EMBO/sd-character-level-ner huggingface dataset:
E. Working model of polarized sEV release from MDCK cells. Apical release of sEVs (mainly CD63-enriched, CD9-positive, Annexin I-negative exosomes) and basolateral release of sEVs (mainly CD9-enriched, CD63-positive, Annexin I-negative exosomes) are mediated by ALIX-Syntenin1-Syndecan1 and ceramide, respectively. Marker sizes on sEVs (colored circles) reflect the abundance of each exosome protein. Ceramide also contributes to apical release of uncharacterized "CD9/CD63-negative sEVs".
Schematic representation of the experimental setup. Changes in pili position were visualized by imaging different confocal planes (z1-3) using spinning-disk confocal microscopy.
(C) Co-immunoprecipitation of Cdc4 using either unphosphorylated or Clb5-Cdk1-phosphorylated Far1(85-150) as bait. The experiment was repeated twice, a representative example is shown.
Schematic of 2019-nCoV S primary structure, colored by domain. Domains that were excluded from the ectodomain expression construct or could not be visualized in the final map are colored white. SS= signal sequence, NTD= N-terminal domain, RBD= receptor-binding domain, SD1= subdomain 1, SD2= subdomain 2, S1/S2= S1/S2 protease cleavage site, S2′= S2′ protease cleavage site, FP= fusion peptide, HR1= heptad repeat 1, CH= central helix, CD= connector domain, HR2= heptad repeat 2, TM= transmembrane domain, CT= cytoplasmic tail. Arrows denote protease cleavage sites.
C. HA-tagged Rab1 and Rab18, but not Rab2, could co-immunoprecipitate endogenous TRAPPII complex but not TRAPPIII complex.
(D) Heat map of expression changes of the same genes as in (B) after one hour of inhibiting TOR kinase with torin1 or caffeine/rapamycin treatment relative to cell before treatment; cells were grown in rich media - YES (data from (Rodríguez-López et al., 2019))
B Recombinant wild-type and G39A Gadd45a were added to the mixtures of oligo DNA and the recombinant H2A/H2B heterodimer or H3/H4 tetramer. The mixtures were separated by 4% non-denaturing PAGE and stained with EB.
H. Left: confocal images of representative SCN slices dual-transfected with pProk2.Cre.T2A.mCherry and Syn.GCaMP6f (top), or pProkR2.Cre.T2A.Venus and Syn.jRCaMP1a (below) (scale bar=500µm). Right, above: representative detrended plots of signal from GCaMP6f (green) traces and pCry1-DIO-Luc, emitted from Prok2+ SCN cells (red). Right, below: representative detrended plots of jRCaMP1a (purple) and pCry1-DIO-Luc emitted from ProkR2+ cells (light green). Orientation bars depict the horizontal axis of the optic chiasm and the vertical axis of the third ventricle for each SCN.
(O) L929 cells were treated with BSA and palmitic acid (100 μM) and transfected with HT-DNA (2 μg/mL) for the indicated times before immunoblotting analysis with the indicated antibodies.
c, schematic representation of subretinal EV injection, shown in (d). Red indicates host cells undergoing Cre-mediated recombination and expressing TdTomato (red);
Average energy expenditure of 3.5- to 4.5-mo-old male and female mice measured at 22oC, 30oC and 4oC in Oxymax chambers under a light/dark period for 12, 10 and 4 h, respectively (CP2-KO/WT/Ucp1ΔL/UCP1-KO: n = 5/5/4/4 male mice and 5/6/5/3 female mice). WT mice were pooled from littermates of CP2-KO mice and Ucp1ΔL mice. *p < 0.05, **p < 0.01 compared with WT mice, one-tailed unpaired Student's t test. All groups of mice showed similar mean body weight (CP2-KO/WT/Ucp1ΔL/UCP1-KO: male, 28.6 ± 1.6/33.4 ± 2.0/29.7 ± 2.6/30.4 ± 2.6 g; female, 26.4 ± 1.8/28.0 ± 1.8/27.6 ± 3.0/27.2 ± 3.0 g)
G U2OS cells transfected with the indicated siRNAs were plated. Cell numbers were determined as described in Experimental Procedures at the indicated time points.
Kinetic characterization of the rhodopsin dark state. Thermal decay of dark state rhodopsin: A) WT, B) T94I and C) G90D rhodopsin. The spectra are normalized to the OD280 and OD500/OD480 at t=0. D) Absorption maximum plotted as a function of time and fitted to a single exponential decay.
Immunoblot analysis showed HEK293 transfected for 48 hours with expression vectors for TCHP, and FLAG-TCHP at N- and C- terminal. total lysates were immunoprecipitated with anti-FLAG antibodies, and blots were probed sequentially with anti-PCM1, anti-FLAG, and anti-ACTIN antibodies. IgG light chains are indicated with Red Ponceau staining. The input totals were analyzed by parallel immunoblotting as a control for the level of expression.
(a) Inhibition of ROCK1 kinase activity prevents metabolic stress-mediated phosphorylation of Beclin1. HeLa cells left untreated or treated with a ROCK1 inhibitor, Y27632 (10 μM), were starved of glucose (4 h) as indicated, and endogenous Beclin1 was immunoprecipitated and blotted against phospho-Ser/Thr antibody. Whole cell lysates were run as inputs for Beclin1 and β-actin.
(a) Whole-cell lysates of HL-1 cells treated with 0.02 μM DOX and transfected with FLAG-tagged Parkin or the FLAG-empty vector were immunoprecipitated with the anti-Flag-M2 antibody and blotted with anti-p53 and Flag antibodies.
E. Immunofluorescence indicates that the phosphorylation level of P38 and ERK1/2 decreased dramatically in LincGET-depleted 2C. Embryos injected with LNA were collected at phCG 48 hours at late 2-cell stage for IF analysis. Scale bar, 50 μm. Three experimental replicates were performed and about 15 embryos were used in each group.F. Quantification of the fluorescence intensity indicates that the phosphorylation level of P38 and ERK1/2 decreased dramatically in LincGET-depleted 2C. Two tailed student's t-test was used for statistical analysis. Related to Figure 3E and Appendix Fig S4B.
B. Comparison of class averages of Elongator purified in buffer containing regular or low salt concentrations (150 mM and 75 mM NaCl, respectively). Densities resembling a second copy of Elp456 is indicated by white triangles.
(E) Two tyrosine sites of ANT1, Y195/Y290 (human origin), were selected and mutated into TAG using a genetic codon extension technique to insert difluorotyrosine into their specific sites to construct two mutant prokaryotic expression vectors of ANT1Y195-F2Y/ANT1Y290-F2Y.
(B) KPC tumor growth delay after treatment with either 5x3 Gy (day 0-4), anti-PD-L1 alone (days 0, 3, 6 and 9; black arrows), anti-CD8 alone (days 0, 3, 6 and 9) or their combinations, as indicated.
B Western blot analysis (probing with an anti-FLAG mAb) to detect cleavage of FdoH cleavage in S. sonneiΔrhom7 with (+)/without (-) FdoI. rhomboid substrates that are uncleaved, cleaved by GlpG are marked by black, red arrows, respectively.
(f) Western blot analysis of MDA-231, T47D and MDA-435 cells treated (48 h) with inhibitors of mTORC1 (RAP, 20 nM), mTORC1 and 2 (PP242, 100 nM), or DMSO (control).
A) His6-tagged EGF domains of Nrg1β and Nrg3 were added to neuronal cultures at the indicated concentrations. Western blot analyses of ErbB4 immunoprecipitates using antibodies against phospho-tyrosine (pY) and ErbB4, and of whole lysates using antibodies against pErk1/2 and pAkt
BAT temperature of WT (n = 5) and Ucp1∆L (n = 6) male mice measured during 12-h light time. *p < 0.05, Student's t test
The intrinsically disordered region (IDR) in MED4. Disorder analysis, protein and gene structures, and Sashimi plots are shown in (B). Splicing of these genes was not affected by the siRNA treatment.
B. Immunoprecipitation (IP) on HeLa cells co-expressing GFP-empty vector (EV), GFP-VPS41WT, GFP-VPS41S285P or GFP-VPS41R662* and FLAG-VPS18. GFP-VPS41WT and GFP-VPS41S285P both interact with FLAG-VPS18 and as shown in Appendix Fig S4A with HA-VPS33A. Interaction between GFP-VPS41R662* and FLAG-VPS18 is strongly reduced. Note that the stop codon in VPS41R662* leads to a truncated protein of lower MW (n=3).
surface area (μm2) (I) in neonatal CMs following treatment with the indicated recombinant proteins. Data are mean ±S.E.M of n=3-4 independent experiments.
(B) Mitochondria were immunolabeled for TOM20 and ATPB and recorded with 3D STED nanoscopy. Image data were deconvolved. Depicted are cross-sections of a mitochondrion (side view).
Quantification of JunB ChIP-seq signals in clusters 1 to 5. (Right) Quantification of ATAC-seq signals in clusters 1 to 5 in wild type and Jun/JunB double KO (DKO) CFPAC1 cells. Central values represent the median, the bars the 25th and 75th percentile and the vertical lines the lower and upper whiskers.
(B) Volcano plot of differentially regulated genes between HS and Rosacea. The red dots show the significantly upregulated genes; blue dots, significantly downregulated genes (P<0.05).
(H) Percentage of surrogate antigen spots colocalizing with endophilin A2, clathrin LC or both markers. Levels of random spot colocalization were calculated using randomized spot coordinates. Data show mean and SEM from 107 cells analyzed from 4 experiments; statistics from one-way ANOVA.
(G) ZEB1, JUN and YAP DNA-binding overlaps at 1,993 genomic sites in MDA-MB-231 cells. Triple overlap is assumed when both JUN and YAP peak summit positions are within 200 bp of a ZEB1 peak summit position.
Representative gel photographs showing mRNA levels of LATS1, LATS2, and YAP in the LATS2-knockout hOSE-MXIV, hOSE-YAP and hOSE-YAPS127A cells examined using semi-quantitative RT-PCR at passage seven.
E, F Histograms of instant eccentricities (left) and 2D plots of adherent surface versus speed (right) of WT naive T cells on 2D surface coated with ICAM-1 and CCL21. In the 2D plot, the 3 populations discussed in the results have been highlighted: a, hardly motile (instant speed <5 µm/min) cell population with low (projected adherent area < 20%,) adhesion, b, hardly motile (instant speed <5 µm/min) cell population with high (projected adherent area > 40 %) adhesion, and c, highly adherent (projected adherent area >20 %) cell population with elevated speed (ranging between 15 and 30 µm/min). Data information: In (E) and (F), histograms of instant eccentricities correspond to > 60 cells and > 2000 contours, and fitted by a double Gaussian for WT naive T cells (means = 0.54, 0.8 and SD = 0.18, 0.06) and a single Gaussian for Arghap45−/− naïve T cells (Mean=0.58, SD =0.18). 2D plots correspond to > 60 cells and > 2000 events. In (F) events which combined null motility and adherence over the recorded time have been excluded.
Detection of endogenous and exogenous Oct4, Sox2, Klf4 and Nanog expression in iPSCs, ESCs and MEFs by RT-PCR.
b, Autophagic activity in apg3 mutants. Wild-type, Δapg3 and apg3C243A cells were grown in rich medium (open bar) and subjected to nitrogen starvation for 4 h (filled bar). The autophagic activity of each cell was assessed by measuring the alkaline phosphatase activity. The apg3C243A mutant showed defective autophagy.
(C) Shortened long bones in the chicken wings injected with CMPD101. The right limb bud was injected with CMPD101, the left one was left as a control. Note the shortened humerus (H), ulna (U) and radius (R) in the CMPD101-injected wing. Mean ± SEM. Mann-Whitney U test; number of animals is indicated. Scale bar, 150 μm.
The levels of PIP2 was also measured using a plate reader after exposure to physiologically relevant stimuli in M-MOPS and primary mouse microglia Data shows the mean±SD of 3 independent experiments were analysed by 2 way ANOVA with Sidak's multiple comparison *=p<0.05, **=p<0.01, ***=p<0.001, ****=p<0.0001. (blue: P522; red: R522).
A RT-qPCR analysis of lincRNA-EPS transcripts in the lincRNA-EPS-stably-overexpressed iBMMs (lincRNA-EPS) and corresponding control cells (EV).
Relative mRNA expression (G) and western blot analysis (H) of PGC1α, PLIN5, and HSL in C2C12 cells transfected with Ago-183/96 and FoxO1 as indicated (n=5 per group for RT-PCR analysis).
(D) A schematic model illustrates the molecular mechanism by which loss of TDP-43 enhances TFEB-mediated expression of ALP genes, blocks autophagosome-lysosome fusion, and induce neurodegeneration. TDP-43 directly targets raptor, a key component of mTORC1, to regulate mTORC1-TFEB signaling. Meanwhile, TDP-43 can affect the autophagosome-lysosome fusion in a Dynactin 1-dependent manner. The current study highlights the role of mTORC1 and Dynactin 1 dysfunction, altered autophagy and lysosomal biogenesis in TDP-43-mediated neurotoxicity.
(A,B) Representative and summary of immunoblots of full-length lanes of lamin B in human dPMNs that were treated with PMA for 0, 0.5, 1, 2, 3 h during NET formation, or apoptotic dPMNs that were induced by PMA for longer term (12 h) treatment (A). β-actin served as loading control
C - The same experimental procedure as described in (B) was applied to HeLa cells treated for 48 h prior to ionomycin treatment (8 µM) with siRNA control or directed against TG2.
(A, B) Interactions between Bcl‐XL, Beclin‐1 and Bad in conditions of autophagy induction. Cells were either treated by nutrient depletion (A) or addition of 1 μM rapamycin, 1 mM lithium chloride, 100 μM L‐690,330 or 50 μM carbamazepine (B), followed by immunprecipitation of Bcl‐XL (as in Figure 2C) and revealing the immunoblots by antibodies specific for Bcl‐XL, Beclin‐1 or Bad.
(C) At 1, 3, 5, 7, and 10 days post-infection cells from (A) were harvested, lysed, fractionated for cytoplasmic and nuclear content, and analyzed for TFEB, ACTB and H3 histone by Western blotting. Left, a representative blot is shown. Right, densitometric analysis of immunoblots from independent donors presented as means ± s.e.m., n = 4.
(B) Immunoprecipitation of endogenous LC3 in HT29 cells. IgG was used as a negative control.
(F-I) Lineage-tracing evidence supports α- to β-cell transdifferentiation. (F) Schema for temporal and spatial lineage tracing. loxP-mediated excision of the STOP-cassette permits heat-inducible expression of the stable fusion-protein H2B-GFP. Control and bactin:igfbp1a-overexpressing Tg(hsp:loxP-mCherry-STOP-loxP-H2B-GFP);Tg(gcg:CRE);Tg(ins:Flag-NTR) larvae were first heat-shocked at 3 dpf to label the glucagon-expressing cells with the stable fluorescent protein H2B-GFP, thereafter treated with MTZ from 3-4 dpf to ablate the β cells, and analyzed at 6 dpf after 2 days of regeneration. Note that the temporal control of the lineage tracing is mediated by a heat-shock.
C-D Overlays of 2D 1H-15N heteronuclear single quantum coherence (HSQC) NMR spectra of BSP3 (C) and BSP34 (D) in 10 mM Ca2+ (red) and 10 mM EDTA (black).
D. Representative anti-YAP immunofluorescence images of densely cultured RPE cells transfected with the indicated plasmids. Green, GFP or V5. Red, YAP. Blue, DAPI. Scale bar, 10 μm.
(c) Immunofluorescence microscopy of LAMP-2A (green) and nuclei (stained with the DNA-binding dye DAPI; blue) in resting TH1 cells (Rest) and TH1 cells activated for 24 h as in a,b (Act) (left), and quantification of lysosomes in cells as at left (right). Original magnification, ×630; scale bar, 10 μm. *P = 0.013 (t-test).
H. Percentage of metaphase U2OS cells that align chromosomes outside of the expected axis (angles ± 15°). Mean of 100 cells per genotype are plotted, n=2. Error bars, SEM. ***, P< 0.0001; ANOVA.
Ribbon diagram and locally sharpened surface representation (transparent= of the three TssJ protomers in orange, labelled TssJ.i, TssJ.o and TssJ' for the inner, outer and additional monomer respectively. In light green and blue are the TssM.i and TssM.o protomers respectively Superimposition of the ribbon diagrams of TssM-TssJ heterodimer within the inner (green-orange) and the outer (blue-orange) pillars Ribbon diagram of the TssM.o (outer pillar) with the TssJ.o and the TssJ' (orange)
(F-I) Lineage-tracing evidence supports α- to β-cell transdifferentiation. (H-I) Representative confocal images at 6 dpf (after 2 days of regeneration) of control and bactin:igfbp1a-overexpressing larvae stained for insulin, glucagon, to-pro, and H2B-GFP. ins+;H2B-GFP+ cells are indicated by the arrowheads, and H' and I' show staining against only insulin and H2B-GFP. Moreover, most insulin+;H2B-GFP+ cells no longer express glucagon. Scale bars: 15 μm.
I. DNA fiber experiments showing decreased replication tract length following UV-B treatment (30J/m2) in HUWE1-depleted HeLa cells. The "n" numbers of fibers analyzed (pooled from three independent experiments), as well as the mean +/- SEM, are indicated on the graphs. P-value is 2.11x10-20.
(E) Re-expression of human Tsc2 rescues mitochondrial responses to insulin. Cultures were serum-starved in Hank's balanced salt solution for 2 hours before stimulation with insulin or amino acids, and were imaged before and 30 minutes after stimulation. Each colored line refers to a single field of view containing 2-5 cells, and each pair of solid and dotted lines of the same color refers to the same field of view. Re-expression of the Flag-WT Tsc2 was corroborated by indirect immun­o­fluorescence (IF). Statistical analyses were performed using Student's two-tailed unpaired t-test
D Confocal image of RalGDS (left) in a giant cell after RacGEF1ΔN recruitment and the corresponding kymograph (right).
V. cholerae ΔvrrA ΔmicV strains carrying the ompT::3XFLAG gene and pMicV, pVrrA, pRybB, or an empty vector control (pCtr) were cultivated in LB to an OD600 of 2.0. RNA and protein samples were collected and analyzed for MicV, VrrA and RybB expression on Northern blots. OmpT::3xFLAG production was tested on Western blots. RNAPα and 5S rRNA served as loading controls for Western and Northern blots, respectively.
F. Overexpression of mutant ABL1 constructs with mutations identified in selected primary lung tumors (Ding et al, 2008) in H157 cells. Values indicate quantified band intensity for p-CRKL, relative to α-tubulin and HA-tagged ABL1.
(A) Correlation between ssGSEA enrichment scores for the mTOR signature versus TAM-MG or TAM-BMDM signatures in TCGA GBM transcriptomic data. Comparison carried out on all IDH-wild-type samples, and in a subgroup specific manner according to Wang's classifier. Size of circle is indicative of Rsquare value and bold outline represents a p-value ≤0.05.
D. HeLa (D) cells pretreated with CHX (1 μg/ml) for 30 min and then stimulated with TNF (10 ng/ml) in the presence of CHX for indicated times were subject to FADD immunoprecipitation, and then analyzed by western blotting.
J) Schematic depicting our working model. During development, Hh tethered to LDs are localised to cortex glial cells, to activate gliogenesis. Non-autonomously, excessive glial Hh inhibits NB cell cycle progression. Upon cortex glial specific FGF activation, increased Hh modified by Fasn1 and Lsd-2 together with increased ROS prevent NB proliferation.
D SPRR5 knockdown efficiency in day 3 (D3) organotypic epidermal tissue (n = 4 epidermal tissue cultures/knockdown group). Data is presented as mean ± SD. Statistical significance was tested by an unpaired t-test and corrected for multiple testing after Bonferroni (* = adj. p-value < 0.05, ** = adj. p-value < 0.01, *** = adj. p‑value < 0.001, and n.s. = not significant).
A) Density maps identifying iDHSs and showing DNase-Seq and H3K4me2 ChIP-Seq peaks in order of increasing DNase-Seq tag count signal for CD4 TB+ compared to TB cells. Also depicted are the locations of 6823 major DHSs that are 5.5 fold induced and a subset 1217 these iDHSs that are 11 fold induced. On the right is the log2 TB+/TB fold change in expression of the closest gene to the corresponding DHS.
C HTM-mediated quantification of γH2AX intensities per nuclei in pancreas explants cultured in vitro for 6 days. Red lines show mean values. Results of two independent experiments are shown. ****P < 0.0001.D Representative images of γH2AX staining in pancreas explants from R26AID+/+p48CRE+/KI (top) or R26AID+/KIp48CRE+/KI mice (bottom) (40× magnification). White arrow points a representative positive cell.
(C) Diagram showing the percentage of up- and down-regulated genes in the RNA-seq experiment comparing NTC vs. shB DVL3 (left panel) and EV vs. DVL3-WT (right panel) in MCF7 cells.
D. Expression and translocation of SidC. The lysates of L. pneumophila strains used for infection were probed for protein expression, ICDH was detected as a loading control (top panel). SidC translocation was detected by probing the saponin-soluble fractions of infected U937 cells with SidC-specific antibodies. Tubulin was probed as a loading control (bottom panel).
(A) Live-cell nanoscopy of HeLa cells. COX8A-SNAP was labeled with SNAP-cell SiR and imaged with STED nanoscopy.
(H) Western blot showing expression of pro-CASP2 and P21 following treatment with dox for the specified number of days. Experiments were performed in PLK4Dox monoclonal knockout cells. (I) Quantification of pro-CASP2 levels following treatment with dox for the specified number of days. Experiments were performed in PLK4Dox monoclonal knockout cells. Each dot displays measurements from a single experiment. Data acquired across n = 6 biological replicates. Mean ± s.e.m.
(C) Dot plot showing the average pixel intensities of the Myc signal at individual parent centrioles in RPE1 cells of the indicated genotypes, either transduced with the indicated lentiviral vectors or left untransduced (mock). Mean values (red lines) ± s.e.m. are reported. N > 50 centrosomes were assessed for each condition in as many individual cells; a.u. = arbitrary units. Kruskal-Wallis test (****P < 0.0001; n.s. = non-significant).
(I) The serum lactate levels were similar to WTFlx in KO-NDUFS3 samples and significantly decreased when compared to KO-GFP levels. The individual KO-NDUFS3 animals are color coded. Green triangles represent the animals injected with rAAV9-eGFP whereas black triangles represent animals which did not receive an rAAV9-eGFP injection. Statistical analysis was performed by One-way ANOVA followed by Tukey post-test. Data represent means ±SEM.
HeLa cells were left untreated or treated with heat shock (HS) at 42˚C for 3 h, alone or with cycloheximide (CHX; 50 μg/ml), or Actinomycin D (Act. D; 3 µM) followed by staining with the dye Amylo-glo.
). CD206+ cells in relation to the percentage of hypoxic (CAIX positive) tumor area (J). Statistical analysis: Kruskall-Wallis (Dunn´s post test). * p < 0.05, ** p < 0.01; data are mean ± SEM
C Si-TRAF3IP3 (oligo #1) were transfected into HEK 293 cells, which were then treated with mock, VSV, SeV, poly(I:C) or HSV-1. After various treatments, IFNB inductions were measured by qPCR.
I. Immunoblotting against PGAM5 in Ifnb+/+ ­and Ifnb-/- CNs with or without rIFN-β treatment for 2 h and quantification.
A) Representative histological H&E staining of sections of the proximal colon and ileum of WT and TMED2 hypomorph mice.
(E-I) Morphological phenotypes of Wip1 morphants. Embryos were injected radially in the marginal zone with Co MO (80 ng), Wip1 MO (80 ng), wt Wip1 (1 ng) and Wip1(D277A) mRNA as indicated and cultured to tadpole stages. Embryos are shown in lateral views with anterior to the left. Un Co, uninjected control. Scale bar, 1 mm. (J) Quantification of the phenotypes shown in (E-I). Severe defects include microcephaly, shortened and kinked body axis, and no eye. Mild defects indicate normal body axis with malformed eyes.
(C) Schematic representation for quantifying actin intensity along the cortex as in D. Segmented line was drawn along the cortex from one equatorial region to the other. Actin intensity across the line is plotted in D.
D. The DNA-binding affinity of DBD was measured by fluorescence anisotropy, titrating the DBD protein against Cy3 3'-labelled ssDNA, dsDNA and G4 DNA The top panel shows binding curves for ss- and dsDNA, the bottom panel shows the binding curve for the G4 DNA substrate.
Normalized mean of elavl3 and gfap intensities in ROI observed in: (f) uninjected (UI) (5 embryos, 62 slices), (g) control (CTRL) (5 embryos, 35 slices) and (h) MBSm (8 embryos, 62 slices) conditions; bars represent mean and SEM; multiple t-test with Benjamini, Krieger and Yekuteli discovery, significance: p<0.05*, p<0.001***, p<0.0001****.
(E) Two control and ATD fibroblast samples were immunoblotted for GRK2. Note the absence of GRK2 protein in the ATD cells. Actin served as a loading control. The data shown are representative of three independent experiments.
B Illustration of the BRAFV600E pathway and the MAPK pathway inhibitors used in the study.
(B) Hek293 cells were thymidine-arrested for 20h, mock- or OHT-treated to induce DSBs by nuclear accumulation of ER-AsiSI and then subjected to ChIP-multiplex PCR