EMBO/sd-character-level-ner huggingface dataset:
(B) Proteins analysis of secreted pro-inflammatory cytokines, IL-6 and TNF-α from primary CD115+ cells. Cells were incubated with 20µM of TLR2-p or scrTLR2-p peptide for 0.5h, then washed and incubated with LTA (5μg/ml), PAM3CSK (0.5μg/ml) or LPS (0.2μg/ml) at 370C for 5h (for TNF-α detection) and 22h (for IL-6 detection). The results are mean± S.E.M of two independent experiments (n=8).
A HeLa FlpIn GFP−GABARAP cells were treated with proteasomal inhibitor (MG132, 2 h) or subjected to amino acid starvation (EBSS, 2 h), before staining with anti−ALFY antibodies. Scale bar, 10 μm.
Survival of age- and sex-matched (8-10 week old) Spata2+/+ (WT) and Spata2-/- (KO) mice injected intraperitoneally (i.p.) with LPS (20 mg/kg bodyweight). Data pooled from three independent experiments are shown. Statistical analysis was performed using long-rank test.
B: Sequence of the peptides used for the pull-down assays. The peptides are composed of an amino-terminal biotin, a linker sequence and the FFAT sequence of STARD3 (residues 200-216), FIP200 (residues 725-741), MIGA2 (residues 286-302), PTPIP51 (residues 151-167), Kv2.1 (residues 584-600), Kv2.2 (residues 599-615), and ORP1 (residues 469-485) either without or with a phosphorylated residue (serine or threonine) at position 4 of the core FFAT motif. The negative control peptide is composed of a random sequence.
Mature Mpl reaches the surface through the conventional ER‐Golgi pathway and bears fully processed N‐linked carbohydrate. Immature Mpl appears to be routed through an autophagic pathway for unconventional secretion, providing an alternate pathway for membrane expression of core‐glycosylated Mpl. Once delivered to the cell surface, both forms of Mpl can be recycled or stored in calcium‐dependent and independent compartments capable of fusion with the plasma membrane. In some cells, such as K562 cells, Mpl is packaged into exosomes and secreted.
B) Larval brains at 6 h ALH from grh-Gal4; UAS-CD8-GFP were labeled with Sas-4, Dpn, and GFP.
C. Localization precisions (mean ± SD) of tracks from multi-GFP-labeled worms. The number of GFP copies was estimated as the following: the dynein-2 heavy chain of CHE-3 forms a dimer, 14 = 2 x 7; IFT-particle subunit CHE-2 is also a dimer, 14 = 2 x 7; IFT-particle subunit DYF-11 can be a tetramer, 12 = 4 x 3; the genetic cross combined 7xGFP::CHE-3 with DYF-11::3XGFP, 26 = 2 x 7 + 4 x 3.
D. The model proteins consist of a fusion between Ura3p and GFP (URA3sol, left) and the amyloid-β-peptide of 42 residues (Aβ) (URA3agg, right). After 18 hours of expression Ura3psol remains homogeneously distributed whereas Ura3pagg is accumulated into intracellular foci.
Detailed views of the hydrophobic interactions of TPRs. There are two kinds of hydrophobic interactions, intra-TPR and inter-TPR. The hydrophobic residues associated with inter-TPR interactions are indicated with asterisks (*).
Representative pictures of mitotic NSC marked by P-Vimentin and PH3 revealed by DAPI at the apical surface of the VZ-like area of hCOs. A representative vertically dividing cell was shown in upper panel, and a representative horizontally dividing cell was shown in lower panel. White dash line indicates the apical surface and splitting plane. Immunofluorescent staining was performed on sections of day 45 wildtype H9 hCOs and RGCC-KO hCOs. Scale bar: 5 μm.
E. Details of brain metastases. Scale Bar is 30µm. F. Quantitation of Proteostat positive dots in primitive vs metastatic melanoma tissues: 6 tissues from metastatic lesions and 6 from primitive melanoma lesions were analysed. For each tissue two sections were quantified. T-test analysis was applied. T-test analysis, ** = p-value<0.01 (N=6, data are mean ±SEM).
A) Caspase 3/7 activation ± 16-hour treatment with varying concentrations of BAM15, DNP, or FCCP (N=3 per condition). 5 μM: BAM15 vs. DNP (P=0.030). 10 μM: BAM15 vs. DNP (P=0.013). 20 μM: BAM15 vs. DNP (P=0.0005), BAM15 vs. FCCP (P=0.036). 40 μM: BAM15 vs. DNP (P=0.018), BAM15 vs. FCCP (P=0.021). 80 μM: BAM15 vs. DNP (P=0.018), DNP vs. FCCP (P=0.004).
(L) Cell-free plasma was derived from breast cancer patients treated with paclitaxel (n=10) or palbociclib (n=9) and the expression levels of CXCL1, CCL2, CCL5 and MMP1 quantified by ELISA. The values represent the ratio between on-treatment and pre-treatment levels for each patient. Data information: Data are means ±SD. Unpaired student t-test (L). *p<0.05, **p<0.01, ***p<0.001, N.S.= Not significant.
(A) Genes co-expressed with the PIDDosome components were examined with respect to the associated Hallmark pathways taking positive (pos) and negative (neg) correlation into account.
(C) Flow cytometry quantification of mCherry/YFP fluorescence in the mutants with GCG1pr FPR background. The data are normalized to the signal values of the wild type (FPR) strain.
Plasma metabolomic changes revealed a trajectory in COVID-19 severity, from healthy control (n=12), mild (n=29), to severe (n=17).
Colon length of colonic section from the Angfl/fl and LyzMcre;Angfl/fl mice on day 8 with (n = 7) or without (n = 3) 2.5% DSS treatment.
[a] Plots of enveloped spike activity waveforms based on targeted extracellular recordings from hippocampal CA3 region perfused into epileptogenic buffer for the indicated genotypes. Upward deflections indicate seizure-like episodes (SLEs). Scale bars, 5% of maximum amplitude.
D. Immunoblotting showing the total amount of OVA in Scramble and Rab22a KD JAWS-II DCs after 90 min and 7 h of infection with TgRHYFPSAG1-OVA parasite at MOI 2 and 6. Fifty µg of total cell lysates were loaded onto each lane. Data are representative of two independent experiments.
B Box plots of the Em/Ad expression ratios of GATA6 (left) and NKX2-1 (right) in FFPE lung tissue sections from controls (Ctrl, n=61) or lung cancer (LC, n=51) patients. Isoform-specific expression of the indicated genes was analyzed by qRT-PCR after total RNA isolation from tissue samples. Each point represents one sample.
(C) Correlation between N-antibody titre, as calculated by Jess, and intracellular neutralization (fold decrease in SARS-CoV-2 replication), as measured by EDNA, in convalescent sera from multiple individuals. (D) Intracellular neutralization of SARS-CoV-2 by titrated serum from two strongly N-antibody positive individuals. ( Data information: All data represents at least three independent replicates. Error bars depict the mean +/- SEM.
(C) Barnes maze test after intraperitoneally injecting TAT (n = 8) or TAT-pS3 (n = 8) peptide in Nedd4-2 WT mice (top), or TAT (n = 9) or TAT-pS3 (n = 8) peptides in Nedd4-2 cKO mice (bottom). Learning curve during 4 training days of Barnes maze task showing the escape latency, number of errors before escaping, and the quadrant occupancy on probe trial at day 5 and at day 12 were assessed.
Alteration of retinal vascular maturation in TfebiEC-/- at p5. Representative images of whole mounts of retina and immunostaining of vascular front and vascular plexus with an anti-iB4 Ab (scale bars: 50 µm). Bar graphs indicate the percent of vascular area versus total area of the retina, the percent of vascular density, the number of branches per field, vessel diameter, the number of filopodia per field and the length of filopodia (mice n=10, mean±SEM; ***p< 0.0001 versus control mice by Student's t-test).
C IL-8 secretion in HEK-hTLR4 and HEK-null2 cells following treatment with cisplatin at the indicated concentrations (n=3 independent biological replicates). Data Information: For all panels actual individual data from each experiment are plotted as box (25th and 75th percentile borders; median central band) with Tukey whiskers. Statistical analyses were assessed by 2-way ANOVA: in C) comparisons between successive concentrations; ; ***, P<.001; ****, P<.0001 Tukey test, C).
Quantification of pentose phosphate pathway (PPP) intermediates; gluconate-6-P (G6P), ribulose-5-P (Rl5P), ribose-5-P (R5P), sedoheptulose-7-P (S7P), fructose-6-P (F6P) and erythrose-4-P (E4P) in human endothelial cells expressing YF or YD eNOS; n=6-8 independent cell batches (Unpaired Student's t test).
Analysis of shScramble (gray)‐, shIP3R(1,3) A (blue)‐, shIP3R(2,3) B (red)‐, and shIP3R(1,3) C (green)‐expressing DCs migrating in micro‐channels (n > 100 cells per condition from 3 independent experiments for shIP3R(1,3) A and shIP3R(1,3) C and two independent experiments for shIP3R(2,3) B).A Velocity fluctuations (ΔV/V0) of immature DCs migrating in micro‐channels. Boxes illustrate 10-90 percentiles of values, and whiskers represent the range of values. P‐values were calculated using a Kruskal-Wallis test.
(C) Volcano plot of mass spectrometry results from a synthetic 5'-biotinylated tRFTyrGUA co-precipitation experiment with cell lysate. Log2 fold enrichment values of proteins identified from tRFTyrGUA relative to scrambled tRF control samples.
(f) A set of RNAi-resistant rescue forms of FoxO1 plasmids were transfected into stable FoxO1-RNAi HCT116 cells in the presence or absence of E64 and pepstatin A. Western blotting was performed to detect p62 degradation and LC3-II accumulation.
Flow cytometry analysis of Mitotracker green and red staining in Gata6-WT and Gata6-KOmye pMɸ (gated on F4/80hi/+ Tim4+) unstimulated (-) or after LPS (100 ng.ml-1), IL-10 (10 ng.ml-1), αIL-10R (5 µg.ml-1) or isotype (5 µg.ml-1) stimulation for 16 h in vitro. Data shown are pooled from 3 independent experiments and normalized to WT unstimulated.
C, D hTERT-RPE1 cells and hTERT-RPE1 cells stably expressing siRNA-resistant GFP-RAB35 were treated and stained for GFP, acetylated tubulin (acetyl. tub.) and DNA. Representative images in (C) of cells treated with Neg or RAB35 siRNA. Regions within white boxes shown at higher magnifications to the right. Scale bars, 10 µm. Cilia length quantifications in (D) are shown as box-and-whisker plots. Horizontal lines show 25, 50 and 75th percentiles; whiskers extend to minimum and maximum values. One representative experiment of three is shown (n ≥ 50 cilia per experimental condition). Statistical significance according to Kruskal-Wallis followed by Dunn's post-hoc test (* P < 0.05, ** P < 0.01, *** P < 0.001, n.s.: non-significant; P-values: hTERT-RPE1-Neg vs. hTERT-RPE1-RAB35-1 P < 0.0001, hTERT-RPE1-Neg vs. hTERT-RPE1-RAB35-1 P < 0.0001, hTERT-RPE1-RAB35-1 vs. GFP-RAB35-RAB35-1 P = 0.0249, hTERT-RPE1-RAB35-2 vs. GFP-RAB35-RAB35-2 P = 0.0056)
The area under the curve (AUC) for the latency to reach the hidden platform was similar in APP/PS1-Stat3WT compared to WT-Stat3WT and WT-Stat3KO mice, but significantly higher in APP/PS1-Stat3KO mice (Kruskal-Wallis test followed by Dunn's multiple comparisons test).
E: USV, Compared to LM controls, the duration of time spent with call emission is strongly reduced in NexCre cTKOs. [Mann-Whitney test ****p < 0.0001].
(F-H) SF268 cells stably expressing Flag-tagged SLFN11 were transfected twice with indicated siRNAs. 48 hr after second transfection, cells were treated with CPT (1 µM). 3 hr later, cells were subjected to immunostaining using anti-RPA2 and anti-Flag antibodies. Representative SLFN11 and RPA2 foci were shown (F). Scale bar, 10 µm. Quantification of RPA2 and SLFN11 foci formation using NIH Image J software (G).
(a) Normal environment with sufficient glucose and nutrients suppresses ROCK1 activity. Bcl-2 thus associates with the Beclin1 core complex (Vps34 and UVRAG) and keeps autophagy in check. (b) When the cellular environment is deprived of nutrients, ROCK1 kinase is stimulated. ROCK1 binds and phosphorylates Beclin1 at T119 and disrupts Beclin1-Bcl-2 interaction. Dissociation of Bcl-2 triggers the Beclin1 core complex to induce autophagy and maintain a balance between cell survival and apoptosis.
B. ERK71 mutants have elevated triacylglycerol (TAG) levels (N=4 replicates of ≥10 larvae/ replicate for each genotype). C. Fat body specific depletion of ERK7 by RNAi (BDSC 56939) leads to increased TAG levels (N=4 replicates of 10 larvae/replicate for each genotype).
RNA-seq of liver 10h post Sham or CLP. Mice (n = 3/group) underwent a sham or CLP operation and were injected with GW7647 (10 µg/g) 6h post-surgery, after 4h (total of 10h), livers were isolated and RNA was prepared. Venn diagram depicting the amounts of genes upregulated (up) or downregulated (dn) by GW7647 in sham and CLP mice (LFC > 0.8 or < -0.8 and P < 0.05).
Representative images of filipin staining in LN229 (up) or LN18 (down) cells treated with different concentration of fatostatin (0 - 20 μM). Scale bar = 30 μm.
C Immunostaining of control (left) and BTHS iPSC-CMs at day 60 post differentiation for cardiac troponin T (cTNT) and Connexin 43 (Cx43). Scale bars: 50µm.
(E) Suppressed LFS-LTD at SC-CA1 synapses of PtenΔC/ΔC mice (P17-21). (n = 10 slices from 6 mice for WT and ΔC, **P < 0.01, Student's t-test). The grey traces represent baseline fEPSP prior to LTD induction. The error bars represent SEM.
Time-lapse images of agarose-embedded cells were taken at RT with supply of fresh PM Glc+ura medium throughout one budding cycle. Only (F) shows fixed cells immunostained for Sed5p. All cells produced the β'-COPVN•Dsl3pVC BiFC pair. Most strains contained plasmids encoding different organelle markers as indicated below. BiFC signals are pseudocolored green, organelle markers are pseudocolored red. Scale bar 5 µm.H. CFPSec4p, marker for secretory vesicles
A. Representative metaphase spread from BRCA2 depleted U2OS cell treated with HU. Scale bar = 5 μM. Arrows indicate the chromosomes enlarged in the insets, two of which show chromatid breaks (*
% of γH2A.X foci co-localising with telomeres (B) in FLAG-tagged TRF1-FokI-D450A- and TRF1-FokI-expressing CMs. Data are mean ± SEM of n=4 independent experiments. >50 cells were analysed per condition. Statistical analysis was performed by two-tailed t-test ***P<0.001.
F. Western blot analysis shows MDGI expression in human glioma cells including patient-derived spheroids (S24, ZH161, ZH305, BT3, BT11, BT12, BT13), patient-derived adherent cells (BT5 and BT5R), and long-term cell lines (U87MG, LN229, LN308). Numbers above the lanes show the relative expression of MDGI compared to the levels of β-tubulin that served as loading control in each cell line. Representative Western blot image of 3 separate experiments is shown.
(a, b) ITC titration profile of Beclin 1 CC domain with Atg14L (a) or UVRAG (b).
(G) USP1 removes K63-linked polyubiquitin chains on Akt in vivo. Akt was immunoprecipitated from the soluble fraction of muscles expressing USP1(C90S) or control plasmids. Mouse IgG was used as a control for non-specific binding. Protein precipitates were subjected to immunoblotting with an antibody against K63-linked polyubiquitin conjugates.
Soluble cytokine level in supernatant of cultured colonic tissue isolated from WT and Ang-/- mice on day 0 (n = 3) or day 9 (n = 7) during 2.5% DSS treatment.
Distribution of R-LPS and S-LPS in Δgmd plac-gmd after 3, 6, 9 and 24 h post-induction analyzed by flow cytometry (one representative example among 3 biological replicates, n = 20,000 events).
B. For each targeted gene, the number of variants (black bars, left y-axis) and the fraction of the single substitution sequence space (green bars, right y-axis) is plotted. The total library size across all genes sums to 16,300 variants
Immunoblot analysis of streptavidin pulldown from proximity biotinylation described in (G). 4.5 h represent newly synthesized histones and 48 h represent pre-existing histones. Wedge represents loading titration: 1x > 0.1x > 0.01x > 0.001x. All other lanes are loaded at 1x concentration. Immunoblot signals were normalized to anti-FLAG signal.   Quantification of anti-FLAG (H3.1-APEX2-3xFLAG) and anti-UBR7 immunoblot represented in (G-H). Lanes 8 and 11 were quantified. Error bar represents mean +/- standard deviation. A two-tailed one-sample t-test was used to calculate p-value (italics) associated with group mean difference from a hypothetical value of 1.0 (represented by dashed line).
A, B Step-wise assembly of MAC on convertase-labeled bacteria. Convertase-labeled bacteria were incubated with C5/C6 or C5/C6/C7 for 15 minutes, and subsequently washed (@) or treated with 10 μg/ml Eculizumab (Ecu). Then, the remaining MAC components (C7-9 for C5/C6 or C8-9 for C5/C6/C7 respectively) were added to the incubation mixture. In the control conditions (Conv-MAC), the remaining MAC components were added to the incubation mixture without washing or adding an inhibitor. (A) Outer membrane (mCherry) and (B) inner membrane damage (% Sytox positive) were determined. Data information: (A-B) Data represent mean ± SD of 3 independent experiments. Statistical analysis was done using a ratio paired two-tailed t-test in which the test conditions were compared to Conv-MAC and displayed only when significant as * p≤0.05.
g, Mice were infected with wild-type L. monocytogenes by i.p. injection and bacterial burdens in livers and spleens were determined by plating (means ± s.d., n = 7 per group, *P < 0.04 by Student's t-test).
(B) The organization of the reticular ER network was classified as class I (normal), class II (mildly disorganized) or class III (highly disorganized). Scale bars: 10 µm. (C) Quantification of the control and subject ER network organization. In each condition, 30 cells were analysed in three independent experiments. Error bars represent mean +/- SD and p-values were calculated using a t-test.
A,B) Mean baseline-detrended bioluminescence profiles from plate wells containing either PER2::LUC U2OS cells with (WT, left panel) or without REV-ERBα (KO, right panel) recorded at 37°C before and after transfer to 18°C for 24h (A) or 5h (B) (grey region) from biological repeat 1. 6 differently colored profiles represent cells synchronized at 6 distinct phases of the circadian period prior to the start of 18°C exposure (time zero).
relative abundance of various RNA species (mean +/- s.d.) in J2 antibody immunoprecipitates from three biological replicates of control and mutant cell lines (I). Multiple testing corrected P-values from unpaired two-tailed t-tests are depicted above each comparison (* P < 0.05, *** P < 0.001).
(E) Western blots detecting pVP30, VP30 and NP levels in EBOV infected HeLa cells upon hnRNP L, hnRNPUL1 or PEG10 knockdown.
(C) Number of γH2AX positive cells in formalin fixed ICL and control tumor sections by immunofluorescence staining and quantification (Scale bars denote 20μm, p<0.0001 for Ch10 and p<0.05 for Ch14).
16-days old MCF10A spheroids grown in matrigel/collagen mix were stimulated for 24h with either macrophage-conditioned or control medium. 3D structures of spheroids stained for DNA (Hoechst 33342 in blue), F-actin (Phalloidin in red) and laminin V (green). Laminin V staining indicates the loss of basal membrane continuity at invasive protrusions. Invasive protrusions are marked with a white arrow.
J. Persistent measurement of GTT for PbkKI/KI or PbkWT/WT mice on HFD (n=4 for each group) or chow diet (n=2 for each group) at various times, i.e., 0, 3rd, 5th, 8th, and 12th week during HFD-feeding. The AUC data of GTT at various time points were shown. *P = 0.0294, (Two way ANOVA). ns, not statistically significant difference.
(C) Still images from a TIRF time-series of p135 (green) binding to either WT (red), or CPA-treated porcine MTs (blue). Right, standard deviation map of p135 binding shows no preference for either type of MT, and quantification of mean fluorescence intensity (arbitrary units) per μm MT for p135 bound to CPA-treated MTs relative to WT MTs in the same chamber (n ≥ 10 MTs quantified for each condition from three independent experiments). Scale bars are 5 μm.
(G-I) HEK293T cells were ((H) transfected with STING and stimulated for 16 h with cGAMP (4 μg/ml) together with the reporter gene constructs indicated. Reporter gene activity was measured 24 h post transfection.
L Quantification of the bioluminescence signal emitted by H2030-BrM established metastases in organotypic cultures at day 7 normalized by the initial value obtained at day 0 and normalized to the organotypic cultures treated with DMSO. Day 0 is considered right before addition of the treatment or DMSO. Values are shown in box-and-whisker plots where each dot is an organotypic culture and the line in the box corresponds to the median. The boxes go from the upper to the lower quartiles and the whiskers go from the minimum to the maximum value (n=17 organotypic cultures treated with DMSO; n=18 organotypic cultures treated with BAY-218, 2 independent experiments). P value was calculated using two-tailed t-test.
Testis suspensions were stained with 2.5 µM DRAQ5 to determine cellular DNA amount. 1C-co = elongated spermatids, 1C = other haploid cells including round spermatids, 2C = spermatogonia, secondary spermatocytes, Sertoli cells, other somatic cells, 4C = primary spermatocytes, G2 spermatogonia.
Double immunolabeling of PDS5A (green, A-E) and SYCP3 (red) in Pds5AB cKO spread spermatocytes at the indicated stages.
G, Impedance-based mean (+/- s.d.) cell index values at the indicated time points of growth after seeding equal numbers of control, W1A and W6A cells, upon treatment with DMSO or Ruxolitinib. For the DMSO treatment: Control (n=4), W1A (n=3) and W6A (n=3). For the Ruxolitinib treatment: Control (n=6), W1A (n=3) and W6A (n=4). From 6 hours after DMSO treatment, there is a statistically significant difference between control and the two mutants (P < 0.05, two tailed t-test), whereas no statistically significant difference is found after Ruxolitinib treatment.
E FADD-D mice lost more weight as compared with WT on 20-h fasting (n = 4 for each genotype). Data are expressed as means ± SEM. *P = 0.0085 (Student's t-test).
J Flow cytometry analysis of BrdU incorporation in Lepr-Cre+Notch3+/- BMSCs after 3D co-cultured with bone marrow ECs (n=3 independent experiments). BrdU was administered at a final concentration of 10 µM from culture day 1 to day 5.
B Top, diagram of ASOs tested below, mapped to their position of complementarity on ApoER2. Bottom, RT-PCR of RNA isolated from HeLa cells transfected with the indicated ASO at a final concentration of 80 nM. RNA spliced forms are labeled. Quantification of the percentage inclusion is shown below the image and calculated as: Inclusion (%)=[exon 19 included/(exon 19 included+exon 19 skipped)] x 100.
Kinesin- and Dynein-dependent anterograde and retrograde particles (1 and 2, respectively) are shown harbouring IFT-A, IFT-B and BBS subcomplexes involved in ciliary cargo transport. Under normal conditions, any misassembly or partial disassembly of proteins from the TZ (3) can be recovered by the retrograde IFT machinery (4). Disruption of retrograde transport (and consequently, anterograde transport) leads to an accumulation of TZ proteins in a short, bulbous cilium as well as impaired TZ assembly and function (as observed in our temperature-sensitive IFT-dynein mutant at the restrictive temperature), phenotypes that are reversible when IFT is restored at the permissive temperature
Vero cells were infected at MOI 1 (or mock infected) and treated with bafilomycin-A1 (BAF-A1 0.2 µM) for the final 6h. Immunoblots probed for STAT1, STAT2, LC3 and GAPDH expression.
Domains of human HOIP and identified ubiquitination sites at K454, K458, K735 and K784.
E, Proteomic analysis highlighting ATF4 targets significantly down-regulated in THEM6 KO LNCaP AI cells when compared to CTL (p-value ≤ 0.05, FC = 1.3). Data information: Data are presented as mean values +/- SD. Data reproducibility: n = 3 independent biological experiments.
F. A375 cells were treated as indicated for 72 hr followed by immunoblotting of indicated proteins.
(B) Histones were isolated by acid extraction from HeLa cells one hour after UV (16 J/m2) or mock treatment and were loaded on a 4-15% gradient SDS-PAGE gel and stained with Coomassie Brilliant Blue. The different fractions originate from the same amount of cells and contain the non-acid-soluble proteins (pellet), histone H1 and high mobility group proteins (H1 fraction) or the core histones (core histone fraction). * indicates 21 kDa protein band, most likely representing histone H1. ** indicates several protein bands ranging between 10-15 kDa most likely representing core histones