and siRNA knockdown in bMECs, AMPK activity assay, PPARγ and SREBP1 expression and localization by Western blot/immunofluorescence, TAG quantification Journal of agricultural and food chemistry Medium 36040348
2023 SENP2 increases CIDEA expression by desumoylating ERRα, which then acts in coordination with PGC-1α to activate CIDEA transcription in adipocytes; palmitate treatment increases both SENP2 and CIDEA expression, and ERRα or SENP2 knockdown eliminates palmitate-induced CIDEA upregulation. SENP2 overexpression in 3T3-L1 adipocytes, siRNA knockdown of SENP2 and ERRα, lipid droplet size measurement, palmitate treatment, qRT-PCR Biochemical and biophysical research communications Medium 37748256
2023 Egr-1 transcription factor regulates Cidea expression in a circadian-coupled manner in mouse liver; Egr-1 deletion disrupts the opposite rhythmic coupling of Egr-1 and Cidea, resulting in increased hepatic triglyceride accumulation and large lipid droplet formation. Egr-1 knockout mouse liver analysis, transcriptional rhythm profiling, lipid droplet and triglyceride quantification, light-induced circadian reset Nature communications Medium 36964140
2023 DNMT3B maintains Cidea promoter methylation to suppress CIDEA expression; LPS-induced reduction of DNMT3B causes promoter hypomethylation of CIDEA, increasing SREBP-1c binding to the CIDEA promoter and activating its expression, promoting hepatic lipid accumulation. DNMT3B overexpression and knockdown in mice and hepatocytes, bisulfite sequencing of CIDEA promoter, CIDEA interference in vivo, lipid accumulation assay Cellular and molecular gastroenterology and hepatology Medium 37703946
2025 In cochlear hair cells, Cidea expression is specifically induced by neomycin damage; Cidea knockout mice show reduced hair cell apoptosis from neomycin and noise exposure. CRISPR/SlugCas9-HF-mediated Cidea editing via AAV delivery significantly reduces hair cell loss. Cidea-null mouse model, neomycin and noise exposure in vivo, CRISPR/Cas9 AAV delivery, hair cell apoptosis quantification Advanced science Medium 41262044

Source papers

Stage 0 corpus · 64 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2003 Cidea-deficient mice have lean phenotype and are resistant to obesity. Nature genetics 405 12910269
2008 Cidea is associated with lipid droplets and insulin sensitivity in humans. Proceedings of the National Academy of Sciences of the United States of America 306 18509062
1998 CIDE, a novel family of cell death activators with homology to the 45 kDa subunit of the DNA fragmentation factor. The EMBO journal 282 9564035
2012 Cidea promotes hepatic steatosis by sensing dietary fatty acids. Hepatology (Baltimore, Md.) 159 22278400
2005 A human-specific role of cell death-inducing DFFA (DNA fragmentation factor-alpha)-like effector A (CIDEA) in adipocyte lipolysis and obesity. Diabetes 156 15919794
2008 Downregulation of AMP-activated protein kinase by Cidea-mediated ubiquitination and degradation in brown adipose tissue. The EMBO journal 139 18480843
2008 A functional interaction between RIP140 and PGC-1alpha regulates the expression of the lipid droplet protein CIDEA. Molecular and cellular biology 136 18794372
2015 The brown adipocyte protein CIDEA promotes lipid droplet fusion via a phosphatidic acid-binding amphipathic helix. eLife 128 26609809
2012 Cidea is an essential transcriptional coactivator regulating mammary gland secretion of milk lipids. Nature medicine 99 22245780
2015 Cidea improves the metabolic profile through expansion of adipose tissue. Nature communications 89 26118629
2007 Transcriptional regulation of Cidea, mitochondrial cell death-inducing DNA fragmentation factor alpha-like effector A, in mouse liver by peroxisome proliferator-activated receptor alpha and gamma. The Journal of biological chemistry 83 17462989
2019 CIDEA Transcriptionally Regulates UCP1 for Britening and Thermogenesis in Human Fat Cells. iScience 79 31563853
2009 Functional analysis of FSP27 protein regions for lipid droplet localization, caspase-dependent apoptosis, and dimerization with CIDEA. American journal of physiology. Endocrinology and metabolism 73 19843876
2008 Evidence for an important role of CIDEA in human cancer cachexia. Cancer research 54 19010897
2005 The CIDEA gene V115F polymorphism is associated with obesity in Swedish subjects. Diabetes 50 16186410
2016 UCP1 inhibition in Cidea-overexpressing mice is physiologically counteracted by brown adipose tissue hyperrecruitment. American journal of physiology. Endocrinology and metabolism 45 27923808
2018 High expression of cell death-inducing DFFA-like effector a (CIDEA) promotes milk fat content in dairy cows with clinical ketosis. Journal of dairy science 41 30594378
2010 Identification of the lipid droplet targeting domain of the Cidea protein. Journal of lipid research 40 20810722
2014 Cidea control of lipid storage and secretion in mouse and human sebaceous glands. Molecular and cellular biology 38 24636991
2010 Sterol-regulatory-element-binding protein 1c mediates the effect of insulin on the expression of Cidea in mouse hepatocytes. The Biochemical journal 37 20575761
2010 Differential roles of CIDEA and CIDEC in insulin-induced anti-apoptosis and lipid droplet formation in human adipocytes. Journal of lipid research 32 20154362
2010 Promoter hypermethylation of CIDEA, HAAO and RXFP3 associated with microsatellite instability in endometrial carcinomas. Gynecologic oncology 32 20211485
2023 The rhythmic coupling of Egr-1 and Cidea regulates age-related metabolic dysfunction in the liver of male mice. Nature communications 31 36964140
2011 Differential regulation of CIDEA and CIDEC expression by insulin via Akt1/2- and JNK2-dependent pathways in human adipocytes. Journal of lipid research 28 21636835
2015 Effects of a High Fat Diet and Voluntary Wheel Running Exercise on Cidea and Cidec Expression in Liver and Adipose Tissue of Mice. PloS one 27 26176546
2022 Ban-xia-xie-xin-tang ameliorates hepatic steatosis by regulating Cidea and Cidec expression in HFD-fed mice. Phytomedicine : international journal of phytotherapy and phytopharmacology 25 35908522
2018 Effects of a high energy and low protein diet on hepatic and plasma characteristics and Cidea and Cidec mRNA expression in liver and adipose tissue of laying hens with fatty liver hemorrhagic syndrome. Animal science journal = Nihon chikusan Gakkaiho 25 30523654
2008 Cell death-inducing DNA fragmentation factor alpha-like effector A (CIDEA) gene V115F (G-->T) polymorphism is associated with phenotypes of metabolic syndrome in Japanese men. Metabolism: clinical and experimental 25 18328351
2007 Regulation of Cidea protein stability by the ubiquitin-mediated proteasomal degradation pathway. The Biochemical journal 25 17711404
2022 METTL16-mediated translation of CIDEA promotes non-alcoholic fatty liver disease progression via m6A-dependent manner. PeerJ 24 36518278
2011 Suppression of FoxO1/cell death-inducing DNA fragmentation factor α-like effector A (Cidea) axis protects mouse β-cells against palmitic acid-induced apoptosis. Molecular and cellular endocrinology 20 21945815
2007 CIDE-A is expressed in liver of old mice and in type 2 diabetic mouse liver exhibiting steatosis. Comparative hepatology 20 17472743
2010 Cide-a and Cide-c are induced in the progression of hepatic steatosis and inhibited by eicosapentaenoic acid. Prostaglandins, leukotrienes, and essential fatty acids 19 20542418
2010 Association of the cell death-inducing DNA fragmentation factor alpha-like effector A (CIDEA) gene V115F (G/T) polymorphism with phenotypes of metabolic syndrome in a Chinese population. Diabetes research and clinical practice 19 21106268
2022 CIDEA Regulates De Novo Fatty Acid Synthesis in Bovine Mammary Epithelial Cells by Targeting the AMPK/PPARγ Axis and Regulating SREBP1. Journal of agricultural and food chemistry 18 36040348
2013 The genetic contribution of CIDEA polymorphisms, haplotypes and loci interaction to obesity in a Han Chinese population. Molecular biology reports 15 24057179
2008 Molecular cloning, chromosomal location and expression pattern of porcine CIDEa and CIDEc. Molecular biology reports 15 18311595
2018 SREBP1c mediates the effect of acetaldehyde on Cidea expression in Alcoholic fatty liver Mice. Scientific reports 14 29352167
2014 Maternal diet amplifies the hepatic aging trajectory of Cidea in male mice and leads to the development of fatty liver. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 14 24481968
2009 Saturated fatty acids stimulate and insulin suppresses CIDE-A expression in bovine mammary epithelial cells. Biochemical and biophysical research communications 14 19427838
2019 Plasticity of histone modifications around Cidea and Cidec genes with secondary bile in the amelioration of developmentally-programmed hepatic steatosis. Scientific reports 13 31745102
2015 PPARγ regulated CIDEA affects pro-apoptotic responses in glioblastoma. Cell death discovery 12 27551468
2014 Adipose tissue CIDEA is associated, independently of weight variation, to change in insulin resistance during a longitudinal weight control dietary program in obese individuals. PloS one 12 24983748
2021 Cell death-associated lipid droplet protein CIDE-A is a noncanonical marker of endoplasmic reticulum stress. JCI insight 11 33661766
2011 CIDEA interacts with liver X receptors in white fat cells. FEBS letters 11 21315073
2009 Acute cold exposure-induced down-regulation of CIDEA, cell death-inducing DNA fragmentation factor-alpha-like effector A, in rat interscapular brown adipose tissue by sympathetically activated beta3-adrenoreceptors. Biochemical and biophysical research communications 11 19577538
2008 Characterization of the human CIDEA promoter in fat cells. International journal of obesity (2005) 11 18607384
2008 Redistribution of cell death-inducing DNA fragmentation factor-like effector-a (CIDEa) from mitochondria to nucleus is associated with apoptosis in HeLa cells. General physiology and biophysics 11 18645223
2023 DNMT3B Alleviates Liver Steatosis Induced by Chronic Low-grade LPS via Inhibiting CIDEA Expression. Cellular and molecular gastroenterology and hepatology 9 37703946
2022 Hypermethylation-Mediated Silencing of CIDEA, MAL and PCDH17 Tumour Suppressor Genes in Canine DLBCL: From Multi-Omics Analyses to Mechanistic Studies. International journal of molecular sciences 9 35409379
2021 Development of CIDEA reporter mouse model and its application for screening thermogenic drugs. Scientific reports 9 34531447
2021 Down-Regulation of CIDEA Promoted Tumor Growth and Contributed to Cisplatin Resistance by Regulating the JNK-p21/Bad Signaling Pathways in Esophageal Squamous Cell Carcinoma. Frontiers in oncology 7 33614508
2025 Hu-lu-su-pian ameliorates hepatic steatosis by regulating CIDEA expression in AKT-driven MASLD mice. Frontiers in pharmacology 6 39958875
2024 Attenuation of brown adipocyte whitening in high-fat diet-induced obese rats: Effects of melatonin and β-hydroxybutyrate on Cidea, Fsp27 and MT1 expression. Diabetes, obesity & metabolism 6 39118207
2023 SUMO-specific protease 2 regulates lipid droplet size through ERRα-mediated CIDEA expression in adipocytes. Biochemical and biophysical research communications 3 37748256
2021 In silico interactions of statins with cell death-inducing DNA fragmentation factor-like effector A (CIDEA). Chemico-biological interactions 3 34022192
2017 Distribution and quantitative analysis of CIDEa and CIDEc in broiler chickens: accounting for differential fat deposition between strains. British poultry science 3 29219006
2025 Comparative effect of high intensity interval training and moderate intensity continuous training on metabolic improvements and regulation of Cidea and Cidec in obese C57BL/6 mice. PloS one 2 40305497
2019 CIDEA and CIDEC are regulated by CREB and are not induced during fasting in grass carp Ctenopharyngodon idella adipocytes. Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology 2 31028911
2025 Activation of Focal Adhesion Pathway by CIDEA as Key Regulatory Axis in Lipid Deposition in Goat Intramuscular Precursor Adipocytes. Animals : an open access journal from MDPI 1 40867704
2025 Cidea Targeting Protects Cochlear Hair Cells and Hearing Function From Drug- and Noise-Induced Damage. Advanced science (Weinheim, Baden-Wurttemberg, Germany) 1 41262044
2021 CIDEA expression in SAT from adolescent girls with obesity and unfavorable patterns of abdominal fat distribution. Obesity (Silver Spring, Md.) 1 34672413
2023 Use of CIDEA Reporter Mouse Model for Screening Thermogenic Fat-Activating Drugs. Methods in molecular biology (Clifton, N.J.) 0 37076679
2022 Exercise-induced beige adipogenesis of iWAT in Cidea reporter mice. BMB reports 0 35000670

Missed literature

Know a paper Affinage missed for CIDEA? Flag it for the maintainers and the community.

No submissions yet.