| 1987 |
SP1 encodes a 696 C-terminal amino acid protein whose sequence-specific DNA-binding activity localizes to the C-terminal 168 amino acids containing three contiguous Zn(II) finger motifs; purified SP1 requires Zn(II) for sequence-specific GC-box binding. |
cDNA cloning, bacterial expression of truncated fragments, DNA-binding assays, zinc chelation experiments |
Cell |
High |
3319186
|
| 1988 |
SP1 bears multiple O-linked N-acetylglucosamine (O-GlcNAc) monosaccharide residues; wheat germ agglutinin specifically inhibits the transcriptional activation but not the DNA-binding function of SP1, demonstrating that O-GlcNAc affects transcriptional activity. |
Lectin inhibition assay, in vitro transcription, glycosylation analysis |
Cell |
High |
3139301
|
| 1988 |
SP1 has distinct functional regions: zinc finger domain for sequence-specific DNA binding, a separate region regulating affinity of DNA binding, and at least two distinct segments contributing to transcriptional activation; bacterially expressed SP1 can stimulate RNA synthesis initiation in vitro. |
Deletion mutagenesis, bacterial expression, in vitro transcription assay |
Science |
High |
3059495
|
| 1989 |
SP1 contains glutamine-rich activation domains that can act synergistically; distally and proximally bound SP1 molecules interact via protein-protein contacts (demonstrated by glutaraldehyde cross-linking) to synergistically stimulate transcription, and a DNA-binding-deficient SP1 mutant retaining glutamine-rich domains can superactivate transcription by interacting with proximally bound SP1. |
Deletion mutagenesis, in vitro transcription, glutaraldehyde cross-linking, co-immunoprecipitation |
Cell |
High |
2512012
|
| 1990 |
A naturally occurring C-to-G mutation at -202 of the G-gamma globin gene increases the sequence's similarity to the SP1 consensus and confers 5–10-fold higher affinity for SP1 in vitro, demonstrating that SP1 binding affinity is sequence-context-dependent and correlates with elevated gamma globin expression in hereditary persistence of fetal hemoglobin. |
Electrophoretic mobility shift assay (EMSA), competitive binding with mutant oligonucleotides |
Molecular and cellular biology |
Medium |
1688466
|
| 1991 |
SP1 is ubiquitously expressed but shows at least 100-fold variation in mRNA and protein levels across cell types; highest levels are found in developing hematopoietic cells, fetal cells, and spermatids, suggesting a regulatory role in differentiation beyond housekeeping gene transcription. |
RNA analysis (Northern blot), immunohistochemical localization |
Molecular and cellular biology |
Medium |
2005904
|
| 1992 |
The retinoblastoma gene product (RB) positively regulates SP1 transcriptional activity in vivo; using a GAL4-SP1 fusion protein, RB was shown to directly enhance SP1-mediated transcription. |
GAL4-SP1 fusion co-transfection, reporter gene assay |
Molecular and cellular biology |
Medium |
1588949
|
| 1993 |
SP1 and YY1 physically interact, and this protein-protein interaction underlies synergistic enhancement of transcription from the adeno-associated virus P5 promoter initiator element when SP1 binding sites are present upstream. |
In vitro co-immunoprecipitation, in vitro transcription assay |
Nature |
High |
8003102
|
| 1993 |
BTEB and SP1 share nearly identical sequence specificities and binding modes for GC box DNA; purified BTEB has a dissociation constant of ~3×10⁻¹⁰ M for BTE binding, comparable to SP1. |
Orthophenanthroline-Cu footprinting, methylation interference, competitive gel mobility shift assay, Kd measurement |
Journal of biochemistry |
Medium |
8276776
|
| 1993 |
DNA-PK phosphorylates SP1 only when both SP1 and DNA-PK are co-localized on the same DNA molecule; DNA-PK is composed of Ku antigen (which directs DNA binding) and a ~350 kDa catalytic subunit, and DNA-PK requires DNA ends for activation. |
In vitro phosphorylation assay, DNA crosslinking, co-immunoprecipitation |
Cell |
High |
8422676
|
| 1994 |
RB stimulates SP1-mediated transcription by liberating SP1 from a ~20 kDa heat-labile negative regulator (Sp1-I); recombinant RB reverses Sp1-I-mediated inhibition of SP1-DNA binding, and Sp1-I is also an RB-associated protein. |
Mobility shift assay, preincubation with anti-RB antibodies, addition of recombinant RB, co-transfection with GAL4-SP1, identification of Sp1-I by protease sensitivity and size |
Molecular and cellular biology |
Medium |
8007947
|
| 1994 |
SP1 DNA-binding activity is redox-sensitive: H₂O₂ treatment of purified SP1 abolishes GC-box binding, which is fully restored by dithiothreitol, indicating that cysteine residues (likely in the zinc fingers) are critical for DNA binding. |
EMSA, DNase I footprinting, H₂O₂ treatment, DTT restoration, purified protein experiments |
European journal of biochemistry |
High |
7925470
|
| 1995 |
STAT1 and SP1 directly and selectively interact in primary cells (without overexpression), and co-occupation of contiguous STAT1 and SP1 DNA-binding sites is required for full interferon-gamma-induced activation of the ICAM-1 gene, revealing a physical basis for STAT1/SP1 transcriptional synergy. |
Co-immunoprecipitation in primary cells, DNA-protein binding assay, transfected reporter assay |
The Journal of biological chemistry |
High |
8530443
|
| 1995 |
TAFII55 (a human TFIID subunit) interacts with SP1 via the SP1 DNA-binding domain (distinct from the glutamine-rich activation domains that interact with Drosophila TAFII110), defining a separate co-activator interaction surface on SP1. |
cDNA cloning, co-immunoprecipitation, domain mapping with GST fusion proteins |
Science |
High |
7824954
|
| 1997 |
O-GlcNAc modification of the glutamine-rich transactivation domain (B-c) of SP1 inhibits protein-protein interactions with Drosophila TAF110 and holo-SP1 in vitro; mutation at the mapped glycosylation site permits transcriptional activation in HeLa cells, suggesting O-GlcNAc prevents untimely protein associations. |
Overexpression and glycosylation mapping, site-directed mutagenesis, in vitro interaction assay with TAF110 and holo-SP1, transfection reporter assay |
Molecular and cellular biology |
High |
9343410
|
| 1997 |
PKA phosphorylates SP1 directly in vitro and stimulates both its DNA-binding and trans-activating properties; PKA agonists and antagonists modulate SP1-dependent transcription in cells, establishing SP1 as a cAMP-responsive transcription factor. |
In vitro phosphorylation of recombinant SP1 by exogenous PKA, reporter gene assay in insect cells, PKA inhibitor/activator treatments |
The Journal of biological chemistry |
High |
9261118
|
| 1997 |
Estrogen receptor (ER) physically interacts with SP1 (demonstrated by immunoprecipitation), enhances SP1-DNA binding in a hormone-independent manner, and enables estrogen-dependent transactivation through GC-rich SP1-binding sites even without a canonical ERE, defining an ERE-independent estrogen signaling pathway via SP1. |
Gel mobility shift assay, co-immunoprecipitation, transient transfection with ER deletion mutants |
Molecular endocrinology |
High |
9328340
|
| 1998 |
RB physically associates with SP1 in all phases of the cell cycle (demonstrated by co-immunoprecipitation and gel-shift supershift), and this association increases SP1-mediated transcription of the dihydrofolate reductase gene through its proximal GC box. |
Co-immunoprecipitation, EMSA supershift, nuclear extract immunodepletion, transient transfection with RB and SP1 |
Oncogene |
High |
9591776
|
| 1999 |
ERK2 directly phosphorylates SP1, and this phosphorylation stimulates SP1 DNA-binding activity; the RAS-ERK pathway (blocked by MEK1 inhibitor PD98059) mediates EGF-inducible SP1 binding and gastrin promoter activation through a GC-rich element. |
In vitro phosphorylation with recombinant ERK2, gel mobility shift assay, MEK inhibitor experiments, co-transfection |
Biochemical and biophysical research communications |
High |
9918860
|
| 1999 |
HDAC1 directly binds to the C-terminal domain of SP1 and mediates transcriptional repression; this interaction is demonstrated by co-immunoprecipitation, and co-expression of E2F1 competes with HDAC1 for SP1 binding, relieving HDAC1-dependent repression. |
Co-immunoprecipitation, trichostatin A treatment, reporter gene assay, E2F1 competition experiment |
Molecular and cellular biology |
High |
10409740
|
| 1999 |
ARC (activator-recruited cofactor) directly interacts with SP1 and strongly enhances SP1-directed transcription on chromatin-assembled DNA templates in vitro, indicating ARC/DRIP is a key chromatin-selective co-activator for SP1. |
In vitro transcription on chromatin templates, co-activator interaction assay |
Nature |
High |
10235267
|
| 1999 |
RAS induces p21(Cip1/Waf1) transcription through GC-rich SP1/SP3-binding sites at -83 to -54 bp of the p21 promoter; mutation of both SP1 sites abolishes RAS-induced transcriptional activation, establishing SP1 as a downstream effector of RAS signaling for p21 induction. |
Conditional/transient Ras expression, promoter deletion/mutation analysis, EMSA |
Oncogene |
Medium |
10597223
|
| 2000 |
SP1 binds to an 80 bp neuronal specificity element in the tau promoter alongside AP-2, and mutation of any of the three protein-binding sites within this element decreases tau gene transcriptional activation; DNase I footprint identifies a third binding region in neuronal cells. |
DNase I footprinting, EMSA, site-directed mutagenesis, reporter gene assay |
Journal of neurochemistry |
Medium |
10987820
|
| 2000 |
Smad3 and Smad4 physically and directly interact with SP1 via their MH1 (Mad-Homology 1) domain; co-incubation of phosphorylated Smad3, Smad4, and SP1 in vitro enhances SP1 binding to the p21 proximal promoter; Smad proteins cooperate with SP1's glutamine-rich transactivation domain to activate p21 transcription. |
GST pull-down, in vitro binding with phosphorylated Smads, EMSA, Drosophila SL-2 cell reconstitution, GAL4 domain fusion assay |
The Journal of biological chemistry |
High |
10878024
|
| 2001 |
Cyclin A-CDK complexes physically interact with SP1 (co-immunoprecipitation) and phosphorylate SP1 in the N-terminal region in vitro and in vivo; cyclin A-CDK-mediated phosphorylation augments SP1 DNA-binding activity and SP1-dependent transcription, with the phosphorylation site mutation abrogating these effects. |
Modified DNA binding site selection/PCR, co-immunoprecipitation, in vitro and in vivo phosphorylation, site-directed mutagenesis, co-transfection reporter assay |
The EMBO journal |
High |
11598016
|
| 2001 |
c-Myc physically interacts with SP1 and SP3 (co-immunoprecipitation and GST pull-down); the central region of c-Myc interacts with the zinc finger domain of SP1, and this interaction may underlie c-Myc-mediated repression of the p21 promoter by sequestering SP1. |
Co-immunoprecipitation, GST pull-down, domain mapping |
Proceedings of the National Academy of Sciences of the United States of America |
High |
11274368
|
| 2001 |
RAR/RXR heterodimers physically interact with SP1, potentiate SP1 binding to GC box motifs, and enhance transactivation of GC-rich promoters lacking a canonical RARE; functional GC box hexanucleotide sequences are required for the RAR/RXR-SP1 interaction. |
Reporter assay, gel shift assay, Western blot, deletion/mutation analysis of GC box motifs |
Molecular endocrinology |
Medium |
11579201
|
| 2002 |
Mutant huntingtin interacts with SP1 and TAFII130, inhibits SP1 binding to DNA in postmortem HD patient brain tissue, and reduces dopamine D2 receptor gene transcription; co-expression of SP1 and TAFII130 reverses mutant huntingtin-mediated transcriptional inhibition and protects striatal neurons from huntingtin toxicity. |
Co-immunoprecipitation, EMSA with postmortem tissue, cell-culture transcription assay, neuronal protection assay |
Science |
High |
11988536
|
| 2002 |
A SNP (SNP309) in the MDM2 promoter increases the affinity of SP1 for this promoter element, resulting in higher MDM2 RNA and protein levels and consequent attenuation of the p53 pathway; this links SP1 binding affinity directly to cancer predisposition. |
Reporter gene assay, EMSA with wild-type vs. SNP309 oligonucleotides, Western blot, clinical association |
Cell |
High |
15550242
|
| 2003 |
BRCA1 interacts directly with SP1 (co-immunoprecipitation), mapping the SP1-binding domain to BRCA1 residues 260–802; this interaction prevents SP1 from binding the IGF-IR promoter and underlies BRCA1-mediated repression of IGF-IR transcription. |
Co-immunoprecipitation, EMSA, GST-tagged BRCA1 fragment binding assay, reporter assay |
FEBS letters |
Medium |
12706836
|
| 2004 |
SP1 and SP3 are organized into distinct, non-overlapping intranuclear domains that infrequently associate with sites of active transcription; both SP1 and SP3 associate with HDAC1, HDAC2, and ERα in MCF-7 cells, but ChIP/re-ChIP shows they do not co-occupy the same TFF1 promoter, demonstrating functional non-equivalence. |
Indirect immunofluorescence with image deconvolution, ChIP and re-ChIP assay, nuclear fractionation |
Molecular biology of the cell |
Medium |
15987735
|
| 2005 |
Smad3 phosphorylated constitutively in scleroderma fibroblasts interacts with both SP1 and the co-activator p300 (demonstrated by immunoprecipitation), enhancing COL1A2 collagen gene promoter activity; combined overexpression of Smad3 and SP1 synergistically activates the TGF-β response in normal fibroblasts. |
Immunoprecipitation, CAT reporter assay, immunoblotting |
Rheumatology |
Medium |
16319104
|
| 2006 |
SP1 overexpression induces apoptosis in all cell types tested; apoptotic pathways are cell-type specific, and the DNA-binding domain of SP1 is required for SP1-induced apoptosis (demonstrated with truncated SP1 lacking the DNA-binding domain). |
Retroviral and inducible overexpression, flow cytometry for apoptosis, truncation mutagenesis |
Oncogene |
Medium |
16715126
|
| 2006 |
Src oncogene induces MMP-2 expression via the ERK/SP1 signaling pathway; activated ERK enhances SP1 binding to the -91/-84 Sp1 site in the MMP-2 promoter, and dominant-negative ERK2 or MEK inhibitor PD98059 reduces SP1 DNA-binding activity and MMP-2 promoter activity. |
RT-PCR, promoter deletion/mutation analysis, EMSA, MEK/ERK inhibitor experiments, dominant-negative ERK2 |
Journal of cellular physiology |
Medium |
16453304
|
| 2007 |
Phosphorylation of SP1 is the major driving force for coupled proteolytic processing, desumoylation, and degradation; Serine-7 enhances ubiquitinylation, Serine-59 regulates N-terminal cleavage (relieving SUMO-1 repression at Lys-16), and CyclinA/Cdk2-mediated phosphorylation of Ser-59 upregulates SP1-dependent transcription; SP1 contains a functional phosphorylation-dependent β-TrCP binding motif. |
Site-directed mutagenesis, in vitro and in vivo ubiquitination/sumoylation assays, kinase inhibitors, reporter gene assay |
Cell cycle |
Medium |
18239466
|
| 2008 |
O-GlcNAc within the second serine/threonine-rich region of SP1 interrupts the physical interaction between SP1 and Oct1, inhibiting cooperative activation of the U2 snRNA gene by SP1 and Oct1. |
Co-immunoprecipitation, reporter gene assay, O-GlcNAc site mapping |
FEBS letters |
Medium |
19070619
|
| 2009 |
O-GlcNAc on SP1 inhibits the physical interaction between SP1 and Elf-1 transcription factors, negatively regulating transcription of the Pem oncofetal protein gene. |
Co-immunoprecipitation, reporter gene assay |
Biochemical and biophysical research communications |
Low |
19285002
|
| 2009 |
SP1 overexpression induces apoptosis through a p53-dependent pathway; wild-type p53 accumulates and activates apoptotic signaling in response to SP1 overexpression (during mitosis, affecting chromatin packaging), whereas p53-null or p53-mutant cells are protected; p53 knockdown rescues SP1-overexpression-induced apoptosis. |
Adenoviral GFP-SP1 expression, flow cytometry (sub-G1, caspase-3 cleavage, annexin-V), p53 shRNA knockdown |
International journal of cancer |
Medium |
19588484
|
| 2009 |
HSP90 interacts with SP1 during mitosis and maintains SP1 stability; disruption of HSP90 (by geldanamycin or shRNA) leads to SP1 degradation via the ubiquitin-proteasome pathway, which is prevented when SP1 is phosphorylated at Thr278/739 by JNK-1; HSP90-SP1 interaction thereby regulates SP1-dependent gene expression (p21 and 12(S)-lipoxygenase). |
Co-immunoprecipitation, geldanamycin treatment, shRNA knockdown, site-directed mutagenesis, ubiquitination assay, reporter gene assay |
Journal of molecular biology |
Medium |
19245816
|
| 2010 |
HDAC1 overexpression induces cellular senescence through a novel SP1/PP2A/pRb pathway: HDAC1 increases SP1 deacetylation, enhances SP1-p300 interaction, and the SP1/p300 complex binds the PP2Ac promoter to induce PP2Ac expression, leading to hypophosphorylation of pRb and cell cycle arrest. |
Tet-off inducible system, co-immunoprecipitation, ChIP, reporter gene assay, Western blotting |
Biochemical and biophysical research communications |
Medium |
21420382
|
| 2010 |
SP1 phosphorylation by PKC-ERK at Thr453 and Thr739 is required for MBP gene transcription in differentiating oligodendrocytes; mutation of these residues decreases MBP transcriptional activity, and PKC regulates SP1 phosphorylation only in differentiating but not precursor cells. |
Site-directed mutagenesis, kinase inhibitor experiments (PD98059, PMA), ChIP, reporter gene assay |
Journal of neuroscience research |
Medium |
20882567
|
| 2011 |
Sumoylated SP1 is targeted for proteasomal degradation by the ubiquitin E3 ligase RNF4; RNF4 binds to sumoylated SP1 (at Lys16) and the C-terminus of SP1; JNK1-mediated phosphorylation of SP1 at Thr739 during mitosis disrupts the SP1-RNF4 interaction, protecting SP1 from degradation and maintaining its levels during cell cycle progression. |
In vitro and in vivo sumoylation/ubiquitination assays, co-immunoprecipitation, domain mapping, site-directed mutagenesis |
Journal of molecular biology |
High |
21983342
|
| 2014 |
SUMO2 negatively regulates SP1 by sumoylating it at K683 (attenuating DNA binding) and at K16 (increasing turnover); SUMO2 also interferes with SP1-p300 coactivator interaction and recruits SP3 as a repressor to β-crystallin promoters; conversely, SUMO1 positively regulates SP1 and forms complexes with it during lens development. |
In vitro sumoylation assay, co-immunoprecipitation, ChIP, overexpression/knockdown in lens cells, site-directed mutagenesis |
Proceedings of the National Academy of Sciences of the United States of America |
High |
24706897
|
| 2018 |
Caspase-3 cleaves SP1 at aspartic acid 183 (a novel caspase cleavage site) during apoptosis induced by DNA damage or TRAIL; the resulting 70 kDa C-terminal fragment (Sp1-70C, aa 184–785) retains transcriptional activity and promotes apoptosis when overexpressed; the D183A mutation confers resistance to cleavage and reduces apoptosis. |
In vitro caspase cleavage assay, site-directed mutagenesis (D183A), ectopic expression of cleavage product, apoptosis assays |
Apoptosis |
High |
29236199
|
| 2019 |
SIRT6 binds to the zinc finger DNA-binding domain of SP1 and represses SP1 transcriptional activity, independently of SIRT6's deacetylase activity; SIRT6 deficiency increases SP1 occupancy at mTOR signaling gene promoters, activating mTOR and increasing global protein synthesis. |
Co-immunoprecipitation (SIRT6-SP1 interaction), ChIP (SP1 occupancy at promoters), pharmacological inhibition of mTOR/SP1, muscle-specific SIRT6 KO mice |
Nucleic acids research |
High |
31372634
|
| 2019 |
SP1 directly binds to the Notch2 gene promoter and governs FOXL2+ pregranulosa cell recruitment and maintenance during primordial folliculogenesis; SP1 knockdown specifically in pregranulosa cells suppresses nest breakdown, oocyte apoptosis, and primordial follicle formation in mice. |
Lgr5-KI reporter mouse model, FOXL2+ cell-specific SP1 knockdown, ChIP for SP1 on Notch2 promoter |
Journal of molecular cell biology |
Medium |
31282930
|
| 2021 |
USP39 deubiquitinates SP1 protein, stabilizes it, and prolongs its half-life; knockdown of USP39 decreases SP1 protein levels and promotes apoptosis and cell cycle arrest, effects reversed by forced SP1 expression. |
Co-immunoprecipitation, ubiquitination assay, protein half-life measurement, USP39 knockdown/SP1 rescue experiments |
Cellular signalling |
Medium |
34197957
|
| 2021 |
ZRANB1 deubiquitinase directly binds SP1 and stabilizes it by deubiquitination; ZRANB1 knockdown decreases SP1 and downstream LOXL2 expression, and SP1 overexpression rescues the suppression of HCC growth and metastasis caused by ZRANB1 knockdown. |
Co-immunoprecipitation, deubiquitination assay, SP1 overexpression rescue, in vitro and in vivo functional assays |
American journal of cancer research |
Medium |
34765294
|
| 2021 |
TRRAP HAT cofactor is required for SP1 binding at target gene promoters (especially microtubule dynamics genes); TRRAP deletion impairs SP1-dependent transcription, and ectopic expression of Stathmin3/4 (SP1/TRRAP targets) ameliorates TRRAP-deficient neuron defects, linking TRRAP-HAT-SP1 to microtubule dynamics and neuroprotection. |
Integrated transcriptomics, ChIP (SP1 binding at promoters), proteomics, conditional KO (Purkinje neurons), ectopic rescue expression |
eLife |
High |
33594975
|
| 2021 |
DNA damage-induced ATM-mediated phosphorylation of SP1 at serine 101 promotes sumoylation of SP1 at lysine 16, which then recruits RNF4 to cause proteasomal degradation of SP1 and drive cellular senescence; SP1 S101A (ATM phospho-null) or K16R (sumo-null) mutations prevent this degradation and reduce senescence markers. |
Site-directed mutagenesis, DNA damage induction, ATM inhibition, senescence marker assays |
GeroScience |
Medium |
34550526
|
| 2022 |
HDAC2 regulates M2-like tumor-associated macrophage phenotype via acetylation of histone H3 and transcription factor SP1; suppression of HDAC2 in macrophages alters the HDAC2-SP1 axis to switch macrophage polarization from M2-like to M1-like, reducing tumor growth and angiogenesis. |
HDAC2 KO in myeloid cells (4 murine lung cancer models), HDAC2 inhibition, co-culture systems, pharmacological class I HDAC inhibition |
Cancer research |
Medium |
37205635
|
| 2022 |
CVB3 infection induces nuclear translocation of SP1, which then binds the TFRC promoter to upregulate TFRC transcription, promoting ferroptosis via iron overload and lipid peroxide accumulation; the SP1/TFRC/Fe axis is required for CVB3-induced ferroptosis. |
Time-course CVB3 infection model, ChIP (SP1 binding to TFRC promoter), TFRC knockdown, cellular ferroptosis markers |
Cell death & disease |
Medium |
35821227
|
| 2022 |
S-sulfhydration of SP1 by hydrogen sulfide (H₂S) inhibits SP1 transcriptional activity at the HDAC6 promoter, leading to reduced HDAC6 expression, decreased MyD88 deacetylation, and suppression of NF-κB-mediated inflammation in adjuvant-induced arthritis. |
In vivo arthritis model, S-sulfhydration assay, SP1 overexpression/knockdown, ChIP (SP1 at HDAC6 promoter), HDAC6 reporter assay |
Antioxidants |
Medium |
35453416
|
| 2023 |
SIRPA phosphorylates SP1 at threonine 278 (Thr278) through ERK activation, protecting SP1 from proteasomal degradation; SP1 in turn activates SLC7A3 expression by binding its promoter, increasing arginine uptake; arginine itself further stabilizes SP1 in an ERK-independent manner, creating a 'SP1 stabilization circle' that promotes osteosarcoma metastasis. |
Phosphorylation assay, co-immunoprecipitation, ChIP (SP1 at SLC7A3 promoter), site-directed mutagenesis, xenograft mouse model |
Cancer letters |
Medium |
37769797
|
| 2024 |
SP1 directly binds the GSDME promoter at the -36 to -28 site and promotes GSDME gene transcription, thereby enhancing caspase-3-mediated pyroptosis in response to chemotherapy drugs; SP1 knockdown or inhibition suppresses GSDME expression and reduces pyroptosis; this regulation synergizes with STAT3 activity and antagonizes DNA methylation. |
ChIP (SP1 on GSDME promoter), SP1 knockdown/inhibition, pyroptosis assays, STAT3 co-regulation analysis |
Cell death & disease |
Medium |
38238307
|