nbp1 Search Results


anti ier5  (Novus Biologicals)
90
Novus Biologicals anti ier5
Anti Ier5, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/nbp1/pm32471508-87-20-22?v=Novus+Biologicals
Average 90 stars, based on 1 article reviews
anti ier5 - by Bioz Stars, 2026-06
90/100 stars
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st6galnac6  (Novus Biologicals)
94
Novus Biologicals st6galnac6
A RT‒qPCR results showing the differential expression of sialyltransferases in EVT cells from NP and RPL samples ( n = 3 NP; n = 3 RPL ). B Immunohistochemical staining of human placental villous tissues showing HLA-G⁺ EVT cell and the expression of ST3GAL4 and <t>ST6GALNAC6,</t> along with positive signals for MAL II (which detects α 2,3-linked sialic acid) and SNA (which detects α 2,6-linked sialic acid) in NP and RPL samples. C Western blot analyses of ST3GAL4 and ST6GALNAC6 protein levels in EVT cells isolated from NP and RPL tissues ( n = 5 per group). D RT‒qPCR analyses of ST3GAL4 and ST6GALNAC6 mRNA levels in EVT cells ( n = 5 per group). E Lectin blot analysis of α 2,3-linked sialylation and α 2,6-linked sialylation in EVT cell via MAL II and SNA in NP and RPL samples ( n = 5 per group). F Immunohistochemical staining of human decidual tissues showing Siglec-7 expression in the NP and RPL groups. G Flow cytometric analysis of Siglec-7 expression in CD3 − CD56⁺ dNK cells from NP and RPL decidual cells ( n = 16 NP; n = 13 RPL ). Comparison of the proportions of the Siglec7⁺ and Siglec7⁻ subsets among CD3⁻CD56⁺ dNK cells revealed a marked imbalance in the RPL samples. Statistical significance was determined via a two-tailed Student’s t test. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001, ns not significant.
St6galnac6, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/nbp1/pmc13031383-319-10-11?v=Novus+Biologicals
Average 94 stars, based on 1 article reviews
st6galnac6 - by Bioz Stars, 2026-06
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rat anti perforin  (Novus Biologicals)
90
Novus Biologicals rat anti perforin
A RT‒qPCR results showing the differential expression of sialyltransferases in EVT cells from NP and RPL samples ( n = 3 NP; n = 3 RPL ). B Immunohistochemical staining of human placental villous tissues showing HLA-G⁺ EVT cell and the expression of ST3GAL4 and <t>ST6GALNAC6,</t> along with positive signals for MAL II (which detects α 2,3-linked sialic acid) and SNA (which detects α 2,6-linked sialic acid) in NP and RPL samples. C Western blot analyses of ST3GAL4 and ST6GALNAC6 protein levels in EVT cells isolated from NP and RPL tissues ( n = 5 per group). D RT‒qPCR analyses of ST3GAL4 and ST6GALNAC6 mRNA levels in EVT cells ( n = 5 per group). E Lectin blot analysis of α 2,3-linked sialylation and α 2,6-linked sialylation in EVT cell via MAL II and SNA in NP and RPL samples ( n = 5 per group). F Immunohistochemical staining of human decidual tissues showing Siglec-7 expression in the NP and RPL groups. G Flow cytometric analysis of Siglec-7 expression in CD3 − CD56⁺ dNK cells from NP and RPL decidual cells ( n = 16 NP; n = 13 RPL ). Comparison of the proportions of the Siglec7⁺ and Siglec7⁻ subsets among CD3⁻CD56⁺ dNK cells revealed a marked imbalance in the RPL samples. Statistical significance was determined via a two-tailed Student’s t test. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001, ns not significant.
Rat Anti Perforin, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/nbp1/pm29158604-213-37-39?v=Novus+Biologicals
Average 90 stars, based on 1 article reviews
rat anti perforin - by Bioz Stars, 2026-06
90/100 stars
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gpx4 for ip  (Novus Biologicals)
93
Novus Biologicals gpx4 for ip
a Ontologies (GREAT analysis) derived from ZNF354A ChIP-seq peaks in HEK293T cells. Histogram displays enriched annotation terms ranked by binomial p value, indicating functional categories significantly associated with ZNF354A-bound genomic regions . b Volcano plot of RNA-seq analysis from U2OS cells (siControl-Ctrl vs. siZNF354A, 72 h), displaying expression changes of 22586 transcripts. Log2 fold change (FC) vs. −log10 P value plotted. Highlighted genes involved in GSH synthesis (MAT1A, SLC7A11, GSTO2, MGST, CTH), iron metabolism (HMOX1, FTH), and mevalonate pathway (HMGCR). Black dots: significantly upregulated genes (FC > 2, P < 0.05). P values were corrected for multiple testing using the Benjamini-Hochberg’s method c Gene Set Enrichment Analysis (GSEA) dot plot highlighting significantly enriched GO-terms in siZNF354A cells. Gene count, gene ratio, and specific p-values indicated. Enrichment scores and p values were computed by permutation testing (10,000 permutations) using ranked gene lists. d GSEA plots for Biological Process BP and Cellular Component CC GO categories. e Model overview of ZNF354A-regulated selenium-/thiol-dependent and independent pathways in phospholipid peroxide detoxification. ZNF354A targets highlighted in green. Main proteins/pathways upregulated by ZNF354A depletion are indicated (see Supplementary Table ). In thiol-dependent pathways <t>GPX4</t> converts phospholipid hydroperoxides (PL-OOH) to alcohols (PL-OH), dependent on glutathione (GSH) synthesis via cystine uptake and reduction. The methionine cycle contributes with precursors. In parallel the NAD(P)H/FSP1/ubiquinone system reduces peroxyl radicals in phospholipids (PLOO•). SLC7A11 (xCT) cystine/glutamate antiporter; TXNRD1 thioredoxin reductase-1; CTH γ-cystathionase; MAT1A methionine adenosyltransferase; GSTs GSH-S-transferases; GSR GSH-disulfide reductase; GPX4 glutathione peroxidase-4; GSSG oxidized glutathione; FSP1 ferroptosis suppressor protein; CoQ10H2 ubiquinol; CoQ10(H), ubiquinone; SEPHS2 selenophosphate synthetase-2; FTH ferritin heavy chain-1; HMGC , 3-hydroxy-3-methylglutaryl-CoA reductase. Created in BioRender. Abrami, L. ( https://BioRender.com/mmywn2r ). Source data provided as a Source Data file. See Data Availability or ( https://tronoapps.epfl.ch/web/krabopedia/ ) for full datasets.
Gpx4 For Ip, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/nbp1/pmc12820049-377-104-113?v=Novus+Biologicals
Average 93 stars, based on 1 article reviews
gpx4 for ip - by Bioz Stars, 2026-06
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anti cd45  (Novus Biologicals)
94
Novus Biologicals anti cd45
a Ontologies (GREAT analysis) derived from ZNF354A ChIP-seq peaks in HEK293T cells. Histogram displays enriched annotation terms ranked by binomial p value, indicating functional categories significantly associated with ZNF354A-bound genomic regions . b Volcano plot of RNA-seq analysis from U2OS cells (siControl-Ctrl vs. siZNF354A, 72 h), displaying expression changes of 22586 transcripts. Log2 fold change (FC) vs. −log10 P value plotted. Highlighted genes involved in GSH synthesis (MAT1A, SLC7A11, GSTO2, MGST, CTH), iron metabolism (HMOX1, FTH), and mevalonate pathway (HMGCR). Black dots: significantly upregulated genes (FC > 2, P < 0.05). P values were corrected for multiple testing using the Benjamini-Hochberg’s method c Gene Set Enrichment Analysis (GSEA) dot plot highlighting significantly enriched GO-terms in siZNF354A cells. Gene count, gene ratio, and specific p-values indicated. Enrichment scores and p values were computed by permutation testing (10,000 permutations) using ranked gene lists. d GSEA plots for Biological Process BP and Cellular Component CC GO categories. e Model overview of ZNF354A-regulated selenium-/thiol-dependent and independent pathways in phospholipid peroxide detoxification. ZNF354A targets highlighted in green. Main proteins/pathways upregulated by ZNF354A depletion are indicated (see Supplementary Table ). In thiol-dependent pathways <t>GPX4</t> converts phospholipid hydroperoxides (PL-OOH) to alcohols (PL-OH), dependent on glutathione (GSH) synthesis via cystine uptake and reduction. The methionine cycle contributes with precursors. In parallel the NAD(P)H/FSP1/ubiquinone system reduces peroxyl radicals in phospholipids (PLOO•). SLC7A11 (xCT) cystine/glutamate antiporter; TXNRD1 thioredoxin reductase-1; CTH γ-cystathionase; MAT1A methionine adenosyltransferase; GSTs GSH-S-transferases; GSR GSH-disulfide reductase; GPX4 glutathione peroxidase-4; GSSG oxidized glutathione; FSP1 ferroptosis suppressor protein; CoQ10H2 ubiquinol; CoQ10(H), ubiquinone; SEPHS2 selenophosphate synthetase-2; FTH ferritin heavy chain-1; HMGC , 3-hydroxy-3-methylglutaryl-CoA reductase. Created in BioRender. Abrami, L. ( https://BioRender.com/mmywn2r ). Source data provided as a Source Data file. See Data Availability or ( https://tronoapps.epfl.ch/web/krabopedia/ ) for full datasets.
Anti Cd45, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/nbp1/bio_rxiv__2024__09__11__612489-380-3-8?v=Novus+Biologicals
Average 94 stars, based on 1 article reviews
anti cd45 - by Bioz Stars, 2026-06
94/100 stars
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txnip  (Novus Biologicals)
94
Novus Biologicals txnip
Fig. 3. Thioredoxin-interacting protein <t>(TXNIP)</t> expression in asthma pathogenesis. (A) Immunohistochemical staining for TXNIP in lung sections from human healthy control and asthma patient (Scale bar = 80 μm) and quantification graph of TXNIP positive area. TXNIP expression is increased in asthma patients, con firming its involvement in the pathogenesis of asthma. Values: mean ± standard deviation (SD) (n = 5 field per group). Significance: **p < 0.01 vs Control by two- tailed t-test. (B) Immunohistochemical staining (Scale bar = 30 μm) and quantification graph of TXNIP positive area and (C) immunofluorescence staining (Scale bar = 30 μm) for TXNIP in lung sections from normal diet (ND)-fed mice and high fat diet (HFD)-fed mice induced with asthma using a protease from Aspergillus oryzae. Lung tissues were stained with TXNIP (green) and DAPI (blue). TXNIP expression in lung tissue was observed to be higher in HFD asthmatic mice than ND asthmatic mice. Values: mean ± SD (n = 7 per group). Significance: *p < 0.05 vs ND Asthma by two-tailed t-test. (D), (E) Western blot analysis of the indicated proteins in the lung tissue and graphs representing the densitometric values of protein expression. <t>NLRP3,</t> <t>NOD-like</t> receptor family pyrin domain containing 3; ASC, apoptosis- associated speck-like protein containing a caspase-recruitment domain; IL-1β, interleukin-1β. Values: mean ± SD (n = 4 per group). Significance: *,**p < 0.05 and 0.01 vs ND Asthma by two-tailed t-test, respectively.
Txnip, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/nbp1/pm38781728-101-7-8?v=Novus+Biologicals
Average 94 stars, based on 1 article reviews
txnip - by Bioz Stars, 2026-06
94/100 stars
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rfp  (Novus Biologicals)
93
Novus Biologicals rfp
Fig. 3. Thioredoxin-interacting protein <t>(TXNIP)</t> expression in asthma pathogenesis. (A) Immunohistochemical staining for TXNIP in lung sections from human healthy control and asthma patient (Scale bar = 80 μm) and quantification graph of TXNIP positive area. TXNIP expression is increased in asthma patients, con firming its involvement in the pathogenesis of asthma. Values: mean ± standard deviation (SD) (n = 5 field per group). Significance: **p < 0.01 vs Control by two- tailed t-test. (B) Immunohistochemical staining (Scale bar = 30 μm) and quantification graph of TXNIP positive area and (C) immunofluorescence staining (Scale bar = 30 μm) for TXNIP in lung sections from normal diet (ND)-fed mice and high fat diet (HFD)-fed mice induced with asthma using a protease from Aspergillus oryzae. Lung tissues were stained with TXNIP (green) and DAPI (blue). TXNIP expression in lung tissue was observed to be higher in HFD asthmatic mice than ND asthmatic mice. Values: mean ± SD (n = 7 per group). Significance: *p < 0.05 vs ND Asthma by two-tailed t-test. (D), (E) Western blot analysis of the indicated proteins in the lung tissue and graphs representing the densitometric values of protein expression. <t>NLRP3,</t> <t>NOD-like</t> receptor family pyrin domain containing 3; ASC, apoptosis- associated speck-like protein containing a caspase-recruitment domain; IL-1β, interleukin-1β. Values: mean ± SD (n = 4 per group). Significance: *,**p < 0.05 and 0.01 vs ND Asthma by two-tailed t-test, respectively.
Rfp, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/nbp1/bio_rxiv__636878-266-15-35?v=Novus+Biologicals
Average 93 stars, based on 1 article reviews
rfp - by Bioz Stars, 2026-06
93/100 stars
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western blot involved antibodies against kir6 1  (Novus Biologicals)
90
Novus Biologicals western blot involved antibodies against kir6 1
Fig. 3. Thioredoxin-interacting protein <t>(TXNIP)</t> expression in asthma pathogenesis. (A) Immunohistochemical staining for TXNIP in lung sections from human healthy control and asthma patient (Scale bar = 80 μm) and quantification graph of TXNIP positive area. TXNIP expression is increased in asthma patients, con firming its involvement in the pathogenesis of asthma. Values: mean ± standard deviation (SD) (n = 5 field per group). Significance: **p < 0.01 vs Control by two- tailed t-test. (B) Immunohistochemical staining (Scale bar = 30 μm) and quantification graph of TXNIP positive area and (C) immunofluorescence staining (Scale bar = 30 μm) for TXNIP in lung sections from normal diet (ND)-fed mice and high fat diet (HFD)-fed mice induced with asthma using a protease from Aspergillus oryzae. Lung tissues were stained with TXNIP (green) and DAPI (blue). TXNIP expression in lung tissue was observed to be higher in HFD asthmatic mice than ND asthmatic mice. Values: mean ± SD (n = 7 per group). Significance: *p < 0.05 vs ND Asthma by two-tailed t-test. (D), (E) Western blot analysis of the indicated proteins in the lung tissue and graphs representing the densitometric values of protein expression. <t>NLRP3,</t> <t>NOD-like</t> receptor family pyrin domain containing 3; ASC, apoptosis- associated speck-like protein containing a caspase-recruitment domain; IL-1β, interleukin-1β. Values: mean ± SD (n = 4 per group). Significance: *,**p < 0.05 and 0.01 vs ND Asthma by two-tailed t-test, respectively.
Western Blot Involved Antibodies Against Kir6 1, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/nbp1/10__1161_slash_hypertensionaha__109__148767-62-0-15?v=Novus+Biologicals
Average 90 stars, based on 1 article reviews
western blot involved antibodies against kir6 1 - by Bioz Stars, 2026-06
90/100 stars
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rat anti cd45 af647  (Novus Biologicals)
94
Novus Biologicals rat anti cd45 af647
Fig. 3. Thioredoxin-interacting protein <t>(TXNIP)</t> expression in asthma pathogenesis. (A) Immunohistochemical staining for TXNIP in lung sections from human healthy control and asthma patient (Scale bar = 80 μm) and quantification graph of TXNIP positive area. TXNIP expression is increased in asthma patients, con firming its involvement in the pathogenesis of asthma. Values: mean ± standard deviation (SD) (n = 5 field per group). Significance: **p < 0.01 vs Control by two- tailed t-test. (B) Immunohistochemical staining (Scale bar = 30 μm) and quantification graph of TXNIP positive area and (C) immunofluorescence staining (Scale bar = 30 μm) for TXNIP in lung sections from normal diet (ND)-fed mice and high fat diet (HFD)-fed mice induced with asthma using a protease from Aspergillus oryzae. Lung tissues were stained with TXNIP (green) and DAPI (blue). TXNIP expression in lung tissue was observed to be higher in HFD asthmatic mice than ND asthmatic mice. Values: mean ± SD (n = 7 per group). Significance: *p < 0.05 vs ND Asthma by two-tailed t-test. (D), (E) Western blot analysis of the indicated proteins in the lung tissue and graphs representing the densitometric values of protein expression. <t>NLRP3,</t> <t>NOD-like</t> receptor family pyrin domain containing 3; ASC, apoptosis- associated speck-like protein containing a caspase-recruitment domain; IL-1β, interleukin-1β. Values: mean ± SD (n = 4 per group). Significance: *,**p < 0.05 and 0.01 vs ND Asthma by two-tailed t-test, respectively.
Rat Anti Cd45 Af647, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/nbp1/pmc13033704-87-24-28?v=Novus+Biologicals
Average 94 stars, based on 1 article reviews
rat anti cd45 af647 - by Bioz Stars, 2026-06
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id2  (Novus Biologicals)
91
Novus Biologicals id2
Fig. 3. Thioredoxin-interacting protein <t>(TXNIP)</t> expression in asthma pathogenesis. (A) Immunohistochemical staining for TXNIP in lung sections from human healthy control and asthma patient (Scale bar = 80 μm) and quantification graph of TXNIP positive area. TXNIP expression is increased in asthma patients, con firming its involvement in the pathogenesis of asthma. Values: mean ± standard deviation (SD) (n = 5 field per group). Significance: **p < 0.01 vs Control by two- tailed t-test. (B) Immunohistochemical staining (Scale bar = 30 μm) and quantification graph of TXNIP positive area and (C) immunofluorescence staining (Scale bar = 30 μm) for TXNIP in lung sections from normal diet (ND)-fed mice and high fat diet (HFD)-fed mice induced with asthma using a protease from Aspergillus oryzae. Lung tissues were stained with TXNIP (green) and DAPI (blue). TXNIP expression in lung tissue was observed to be higher in HFD asthmatic mice than ND asthmatic mice. Values: mean ± SD (n = 7 per group). Significance: *p < 0.05 vs ND Asthma by two-tailed t-test. (D), (E) Western blot analysis of the indicated proteins in the lung tissue and graphs representing the densitometric values of protein expression. <t>NLRP3,</t> <t>NOD-like</t> receptor family pyrin domain containing 3; ASC, apoptosis- associated speck-like protein containing a caspase-recruitment domain; IL-1β, interleukin-1β. Values: mean ± SD (n = 4 per group). Significance: *,**p < 0.05 and 0.01 vs ND Asthma by two-tailed t-test, respectively.
Id2, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/nbp1/pm24860143-250-2-15?v=Novus+Biologicals
Average 91 stars, based on 1 article reviews
id2 - by Bioz Stars, 2026-06
91/100 stars
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dihydrolipoamide dehydrogenase dld  (Novus Biologicals)
93
Novus Biologicals dihydrolipoamide dehydrogenase dld
Parkin Deficit or Overexpression in Rat Nucleus Accumbens Changes Aerobic Respiration in Opposite Directions. ( A , B ) Gene set enrichment analysis (GSEA)-enrichment plots showing protein sets from GOBP_AEROBIC RESPIRATION signature significantly overrepresented ( p < 0.05) in parkin knockout (PKO) or parkin overexpression (PO) rat nucleus accumbens, as compared to wild-type nucleus accumbens. ( C , D ) Hierarchical clustering heatmap of the leading-edge proteins from the GOBP_AEROBIC_RESPIRATION ( p < 0.05) in PKO NAc and PO NAc. Three Krebs cycle enzymes, citrate synthase (CS), mitochondrial malonate <t>dehydrogenase</t> (MDH2), and <t>dihydrolipoamide</t> S-succinyltransferase (DLST), were decreased in PKO NAc and increased in PO NAc relative to wild-type NAc (red arrows).
Dihydrolipoamide Dehydrogenase Dld, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/nbp1/pmc12292523-166-82-87?v=Novus+Biologicals
Average 93 stars, based on 1 article reviews
dihydrolipoamide dehydrogenase dld - by Bioz Stars, 2026-06
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cd274 pd l1  (Novus Biologicals)
92
Novus Biologicals cd274 pd l1
Parkin Deficit or Overexpression in Rat Nucleus Accumbens Changes Aerobic Respiration in Opposite Directions. ( A , B ) Gene set enrichment analysis (GSEA)-enrichment plots showing protein sets from GOBP_AEROBIC RESPIRATION signature significantly overrepresented ( p < 0.05) in parkin knockout (PKO) or parkin overexpression (PO) rat nucleus accumbens, as compared to wild-type nucleus accumbens. ( C , D ) Hierarchical clustering heatmap of the leading-edge proteins from the GOBP_AEROBIC_RESPIRATION ( p < 0.05) in PKO NAc and PO NAc. Three Krebs cycle enzymes, citrate synthase (CS), mitochondrial malonate <t>dehydrogenase</t> (MDH2), and <t>dihydrolipoamide</t> S-succinyltransferase (DLST), were decreased in PKO NAc and increased in PO NAc relative to wild-type NAc (red arrows).
Cd274 Pd L1, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/nbp1/pm31583120-225-11-14?v=Novus+Biologicals
Average 92 stars, based on 1 article reviews
cd274 pd l1 - by Bioz Stars, 2026-06
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Image Search Results


A RT‒qPCR results showing the differential expression of sialyltransferases in EVT cells from NP and RPL samples ( n = 3 NP; n = 3 RPL ). B Immunohistochemical staining of human placental villous tissues showing HLA-G⁺ EVT cell and the expression of ST3GAL4 and ST6GALNAC6, along with positive signals for MAL II (which detects α 2,3-linked sialic acid) and SNA (which detects α 2,6-linked sialic acid) in NP and RPL samples. C Western blot analyses of ST3GAL4 and ST6GALNAC6 protein levels in EVT cells isolated from NP and RPL tissues ( n = 5 per group). D RT‒qPCR analyses of ST3GAL4 and ST6GALNAC6 mRNA levels in EVT cells ( n = 5 per group). E Lectin blot analysis of α 2,3-linked sialylation and α 2,6-linked sialylation in EVT cell via MAL II and SNA in NP and RPL samples ( n = 5 per group). F Immunohistochemical staining of human decidual tissues showing Siglec-7 expression in the NP and RPL groups. G Flow cytometric analysis of Siglec-7 expression in CD3 − CD56⁺ dNK cells from NP and RPL decidual cells ( n = 16 NP; n = 13 RPL ). Comparison of the proportions of the Siglec7⁺ and Siglec7⁻ subsets among CD3⁻CD56⁺ dNK cells revealed a marked imbalance in the RPL samples. Statistical significance was determined via a two-tailed Student’s t test. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001, ns not significant.

Journal: Cell Death & Disease

Article Title: Deficient extravillous trophoblast invasion caused by impaired sialylation–Siglec-7 interaction contributes to recurrent pregnancy loss

doi: 10.1038/s41419-026-08503-9

Figure Lengend Snippet: A RT‒qPCR results showing the differential expression of sialyltransferases in EVT cells from NP and RPL samples ( n = 3 NP; n = 3 RPL ). B Immunohistochemical staining of human placental villous tissues showing HLA-G⁺ EVT cell and the expression of ST3GAL4 and ST6GALNAC6, along with positive signals for MAL II (which detects α 2,3-linked sialic acid) and SNA (which detects α 2,6-linked sialic acid) in NP and RPL samples. C Western blot analyses of ST3GAL4 and ST6GALNAC6 protein levels in EVT cells isolated from NP and RPL tissues ( n = 5 per group). D RT‒qPCR analyses of ST3GAL4 and ST6GALNAC6 mRNA levels in EVT cells ( n = 5 per group). E Lectin blot analysis of α 2,3-linked sialylation and α 2,6-linked sialylation in EVT cell via MAL II and SNA in NP and RPL samples ( n = 5 per group). F Immunohistochemical staining of human decidual tissues showing Siglec-7 expression in the NP and RPL groups. G Flow cytometric analysis of Siglec-7 expression in CD3 − CD56⁺ dNK cells from NP and RPL decidual cells ( n = 16 NP; n = 13 RPL ). Comparison of the proportions of the Siglec7⁺ and Siglec7⁻ subsets among CD3⁻CD56⁺ dNK cells revealed a marked imbalance in the RPL samples. Statistical significance was determined via a two-tailed Student’s t test. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001, ns not significant.

Article Snippet: The membranes were probed with antibodies against ST3GAL4 (Santa Cruz), ST6GALNAC6 (NOVUS), LAMP1 (Santa Cruz), CD151 (Santa Cruz), CD276 (Santa Cruz), ITGA2 (Santa Cruz), Siglec-7 (R&D Systems), phospho-STAT3 (Tyr705) (Cell Signaling Technology), STAT3 (Cell Signaling Technology), SHP-2 (Sigma), and GAPDH (ABclonal).

Techniques: Quantitative Proteomics, Immunohistochemical staining, Staining, Expressing, Western Blot, Isolation, Comparison, Two Tailed Test

Structural modeling using AlphaFold3 predicts potential recognition interfaces between CD276 ( A ), CD151 ( B ), ITGA2 ( C ), LAMP1 ( D ) with Siglec-7. Lectin pull-down assays demonstrated that both α 2,6- and α 2,3-linked sialylation of CD276 ( E ), CD151 ( F ), ITGA2 ( G ), and LAMP1 ( H ) were decreased in EVT cells derived from RPL compared with those from NP. Co-immunoprecipitation analysis further revealed that the interaction between these glycoproteins and Siglec-7 was correspondingly reduced in RPL-EVT cells. To validate this regulatory relationship, we overexpressed ST6GALNAC6 in HEK-293FT cells. Overexpression of ST6GALNAC6 increased α 2,6- and α 2,3-linked sialylation of CD276 ( I ), CD151 ( J ), ITGA2 ( K ), and LAMP1 ( L ). Co-immunoprecipitation analysis confirmed that ST6GALNAC6 enhances the sialylation of multiple membrane glycoproteins and thereby promotes their interaction with Siglec-7.

Journal: Cell Death & Disease

Article Title: Deficient extravillous trophoblast invasion caused by impaired sialylation–Siglec-7 interaction contributes to recurrent pregnancy loss

doi: 10.1038/s41419-026-08503-9

Figure Lengend Snippet: Structural modeling using AlphaFold3 predicts potential recognition interfaces between CD276 ( A ), CD151 ( B ), ITGA2 ( C ), LAMP1 ( D ) with Siglec-7. Lectin pull-down assays demonstrated that both α 2,6- and α 2,3-linked sialylation of CD276 ( E ), CD151 ( F ), ITGA2 ( G ), and LAMP1 ( H ) were decreased in EVT cells derived from RPL compared with those from NP. Co-immunoprecipitation analysis further revealed that the interaction between these glycoproteins and Siglec-7 was correspondingly reduced in RPL-EVT cells. To validate this regulatory relationship, we overexpressed ST6GALNAC6 in HEK-293FT cells. Overexpression of ST6GALNAC6 increased α 2,6- and α 2,3-linked sialylation of CD276 ( I ), CD151 ( J ), ITGA2 ( K ), and LAMP1 ( L ). Co-immunoprecipitation analysis confirmed that ST6GALNAC6 enhances the sialylation of multiple membrane glycoproteins and thereby promotes their interaction with Siglec-7.

Article Snippet: The membranes were probed with antibodies against ST3GAL4 (Santa Cruz), ST6GALNAC6 (NOVUS), LAMP1 (Santa Cruz), CD151 (Santa Cruz), CD276 (Santa Cruz), ITGA2 (Santa Cruz), Siglec-7 (R&D Systems), phospho-STAT3 (Tyr705) (Cell Signaling Technology), STAT3 (Cell Signaling Technology), SHP-2 (Sigma), and GAPDH (ABclonal).

Techniques: Derivative Assay, Immunoprecipitation, Over Expression, Membrane

A Microfluidic implantation-on-a-chip model was established by seeding EVT cells into the fetal chamber and HUVEC cells into the maternal chamber. A layer of low-growth-factor matrigel containing NK-92MI cells was introduced into the central chamber to mimic the decidual–trophoblast interface. Figure created with BioRender.com ( https://BioRender.com/x60p1q7 ). B EVT cells displayed increased invasion depth and area over time within the chip-based implantation model. C , D Recombinant ST3GAL4 and ST6GALNAC6 were added individually or in combination to RPL-derived EVT cells. The matrigel was supplemented with either Siglec-7⁺ or Siglec-7⁻ NK-92MI cells. Images were acquired after 24 h using an Olympus confocal microscope. Quantification revealed that ST6GALNAC6, alone or in combination with ST3GAL4, significantly enhanced the invasion depth and area of RPL EVT cells. ST3GAL4 alone had a minimal effect. All glycosyltransferase treatments improved invasiveness in the presence of Siglec-7⁺ NK cells. The data are presented as the means ± SDs. Statistical analysis was performed via one-way ANOVA. * P < 0.05, ** P < 0.01, *** P < 0.001, ns not significant.

Journal: Cell Death & Disease

Article Title: Deficient extravillous trophoblast invasion caused by impaired sialylation–Siglec-7 interaction contributes to recurrent pregnancy loss

doi: 10.1038/s41419-026-08503-9

Figure Lengend Snippet: A Microfluidic implantation-on-a-chip model was established by seeding EVT cells into the fetal chamber and HUVEC cells into the maternal chamber. A layer of low-growth-factor matrigel containing NK-92MI cells was introduced into the central chamber to mimic the decidual–trophoblast interface. Figure created with BioRender.com ( https://BioRender.com/x60p1q7 ). B EVT cells displayed increased invasion depth and area over time within the chip-based implantation model. C , D Recombinant ST3GAL4 and ST6GALNAC6 were added individually or in combination to RPL-derived EVT cells. The matrigel was supplemented with either Siglec-7⁺ or Siglec-7⁻ NK-92MI cells. Images were acquired after 24 h using an Olympus confocal microscope. Quantification revealed that ST6GALNAC6, alone or in combination with ST3GAL4, significantly enhanced the invasion depth and area of RPL EVT cells. ST3GAL4 alone had a minimal effect. All glycosyltransferase treatments improved invasiveness in the presence of Siglec-7⁺ NK cells. The data are presented as the means ± SDs. Statistical analysis was performed via one-way ANOVA. * P < 0.05, ** P < 0.01, *** P < 0.001, ns not significant.

Article Snippet: The membranes were probed with antibodies against ST3GAL4 (Santa Cruz), ST6GALNAC6 (NOVUS), LAMP1 (Santa Cruz), CD151 (Santa Cruz), CD276 (Santa Cruz), ITGA2 (Santa Cruz), Siglec-7 (R&D Systems), phospho-STAT3 (Tyr705) (Cell Signaling Technology), STAT3 (Cell Signaling Technology), SHP-2 (Sigma), and GAPDH (ABclonal).

Techniques: Recombinant, Derivative Assay, Microscopy

a Ontologies (GREAT analysis) derived from ZNF354A ChIP-seq peaks in HEK293T cells. Histogram displays enriched annotation terms ranked by binomial p value, indicating functional categories significantly associated with ZNF354A-bound genomic regions . b Volcano plot of RNA-seq analysis from U2OS cells (siControl-Ctrl vs. siZNF354A, 72 h), displaying expression changes of 22586 transcripts. Log2 fold change (FC) vs. −log10 P value plotted. Highlighted genes involved in GSH synthesis (MAT1A, SLC7A11, GSTO2, MGST, CTH), iron metabolism (HMOX1, FTH), and mevalonate pathway (HMGCR). Black dots: significantly upregulated genes (FC > 2, P < 0.05). P values were corrected for multiple testing using the Benjamini-Hochberg’s method c Gene Set Enrichment Analysis (GSEA) dot plot highlighting significantly enriched GO-terms in siZNF354A cells. Gene count, gene ratio, and specific p-values indicated. Enrichment scores and p values were computed by permutation testing (10,000 permutations) using ranked gene lists. d GSEA plots for Biological Process BP and Cellular Component CC GO categories. e Model overview of ZNF354A-regulated selenium-/thiol-dependent and independent pathways in phospholipid peroxide detoxification. ZNF354A targets highlighted in green. Main proteins/pathways upregulated by ZNF354A depletion are indicated (see Supplementary Table ). In thiol-dependent pathways GPX4 converts phospholipid hydroperoxides (PL-OOH) to alcohols (PL-OH), dependent on glutathione (GSH) synthesis via cystine uptake and reduction. The methionine cycle contributes with precursors. In parallel the NAD(P)H/FSP1/ubiquinone system reduces peroxyl radicals in phospholipids (PLOO•). SLC7A11 (xCT) cystine/glutamate antiporter; TXNRD1 thioredoxin reductase-1; CTH γ-cystathionase; MAT1A methionine adenosyltransferase; GSTs GSH-S-transferases; GSR GSH-disulfide reductase; GPX4 glutathione peroxidase-4; GSSG oxidized glutathione; FSP1 ferroptosis suppressor protein; CoQ10H2 ubiquinol; CoQ10(H), ubiquinone; SEPHS2 selenophosphate synthetase-2; FTH ferritin heavy chain-1; HMGC , 3-hydroxy-3-methylglutaryl-CoA reductase. Created in BioRender. Abrami, L. ( https://BioRender.com/mmywn2r ). Source data provided as a Source Data file. See Data Availability or ( https://tronoapps.epfl.ch/web/krabopedia/ ) for full datasets.

Journal: Nature Communications

Article Title: Identification of a lipid oxygen radical defense pathway and its epigenetic control

doi: 10.1038/s41467-025-67304-4

Figure Lengend Snippet: a Ontologies (GREAT analysis) derived from ZNF354A ChIP-seq peaks in HEK293T cells. Histogram displays enriched annotation terms ranked by binomial p value, indicating functional categories significantly associated with ZNF354A-bound genomic regions . b Volcano plot of RNA-seq analysis from U2OS cells (siControl-Ctrl vs. siZNF354A, 72 h), displaying expression changes of 22586 transcripts. Log2 fold change (FC) vs. −log10 P value plotted. Highlighted genes involved in GSH synthesis (MAT1A, SLC7A11, GSTO2, MGST, CTH), iron metabolism (HMOX1, FTH), and mevalonate pathway (HMGCR). Black dots: significantly upregulated genes (FC > 2, P < 0.05). P values were corrected for multiple testing using the Benjamini-Hochberg’s method c Gene Set Enrichment Analysis (GSEA) dot plot highlighting significantly enriched GO-terms in siZNF354A cells. Gene count, gene ratio, and specific p-values indicated. Enrichment scores and p values were computed by permutation testing (10,000 permutations) using ranked gene lists. d GSEA plots for Biological Process BP and Cellular Component CC GO categories. e Model overview of ZNF354A-regulated selenium-/thiol-dependent and independent pathways in phospholipid peroxide detoxification. ZNF354A targets highlighted in green. Main proteins/pathways upregulated by ZNF354A depletion are indicated (see Supplementary Table ). In thiol-dependent pathways GPX4 converts phospholipid hydroperoxides (PL-OOH) to alcohols (PL-OH), dependent on glutathione (GSH) synthesis via cystine uptake and reduction. The methionine cycle contributes with precursors. In parallel the NAD(P)H/FSP1/ubiquinone system reduces peroxyl radicals in phospholipids (PLOO•). SLC7A11 (xCT) cystine/glutamate antiporter; TXNRD1 thioredoxin reductase-1; CTH γ-cystathionase; MAT1A methionine adenosyltransferase; GSTs GSH-S-transferases; GSR GSH-disulfide reductase; GPX4 glutathione peroxidase-4; GSSG oxidized glutathione; FSP1 ferroptosis suppressor protein; CoQ10H2 ubiquinol; CoQ10(H), ubiquinone; SEPHS2 selenophosphate synthetase-2; FTH ferritin heavy chain-1; HMGC , 3-hydroxy-3-methylglutaryl-CoA reductase. Created in BioRender. Abrami, L. ( https://BioRender.com/mmywn2r ). Source data provided as a Source Data file. See Data Availability or ( https://tronoapps.epfl.ch/web/krabopedia/ ) for full datasets.

Article Snippet: The antibodies and reagents were acquired from: ATF2 (Abcam: ab_131484; RRID: AB_11156678, rabbit: 1:2000x), ATF2 (Abcam: E243 ab32160, RRID: AB_2243137, rabbit: 1:2000x), phosphor-ATF2 (T69) (Abcam: 131106; RRID: AB_11157608;rabbit:1:1000x), GAPDH (Thermofisher: 398600; RRID: AB_2533438; mouse: 1:4000x), ZDHHC20 (Sigma: SAB4501054; RRID: AB_10744838; rabbit: 1:2000x), HA-HRP (Roche: 112013819001; RRID: AB_390917; rat: 1:5000x), KAP1 (Abcam: ab_109289; RRID: AB_10863057, rabbit: 1:1000x), phosphor-KAP1 S473 was generated in D. TRONO laboratory using the following peptide krsrSgegevsgl (rabbit: 1:500x), Nucleocapside N SARS-CoV-2 (Genetex: GTX135357; RRID: AB_2868464; rabbit 1:4000x), FLAG (Sigma: F3165; RRID: AB_259529; mouse: 1:2000x), phosphor-Threonine-Serine (BD: 612548; RRID: AB_399843; rabbit: 1:1000x), GPX4 for WB (Cell Signalling: 52455; RRID: AB_2924984, rabbit: 1:1000x), GPX4 for IP (MA5-49216, RRID: AB_3074874, mouse 1:2000x), SETDB1 (Novus Biologicals: NBP1_51677; RRID: AB_11002952, mouse: 1:2000x), NRF2 (Abnova: H00004780; RRID:566020, mouse: 1:2000x), V5-HRP (Sigma: V2260; RRID: AB_261857, mouse: 1:2000x), Actin (Millipore: MAB1501; RRID: AB_2223041, mouse: 1:4000x), MAT1A (Abcam: 129176; RRID: AB_11145300, rabbit: 1:2000x), ZNF354A (Santa Cruz: 81140; RRID: AB_1131557, mouse: 1:1000x), MAT1A (Abcam: ab1129176, RRID: AB_11145300, rabbit: 1:1000x), Myc (Millipore: 9E10, 05-419, RRID: AB_309725, mouse: 1:3000x), and HRP-conjugated secondary antibodies (GE-Healthcare).

Techniques: Derivative Assay, ChIP-sequencing, Functional Assay, RNA Sequencing, Expressing

a–c Lipid peroxides measured by flow cytometry (Bodipy-C11, Liperfluo) and membrane permeability (propidium iodide) in U2OS cells transfected with siControl or siZNF354A (72 h) ± RSL3 (3 μM, 24 h). Mean ± SEM; dots indicate biologically independent experiments.; p values compare to siControl, by two-way ANOVA, Tukey’s test. d Viability (ATP detection) of U2OS cells (siControl or siZNF354A, 72 h) ± RSL3 (3 μM) or H₂O₂ (50 µM, 16 h). Mean ± SD; representative assay (of three), n = 36.; p values compare to siControl, by two-way ANOVA, Sidak’s test. e , f Lipid peroxidation ( e ) and viability ( f ) of U2OS cells expressing wild-type (WT) or KRAB-binding mutant ZNF354A ± ferrostatin-1 (Fer-1, 15 µM, added at 0 and 48 h post-transfection). Mean ± SEM and dots represent biologically independent experiments ( e ). Mean ± SD normalized to untreated controls (empty plasmid) of representative assay (of three) n = 33 ( f ). p values compare untreated controls vs Fer-1, by two-way ANOVA, Holm-Sidak’s test. g Viability (as in f) of HeLa cells expressing ZNF354A, supplemented with FSP1, GPX4, GPX4 + N-Acetyl-Cysteine (NAC, 1 mM), or NAC alone. Mean ± SD; representative assay (of three), n = 33.; p values compare untreated controls at each time point, by two-way ANOVA, Sidak’s test. h Cellular level of GSH was measured in control cells and upon silencing of ZNF354A or GPX4 and upon over expression of ZNF354A. Mean ± SEM. and dots represent biologically independent experiments, p values obtained, by two-way ANOVA, Tukey’s test. i , Western blot of total cell extracts (TCE) and ZNF354A immunoprecipitates (IP) from indicated cancer cells, showing Short-S (42 kDa), 20 L isoforms ( ~ 49, 62, 69 kDa), GAPDH (loading control), total ZNF354A, and phospho-Ser/Thr proteins. j Viability (as in d) of cancer cells (from h) ± RSL3 (3 μM) or H₂O₂ (50 µM, 16 h). Viability normalized to untreated controls (100%). Mean ± SD; representative assay ( n = 35). p values compare each condition to HepG2 reference, by two-way ANOVA, Dunnett’s test.

Journal: Nature Communications

Article Title: Identification of a lipid oxygen radical defense pathway and its epigenetic control

doi: 10.1038/s41467-025-67304-4

Figure Lengend Snippet: a–c Lipid peroxides measured by flow cytometry (Bodipy-C11, Liperfluo) and membrane permeability (propidium iodide) in U2OS cells transfected with siControl or siZNF354A (72 h) ± RSL3 (3 μM, 24 h). Mean ± SEM; dots indicate biologically independent experiments.; p values compare to siControl, by two-way ANOVA, Tukey’s test. d Viability (ATP detection) of U2OS cells (siControl or siZNF354A, 72 h) ± RSL3 (3 μM) or H₂O₂ (50 µM, 16 h). Mean ± SD; representative assay (of three), n = 36.; p values compare to siControl, by two-way ANOVA, Sidak’s test. e , f Lipid peroxidation ( e ) and viability ( f ) of U2OS cells expressing wild-type (WT) or KRAB-binding mutant ZNF354A ± ferrostatin-1 (Fer-1, 15 µM, added at 0 and 48 h post-transfection). Mean ± SEM and dots represent biologically independent experiments ( e ). Mean ± SD normalized to untreated controls (empty plasmid) of representative assay (of three) n = 33 ( f ). p values compare untreated controls vs Fer-1, by two-way ANOVA, Holm-Sidak’s test. g Viability (as in f) of HeLa cells expressing ZNF354A, supplemented with FSP1, GPX4, GPX4 + N-Acetyl-Cysteine (NAC, 1 mM), or NAC alone. Mean ± SD; representative assay (of three), n = 33.; p values compare untreated controls at each time point, by two-way ANOVA, Sidak’s test. h Cellular level of GSH was measured in control cells and upon silencing of ZNF354A or GPX4 and upon over expression of ZNF354A. Mean ± SEM. and dots represent biologically independent experiments, p values obtained, by two-way ANOVA, Tukey’s test. i , Western blot of total cell extracts (TCE) and ZNF354A immunoprecipitates (IP) from indicated cancer cells, showing Short-S (42 kDa), 20 L isoforms ( ~ 49, 62, 69 kDa), GAPDH (loading control), total ZNF354A, and phospho-Ser/Thr proteins. j Viability (as in d) of cancer cells (from h) ± RSL3 (3 μM) or H₂O₂ (50 µM, 16 h). Viability normalized to untreated controls (100%). Mean ± SD; representative assay ( n = 35). p values compare each condition to HepG2 reference, by two-way ANOVA, Dunnett’s test.

Article Snippet: The antibodies and reagents were acquired from: ATF2 (Abcam: ab_131484; RRID: AB_11156678, rabbit: 1:2000x), ATF2 (Abcam: E243 ab32160, RRID: AB_2243137, rabbit: 1:2000x), phosphor-ATF2 (T69) (Abcam: 131106; RRID: AB_11157608;rabbit:1:1000x), GAPDH (Thermofisher: 398600; RRID: AB_2533438; mouse: 1:4000x), ZDHHC20 (Sigma: SAB4501054; RRID: AB_10744838; rabbit: 1:2000x), HA-HRP (Roche: 112013819001; RRID: AB_390917; rat: 1:5000x), KAP1 (Abcam: ab_109289; RRID: AB_10863057, rabbit: 1:1000x), phosphor-KAP1 S473 was generated in D. TRONO laboratory using the following peptide krsrSgegevsgl (rabbit: 1:500x), Nucleocapside N SARS-CoV-2 (Genetex: GTX135357; RRID: AB_2868464; rabbit 1:4000x), FLAG (Sigma: F3165; RRID: AB_259529; mouse: 1:2000x), phosphor-Threonine-Serine (BD: 612548; RRID: AB_399843; rabbit: 1:1000x), GPX4 for WB (Cell Signalling: 52455; RRID: AB_2924984, rabbit: 1:1000x), GPX4 for IP (MA5-49216, RRID: AB_3074874, mouse 1:2000x), SETDB1 (Novus Biologicals: NBP1_51677; RRID: AB_11002952, mouse: 1:2000x), NRF2 (Abnova: H00004780; RRID:566020, mouse: 1:2000x), V5-HRP (Sigma: V2260; RRID: AB_261857, mouse: 1:2000x), Actin (Millipore: MAB1501; RRID: AB_2223041, mouse: 1:4000x), MAT1A (Abcam: 129176; RRID: AB_11145300, rabbit: 1:2000x), ZNF354A (Santa Cruz: 81140; RRID: AB_1131557, mouse: 1:1000x), MAT1A (Abcam: ab1129176, RRID: AB_11145300, rabbit: 1:1000x), Myc (Millipore: 9E10, 05-419, RRID: AB_309725, mouse: 1:3000x), and HRP-conjugated secondary antibodies (GE-Healthcare).

Techniques: Flow Cytometry, Membrane, Permeability, Transfection, Expressing, Binding Assay, Mutagenesis, Plasmid Preparation, Control, Over Expression, Western Blot

a–d Incorporation of 3 H-palmitic acid ( 3 H-palm) in GPX4 from U2OS cells silenced for 72 h with pooled ( a ) or individual ( c ) ZDHHC siRNAs. Cells were metabolically labeled for 3 h at 37 °C with 3 H-palm; GPX4 was immunoprecipitated (IP-GPX4), resolved by SDS–PAGE, and analyzed by Western blot (WB) and autoradiography ( 3 H-palm). The levels of 3 H-palm incorporation in siControl (Ctrl) were set to 100% and results are mean ± SEM, and each dot represents an independent experiment ( n = 3). p values compare siCtrl, two-way ANOVA, Dunnett’s test. e HEK WT or ZDHHC20-KO cells were incubated with 100 μM C16:0-azide for the indicated times or with palmitic acid for 8 h. Incorporated C16:0-azide was detected by click chemistry with alkyne-mPEG 5 K (200 μM), followed by SDS–PAGE and WB for GPX4. Results are representative of three independent experiments. f–h same as in ( a ), for ( f ), HEK WT (Ctrl) or ZDHHC20-KO cells, recomplemented with empty vector or short/long ZDHHC20 or ( h ) U2OS cells left untreated or treated for 4 h with 50 μM H₂O₂. For f Myc-ZDHHC20 expression was confirmed by WB. The levels of 3 H-palm incorporation were set to 100% in Control-WT cells for g, or untreated control cells, in ( h ). Results are mean ± SEM, and each dot represents an independent experiment ( g ) n = 4 and h n = 6). p values comparing to Ctrl or as indicated by, ( g ) two-way ANOVA, Tukey’s test, and ( h ) Two-tailed Student’s t-test. i Cellular glutathione measured in U2OS cells, siCtrl or siZDHHC20 (72 h) alone or recomplemented with short/long ZDHHC20 (24 h). Data are mean ± SEM from one of three independent experiments ( n = 6). p values by, two-way ANOVA, Tukey’s test j Viability assessed using Promega Glo ATB detection in U2OS cells as in i, treated as in ( h ). Data are mean ± SEM from one of three independent experiments ( n = 36 replicates). p values by, two-way ANOVA, Tukey’s test k Proposed Model: Under homeostasis, ATF2–SETDB1–KAP1–ZNF354A repress antioxidant genes. Lipid peroxide accumulation activates p38/JNK signaling, leading to ZNF354A dissociation and induction of antioxidant responses. Created in BioRender. abrami, I ( https://BioRender.com/gvmrwgl ).

Journal: Nature Communications

Article Title: Identification of a lipid oxygen radical defense pathway and its epigenetic control

doi: 10.1038/s41467-025-67304-4

Figure Lengend Snippet: a–d Incorporation of 3 H-palmitic acid ( 3 H-palm) in GPX4 from U2OS cells silenced for 72 h with pooled ( a ) or individual ( c ) ZDHHC siRNAs. Cells were metabolically labeled for 3 h at 37 °C with 3 H-palm; GPX4 was immunoprecipitated (IP-GPX4), resolved by SDS–PAGE, and analyzed by Western blot (WB) and autoradiography ( 3 H-palm). The levels of 3 H-palm incorporation in siControl (Ctrl) were set to 100% and results are mean ± SEM, and each dot represents an independent experiment ( n = 3). p values compare siCtrl, two-way ANOVA, Dunnett’s test. e HEK WT or ZDHHC20-KO cells were incubated with 100 μM C16:0-azide for the indicated times or with palmitic acid for 8 h. Incorporated C16:0-azide was detected by click chemistry with alkyne-mPEG 5 K (200 μM), followed by SDS–PAGE and WB for GPX4. Results are representative of three independent experiments. f–h same as in ( a ), for ( f ), HEK WT (Ctrl) or ZDHHC20-KO cells, recomplemented with empty vector or short/long ZDHHC20 or ( h ) U2OS cells left untreated or treated for 4 h with 50 μM H₂O₂. For f Myc-ZDHHC20 expression was confirmed by WB. The levels of 3 H-palm incorporation were set to 100% in Control-WT cells for g, or untreated control cells, in ( h ). Results are mean ± SEM, and each dot represents an independent experiment ( g ) n = 4 and h n = 6). p values comparing to Ctrl or as indicated by, ( g ) two-way ANOVA, Tukey’s test, and ( h ) Two-tailed Student’s t-test. i Cellular glutathione measured in U2OS cells, siCtrl or siZDHHC20 (72 h) alone or recomplemented with short/long ZDHHC20 (24 h). Data are mean ± SEM from one of three independent experiments ( n = 6). p values by, two-way ANOVA, Tukey’s test j Viability assessed using Promega Glo ATB detection in U2OS cells as in i, treated as in ( h ). Data are mean ± SEM from one of three independent experiments ( n = 36 replicates). p values by, two-way ANOVA, Tukey’s test k Proposed Model: Under homeostasis, ATF2–SETDB1–KAP1–ZNF354A repress antioxidant genes. Lipid peroxide accumulation activates p38/JNK signaling, leading to ZNF354A dissociation and induction of antioxidant responses. Created in BioRender. abrami, I ( https://BioRender.com/gvmrwgl ).

Article Snippet: The antibodies and reagents were acquired from: ATF2 (Abcam: ab_131484; RRID: AB_11156678, rabbit: 1:2000x), ATF2 (Abcam: E243 ab32160, RRID: AB_2243137, rabbit: 1:2000x), phosphor-ATF2 (T69) (Abcam: 131106; RRID: AB_11157608;rabbit:1:1000x), GAPDH (Thermofisher: 398600; RRID: AB_2533438; mouse: 1:4000x), ZDHHC20 (Sigma: SAB4501054; RRID: AB_10744838; rabbit: 1:2000x), HA-HRP (Roche: 112013819001; RRID: AB_390917; rat: 1:5000x), KAP1 (Abcam: ab_109289; RRID: AB_10863057, rabbit: 1:1000x), phosphor-KAP1 S473 was generated in D. TRONO laboratory using the following peptide krsrSgegevsgl (rabbit: 1:500x), Nucleocapside N SARS-CoV-2 (Genetex: GTX135357; RRID: AB_2868464; rabbit 1:4000x), FLAG (Sigma: F3165; RRID: AB_259529; mouse: 1:2000x), phosphor-Threonine-Serine (BD: 612548; RRID: AB_399843; rabbit: 1:1000x), GPX4 for WB (Cell Signalling: 52455; RRID: AB_2924984, rabbit: 1:1000x), GPX4 for IP (MA5-49216, RRID: AB_3074874, mouse 1:2000x), SETDB1 (Novus Biologicals: NBP1_51677; RRID: AB_11002952, mouse: 1:2000x), NRF2 (Abnova: H00004780; RRID:566020, mouse: 1:2000x), V5-HRP (Sigma: V2260; RRID: AB_261857, mouse: 1:2000x), Actin (Millipore: MAB1501; RRID: AB_2223041, mouse: 1:4000x), MAT1A (Abcam: 129176; RRID: AB_11145300, rabbit: 1:2000x), ZNF354A (Santa Cruz: 81140; RRID: AB_1131557, mouse: 1:1000x), MAT1A (Abcam: ab1129176, RRID: AB_11145300, rabbit: 1:1000x), Myc (Millipore: 9E10, 05-419, RRID: AB_309725, mouse: 1:3000x), and HRP-conjugated secondary antibodies (GE-Healthcare).

Techniques: Metabolic Labelling, Labeling, Immunoprecipitation, SDS Page, Western Blot, Autoradiography, Incubation, Plasmid Preparation, Expressing, Control, Two Tailed Test

Fig. 3. Thioredoxin-interacting protein (TXNIP) expression in asthma pathogenesis. (A) Immunohistochemical staining for TXNIP in lung sections from human healthy control and asthma patient (Scale bar = 80 μm) and quantification graph of TXNIP positive area. TXNIP expression is increased in asthma patients, con firming its involvement in the pathogenesis of asthma. Values: mean ± standard deviation (SD) (n = 5 field per group). Significance: **p < 0.01 vs Control by two- tailed t-test. (B) Immunohistochemical staining (Scale bar = 30 μm) and quantification graph of TXNIP positive area and (C) immunofluorescence staining (Scale bar = 30 μm) for TXNIP in lung sections from normal diet (ND)-fed mice and high fat diet (HFD)-fed mice induced with asthma using a protease from Aspergillus oryzae. Lung tissues were stained with TXNIP (green) and DAPI (blue). TXNIP expression in lung tissue was observed to be higher in HFD asthmatic mice than ND asthmatic mice. Values: mean ± SD (n = 7 per group). Significance: *p < 0.05 vs ND Asthma by two-tailed t-test. (D), (E) Western blot analysis of the indicated proteins in the lung tissue and graphs representing the densitometric values of protein expression. NLRP3, NOD-like receptor family pyrin domain containing 3; ASC, apoptosis- associated speck-like protein containing a caspase-recruitment domain; IL-1β, interleukin-1β. Values: mean ± SD (n = 4 per group). Significance: *,**p < 0.05 and 0.01 vs ND Asthma by two-tailed t-test, respectively.

Journal: Redox biology

Article Title: The absence of thioredoxin-interacting protein in alveolar cells exacerbates asthma during obesity.

doi: 10.1016/j.redox.2024.103193

Figure Lengend Snippet: Fig. 3. Thioredoxin-interacting protein (TXNIP) expression in asthma pathogenesis. (A) Immunohistochemical staining for TXNIP in lung sections from human healthy control and asthma patient (Scale bar = 80 μm) and quantification graph of TXNIP positive area. TXNIP expression is increased in asthma patients, con firming its involvement in the pathogenesis of asthma. Values: mean ± standard deviation (SD) (n = 5 field per group). Significance: **p < 0.01 vs Control by two- tailed t-test. (B) Immunohistochemical staining (Scale bar = 30 μm) and quantification graph of TXNIP positive area and (C) immunofluorescence staining (Scale bar = 30 μm) for TXNIP in lung sections from normal diet (ND)-fed mice and high fat diet (HFD)-fed mice induced with asthma using a protease from Aspergillus oryzae. Lung tissues were stained with TXNIP (green) and DAPI (blue). TXNIP expression in lung tissue was observed to be higher in HFD asthmatic mice than ND asthmatic mice. Values: mean ± SD (n = 7 per group). Significance: *p < 0.05 vs ND Asthma by two-tailed t-test. (D), (E) Western blot analysis of the indicated proteins in the lung tissue and graphs representing the densitometric values of protein expression. NLRP3, NOD-like receptor family pyrin domain containing 3; ASC, apoptosis- associated speck-like protein containing a caspase-recruitment domain; IL-1β, interleukin-1β. Values: mean ± SD (n = 4 per group). Significance: *,**p < 0.05 and 0.01 vs ND Asthma by two-tailed t-test, respectively.

Article Snippet: The primary antibodies used were as follows: TXNIP (Novus Biologicals, Littleton, CO, USA, 1:1000 dilution), NOD-like receptor family pyrin domain containing 3 (NLRP3; Bioss Inc., Woburn, MA, USA, 1:1000 dilution), apoptosis-associated speck-like protein containing a caspase-recruitment domain (ASC; Novus Biologicals, 1:1000 dilution), Caspase 1 (full length) (Novus Biologicals, 1:1000 dilution), Cleaved Caspase 1 (Cell Signaling Technology, Danvers, MA, USA, 1:1000 dilution), Pro IL-1β (Novus Biologicals, 1:1000 dilution), and Cleaved IL-1β (Cell Signaling Technology, 1:1000 dilution).

Techniques: Expressing, Immunohistochemical staining, Staining, Control, Standard Deviation, Two Tailed Test, Immunofluorescence, Western Blot

Parkin Deficit or Overexpression in Rat Nucleus Accumbens Changes Aerobic Respiration in Opposite Directions. ( A , B ) Gene set enrichment analysis (GSEA)-enrichment plots showing protein sets from GOBP_AEROBIC RESPIRATION signature significantly overrepresented ( p < 0.05) in parkin knockout (PKO) or parkin overexpression (PO) rat nucleus accumbens, as compared to wild-type nucleus accumbens. ( C , D ) Hierarchical clustering heatmap of the leading-edge proteins from the GOBP_AEROBIC_RESPIRATION ( p < 0.05) in PKO NAc and PO NAc. Three Krebs cycle enzymes, citrate synthase (CS), mitochondrial malonate dehydrogenase (MDH2), and dihydrolipoamide S-succinyltransferase (DLST), were decreased in PKO NAc and increased in PO NAc relative to wild-type NAc (red arrows).

Journal: Biomolecules

Article Title: The Proteomic Landscape of Parkin-Deficient and Parkin-Overexpressing Rat Nucleus Accumbens: An Insight into the Role of Parkin in Methamphetamine Use Disorder

doi: 10.3390/biom15070958

Figure Lengend Snippet: Parkin Deficit or Overexpression in Rat Nucleus Accumbens Changes Aerobic Respiration in Opposite Directions. ( A , B ) Gene set enrichment analysis (GSEA)-enrichment plots showing protein sets from GOBP_AEROBIC RESPIRATION signature significantly overrepresented ( p < 0.05) in parkin knockout (PKO) or parkin overexpression (PO) rat nucleus accumbens, as compared to wild-type nucleus accumbens. ( C , D ) Hierarchical clustering heatmap of the leading-edge proteins from the GOBP_AEROBIC_RESPIRATION ( p < 0.05) in PKO NAc and PO NAc. Three Krebs cycle enzymes, citrate synthase (CS), mitochondrial malonate dehydrogenase (MDH2), and dihydrolipoamide S-succinyltransferase (DLST), were decreased in PKO NAc and increased in PO NAc relative to wild-type NAc (red arrows).

Article Snippet: Proteins were transferred to PVDF membrane (EMD Millipore, Burlington, MA, USA) at 400 mA, blocked with 5% non-fat dried milk dissolved in TBST (10 mM Tris, 150 mM NaCl, and 0.05% Tween-20), and incubated overnight at 4 °C with the following primary antibodies (diluted in 5% milk-containing TBST) against the following proteins: citrate synthase (CS) (NBP2-13878, 1:1000 Novus Biologicals, Centennial, CO, USA), dihydrolipoamide S-succinyltransferase (DLST) (PA5-51794, 1:1000,Invitrogen Life Technologies, Carlsbad, USA), mitochondrial malate dehydrogenase (MDH2) (9610, 1:1000, Cell Signaling, Danvers, MA, USA), dihydrolipoamide dehydrogenase (DLD) (NBP1-31302, 1:1000, Novus Biologicals, Centennial, CO, USA), 2-oxoglutarate dehydrogenase (OGDH) (15212-1-AP, 1:500, Proteintech Group Inc., Rosemont, IL, USA), mitochondrial complex I (mouse anti-NDUFS3 subunit, ab110246, 1: 2000, Abcam Inc., Waltham, MA, USA), complex II (mouse anti-SDHA subunit, ab14715, 1:2500, Abcam Inc., Waltham, MA, USA), complex III (mouse anti-UQCRC2 subunit, ab14745, 1:1000, Abcam Inc., Waltham, MA, USA), complex IV (rabbit anti-subunit IV, 4844, 1:1000, Cell Signaling Technology, Danvers, MA, USA), ß-actin (ab8227, 1:1000, Abcam Inc., Waltham, MA, USA), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (2174, Cell Signaling Technology, 1:2000, Danvers, MA, USA).

Techniques: Over Expression, Knock-Out

Parkin Deficit or Overexpression in Rat Nucleus Accumbens Changes Krebs Cycle Enzyme Levels in Opposite Directions. SDS-PAGE and western blotting showed statistically significant differences between parkin knockout (PKO) and parkin-overexpressing (PO) rats, as well as between these groups and wild-type (WT) controls. ( A ) dihydrolipoamide dehydrogenase (DLST), ( B ) mitochondrial malate dehydrogenase (MDH2), ( C ) 2-oxoglutarate dehydrogenase (OGDH), ( D ) dihydrolipoyl dehydrogenase (DLD), and ( E ) citrate synthase (CS). One-way ANOVA with Holm-Sidak’s post hoc test). * p < 0.05, ** p < 0.01, *** p < 0.001, n = 7/group. The data is expressed as mean ± SEM. ( F ) CS levels show a positive correlation with parkin levels ( p < 0.05, Pearson correlation test). Abbreviations: GAPDH, glyceraldehyde 3-phosphate dehydrogenase.

Journal: Biomolecules

Article Title: The Proteomic Landscape of Parkin-Deficient and Parkin-Overexpressing Rat Nucleus Accumbens: An Insight into the Role of Parkin in Methamphetamine Use Disorder

doi: 10.3390/biom15070958

Figure Lengend Snippet: Parkin Deficit or Overexpression in Rat Nucleus Accumbens Changes Krebs Cycle Enzyme Levels in Opposite Directions. SDS-PAGE and western blotting showed statistically significant differences between parkin knockout (PKO) and parkin-overexpressing (PO) rats, as well as between these groups and wild-type (WT) controls. ( A ) dihydrolipoamide dehydrogenase (DLST), ( B ) mitochondrial malate dehydrogenase (MDH2), ( C ) 2-oxoglutarate dehydrogenase (OGDH), ( D ) dihydrolipoyl dehydrogenase (DLD), and ( E ) citrate synthase (CS). One-way ANOVA with Holm-Sidak’s post hoc test). * p < 0.05, ** p < 0.01, *** p < 0.001, n = 7/group. The data is expressed as mean ± SEM. ( F ) CS levels show a positive correlation with parkin levels ( p < 0.05, Pearson correlation test). Abbreviations: GAPDH, glyceraldehyde 3-phosphate dehydrogenase.

Article Snippet: Proteins were transferred to PVDF membrane (EMD Millipore, Burlington, MA, USA) at 400 mA, blocked with 5% non-fat dried milk dissolved in TBST (10 mM Tris, 150 mM NaCl, and 0.05% Tween-20), and incubated overnight at 4 °C with the following primary antibodies (diluted in 5% milk-containing TBST) against the following proteins: citrate synthase (CS) (NBP2-13878, 1:1000 Novus Biologicals, Centennial, CO, USA), dihydrolipoamide S-succinyltransferase (DLST) (PA5-51794, 1:1000,Invitrogen Life Technologies, Carlsbad, USA), mitochondrial malate dehydrogenase (MDH2) (9610, 1:1000, Cell Signaling, Danvers, MA, USA), dihydrolipoamide dehydrogenase (DLD) (NBP1-31302, 1:1000, Novus Biologicals, Centennial, CO, USA), 2-oxoglutarate dehydrogenase (OGDH) (15212-1-AP, 1:500, Proteintech Group Inc., Rosemont, IL, USA), mitochondrial complex I (mouse anti-NDUFS3 subunit, ab110246, 1: 2000, Abcam Inc., Waltham, MA, USA), complex II (mouse anti-SDHA subunit, ab14715, 1:2500, Abcam Inc., Waltham, MA, USA), complex III (mouse anti-UQCRC2 subunit, ab14745, 1:1000, Abcam Inc., Waltham, MA, USA), complex IV (rabbit anti-subunit IV, 4844, 1:1000, Cell Signaling Technology, Danvers, MA, USA), ß-actin (ab8227, 1:1000, Abcam Inc., Waltham, MA, USA), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (2174, Cell Signaling Technology, 1:2000, Danvers, MA, USA).

Techniques: Over Expression, SDS Page, Western Blot, Knock-Out