Journal: International journal of molecular medicine

Article Title: Astragaloside IV attenuates the H2O2-induced apoptosis of neuronal cells by inhibiting α-synuclein expression via the p38 MAPK pathway.

doi: 10.3892/ijmm.2017.3157

Figure Lengend Snippet: Figure 5. Astragaloside IV (AS-IV) decreases the hydrogen peroxide (H2O2)-induced phosphorylation of p38, but has no effect on the phosphorylation of c-Jun kinase (JNK) or extracellular signal-regulated kinase (ERK). Western blot analysis showing the levels of (A) phosphorylated p38, (B) phosphorylated ERK1/2 and (C) phosphorylated JNK in the H2O2-exposed groups. (A) Effects of AS-IV (200 µmol/l) pre-treatment on the levels of phosphorylated p38 compared with those of the H2O2 group. The data are the means ± SEM (n=3). **P<0.01 vs. control (untreated cells); #P<0.05 vs. H2O2 (300 µmol/l); ##P<0.01 vs. H2O2 (300 µmol/l).

Article Snippet: The Annexin V-fluorescein isothiocyanate (FITC) apoptosis detection kit was obtained from Keygen Biotech co., ltd. (nanjing, china). fetal bovine serum (fBS) and Dulbecco's modified Eagle's medium/F12 (DMEM/f12) were both purchased from gibco (grand island, nY, uSa). anti-α-synuclein antibody (#ab138501) was purchased from epitomics (Burlingame, ca, uSa). anti-β-actin (#3700), antiBcl-2 (#15071) and anti-Bax (#5023) monoclonal antibodies were all purchased from cell Signalling technology, inc. (Beverly, ma, uSa). anti-p38 mitogen-activated protein kinase (maPK; sc-7972), anti-p-p38 (sc-17852-r), anti-p-jnK (sc-293136), antierK1/2 (sc-514302), anti-p-erK1/2 (sc-16981-r) and anti-tH (sc-7847) mono clonal antibodies were all purchased from Santa cruz Biotechnology, inc. (Santa cruz, ca, uSa). all of the other reagents were of analytical grade.

Techniques: Phospho-proteomics, Western Blot, Control

Journal: International journal of molecular medicine

Article Title: Astragaloside IV attenuates the H2O2-induced apoptosis of neuronal cells by inhibiting α-synuclein expression via the p38 MAPK pathway.

doi: 10.3892/ijmm.2017.3157

Figure Lengend Snippet: Figure 6. Chemical inhibitor targeting p38 kinase (SB203580) inhibits the expression of α-synuclein (α-syn) and increases the expression of tyrosine hydroxy- lase (TH) in SH-SY5Y cells. (A) Incubation with SB203580 in the SH-SY5Y cells decreased the expression of α-syn compared with the hydrogen peroxide (H2O2) group as shown by western blot analysis. (B) Results of the double immunofluorescence assay in SH-SY5Y cells. The data are the means ± SEM (n=3). **P<0.01 vs. control (untreated cells); #P<0.05 vs. H2O2 (300 µmol/l).

Article Snippet: The Annexin V-fluorescein isothiocyanate (FITC) apoptosis detection kit was obtained from Keygen Biotech co., ltd. (nanjing, china). fetal bovine serum (fBS) and Dulbecco's modified Eagle's medium/F12 (DMEM/f12) were both purchased from gibco (grand island, nY, uSa). anti-α-synuclein antibody (#ab138501) was purchased from epitomics (Burlingame, ca, uSa). anti-β-actin (#3700), antiBcl-2 (#15071) and anti-Bax (#5023) monoclonal antibodies were all purchased from cell Signalling technology, inc. (Beverly, ma, uSa). anti-p38 mitogen-activated protein kinase (maPK; sc-7972), anti-p-p38 (sc-17852-r), anti-p-jnK (sc-293136), antierK1/2 (sc-514302), anti-p-erK1/2 (sc-16981-r) and anti-tH (sc-7847) mono clonal antibodies were all purchased from Santa cruz Biotechnology, inc. (Santa cruz, ca, uSa). all of the other reagents were of analytical grade.

Techniques: Expressing, Incubation, Western Blot, Control

Journal: Molecular medicine reports

Article Title: Ligustrazine attenuates the platelet-derived growth factor-BB-induced proliferation and migration of vascular smooth muscle cells by interrupting extracellular signal-regulated kinase and P38 mitogen-activated protein kinase pathways.

doi: 10.3892/mmr.2015.3383

Figure Lengend Snippet: Figure 5. Ligustrazine suppresses PDGF‑BB‑stimulated activation of ERK and p38 MAPK signaling in VSMCs. Western blotting was used to determine the activity of ERK and p38 MAPK signaling in each group. Control VSMCs were cultured for 48 h without any treatment. PDGF‑BB VSMCs were treated only with PDGF‑BB for 48 h. PDGF‑BB+ligustrazine VSMCs were treated with ligustrazine and PDGF‑BB for 48 h. **P<0.01, vs. control. VSMC, vascular smooth muscle cell; PDGF, platelet‑derived growth factor; ERK, extracellular signal‑related kinase; MAPK, mitogen‑activated protein kinase.

Article Snippet: Mouse monoclonal anti-desmin (1:100; sc-365130), anti-smoothelin (1:50; sc-376902), anti-phosphorylated (phosph)-ERK (1:100; sc-136521), anti-total ERK (1:50; sc-135900), anti-phospho-p38 (1:50; sc-81621), anti-total p38 (1:100; sc-7973), anti-cyclin-dependent kinase (CDK)2 (1:100; sc-6248), anti-CDK4 (1:50; sc-23896), anti-cyclin D1 (1:50; sc-450), anti-cyclin E (1:100; sc-48420) and anti-glyceraldehyde 3-phosphate dehy drogenase (GAPDH; 1:50; sc-365062) primary antibodies as well as rabbit anti-mouse horseradish peroxidase-conjugated secondary antibodies (1:5,000; sc-358914) were obtained from Santa Cruz Biotechnology, Inc., (Santa Cruz, CA, USA).

Techniques: Activation Assay, Western Blot, Activity Assay, Control, Cell Culture

Journal: Oncotarget

Article Title: The oncogenic receptor ErbB2 modulates gemcitabine and irinotecan/SN-38 chemoresistance of human pancreatic cancer cells via hCNT1 transporter and multidrug-resistance associated protein MRP-2.

doi: 10.18632/oncotarget.3414

Figure Lengend Snippet: Figure 5: Identification of the signaling pathways involved in resistance to SN-38 in ErbB2-KD cells and MRP2 expression regulation. A. Western blots were performed to analyze the expression and phosphorylation of ERK1/2, JNK, p38, NF-κB, Akt and β-actin in CAPAN-2 NT and ErbB2-KD cells. The density of each marker was measured and phosphorylated/constitutive or protein/β-actin ratio was determined and represented as histograms. Expression in NT cells was arbitrarily set to 1. Three independent experiments were performed. B. Cell survival rate was measured following Erk1/2, JNK and NF-κB inhibition in CAPAN-1 and CAPAN-2 cells using specific siRNA during 48 h before SN-38 treatment. C. CAPAN-1 and CAPAN-2 cells were transiently transfected with ErbB2, Erk1/2, JNK, NF-κB or control siRNA for 48 h. qPCR were performed to analyze the expression of MRP2.

Article Snippet: Transient inhibitions of ABCG2 (sc-41151), MRP1 (sc-35962) MRP2 (sc-35963), Akt (sc-43609) and p38 (sc-29433) were performed using a pool of siRNA designed by Santa Cruz Biotechnology following cell transfection with Effectene® (Qiagen) as described by the manufacturer.

Techniques: Protein-Protein interactions, Expressing, Western Blot, Phospho-proteomics, Marker, Inhibition, Transfection, Control

Journal: The Journal of biological chemistry

Article Title: Knocking out p38α+p38β+p38γ is required to abort the myogenic program in C2C12 myoblasts and to impose uncontrolled proliferation.

doi: 10.1016/j.jbc.2025.108281

Figure Lengend Snippet: Figure 3. A pan p38 inhibitor, as well as a α β s

Article Snippet: C2p38α-/- cells were produced using a p38α CRISPR/Cas9 KO plasmid (Santa Cruz, sc-424051).

Techniques:

Journal: Stem cells (Dayton, Ohio)

Article Title: DAPK1 Interacts with the p38 Isoform MAPK14, Preventing Its Nuclear Translocation and Stimulation of Bone Marrow Adipogenesis.

doi: 10.1093/stmcls/sxac013

Figure Lengend Snippet: Figure 4. The p38 pathway is responsible for DAPK1-related MSC adipogenic differentiation. Intergroup differential volcanic map (A) and the results of GO analysis (B) and KEGG pathway analysis (C) of RNA sequencing data from DAPK1-knockdown and the control MSCs. (D) GSEA identified p38 MAPK pathway from genes of DAPK1-knockdown MSCs and the control MSCs. Normalized enrichment score (NES) and nominal P-value (NOM p-val) are shown. The right panel shows the heat map of gene array in DAPK1-knockdown MSCs (S3) compared with the control (NC) related to p38 MAPK pathway. n = 2 MSCs per group. (E) Pathway inhibitors were used to detect the effects of the enriched pathways by GSEA on DAPK1-related MSC adipogenic differentiation on day 14. Scale bar = 200 μm. (F) Lipid accumulation shown by the ORO staining results in panel E was quantified. (G) The mRNA levels of PPARγ, C/EBPα and FABP4 in DAPK1-knockdown MSCs treated with or without SB203580 in adipogenic differentiation medium for 7 days. (H) Left showed the immunoblot results of activation of major signaling pathways in the DAPK1 knockdown and DAPK1-overexpressing MSCS in adipogenic differentiation medium for 7 days. Right showed the quantification results of immunoblot. (I) Immunoblots for MAPK14, MAPK11, MAPK12, MAPK13, p-p38-T (total p-p38), and GAPDH after IP from MSCs treated with S1 (Si-DAPK1) or the NC as a control with nonspecific IgG (IgG) and anti-p-p38 as indicated. Input: 20 µg of protein of the extracts without IP was loaded. (J) ORO staining and quantification to detect lipid accumulation in DAPK1-knockdown MSCs treated with or without the MAPK14 inhibitor MAPK-IN-1in adipogenic differentiation medium for 14 days. Human MSCs were used in the above tests. Scale bar = 200 μm. Data are presented as the means ± SEMs. *P < .05, **P < .01, ***P < .001. n = 3 independent experiments with 3 different MSCs per group.

Article Snippet: Erlotinib (EGFR pathway inhibitor, HY-50896, MCE), capivasertib (FOXO pathway inhibitor, HY-15431, MCE), SB203580 (p38 MAPK pathway inhibitor, HY-10256, MCE), MAPK-IN-1 (MAPK14 inhibitor, HY-18874, MCE), and MAPK13-IN-1 (MAPK13 inhibitor, HY-18850, MCE) were used in our study.

Techniques: RNA Sequencing, Knockdown, Control, Staining, Western Blot, Activation Assay, Protein-Protein interactions

Journal: Stem cells (Dayton, Ohio)

Article Title: DAPK1 Interacts with the p38 Isoform MAPK14, Preventing Its Nuclear Translocation and Stimulation of Bone Marrow Adipogenesis.

doi: 10.1093/stmcls/sxac013

Figure Lengend Snippet: Figure 5. DAPK1 interacts with MAPK14 in vitro and in vivo. (A) Immunoprecipitates obtained from human MSC extracts (5 µg of protein) with nonspecific IgG or antibody against DAPK1 were stained with Coomassie Blue. (B) The peptide sequences of the DAPK1 and MAPK14 proteins were detected in the co-IP complex. (C) Co-IP of 500 µg of protein from human MSCs with nonspecific IgG (IgG), anti-DAPK1, or anti-MAPK14 as indicated. Input: Twenty micrograms of protein extract without IP was loaded. (D) Colocalization of DAPK1 and MAPK14 in human MSCs. Scale bar = 50 μm. 293T cells transfected with Flag-tagged DAPK1 and HA-tagged MAPK14 were subjected to immunoprecipitation and immunoblot analysis (E) and immunofluorescence doubling staining (F) with the indicated antibodies. Scale bar = 20 μm.

Article Snippet: Erlotinib (EGFR pathway inhibitor, HY-50896, MCE), capivasertib (FOXO pathway inhibitor, HY-15431, MCE), SB203580 (p38 MAPK pathway inhibitor, HY-10256, MCE), MAPK-IN-1 (MAPK14 inhibitor, HY-18874, MCE), and MAPK13-IN-1 (MAPK13 inhibitor, HY-18850, MCE) were used in our study.

Techniques: In Vitro, In Vivo, Staining, Co-Immunoprecipitation Assay, Transfection, Immunoprecipitation, Western Blot, Immunofluorescence

Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research

Article Title: Puerarin Attenuates Cardiac Hypertrophy Partly Through Increasing Mir-15b/195 Expression and Suppressing Non-Canonical Transforming Growth Factor Beta (Tgfβ) Signal Pathway

doi: 10.12659/MSM.895877

Figure Lengend Snippet: Primer sequences for qRT-PCR.

Article Snippet: The ready-to-use Smad2/3 and Smad4 shRNA lentiviral particles (sc-37239-V and sc-29485-V) and p38 shRNA lentiviral particles (sc-29434-V) were purchased from Santa Cruz Biotech (Santa Cruz, CA, USA).

Techniques:

Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research

Article Title: Puerarin Attenuates Cardiac Hypertrophy Partly Through Increasing Mir-15b/195 Expression and Suppressing Non-Canonical Transforming Growth Factor Beta (Tgfβ) Signal Pathway

doi: 10.12659/MSM.895877

Figure Lengend Snippet: Puerarin suppresses the canonical and non-canonical TGFβ signal pathways partially through miR-15b and miR-195. ( A ) QRT-PCR analysis of the TGFβ receptors (TGFBR1, TGFBR2 and TGFBR3), canonical (Smad2, Smad3, Smad4, and Smad7) and non-canonical TGFβ signal members (TAK1 and p38) in the ventricular tissues in the sham, Ang II-infused, and puerarin groups. ( B ) Western blot analysis of Smad2, Smad3, Smad4, Smad7, TAK1, and p38 expression in the groups indicated in Figure A. ( C ) QRT-PCR analysis of miR-15 family expression in the primary cardiomyocytes after treatment with puerarin. ( D, E ) QRT-PCR analysis of miR-15b and miR-195 expression in the primary cardiomyocytes after infection with the pLV-miR-15b and pLV-miR-195 expression ( D ) or the pLV-miR-15b and pLV-miR-195 locker lentiviral particles ( E ). ( F, G, H ) QRT-PCR analysis Smad2, Smad3, Smad4, Smad7, and p38 expression in the primary cardiomyocytes with miR-15b or miR-195 overexpression ( F ) or miR-15b or miR-195 knockdown ( G ) or after treatment with puerarin with or without knockdown of endogenous miR-15b and miR-195 ( H ). * Comparison with NC group; # comparison with puerarin group. * and # p<0.05, ** and ## p<0.01, *** and ### p<0.001.

Article Snippet: The ready-to-use Smad2/3 and Smad4 shRNA lentiviral particles (sc-37239-V and sc-29485-V) and p38 shRNA lentiviral particles (sc-29434-V) were purchased from Santa Cruz Biotech (Santa Cruz, CA, USA).

Techniques: Quantitative RT-PCR, Western Blot, Expressing, Infection, Over Expression, Knockdown, Comparison

Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research

Article Title: Puerarin Attenuates Cardiac Hypertrophy Partly Through Increasing Mir-15b/195 Expression and Suppressing Non-Canonical Transforming Growth Factor Beta (Tgfβ) Signal Pathway

doi: 10.12659/MSM.895877

Figure Lengend Snippet: MiR-15b attenuates cardiac hypertrophy through the non-canonical TGFβ pathway. ( A, B ) QRT-PCR analysis of mRNA expression of ANP, BNP, and β-MHC in the primary cardiomyocytes after knockdown of endogenous miR-15b ( A ) or knockdown of endogenous TAK1 or p38 separately ( B ). ( C–H ) Measurement of cell surface area ( C, D ), the rate of protein synthesis ( E, F ), and the total protein content ( G, H ) in the cardiomyocytes after knockdown of endogenous miR-15b ( C, E, G ) or knockdown of endogenous TAK1 or p38 separately ( D, F, H ). * Comparison with shRNA NC group; # comparison with Ang II+ shRNA NC group. * and # p<0.05, ** and ## p<0.01, *** and ### p<0.001.

Article Snippet: The ready-to-use Smad2/3 and Smad4 shRNA lentiviral particles (sc-37239-V and sc-29485-V) and p38 shRNA lentiviral particles (sc-29434-V) were purchased from Santa Cruz Biotech (Santa Cruz, CA, USA).

Techniques: Quantitative RT-PCR, Expressing, Knockdown, Comparison, shRNA

Journal: iScience

Article Title: EZH2 T367 phosphorylation activates p38 signaling through lysine methylation to promote breast cancer progression

doi: 10.1016/j.isci.2022.104827

Figure Lengend Snippet: EZH2 methylates p38α, and EZH2 phosphorylation at T367 is critical for p38α methylation and phosphorylation in TNBC (A) Co-immunoprecipitation (co-IP) and immunoblots of methylated p38α in a panel of breast cancer cells. EZH2 shRNA knockdown decreased methylated p38α. (B) Lysine N-methyltransferase (KMTase) activity assay in whole-cell lysates of MDA-MB-231 cells at the indicated conditions. KMTase activity was assessed using 0.1 mg/mL of human recombinant p38α and measuring S-adenosyl homocysteine (SAH) production detected by bioluminescence. shEZH2 and EPZ significantly reduced methylated p38α compared to control (lanes 1–3), which was rescued by WT-EZH2 (lane 4). EPZ reduced methylated p38α compared to WT-EZH2 (lanes 4–5). Bars depict mean ± SEM, ∗p ≤ 0.05. (C) KMTase activity assay in whole-cell lysates of T4 and Vari068 patient-derived TNBC cells control and treated with EPZ as in (B). Bars show mean ± SEM, ∗p ≤ 0.05. (D) IP and immunoblots of methylated p38α in MDA-MB-231 cells transduced with scrambled shRNA (control) or 3′ UTR EZH2-targeting shRNA (shEZH2) rescued with Myc-tagged WT-EZH2, T367A-EZH2, or vector (pBabe). (E) Immunoblot of cells in (D).

Article Snippet: Recombinant GST-p38α , BPS Bioscience , Cat #40070.

Techniques: Methylation, Immunoprecipitation, Co-Immunoprecipitation Assay, Western Blot, shRNA, Activity Assay, Recombinant, Derivative Assay, Transduction, Plasmid Preparation

Journal: iScience

Article Title: EZH2 T367 phosphorylation activates p38 signaling through lysine methylation to promote breast cancer progression

doi: 10.1016/j.isci.2022.104827

Figure Lengend Snippet: EZH2 methylates p38α protein at lysine 139 and lysine 165 leading to enhanced p38α protein stability (A) Schematic representation of p38 protein indicating the position of its functional domains and methylation sites (red dots). The amino acid positions of each domain are indicated below the structures. The table summarizes the unique sites of methylation identified by LC-MS-MS analyses of methylated proteins. Recombinant histone H3 and GST-p38α were incubated with or without recombinant PRC2 complex (EZH2/EED/SUZ12/RbAp48/AEBP2) and S-adenosyl methionine methyl donor in sodium phosphate-buffered HMTase buffer solution for one hour at 37°C. Samples were subsequently run on a gel and digested in-gel using trypsin or Arg-C and analyzed for monomethylation, dimethylation, and trimethylation by LC-MS/MS. The presence of methylation was confirmed by β- and γ-ion. (B) Pulse-chase analysis of MDA-MB-231 shVector and shEZH2 treated with 100 μg/mL of cycloheximide (CHX) at the indicated time points. Cell extracts were immunoblotted with anti-EZH2 and anti-p38α. α-Tubulin was used as the loading control. (C) Pulse-chase analysis for MDA-MB-231 treated with vehicle (control) or GSK-343 (1 μM) for 48 h and treated with 100 μg/mL of cycloheximide (CHX) at the indicated time points. Cell extracts were immunoblotted with anti-EZH2 and anti-p38α. α-Tubulin was used as the loading control. (D) HA-tagged p38α wild-type and p38α mutants K139A, K165A, and K139A/K165A were transduced into MDA-MB-231 cells and subjected to IP and WB using anti-p38α and anti-pan methyl-K antibody. Actin was used as the loading control. (E) CHX pulse-chase assay of cells in (D). (F) Ubiquitination assay. Indicated cells were treated with the proteasome inhibitor MG-132 (50 μM) for 5 h or vehicle. Whole-cell extracts were subsequently immunoprecipitated by anti-magnetics A beads followed by immunoblot using antibodies against ubiquitin and p38α. (G) Invasion assay of MDA-MB-231 cells transduced with HA-tagged p38α wild-type and p38α mutants K139A, K165A, and K139A/K165A. Scale bar, 10 μm. Bars show mean ± SEM, ∗p ≤ 0.05.

Article Snippet: Recombinant GST-p38α , BPS Bioscience , Cat #40070.

Techniques: Functional Assay, Methylation, Liquid Chromatography with Mass Spectroscopy, Recombinant, Incubation, Pulse Chase, Ubiquitin Assay, Immunoprecipitation, Western Blot, Invasion Assay, Transduction

Journal: iScience

Article Title: EZH2 T367 phosphorylation activates p38 signaling through lysine methylation to promote breast cancer progression

doi: 10.1016/j.isci.2022.104827

Figure Lengend Snippet: Combined targeting of EZH2 and p38 enzymatic activities reduces primary breast cancer growth and metastasis (A) Primary tumor growth curves of NOD/SCID mice orthotopically implanted with MDA-MB-231 cells. When primary tumors reached 100 mm 3 , mice were treated intraperitoneally with EPZ-6438 (10 mg/kg/day), SB202190 (p38i, 1 mg/kg/day), combination, or control (4% DMSO-30% PEG 300-5% Tween 80), 5 days/week for 56 days (n = 10/group). Primary tumor growth as assessed by caliper measurements, shown as mean ± SEM. (B) Quantification of tumor volume at day 56 shown as mean ± SEM. (C) MDA-MB-231 cells were injected intracardially in nude mice (n = 10/group) and treated as in (A), for 3 weeks. Bars show the number of metastases per mouse in each group on day 21 after heart inoculation ±SEM. (D) Representative H&E-stained sections of lung metastases. Magnification 600x. Scale bar 50 μm. (E) Co-immunoprecipitation and immunoblots of methylated p38α in whole-cell lysates of primary MDA-MB-231 xenograft tumors derived from (A). (F) Immunoblots for the indicated proteins in lysates obtained from the MDA-MB-231 primary orthotopic xenografts in (A). For A-C, ∗p ≤ 0.05; ∗∗p ≤ 0.01; ∗∗∗p ≤ 0.005; ∗∗∗∗p ≤ 0.0001.

Article Snippet: Recombinant GST-p38α , BPS Bioscience , Cat #40070.

Techniques: Injection, Staining, Immunoprecipitation, Western Blot, Methylation, Derivative Assay

Journal: iScience

Article Title: EZH2 T367 phosphorylation activates p38 signaling through lysine methylation to promote breast cancer progression

doi: 10.1016/j.isci.2022.104827

Figure Lengend Snippet: Combined inhibition of EZH2 methyltransferase and p38 kinase activities reduce AKT signaling in vivo (A) RNA sequencing studies of mammary tumors treated with EPZ-6438 (10 mg/kg/day), SB202190 (p38i, 1 mg/kg/day), combination, or control (4% DMSO-30% PEG 300-5% Tween 80) and excised at day 56. The graph shows significantly deregulated pathways by the combination EPZ/p38i vs. control. (B) Immunoblot of primary xenografts treated as indicated in (A). Combined EPZ/p38i reduces p -AKT compared to single inhibitors. (C) Immunoblots for pAKT and total AKT in MDA-MB-231 cells transduced with HA-tagged WT-p38α, K139A-p38α, K165A-p38α, and K139A/K165A-p38α. P38α mutants display reduced pAKT levels compared to WT-p38α. (D) Immunoblots of MDA-MB-231 EZH2 KD rescued with Myc-tagged WT-EZH2, T367A-EZH2, or vector (pBabe) show that T367 phosphorylation is necessary to upregulate pAKT1 without changes in total AKT1. (E) Representative images of human primary invasive carcinomas. Case 1 shows an invasive high-grade ductal carcinoma with concordant high cyto-pEZH2-T367 and high pAKT, while case 2 shows an intermediate-grade invasive carcinoma with low expression of both proteins. Bars, 50 μm. (F) Schematic illustrating our working model of EZH2 function in breast cancer through H3K27me3-dependent and independent activities. P and Me represent phosphorylation and methylation, respectively.

Article Snippet: Recombinant GST-p38α , BPS Bioscience , Cat #40070.

Techniques: Inhibition, In Vivo, RNA Sequencing Assay, Western Blot, Transduction, Plasmid Preparation, Expressing, Methylation

Journal: iScience

Article Title: EZH2 T367 phosphorylation activates p38 signaling through lysine methylation to promote breast cancer progression

doi: 10.1016/j.isci.2022.104827

Figure Lengend Snippet:

Article Snippet: Recombinant GST-p38α , BPS Bioscience , Cat #40070.

Techniques: Plasmid Preparation, Derivative Assay, Recombinant, In Situ, Staining, RNA Sequencing Assay, ChIP-sequencing, shRNA, Software