EMBO/sd-character-level-ner huggingface dataset:
Figure 1Mouse qPCR array analysis was performed with Colo357 and MiaPaca-2 orthotopic tumor samples treated with saline (control) or 2G8 (n = 3/group) to detect changes of mouse stromal gene expression after treatment. A heat map was generated with ratios of gene expression (2G8 vs. control). ELISA-based Quansys mouse chemokine assay was performed with Capan-1 (Cap), MiaPaCa-2 (Mia), Colo357 (Colo), and C5LM2 (C5) orthotopic tumor samples treated with saline (control) or 2G8 (n = 3/group) to detect mouse chemokine changes after treatment. Change of mouse IL-6 was shown. KIC were treated for 4 weeks and KPC mice were treated for 55 days with Mac84 (control) or 2G8. Tumors from were collected for mouse IL-6 ELISA (n = 6/group). KIC mice were treated for 4 weeks and KPC mice were treated for 55 days with Mac84 (control) or 2G8. The activation of SMAD2 (P-Ser465/467) (E and H-I), STAT3 (P-Tyr705) (F and J-K) and expression of IL-6R (G) was detected by immunohistochemistry (n = 4/group).
Fig.Figure 3A. Coronal HE-stained brain sections of a P18 Mpdz+/+ mouse (out of a total of three) showing the 3rd ventricle, and the proximal and distal sections of the aqueduct of Sylvius; these features are marked by arrows in the insets. B. The same, for P18 Mpdz-/- mice. C. Top views of brains of P7 Mpdz+/+ and Mpdz-/- mice that show the sites of Evans blue injection, and the midline planes (dashed line) sectioned to produce the sagittal images below. They show the extent of Evans blue spread in the ventricles and surrounding tissue (one out of three experiments). In, injection; LV, lateral ventricle; SA, Sylvian Aqueduct; V3, third ventricle; V4, fourth ventricle. Scale bars, 1 mm; insets, 0.25 mm.
Figure 5A, Cell viability of BT308NS, measured 48 h after IR (2 or 5 Gy) in the absence (mock) or in the presence of 10 ng/ml HGF (fold vs. non-irradiated mock treated cells, mock). Ctrl: non-irradiated cells. *: t-test (5 Gy + HGF) vs. (5 Gy), p<0.0001. B, Flow-cytometry analysis of Annexin V/DAPI incorporation in BT308NS irradiated (5 Gy) in the absence (mock) or in the presence of HGF. Histograms show the percentage of Annexin V-positive cells 48 h after IR. Ctrl: non-irradiated cells. C, Cell viability of BT308NS, irradiated in the absence (5 Gy) or in the presence (5 Gy + JNJ) of the MET inhibitor JNJ38877605 (500 nM), and analyzed at the indicated time points. Vehicle: non-irradiated cells (fold vs. vehicle-treated cells at time 0, mock). *: t-test, p<0.01. D, Cell viability as in C, measured 5 days after IR (1-10 Gy, fold vs. vehicle-treated cells, mock). *: t-test, p<0.03. E, Flow-cytometry analysis of Annexin V/DAPI incorporation in BT308NS irradiated (5 Gy) in the absence (vehicle) or in the presence (JNJ) of JNJ38877605. Histograms show the percentage of Annexin V-positive cells 36 h after IR. Ctrl: non-irradiated cells. *: t-test (5 Gy + JNJ) vs. (5 Gy), P=0.01. F, Western blot of BT308NS showing caspase 3 activation (cleaved casp-3), at the indicated time points after IR in the absence (-) or in the presence (+) of JNJ38877605. Vinculin was used as loading control. G, Clonogenic assay with METneg and METhigh subpopulations sorted from BT308NS, irradiated (5 Gy) in the absence (vehicle) or in the presence of MET inhibitors (JNJ38877605 and Crizotinib, 500 nM). Ctrl: non-irradiated cells. *: t-test, p<0.0004. H, LDA (sphere forming assay) with METneg and METhigh subpopulations sorted from BT308NS, measuring GSC frequency after irradiation in the absence (5 Gy) or in the presence (5 Gy + JNJ) of JNJ38877605. Vehicle: non-irradiated vehicle-treated cells. *: 2 test, P=0.0002. I, Flow cytometry analysis of phosphorylated histone H2AX (H2AX) in the whole BT308NS at the indicated time points after IR in the absence (5 Gy) or in the presence (5 Gy + JNJ) of JNJ38877605 (fold vs. non-irradiated cells at time 0, mock). *: t-test, p<0.05. J, Neutral comet assay with BT308NS performed 24 h after IR in the absence (5 Gy) or in the presence (5 Gy + JNJ) of JNJ38877605. Vehicle: non-irradiated vehicle-treated cells. Comet tail's length is proportional to DSB extent. Data are represented as mean ± SEM or ± CI in H.
/6 architecture upon binding of ATP and plasmidDNA.Figure 6A. Crosslinks in the Smc5/6 octamer identified by XL-MS without substrate addition (left panel) and with plasmidDNA and ATP (right panel). As in Fig 1C using ATPase buffer. Only intra- and inter-links of the Smc5/6 dimer are displayed here. Other cross-links are shown in panel (B), (C) B. Crosslinks of Nse3/4 detected by XL-MS. Same experiment as in (A) using the Smc5/6 octamer in ATPase buffer. Cross-links between Nse3 and Nse4 as well as their cross-links to Smc5 and Smc6 are displayed. Lines in black colours indicate cross-links observed with and without substrates, in oranges colours only without substrates and in dashed lines in green colours only with substrate addition. C. Cross-links of Nse1/3/4 to Nse5/6. Same experiment as in (A) and (B). Display as in (B).
Figure 714C accumulation (cpm/mg x ml-1) in HCT116 WT and R248W mutant TP53 cells +-transfected with MRP1 or xCT siRNA following 24h of 14C -APR-246 treatment +/- MK-571 . Indicated values are mean values from four MRP1 siRNAs (n ≥ 3), three xCT siRNAs (n = 1-2) and two control siRNAs (n ≥ 3). Mean 14C -accumulation after treatment and n of individual siRNAs is shown in Table S4 . Data for control and MRP1 siRNA after 14C -APR-246 treatment is also shown in Fig 3D. Growth suppression in HCT116 WT and R248W cells transfected with MRP1 or xCT siRNA after 48h of APR-246 treatment as shown by WST-1 assay. Indicated values are mean values of four MRP1 siRNAs (n ≥ 3), three xCT siRNAs (n =1-2) and two control siRNAs (n ≥ 3). Data for control and MRP1 siRNA after APR-246 single treatment are also included in Fig 1I. Values and n for individual siRNA shown in Fig. S7C. Total intracellular glutathione (GSH + GSSG per 106 cells) in HCT116 WT cells as shown by GR re-cycling assay 48h post transfection of siRNA. Indicated values are means from four MRP1 siRNAs (n = 3), two xCT siRNA (n = 2-3) and two control siRNA (n = 2-3). Total intracellular glutathione (GSH + GSSG per 106 cells) in HCT116 WT and R248W cells measured by GR re-cycling assay after 24h of MK-571 or sulfasalazine (SSZ) treatment (n ≥ 3, except SSZ where n = 2, n indicated by dots). 14C accumulation (cpm/mg x ml-1) in HCT116 WT and R248W cells at 24h treatment with 14C -APR-246, combined with MK-571 or sulfasalazine (SSZ), (n ≥ 4, except SSZ where n = 2, n indicated by dots). Data for 14C -APR-246 +/- MK-571 is also shown in Fig 3C and S3D. Protein concentration of HCT116 WT and R248W assessed by DCTM Protein assay at 24h treatment with APR-246 +/- MK-571 or sulfasalazine (SSZ), or untreated (n ≥ 4, except SSZ where n = 2, n indicated by dots) OVCAR-3 (R248Q TP53) confluence by IncuCyte® during 72h treatment with APR-246 +/- MK-571 or sulfasalzine (SSZ) (n = 3). Part of the data are shown in Fig 1G. Growth suppression in OVCAR-3 cells as determined by IncuCyte® during 72h treatment with APR-246 +/- MK-571 or sulfasalazine (SSZ) depicted as heatmaps (n = 3).
Figure 1(A) Total lysates of different mouse organs underwent immunoblotting analysis using anti-Pdia4 and anti-actin antibodies. Data information: Data from 3 experiments are presented as the mean ± SD. (B) Confocal analysis of Pdia4 and insulin (Ins) or glucagon (Gcg) in mouse islets. The tissues were stained with the indicated antibodies and analyzed using a confocal microscope. Scale bar = 100 μm. Data information: Data from 3 experiments are presented as the mean ± SD. (C) Min6 cells were treated with glucose and palmitate at the indicated dosages. Total lysate underwent immunoblotting analysis using the indicated antibodies. (D) Human islets were treated with glucose and palmitate at the indicated dosages, followed by immunoblotting analysis. ( Data information: Data from 3 experiments are presented as the mean ± SD. (E) The islets of WT BKS and diabetic Leprdb/db mice underwent immunoblotting analysis. Data information: Data from 3 experiments are presented as the mean ± SD. (F) IHC analysis of the islets from Leprdb/db and Lepob/ob mice at the indicated ages using anti-Pdia4 antibody and hematoxylin. Scale bar = 100 μm. The dash circles indicate islet regions. Data information: Data from 3 experiments are presented as the mean ± SD. (G) Sera from wild-type (WT) BKS and Leprdb/db mice, aged 4, 8, and 18 weeks, B6 mice, fed with a normal diet (ND) and a high fat diet (HFD) for 4 weeks, and humans, healthy volunteers and diabetic patients (T2D), were quantified for Pdia4 level using an anti-Pdia4 ELISA kit. Data information: Data from 3 experiments more are presented as the mean ± SD. One-way ANOVA test was used for statistical analysis of differences between groups, and P (*) < 0.05; P (**) < 0.01 and P (***) < 0.001 are considered statistically significant. (H) Immunoblotting analysis of Pdia4 and markers in the cytosolic (Cyto), nuclear (Nuc), membrane (Mem), mitochondrial (Mito), and ER compartments of Ming 6 cells using the indicated antibodies. Data information: Data from 3 experiments are presented as the mean ± SD.
a) Endogenous STUB1 protein is downregulated at replicative senescence.f3(a) Endogenous STUB1 protein is downregulated at replicative senescence. Immunoblot was performed using early-passage (Y) and replicatively senescent (S) fibroblasts (the same set of cells without treatment as in Fig. 1c). (b) STUB1 mRNA is downregulated at replicative senescence. The same set of cells as in a were examined by qRT-PCR. Data were from triplicate experiments (mean±s.d.). *P0.01; **P0.001 (Student's t-test). (c) Knockdown of STUB1 represses Δ133p53α. MRC-5 fibroblasts (30 PDLs) were transfected with two siRNAs against STUB1 (no. 1 and no. 2) and control siRNA. At 4 days after transfection, immunoblots were performed using anti-STUB1, anti-Δ133p53α, DO-1 (detecting full-length p53), CM1 (detecting both Δ133p53α and full-length p53), anti-p62/SQSTM1 and anti-β-actin antibodies. (d) STUB1 knockdown inhibits cell proliferation. MRC-5 fibroblasts (30 PDLs) were seeded on six-well plates on day 0 (4 × 104 cells per well in 6-well plate; nine wells for each siRNA). Cells were counted on days 1, 4 and 7 (three wells each; mean±s.d.), while siRNA transfection was performed on days 1 and 4. *P0.01 (Student's t-test). (e) STUB1 knockdown induces cellular senescence. The siRNA transfection was performed as in c and repeated 4 days later, followed by incubation for 3 days and SA-β-Gal staining. Percentages of SA-β-Gal-positive cells were from triplicate experiments (mean±s.d.). **P0.001 (Student's t-test). (f,g) STUB1 knockdown upregulates p21WAF1 and IL-8. The same set of cells as in e were examined in qRT-PCR for p21WAF1 mRNA (f) and IL-8 mRNA (g). Data were from triplicate experiments (mean±s.d.). **P0.001 (Student's t-test). (h) Δ133p53α rescues STUB1 knockdown-induced senescence. MRC-5 fibroblasts were transfected with STUB1 siRNA (no. 1) as in e. At the next day after the second transfection (on day 5), the cells were transduced with a lentiviral vector driving Δ133p53α or its vector control. At 5 days after the lentiviral transduction, the cells were stained for SA-β-Gal activity. Representative pictures (left) and quantitative data (right) are shown. Percentages of SA-β-Gal-positive cells were from triplicate experiments (mean±s.d.). **P0.001 (Student's t-test).
Figure 1Schematic representation of the B. cereus endospore. IM: inner membrane, OM: outer membrane. Together, spore core, IM, spore wall, cortex, OM and spore coat make the spore body, surrounded by the exosporium. S- and L-Ena represent staggered and ladder type endospore appendages - see this study Negative stain TEM image of B. cereus NVH 0075-95 endospore, showing spore body (SB), exosporium (E), and endospore appendages (Ena), which emerge from the endospore individually or as fiber bundles. At the distal end, Enas terminate in a single or multiple thin ruffles (R). Schematic drawing of S- and L-Ena appearance and their orientation relative to the spore. cryoEM images (left) and negative stain 2D class averages of single S-Ena (E) and L-Ena (F) fibers. S-Ena show ~100 Å diameter and a helical or staggered appearance with a ~37 Å rise, whereas L-Ena have a ~80 Å diameter and appear as stacked disks of ~40 Å height and ~60 Å translation along the fiber. L- and S-Ena show, respectively, a single or multiple ruffle(s) (black arrow, labeled 'R') at the distal end of fiber. Length distribution of S- and L-Enas and number of Enas per endospore (inset), (n=1023 individual Enas, from 150 endospores, from 5 batches). Dashed and dotted lines show median and first (lower) and third (upper) quartile, resp. See also Fig EV1.
Figure 5De novo shoot regeneration using Col and scr mutants; scr-3 (A and B) and scr-6 (A and C). Explants with shoots were scored at indicated days on SIM using Col and scr-3 root explants that had been pre-incubated on CIM for 2 w (B) or Col and scr-6 hypocotyl explants that had been pre-incubated on CIM for 1 w (C). Scale bar: 1 mm. De novo shoot regeneration of Col, wox5-3, scr-3, and wox5-3 scr-3. The percentage of root explants with shoots (E) and the number of shoots per root explant (F) were scored at 15 d on SIM. The explants had been pre-incubated on CIM for 2 w before transfer onto SIM. Scale bar: 1 cm. Transcript levels of PLT1 (G) and PLT2 (H) in Col, wox5-3, scr-3, and wox5-3 scr-3 roots (R), 1 w CIM explants (C), and 1 w CIM + 2 w SIM explants (S2W) as determined by RT-qPCR. Levels of Col R were set to 1 after normalization with UBQ10.
c-Maf regulates Th2-associated gene expression in ILC2s.Figure 5(A) Principal component analysis of c-Maf knocked-down (empty circles) and WT (filled circles) mILC2s, performed using all genes (n=13855) detected by mRNA sequencing. Numbers indicate mouse IDs. (B) Volcano plot showing genes more expressed in mILC2s purified from Id2-CreERT2-c-Maffl/fl mice (dark red), genes more expressed in mILC2s purified from Id2-CreERT2+c-Maffl/fl mice (dark blue), and genes not significantly differentially expressed (grey). The horizontal dashed line depicts the significance threshold at BH-adj. p-value=0.02, while the vertical dashed lines depict an absolute log2(fold change) threshold=1. (C) Over-representation analysis of genes defining Th2, Th1 and Th17 cells (see Supplementary Table EV2 for a list of genes included in each signature) either for genes upregulated or downregulated in c-Maf WT ILC2s versus c-Maf knocked-down ILC2s. (D) Genomic location of the top matches (red rectangles) of the mouse c-Maf binding profile (shown at the top) and of the MARE sequence identified by (Ho et al, 1996). Motif search was performed within 2 types of regions (purple rectangles): 1) The promoters of IL-4, IL-5 and IL-13, and 2) within open chromatin regions identified in 2 replicates of lung ILC2s or lung Th2 cells (dark blue tracks). The ATAC sequencing data (shown as bigwig coverage tracks) was retrieved from GEO (GSE77695). For each match of the c-Maf binding motif, numbers in parentheses indicate the log-likelihood ratio score and the raw p-value calculated by the FIMO tool. The transcripts of each gene are shown at the bottom of each panel. Mouse genome = mm9 and Integrative Genomics Viewer = v.2.8.0 (E) ChIP-qPCR analysis of c-Maf occupancy on IL-4, IL-5 and IL-13 promoters in untreated mouse and human ILC2s (IL-2 stimulation) and in mouse and human ILC2s treated with IL-33 (n=3 biological replicates). (F) Dot plot showing over-represented Gene Ontology gene sets among genes upregulated in wildtype compared to c-Maf knocked-down ILC2s. The color scale depicts the adjusted p-value, while the size of the dots and x-axis depict the absolute number or the proportion of upregulated genes included in each gene set, respectively. (G) Sum of z-scores per sample of all genes upregulated in ST2+ Th2 cells and memory CD8 T cells (see Supplementary Table EV2 for a list of genes). The central band indicates the median, the box encompasses the interquartile range, and the whiskers reach the values that are within a distance of 1.5 times the interquartile range (either from the lower or upper quartile). The heatmap shows the z-scores of memory CD8 T cell genes significantly downregulated in c-Maf knocked-down ILC2s.
WIPI2 Binds Atg16L1 though R108E and R125E in a Solute-Exposed Cleft in WIPI2.Figure 4(A) Lysates from HEK293A cells transiently expressing GFP, GFP-WIPI1a, GFP-WIPI2a, GFP-WIPI2b, or GFP-WIPI2b FTTG mutant were used for GFP-Trap. Endogenous Atg16L1 binding was analyzed by immunoblot.(B) Statistical analysis of (A) was performed by one-way ANOVA with Tukey's posttest. SEM for n = 3. ∗p < 0.05. (C) Model of WIPI2b based on crystal structure of Kluyveromyces marxianus Atg18 (Protein Data Bank ID 3VU4) (Watanabe et al., 2012). The β1-β2 loop colored yellow is the site of an18 aa insertion in WIPI2a. (D) GFP-Trap from HEK293A cells transiently expressing GFP, GFP-WIPI1a, GFP-WIPI2b, GFP-WIPI2b R108E, GFP-WIPI2b R125E, or GFP-WIPI2b R108E R125E was mixed with in vitro translated 35S-labeled FLAG-Atg16L1 and analyzed by autoradiography. (E) Lysates from HEK293A cells transiently expressing GFP, GFP-WIPI2b, GFP-WIPI2b ΔCT, GFP-WIPI2a, GFP-WIPI1a, or GFP-WIPI1a ΔCT were used for GFP-Trap. Endogenous Atg16L1 binding was analyzed by immunoblot.(F) Statistical analysis of (E) was performed by one-way ANOVA with Tukey's posttest. SEM for n = 2. ∗p < 0.05. (G) Lysates from HEK293A cells transiently expressing GFP-WIPI2b WT, GFP-WIPI2b R108E, R125E, or R108E R125E were mixed with lysates from HEK293A cells transiently expressing FLAG-Atg16L1 WT, E226R, E230R, or E226R E230R in all possible permutations. Protein complexes from mixed lysates were immunoprecipitated using GFP-Trap, followed by immunoblot analysis.(H) Statistical analysis of (G) was performed by one-way ANOVA with Tukey's posttest. SEM from n = 3. ∗p < 0.05. (I) CLEM analysis of HEK293 cells treated with siRNA to WIPI2 were transfected with GFP-WIPI2b RERE and starved in EBSS. Bright-field image (top), GFP-WIPI2 RERE signal (middle), TEM of selected cell (bottom). Boxed area shown in (J). Scale bars represent 10 μM for bright-field and confocal and 5 μM for TEM.(J) High-magnification TEM of boxed area in (I). Arrows indicate open phagophores in the vicinity of ER and mitochondria (M), which contain GFP-WIPI2b RERE. See also Figures S4 and S5 and Table S1.
Loss of acetylated histones is independent of transcription inhibition.Figure 4(A) Representative western blots of histone acetylation levels of HeLa cells lysed at indicated time points after UV irradiation (16 J/m2, left panel), α-amanitin (second panel, 100 µg/ml), THZ1 (third panel, 1 μM) or flavopiridol (right panel, 1 μM) treatment. Blots were stained with α-acetyl-lysine (top panel), α-histone H4 (middle panel) and α-tubulin (bottom panel) (B) Quantified histone acetylation levels, normalized against histone H4 levels for quantification. Average of at least 3 experiments. Error bars represent SEM. Significant differences between UV-irradiated and inhibitor treated conditions are indicated with * (p<0.1) (C) Representative western blots of histone acetylation levels of HeLa cells pre-treated with transcription inhibitors (mock (left), THZ1 (middle, 1 μM) or flavopiridol (right, 1 μM) an hour before UV irradiation and lysed at the indicated time points after UV (16J/m2). Blots were stained with the indicated antibodies (D) Quantification of α-acetyl-lysine signal, normalized against histone H4 levels. Average of 5 experiments. Error bars represent SEM. Significant differences, calculated by T-test, between UV treated and mock treated conditions are indicated with * (p<0.1), ** (p<0.05) and *** (p<0.01)
Isoform specificity of neurexin-neurexophilin interactions.Figure 5Comparison of binding affinities of Nxph1 binding to different Nrxn1-3 LNS2 isoforms. Comparison of binding affinities for Nxph3 binding to Nrxn1-3 LNS2SS2-.
Figure 1 (A) Fractionation of nuclear and cytosolic compartments using a standard NP-40 lysis protocol and immunoblotting with chaperone specific antibodies  (B) Immunofluorescence of histone chaperones in fixed cells using the same antibodies used in (A). Cells are segregated into those undergoing replication and those that are not. Scale bar represents 5 μm  (C) Quantification of nuclear localisation shown in (B). Boxes represent the lower quartile, median and upper quartile. Whiskers represent 1.5 times the interquartile range (D) Real-time imaging of cells undergoing biochemical fractionation. sNASP is tagged with mCherry, whilst LamnA/C is tagged with EGFP. The left column of panels represents a maximum intensity projection. The time course on the right represents a plane in the z dimension reconstructed from 20 z-stacks penetrating 20 μm into the medium. Scale bars represent 5 μm  (E) Quantification of nuclear leakage shown in (D). Z-stacks were flattened using a maximum intensity projection with the nuclear fluorescent signal over time plotted as a percentage of maximum (normalised). Data points represent the mean of 15 measurements with error bars representing the s. e. m.
Figure 4A) Volcano plot showing the expression changes with a minimal fold change of 3 (FC=3) at genome-wide levels in AhCre Eed-/- crypts relative to AhCre Eed+/+ crypts 15 days after β-naphthoflavone administration. B) Bar plot showing the percentage of H3K27me3-positive promoters among the differentially regulated genes in Eed-/- crypts. All gene promoters and 5 independent random sampling of 167 gene promoters extracted the mouse genome are presented as specificity controls. C) Intensity profiles for H3K27me3 and SUZ12 occupancy at the promoters of up-regulated genes with respect to down-regulated genes in Eed-/- crypts. D) Genomic snapshots of the Cdkn2a locus showing SUZ12 occupancy and H3K27me3 deposition at the promoter regions of both the p16 and the ARF isoforms. E) Genomic snapshots of the RNAseq profile of the Cdkn2a locus in AhCre Eed+/+ and AhCre Eed-/- crypts 15 days after β-naphthoflavone administration. F) Expression analysis by qRT-PCR (mean ± SD) of both Cdkn2a isoforms (p16Ink4A and p19Arf) in AhCre Eed+/+ and AhCre Eed-/- crypts 15 days after β-naphthoflavone administration. G) Gene set enrichment analysis (GSEA) using specific secretory and enterocytic transcriptional signatures with respect to the list of up-regulated genes in Eed-/- crypts.
MICAL1 can oxidize Tpm-saturated filaments and does not affect Tpm unbinding.Figure 3A. Time-lapse images of Tpm-saturated actin filament depolymerizing from their barbed end (BE), with or without MICAL1. Depolymerization is initiated at time t=0 from a non-oxidized actin filament. The increase in the depolymerization rate reflects the oxidation of actin with time. Tpm is labeled with neonGreen (nGr), and actin is unlabeled. B. Barbed end depolymerization rate as a function of the exposure time to either 100 nM nGr-Tpm1.8 alone ("no MICAL1"), or supplemented with 100 nM MICAL1 and 12 µM NADPH. N = 31 (1 experiment) and 29 (1 experiment) filaments, without and with MICAL1, respectively. Lines: mean velocity. Shaded surfaces: S.D. C. Time-lapse images showing the disassembly of Tpm domains. Filaments were saturated with 100 nM nGr-Tpm1.8 before the experiment and Tpm was removed from solution at time t=0 (the solution contains 0.6 µM unlabeled G-actin to prevent filament depolymerization). PE and BE indicate F-actin pointed and barbed end, respectively. D. Disassembly rate of single Tpm domains, at boundaries located towards the pointed end (PE) and towards the barbed end (BE) of actin filaments. N = 100 (non-oxidized F-actin, 4 experiments) and 50 (oxidized F-actin, 2 experiments) domains per direction. Bars: mean and S.D. P-value (t-test) = 0.27 (BE) and 0.12 (PE).