EMBO/sd-character-level-ner huggingface dataset:
Mitosis is more frequent at the PS, and PS mitotic rounding is not always apical.Figure 4(a) Graphic representation of a transverse section from an E6.5 embryo. The epiblast is divided in three distinct regions: anterior (red), posterior (green) and PS (blue). The PS region is defined as the area where the basement membrane (yellow) is degraded. b) Representation of cell and mitosis disposition at the PS. Apical mitoses are in red, non-apical mitoses in cyan and mesenchymal mitoses in green. Mitosis is considered non-apical when occurring away from the epiblast apical border at a minimum distance corresponding to the size of one nucleus (± 10μm), in a cell that has not crossed the perforated basement membrane, retains its apical attachment and does not display a mesenchymal phenotype. (c) Z-projections of transverse sections from E6.5 (top), E6.75 (mid) and E7 (bottom) embryos. Samples were stained for F-actin (Phalloidin, grey) and mitosis (Phh3, magenta) on the left and nuclei (DAPI, cyan) and basement membrane (collagen IV, yellow) on the right. Yellow arrowheads show non-apical mitosis. White arrows delimitate borders of the basement membrane degradation region. A: anterior, P: posterior. (d) Mitotic Index (Phh3/DAPI) in percentage at the anterior, posterior, and PS regions of E6.5 (top), E6.75 (mid) and E7 (bottom) embryos. The posterior region quantification excludes counts from the PS region. (e) Ratio of non-apical mitosis (non-apical Phh3/ Phh3, normalized by number of nuclei) in percentage at the anterior, posterior, and PS regions of E6.5 (top), E6.75 (mid) and E7 (bottom) embryos. (f) Violin plots representing the distribution of cells in G2/M phase in cells with high, compared to low, Brachyury expression, among cells annotated as primitive streak and mesoderm harvested from E6.5, E7, and E7.25 embryos. Violin plots are overlaid with white box plots marking 25th percentile, median and 75th percentile.
Figure 4A. Graph showing the relative abundance of undigested DNA (145 bp) as a function of time during digestion with micrococcal nuclease (MN-ase) for the CENP-A nucleosome (red), the CENP-A/CENP-CCR complex (blue) and the CENP-A/CENP-Cmotif complex (black). B. Overlay of three cryoEM maps (grey, blue and green) of the CENP-A nucleosome obtained by sorting on the DNA entry/exit site (Figure EV2F). Distance between most open (grey) and most closed (green) map is 2 Å. The entry/exit site is boxed and the corresponding model is shown on the right. Note that the density of the H2A C-terminus is well defined. C. Overlay of three cryoEM maps (grey, blue and green) of the CENP-A/CENP-CCR complex obtained by sorting on the DNA entry/exit site (Figure EV4F). The distance between the most open (grey) and most closed (green) maps is 9 Å. Map assigned to CENP-CCR is shown in magenta. The entry/exit site is boxed and the corresponding model is shown on the right. Note the absence of a clearly defined density of the H2A C-tail (indicated by the dotted circle). D. Same type of data as in (A) for the CENP-A nucleosome assembled with tailless H2A (H2A, 1-109) alone (pink) and in complex with CENP-CCR (light blue). E. Schematic representation of the interplay between the N-terminus of H3 or CENP-A and the C-terminus of H2A in regulating flexibility of nucleosomal DNA wrap. DNA (cyan); longer H3 αN (green); shorter CENP-A αN (red); H2A C-terminus (yellow); CENP-C (magenta).
SCOC regulates FEZ1's interaction with the ULK1 complex.Figure 6(A) FEZ1 interacts with both the kinase domain (1-278) and the proline-serine rich spacer of ULK1 (279-828). GFP‐ or Myc‐tagged ULK1 fragments were in vitro translated with 35S‐methionine and subjected to GST‐pulldown assays using GST and GST-FEZ1 purified from E. coli (bottom). Bound proteins were detected by autoradiography following SDS-PAGE (top). (B) ULK1 interacts with FEZ1. ULK1 was immunoprecipitated from HEK293 lysates with anti‐ULK1 and bound ULK1 and FEZ1 were detected with anti‐ULK1 and anti‐FEZ1 antibodies. Input lysate (Inp). (C) The FEZ1-GFP and Myc-ULK1 interaction is unaffected by amino‐acid starvation. Anti‐Myc and ‐GFP blots after HEK293 cells were co‐transfected with FEZ1-GFP and Myc-ULK1, incubated in FM or ES for 2 h, harvested and the complex was immunoprecipitated using anti‐GFP antibody. (D) BN-PAGE reveals SCOC and FEZ1 are in a complex. FEZ1-GFP, FLAG-SCOC and Myc-ULK1 wild type or kinase‐inactive ULK1K46I (ULK1KI) were co‐expressed in HEK293 cells. Anti‐GFP, ‐FLAG and ‐Myc western blots are shown for the BN-PAGE gel (top) or the SDS-PAGE gel (bottom). In GFP and FLAG western blots, two different exposures of the same BN-PAGE blot are shown spliced together. (E) siRNA depletion of ULK1 does not affect the interaction of FEZ1 with SCOC. RF or ULK1 siRNA‐treated cells were co‐transfected with FEZ1-GFP and FLAG-SCOC, then incubated and immunoprecipitated as in (C). Western blot of lysates for ULK1, GFP and FLAG, and immunoprecipitates with GFP and FLAG antibodies. (F) siRNA depletion of SCOC reduces FEZ1-ULK1 complex. HEK293 cells treated with either SCOC or ULK1 siRNAs were transfected with FEZ1-GFP. FEZ1-GFP was detected with anti‐GFP in both BN-PAGE and SDS-PAGE. Endogenous ULK1 was detected with anti‐ULK1 antibody. Arrowheads indicate a FEZ1-GFP and endogenous ULK1 complex at 200 kDa and a larger MW complex >1236 kDa also detected in (D) in the triple transfection. The 200 KDa complex is sensitive to loss of SCOC and ULK1. (G) SCOC can reduce the interaction of ULK1 with MBP-FEZ1. Immobilised MBP-FEZ1 was incubated with in vitro 35S‐methionine‐labelled Myc-ULK1. Addition of increasing amounts of in vitro translated 35S‐methionine SCOC reduced the amount of Myc-ULK1 bound. Top and bottom panels are as described in (A).
Figure 5A Representative images of 1205 cells cultivated on collagen-I (Coll-I) or FRC-derived ECM for 48 h prior treatment with vehicle or 5 µM BRAFi or 2 µM BRAFi plus 0.01 µM MEKi for 96 h. Immunofluorescence for Phospho-DDR1 (P(Y792)-DDR1) (red; left panels) and Phospho-DDR1/2 (P(Y796)-DDR1/P(Y740)-DDR2) (red; right panels), F-actin (green) and nuclei (blue) is shown. Enlarged images of P-DDR1 and P-DDR1/2 immunostaining are shown. White arrows indicate P-DDR1 and P-DDR1/2 cell membrane linear clustering. Scale bar, 25 µm (enlarged images: scale bar, 10 µm). B Quantification of globular versus linear clusters of Phospho-DDR1 (left panels) and Phospho-DDR1/2 (right panels) from immunofluorescence staining shown in (A) using Image J software. Prior the quantification of DDRs clusters a "subtract background" function of ImageJ has been applied to all images. In order to quantify clusters, the IsoData threshold has been used. Clusters with circularity 0.3 to 1 has been defined as "globular" and clusters with circularity 0 to 0.29 has been defined as "linear". Data are from >20 individual cells (n = 3). Error bars reflect mean ± s.d. Values for each treated condition are compared to the vehicle control. 2way ANOVA followed by Dunnett's multiple comparisons test. C Quantification of globular versus linear clusters of Phospho-DDR1 and Phospho-DDR1/2 from immunofluorescence staining shown in Fig EV4A of 1205Lu cells cultivated on HDF- or MAF-derived ECM and treated with the indicated targeted drugs as described in (A). Data are from >20 individual cells. Error bars reflect mean ± s.d. Values for each treated condition are compared to the vehicle control. 2way ANOVA followed by Dunnett's multiple comparisons test.
Figure 1A. H3122 cells expressing endogenous EML4-ALK V1 and HEK293 transfected with YFP-EML4-ALK V1 WT and KD were stained for either anti-ALK or anti-GFP (green), anti-α-tubulin (red), and DAPI (blue). Scale bars, 10 μm; magnified views of a selected area are shown. B. Violin plots showing the number of EML4-ALK V1 cytoplasmic foci per cell. Data represents 30-50 counts from three biological replicates. ***P<0.001, ****P<0.0001 in comparison to HEK293 YFP-EML4-ALK-V1 KD by one-way ANOVA analysis. C. H2228 cells expressing endogenous EML4-ALK V3 and HEK293 transfected with YFP-EML4-ALK V3 WT and KD were stained for either anti-ALK or anti-GFP (green), anti-α-tubulin (red), and DAPI (blue). Scale bars, 10 μm; magnified views of a selected area are shown. D. Violin plots showing the number of EML4-ALK V3 cytoplasmic foci per cell. Data represents 30-50 counts from four biological replicates. ***P<0.001, ****P<0.0001 in comparison to HEK293 YFP-EML4-ALK-V3 KD by one-way ANOVA analysis. E. Time-lapse imaging of transfected HEK293 YFP-EML4-ALK V1 WT to observe the movement of cytoplasmic foci. Representative still images are shown of an area of cytoplasm containing YFP-EML4-ALK V1 WT and V3 WT foci at the times indicated. Scale bar, 1 μm. F. Time-lapse imaging of transfected HEK293 YFP-EML4-ALK V3 WT to observe the movement of cytoplasmic foci. Representative still images are shown of an area of cytoplasm containing YFP-EML4-ALK V1 WT and V3 WT foci at the times indicated. Scale bar, 1 μm. G. Kymographs showing the movement of YFP-EML4-ALK V1 WT, YFP-EML4-ALK V3 WT and YFP-EML4-ALK V3 KD over the duration of the observation period. Scale bars; 1 μm horizontal; seconds vertical. H. Whisker plot showing the calculated velocity of single events in the kymograph. Data represent 20 counts from 10 kymographs. n=2. Error bar represents SD of two biological replicates. *P< 0.05 in comparison to YFP EML4-ALK V3 KD by unpaired t test.
DNA with a 3' overhang stimulates SUMO modification of RPA by Siz2.Figure 2SUMO conjugation assays performed under multiple turnover conditions using Siz2∆CT and different RPA-DNA complexes. SDS-PAGE gels were stained with Coomassie. Bands for Mw marker are fully annotated in Figure 1B.
Figure 6WT and Spata2 CRISPR knock out (KO) iBMDMs stably expressing GFP-ASC were pretreated with DMSO or PLK4 inhibitor Centrinone at a concentration of 150nM for 2 days, primed with LPS, and stimulated with Nigericin for 1 h. GFP-ASC specks were imaged by confocal microscope, and percentage of ASC speck-positive cells was quantified. Co-immunoprecipitation analysis of NEK7/NLRP3 interaction in iBMDMs stably expressing Flag-NEK7 that were transduced with control or PLK4-specific shRNA. The cells were untreated, primed with LPS, or primed with LPS and stimulated with Nigericin. Flag-NEK7 was immunoprecipitated and the association of endogenous NLRP3 was assessed by immunoblot analysis. Relative levels of NLRP3 in immunoprecipitates were normalized to Flag-NEK7 and shown below. Co-immunoprecipitation analysis of NEK7/NLRP3 interaction in HEK293 cells transfected with HA-NEK7 and Flag-NLRP3 along with (+) or without (-) GFP-PLK4. The cells were either treated (+) or not treated (-) with the PLK4 inhibitor Centrinone. iBMDMs stably expressing Flag-tagged NEK7 or NEK7 mutant S204A were treated with LPS. Anti-Flag immunoprecipitates were prepared for immunoblot analysis for the interaction between NEK7 and endogenous NLRP3. Immunoblot analysis of active caspase-1 (p20) in supernatants (Sup) and the indicated proteins in cell extracts (Cell ext) of iBMDMs stably expressing WT NEK7 or NEK7 mutant (S204A), primed with LPS and stimulated with nigericin. iBMDMs stably expressing Flag-tagged WT NEK7 or NEK7 mutant S204A were left untreated or stimulated with LPS for indicated time. Anti-Flag immunoprecipitates were prepared for immunoblot analysis for NEK7 phosphorylation at Ser 204 (P-NEK7). iBMDMs stably expressing Flag-tagged WT NEK7 were left untreated or pretreated with PLK4 inhibitor Centrinone, and stimulated without or with LPS for 4h. Anti-Flag immunoprecipitates were prepared for immunoblot analysis for NEK7 phosphorylation at Ser 204. iBMDMs stably expressing GFP-tagged PLK4 and parental iBMDMs were left untreated or stimulated with LPS for 4h. Anti-GFP immunoprecipitates were prepared for immunoblot analysis for the interaction between GFP-PLK4 and endogenous NEK7.
Figure 5A Oligomers assembled from H1-nucleosomal arrays were stained with DAPI and examined using FM. Shown are representative images obtained in 4 mM and 5 mM MgCl2.B Control FM images obtained in 0, 1 and 3 mM MgCl2. C H1-nucleosomal array oligomers were negatively stained and visualized by TEM. Shown in the left panel is a representative image obtained in 4 mM MgCl2. Shown in the right panel is an image of the interior of the oligomer (white arrow, left panel) after cropping and re-scaling.
Figure 7A Phos-tag band-shift assay of Hog1 phosphorylation. KT235 (ΔS/O/H/M ssk2/22Δ hog1Δ STE11-Q301P) was transformed with pRS416-Hog1 (WT) or its indicated mutant derivatives. Cell extracts were prepared from fresh cultures without applying osmostress. For each HOG1 mutant plasmid, three independent cultures were assayed. Data information: Error bars are SEM (n=3). B. the yeast strains KT260 (ssk2/22Δ ste11Δ hog1Δ), KT235 (ΔS/O/H/M ssk2/22Δ hog1Δ STE11-Q301P), and KT248 (ΔS/O/H/M ssk2/22Δ hog1Δ pbs2Δ) carrying YCplac22I'-Pbs2-DD, were used. Data information: Error bars are SEM (n=3). C. KT250 (ΔS/O/H/M ssk2/22Δ hog1Δ STE11-WT) and KT235 (ΔS/O/H/M ssk2/22Δ hog1Δ STE11-Q301P) were transformed with pRS416-Hog1 (WT) or pRS416-Hog1-N149H D162G (N149H D162G) together with pRS414-8xCRE-lacZ. Expression of the Hog1 reporter gene 8xCRE-lacZ in the absence of osmostress was assayed. Data information: (C) Error bars are SEM (n=4). D. KT248 (ΔS/O/H/M ssk2/22Δ hog1Δ pbs2Δ) was transformed with pRS416-Hog1 (WT) or its indicated mutant derivatives together with pRS414-8xCRE-lacZ. Expression of the Hog1 reporter gene 8xCRE-lacZ in the absence of osmostress was assayed. Data information: Error bars are SEM (n=3). E-F. Phos-tag band-shift assay of Hog1 phosphorylation. Yeast strains of the indicated genotypes (shown below the graph) were transformed with pRS416-Hog1 (WT) or its indicated mutant derivatives (shown inside the graph). Strain used: (E) FP4, KT259, KT260, KT292, and KY523; and (F) KY523, KT293, KT294, and KT295. N/H, N149H; D/G, D162G. Data information: Error bars are SEM (n=3). G. A schematic model showing that the lack of osmotic enhancement of the Pbs2-Hog1 reaction prevents the basal Hog1 activation.
a, Tumour volume before/after KRas ablation (+/−KRas) (n = 6).f1a, Tumour volume before/after KRas ablation (+/−KRas) (n = 6). b, Histology depicting tumour remnants (×10). c, Immunofluorescence of KRas-expressing tumour (+KRas), regressed tumour (−KRas) and regressed tumours 48 h after KRas re-activation (−KRas re-ON) for Ki67 (red), CD44 (green) and 4′,6-diamidino-2-phenylindole (DAPI; blue) (×40). d, Limiting dilution transplantation, TIC frequency. Genetic model: +KRas (black) versus -KRas (grey) ex vitro (n = 4) or ex vivo (n = 2). Pharmacological downregulation: control (black) versus treated spheres (grey; AZD8330 plus BEZ235 (AZD+BEZ)) (n = 2). Ctrl, control. e, Exome sequencing: allele frequencies after KRas re-activation in SCs (Re-ON) versus KRas-expressing cells (Reference) at 40,383 and 44,182 SNVs for two independent tumours. f, Annexin V in spheres +/−KRas with respect to CD44/CD133 expression. Percentage of live, apoptotic (Apo) and necrotic (Nec) cells are reported (n = 3). g, Immunohistochemistry of −KRas tumours for CD44 (blue) and CD133 (red) (×20-40). h, Immunophenotyping of +/−KRas tumours for CD44/CD133/aldefluor. i, GSEA of pathways enriched in −KRas versus +KRas cells. Normalized enriched scores (NES) are reported. Data are mean ± standard deviation (s.d.).
Figure 8 (A) Representative immunoblots of mitochondrial lysates of HEK cells separated on a 20-42.5% iodixanol gradients probed for LETM1, PDH and TFAM  (B) Left panel: immunoblot analysis of total PDH protein levels and the inactive phosphorylated (repressed form), PDHS293, in control (C1, C3), WHS LETM1+/- (S1, S3, S4) and WHS LETM1+/+ (S5) fibroblasts. Center and Right panels: Immunoblot analysis of PDK3 in control (C1-C3), WHS LETM1+/- (S1, S3 and S4) and WHS LETM1+/+ (S5) fibroblasts  (C) Left panel: change in cell confluence of control (C1-C3), WHS LETM1+/- (S1-S4) and WHS LETM1+/+ (S5) fibroblasts grown in BHB over the course of 188 h. Data are expressed as means ± SEM of n=3 independent experiments. Right panel: images of control and WHS LETM1+/- S4 cells growing either in the presence of 25 mM glucose (HG) or BHB (KB) for 6 days. Scale bar 300 µm  (D) Confocal images of control cells (C1) grown for 24 h in the presence of BHB and immunolabeled with anti-TOM20 (red) and anti-DNA (green), and DAPI stained (blue)  (E) Proportion of cells that displayed mtDNA aggregation during the KB treatment (panel i - control cells (C1, C2), and WHS LETM1+/+ (S5) fibroblasts; panel ii - LETM1+/- (S1, S2, S4) fibroblasts). At least 50 cells per cell line were counted at the indicated time points. Data are expressed as mean ± SEM of n=3 independent experiments
Figure 5(A) Precursor frequency in CLK21, CLK09 and CLK19 adoptively transferred mice. 8-weekold CD45.1 mice were adoptively transferred with 5×105, 1×105 or 2×104 CD45.2 B cells from CLK21, CLK09 or CLK19 KI mice one day before immunization with eOD-GT8 60mer. 12h post adopt transfer, splenocytes were isolated and detected by FACS. X-axis represents the cell number of transferred CD45.2 B cells, y-axis represents the precursor frequency which is defined as (Number of CD45.2 binders)/(Number of B cells) for three lines. Each circle represents each mouse in each group. n=2-4 mice/group for CLK21 and CLK09; n=3 mice/group for CLK19. Bars indicate mean ± SD from mice in each group. (B) CD45.2 frequency within GCs on Day 8 in CLK adoptively transferred mice with different precursor frequency. Adoptively transferred mice with different precursor frequency were immunized with eOD-GT8 60 mer, on Day 8, the splenocytes were isolated and the CD45.2 populations were detected by FACS with the marker SSL+B220+CD95+CD38-CD45.2+. Gated plots represent the CD45.2 frequency within GCs. (C) Quantification of the frequency of CD45.2 and CD45.2 binders. Upper graph shows the quantification of CD45.2 frequency among GC in three adoptively transferred mouse models after the immunization of eOD-GT8 60mer. The graphs below show the frequency of GC CD45.2 binders. X-axis represents the different precursor frequency group. Y-axis represents the percentage of GC (upper) and GC CD45.2 B cells (lower) respectively. Each circle represents one mouse. Mice from two independently repeated experiments were analyzed, n=5-10 mice/group. Bars indicate geometric mean and geometric SD from mice in each group. Significant differences were calculated with Student's t-test and shown as: p > 0.05, no statistical significance (ns), *p < 0.05, **p <0.01, ***p < 0.001, ****p < 0.0001. All p value analyses were calculated by GraphPad Prism V8.0.
Figure 2Autosharpened and masked cryo-EM density (Level 0.728) of the physiological complex in different orientations Ribbon diagram of the VgrG and Tle1 pseudoatomic structure, coloured according to the chain and in different orientations Full VgrG structure composed of the experimentally-obtained spike (red) and the homology model of the base (dark red) Structure of the VgrG spike at different planes
Metformin inactivates HSF1 to retard tumor growth.Figure 7A, B A2058 cells were transduced with lentiviral scramble or HSF1-targeting (hA6 and hA9) shRNAs. (A) Cell numbers were quantitated by Hoechst 33342 DNA staining (mean ± SD, n = 4, two-way ANOVA, ***P < 0.001). (B) Protein levels were measured by immunoblotting. C A2058 cells stably expressing LacZ or HSF1 were grown in medium containing 4.5, 1.0, or 0.45 g/l glucose. Following treatment with 10 μM metformin, cell proliferation was measured by Hoechst 33342 DNA staining (mean ± SD, n = 5, two-way ANOVA, ***P < 0.001). D, E 1 × 106 LacZ- or HSF1-expressing A2058 cells were transplanted into female NOD/SCID mice. One day after transplantation, metformin was administered via drinking water at 1 mg/ml. Tumor incidence (log-rank test; D) and volumes (E) were measured (mean ± SEM, two-way ANOVA n.s., not significant, *P < 0.05, **P < 0.01, ***P < 0.001). Tumor growth curves were fitted to exponential growth models to calculate tumor doubling time (DT). F Individual proteins were measured by immunoblotting using lysates of three tumors from each treatment group. G Protein levels were measured by immunoblotting using lysates of mouse liver tissues. H A2058 cells stably expressing FLAG-HSF1WT or FLAG-HSF1S121A were treated with 10 μM metformin for 7 days. Protein levels were measured by immunoblotting. I A2058 cells stably expressing HSF1WT or HSF1S121A were grown in Corning®ultra-low attachment 96-well culture plates with 10 μM metformin and different concentrations of glucose for 7 days, 10,000 cells per well. Viable cells were counted by Guava flow cytometer using ViaCount® reagent (mean ± SEM, n = 8, Student's t-test, n.s., not significant, **P < 0.01, ***P < 0.001). J Tukey box plots showing the inverse correlation between AMPKα Thr172 phosphorylation and HSP mRNA expression in ccRCC. Patients were stratified on the median value of AMPKα Thr172 phosphorylation reverse-phase protein array (RPPA) scores (Student's t-test). K Schematic depiction of the suppression of HSF1 and disruption of proteostasis by AMPK in malignant transformation.
Figure 3A-D Live confocal images of ddaC neurons at WP stage and 7 h APF. Efa6FL or Efa6Nterm-overexpressing neurons (B, C) showed precocious pruning phenotype at 7 h APF, compared to the control and Efa6ΔMTED-overexpressing neurons (A, D) in which most dendrites remained attached to the soma at the same time point. Red arrowheads point to the ddaC somas. Dorsal dendrites are marked by red arrows. E Quantification of precocious pruning defects as indicated by the percentage of dorsal dendrites attached to the soma at 7 h APF. F-I Confocal images of da sensory neurons expressing Efa6-Ki-GFP (F), or UAS-Efa6-GFP driven by ppk-Gal4 (H) were co-stained with GFP (Green) and Nrg (Magenta) at wL3 stage. (G, I) Confocal images of the epidermal cells expressing Efa6-Ki-GFP (G) or UAS-Efa6-GFP driven by A58-Gal4 (I) were co-stained with GFP (Green) and Dlg (Magenta) at wL3 stage. The ddaC soma is marked by dashed lines.
Expression of Ldb2 in the specific regions in the mouse brains A.Figure 1A. Schematic representation of the human LDB2 protein. Positions for the variants found in bipolar patients are also shown. The shorter isoform predicted from the splice variant (Tran et al, 2006) is shown below. B. Multiple alignments of the N-terminal regions of the human and mouse LDB family. Please note that the N-terminal regions are highly diverged between LDB1/Ldb1 and LDB2/Ldb2. The bar indicated the position for the peptide for antibody production. C. Tissue distribution of the Ldb2 protein. Representative western-blot image is shown. Yellow asterisks indicate uncharacterized bands. D. Expression of Ldb2 in the cerebral cortex. DAPI-stained nuclei visualized (right) in the cerebral cortex. E. Expression of Ldb2 in the amygdala. LA; lateral amygdala, BLA; basolateral amygdala, Ce; central nucleus of amygdala. F-G. Expression of Ldb2 in neurons. The merged images obtained with Ldb2 (stained in green) and NeuN (stained in red) antibodies are shown for cerebral cortex layers I-VI and the amygdala (F). most of Ldb2-positive cells are NeuN-positive. G. NeuN-positive cells/Ldb2-positive cells (left) and Ldb2-positive cells/NeuN-positive cells were counted in cerebral cortex layers I-VI.
DNA duplex processing by the combined activity of Sgs1, Dna2 and RPA A Sketch of DNA processing by the Sgs1-Dna2-RPA complex.Figure 3A Sketch of DNA processing by the Sgs1-Dna2-RPA complex. B Typical dsDNA processing event. The dashed red line connects the minima at the end of the rewinding sections The inset shows a DNA unwinding event in the presence of nuclease-dead Dna2 E675A and RPA. C Histograms of the observed unwinding and rewinding rates (green bars) with mean values of 69 ± 3 bp/s (N = 365) and 74 ± 5 bp/s (N = 282), respectively. White bars show for comparison the unwinding and rewinding velocities of Sgs1 in the presence of RPA