EMBO/sd-character-level-ner huggingface dataset:
(I) Transverse view of microtubule triplet STA in T. mirabilis. Microtubule protofilaments are indicated, as are the positions of the pinhead and the C-link (the A-link lies on the edge of the volume and is thus less well resolved in this STA - for better views see STA centered on A-C linker in panel K). At this contour level, MIPs are not visible. Arrowheads indicate external densities at the A-B and B-C inner junctions; chevron indicates C-stretch. Double arrowheads point to viewing directions shown in (J, K). (J) Longitudinal view of T. mirabilis STA centered on the pinhead, from the viewing point indicated in (I). Location of pinhead consisting of pinfeet (PinF1 and PinF2) and pinbody (PinB) are indicated, as are microtubule protofilaments A3/A4. The average distance between pinfeet elements is 8.4 ± 0.5 nm in each case (both N=5). Corresponding transverse view is shown below. (K) Longitudinal view of T. mirabilis STA centered on the A-C linker, from the viewing point indicated in (I). Microtubule protofilaments A8/A9 and C9/C10 of two adjacent triplets are indicated, as are the connected A- and C-links. The average distance between A- and C-links is 8.4 ± 0.9 nm (N=6) and 8.4 ± 0.3 nm (N=5), respectively. Corresponding transverse views are shown below, chevrons point to connections.
XBP-1S mRNA levels in LNCaP xenografts from animals treated with toyocamycin or vehicle. Tumors were harvested, RNA-extracted, and qPCR performed. Error bars indicate SEM. *P = 0.04 for LNCaP and **P = 0.02 for VCaP using unpaired Student's t-test.
RBM47 is an ISG and induced by viral infection. RBM47 binds to the 3'UTR of IFNAR1 mRNA, stabilizes it, and amplifies IFNAR1 signaling.
(H) Average TMRM staining intensity in Flp-In 293 HA-GFP or Flp-In 293 HA-IKKε cells treated with doxycycline (Dox) and DCA (both for 16 hours). Data are normalised to non-treated Flp-In 293 HA-IKKε cells.
A. Cartoon representation of the Dln1 dimer (PDB 4ZNO). Subunit A is colored in gray. The lectin module of subunit B is colored in yellow, whereas the middle and C-terminal moieties of the aerolysin module are colored in hot pink and green, respectively. The pre-stem hairpin is colored in blue. The bound sucrose molecules are shown as light pink sticks.B. The dimeric interface. Residues involved in dimeric interactions are shown as sticks.
Schematic representation of RHIM fibrils formed by full-length proteins with partner domains (e.g. kinase or RNR, coloured green) flanking either side of the amyloid core formed by RHIMs (coloured grey)
(D) AlphaScreen® assessment of the impact on the FLIP-FADD interaction of unstapled and stapled peptides corresponding to the FADD α1 helix.
B) Surface representation of the hMPV F structure in the postfusion conformation (Mas et al., 2016). One of the protomers is shown as a blue ribbon. Antigenic site II is magnified and colored as in (A) for the F-415 and F-416 chimeras.
Gene expression of major transcriptional regulators of energy metabolism HIF-1α) and stress responses (ATF4) in heart at P150. (n=6/group) Box plot whiskers represent quartiles, maximum and minimum value (relative fold change 'FC' to WT). Statistics: one-way ANOVA followed by Tukey's test.
K: Ambroxol blocks ATP-induced IL-6 release in hEGCs; Protein release measurement by ELISA of IL-6 in hEGCs. Cells were treated with ATP (200 µM) alone or together with ambroxol (20 µM) for 24h; n=6, hEGCs.
Thymocytes isolated from WT and Cd4cre A1fl/fl mice were stained with anti-CD4, anti-CD8, anti-CD25 and anti-Foxp3 antibodies and were gated on 4SP thymocytes. Representative images are shown (upper panel). The percentages of CD25+Foxp3+ 4SP thymocytes (thymic Treg cells) were compared between WT and Cd4cre A1fl/fl mice (lower panel).
The significant spine density deficit of AAV-Venus injected cDKO mice (red bar) in basal (J) and apical dendrites (K) was comparable and not significantly different (nsp>0.05) from that of AAV-APPsβ injected cDKO mice (blue bar). White bar: AVV-Venus injected LM controls. Images are maximum projections of z-stacks. Scale bar: 5 µm. Spine density is normalized to LM control levels. Age: 5-6 months; n=number of neurons (from 5 animals per condition). Data represent mean ± SEM. Data were analyzed by one-way ANOVA followed by Bonferroni´s post-hoc test. *p<0.05, **p<0.01, ***p<0.001, ****p<0.0001 .
cytokines in culture supernatants among naive 2D2 CD4+ T cells stimulated with MOG(35-55) plus DCs treated
E. Cumulative hippocampus-dependent strategy scores during the Barnes maze training (One-way ANOVA). n = 10 per group. F. Number of visits to the escape hole during probe test (n = 10/group, One-Way ANOVA). Data information: Bars and error bars indicate mean ± SEM.
(D) Selected gene expression changes (top) and enriched gene sets (bottom) taken from RNA-seq analysis of BV-2 cells with stable retroviral expression of Siglec constructs, 2xY->F, and empty vector controls. Heatmaps share a colormap range of 0.25 to 4 for z-score values (top), normalized enrichment scores (NES, bottom).
Deletion of cTAZ promoted nuclear accumulation of STAT1 upon IFN-α stimulation. RKO (WT and cTAZ-/-) cells treated with or without IFN-α (50 ng/ml) for 1 hour, fixed, and subjected to IF using STAT1 antibody (green). DNA was labeled by DAPI (blue). Scale bar, 50 μm. Quantification was performed using ImageJ software (right). N>C: nuclear; N=C: nuclear plus cytoplasmic; N<C: cytoplasmic localization.
Crosslinks (red dotted lines) connecting residues (shown in red spheres) between either CC1B (upper panel, in yellow) or CC1A (lower panel, in purple) and the pointed end (light orange and light brown).
(B, The IP complexes were subjected to in vitro kinase assay using phosphatidylinositol as substrate. The products radiolabeled PI3P were separated by TLC and detected by autoradiography. Data are mean ± SD of three independent experiments. The significance of differences between different assays was determined using One-way ANOVA analysis followed Dunn's multiple-comparison posttest, NS: not significant; *p ≤ 0.05.
B-F: TEM images o VAP-A and VAP-B (E: siVAP-A/VAP-B -silenced HeLa cells. An interpretation scheme representing contacts between organelles is shown on the right; the ER, endosomes and ILV are in dark, light and medium gray, respectively. Mitochondria and Golgi are in pink and light green, respectively. Scale bars: 500 µm
D BETA plot of combined computational analysis of histone Kcr ChIP-seq and RNA-seq data, peak regions located in bivalent promoters with increased histone Kcr as input.
(N) UMAP (left panel) and violin plots (right panel) of Col1a1 expression in murine wound fibroblasts. Raw scRNA-seq data are derived from (Haensel et al., 2020, Data ref: Haensel et al 2020).
(A) Poly(GP) levels were measured by MSD immunoassay in C9orf72 patient iPSC-motor neurons treated for 7 days with 8-16 µM of the G4C2 repeat G-Q binding small molecules DB1247, DB1247 and DB1273. Treatment with DB1246 or DB1273 leads to a significant reduction in poly(GP) levels relative to vehicle-treated controls. Data are shown as the mean and SEM of 3 independent C9orf72 iPSC lines, with 1-6 differentiations per line. *p<0.05, **p<0.01, *** p<0.001, one sample two-tailed t-test versus normalised control. p=0.0068 (DB1246, 12 µm), p=0.0417 (DB1246, 16 µm), p=0.0196 (DB1247, 8 µm), p=0.0002 (DB1273, 8 µm), p=0.0194 (DB1273, 12 µm), p=0.0062 (DB1273, 16 µm)
(C) Immortalized patient-derived skin fibroblasts transiently expressing wildtype or mutant COA7 (COA7-Y137C and COA7-Ex2∆) for 48 h were treated with bortezomib (20 nM) during the last 12 h. The fibroblasts were harvested, and complex IV activity was measured in digitonized cellular extracts. The results of three biological replicates were quantified and normalized to empty vector-bortezomib treated samples and the data are expressed as a mean ± SEM (n=3, *p=0.01 [Empty vector vs COA7- Wt], *p=0.005 [Empty vector vs COA7 - Y137C]).
qPCR of p21 induction upon DNA damage (10 Gy, 2h) with and without 0.4 M sorbitol. Mean ± standard deviation is indicated.
B, B1 Stress induced by subcutaneous injection of formalin‐triggered co‐expression of c‐fos and CRH in secretagogin+ paraventricular neurons (arrowheads). Scale bars: 300 μm (B), 25 μm (B1).
(G) Non-acetylation modifiable mutation of β-cat at K49 (K49R), not K19 (K19R), abolished the anti-apoptotic effect of Tau. N2a cells were co-transfected with Tau40 and β-cat WT, or K49R, or K19R for 48 h, and then treated with 0.5 μM STP for 4 h. The cell viability was measured by CCK8 assay (n=8 biological replicates each group). Data information: Data are expressed as mean ± SEM, *, P<0.05; **, P<0.01, ***, P<0.001 vs Vec plus STP ; #, P<0.05, ##, P<0.01, ###, P<0.001 vs vs β-cat + Vec plus STP (G) ; $$$, P<0.001 vs β-cat + Tau plus STP (G) ; &&&, P<0.001 vs β-cat K49R+ Tau plus STP (G). ♧♧♧, P<0.001 vs vec Data were analyzed by one-way ANOVA.
E, Average clockwise interval length, calculated as the inverse of the fast (blue) and slow (red) rate constants
Heat map of ratio ∆F/F (change in fluorescence to total fluorescence) in AWB::GCaMP3 neuron upon the addition (10 s) or the removal (130 s) of 1-undecene. Each row represents an individual worm recorded for 180 s under 1:100 dilution of 1-undecene, in 11 s-130 s window.
(d) Quantification of total tumour numbers per gut in sacrificed Vil Apc, Vil Apc Huwe1het and Vil Apc Huwe1hom mice. Deletion of Huwe1 led to a significant increase in the number of tumours per gut (Mann Whitney, n ≥ 5).
The stalling of replication forks is sensed as replication stress and leads to the exposure of ssDNA, which is recognized by RPA. In response to replication stress, the ATR/Chk1 pathway inhibits CDC25 in order to establish the G2/M checkpoint and prevent mitotic entry. In addition, the formation of GMGs is induced upon replication stress in late G2 and prophase nuclei. GMGs represent assemblies of TIAR together with components of the transcription, splicing and replication machineries, possibly reflecting active transcription at sites of stalled replication. TIAR retains CDK1 in GMGs and contributes to CDK1 inhibition during G2/M checkpoint activation. APH, DNA polymerase inhibitor aphidicolin; ATR inhibitor ATRi (ETP-46464); Chk1 inhibitors Gö6976 and UCN-01 (UCN).
(i) Midguts dissected from animals expressing mCherry-Atg8a in all cells, and expressing UbIR specifically in GFP-marked clones of cells at puparium formation. Representative images are shown.
e, The cell invasion (transwell, e) activity were determined in A549 cells co-transfected with cDNAs for GFP-tagged ISX and mCherry-tagged BRD4 mutants. Data are presented as mean ± SD in bar graph (p < 0.001, Student's t‐test) of 3 independent experiments, each performed in triplicate. Data information: Each experiment was repeated at least three times.
B Colocalization of K63- and K48-linked ubiquitin conjugates on individual lysosomes. Cells expressing GFP-TAB2-NZF (K63-sensor) were treated as in (A) and stained for K48 chains and LAMP1. Note that the apparent nuclear localization of the sensor is a consequence of the extraction procedure (van Wijk et al., 2012).
Schematics (A) of the experiment to examine the effect of T cell depletion on 5-FU response, during which anti-CD4/anti-CD8 antibodies (Ab), control IgG Ab, or anti-NK1.1 Ab were administrated on day 5 and day 9.
C, D Heatmap (C) and table (D) of FPKM values for selected genes in fdWT and fdsc-αDEC-pulsed DCs.
D. Photographs of vehicle- or tamoxifen-treated Ssrp1fl/fl; CreERT2+/+ mice seven days after start of treatment.
C. Organoids generated from WT, mutant, and null p53 cell lines. Scale bar: 100μm. D. Quantification of the portion of organoids exhibiting a solid, intermediate or stratified morphology (> 37 organoids from 2-3 cell lines per group).
(C) Total cell lysates were pulled down with anti-Rac1 or IgG isotype control antibody prior to immunoblotting. Uninfected cells serve as negative control. IP: immunoprecipitation; IB: immunoblotting.
J TEER value of Caco-2 cell monolayers after incubation with or without Tolimidone (10 μM) for 24 h was analyzed (n = 9 independent experiments). Data information: Data are means ± SD. One-way ANOVA followed by Bonferroni post hoc test was used for statistical analyzes. *p < 0.05; **p < 0.01; ***p < 0.001.
(A) Left panel shows the individual channels and overlaid images of confocal live cell imaging of HeLa cells overexpressing GFP-Bax (green) and mito-dsRed (magenta) at 0 and 85 minutes after apoptosis induction with STS 1µM. Right panel shows zoomed overlaid images of HeLa cells following GFP-Bax translocation (green) and mitochondrial fragmentation (magenta) during apoptosis induction with STS 1µM. Scale bars, 10 µm (left) and 2 µm (right)(B) Reconstructed dual-color superresolution image of GFP-Bax overexpressing HeLa cells. GFP-Bax was imaged by immunosstaining with AF647-anti-GFP-nanobodies and mitochondria were immunostained with CoxIV (primary) and cf680 (secondary) antibodies. Image was acquired 3h after STS treatment. Left panel shows the cell overview (scale bar, 5 µm), right panel up shows the overview inset (scale bar, 500nm) and right panel down shows a non-random linear GFP-Bax assembly at mitochondria (scale bar, 100nm).(C) Reconstructed dual-color superresolution image of HeLa cells co-overexpressing mMaple-mito and GFP-Bax and stained with AF647-anti-GFP-nanobodies. Image was acquired 3h after STS treatment. Lower panel shows enlarged insets corresponding to the white rectangles in the upper panel. Scale bars, 1 µm (overview) and 100 nm (insets)
H, I BIC1-mediated hypocotyl elongation was reduced by the addition of SRDX motif. Seedlings were grown for 5 days under long-day conditions. Images of the representative seedlings are shown in (H), and the hypocotyl lengths of the indicated genotypes were measured and are shown in (I). #1, #2, #3 represent different 35S:BIC1-SRDX-Flag transgenic lines. Data are means ± SD (n>20). **p < 0.01, as determined by Student's t-test. Scale bar, 2 mm.
b, c Phospho-sites identified after TiO2 enrichment b and phospho-tyrosine immunoprecipitation (pY-IP) c. Left panel: pie chart presenting the proportion of identified phosphorylated serines (pS), threonines (pT) and tyrosines (pY) in the two data sets. Right panel: cumulative number of unique identified phospho-sites across the biological replicates (3 and 4 independent experiments for the TiO2 and pY-IP, respectively). Phosphorylated serines, threonines and tyrosines are presented individually next to the total number of identified sites (pSTY). The phospho-sites that were not previously reported in any species in the PhosphoSitePlus database (www.phosphosite.org) are reported in isolation in the graph on the right.
A Tumor weight in KIC mice treated with βOHB (100mg/kg/day, i.p.) or 0.9% NaCl (i.p.) (n=13 mice for NaCl and n=15 mice for βOHB). Data are expressed as mean ± SEM. Significance was defined by Mann-Whitney test. *: p<0.05.
CLSM imaging of fresh Npc2+/hypo IMCs stained with filipin (cyan) and LAMP2 immunofluorescence (purple). Scale bars, 5 μm. Coarse structures strongly stained with filipin are surrounded by cytoplasmic membranous staining of LAMP2. Single-colour greyscale images are also demonstrated in the middle (filipin) and right (LAMP2).
F) Comparison of the mean laser recoil velocities in phase 3 for P35 overexpressing nests (green) with wild type (blue) at different distances (-40 - n = 17, -10 - n = 20, +40 - n = 15) Error bars represent Standard Deviations.
Quantification of localization of PG insertion sites from (A). Numbers are mean percentages. n = 393 bacteria (3 biological replicates).
N. Representative image of RGC axons. White, red and blue arrows indicate, respectively, co-localized, single MB, and single pre-miR-181a-1 puncta. Scale bars: 5µm.
C FACS analysis of MitoT on CD3+ human T cells after mitoception with increasing amounts of UC-MSC MT corresponding to the same cell number ratios used in co-culture experiments (n=4 biological replicates, with 4 different donors of UC-MSCs). Graph shows mean ± SEM and statistical analysis by Student's t-test.
G Heterochromatic silencing assays of wild-type and clr4 mutant strains. Silencing at the mating-type Kint2::ura4+ was evaluated.
Subcellular protein fractionation of several ER resident proteins in HEK293T cells treated with the indicated concentrations of Tm or Tg for 16 hours using Digitonin (NP40 represents the membrane fraction extracted with NP40 Cell Lysis Buffer) or differential centrifugation protocols, representative western blots are showed.
G Quantization of blots in F and normalized for loading to γ-tubulin. PTEN and LC3-II are significantly increased in cells transfected with TFEB with *P = 0.032 and 0.036, respectively (Student's t-test, n = 3).
G ChIP assays of H3K18Ac enrichment at the indicated loci as described in Figure 5H. H3K18Ac enrichment adjacent to the induced DSB in control and SIRT7 depleted cells (bottom left), or in cells overexpressing SIRT7 in the presence or absence of PARP inhibitors (PARPi) (bottom right) (mean ± SEM; one of two independent experiments is shown).*P < 0.05; **P < 0.01; ***P < 0.001; ****P < 0.0001 by ANOVA Single Factor.
F mRNA levels of bec‐1, epg‐8, lgg‐1, and atg‐7 are upregulated in dbl‐1(wk70), sma‐2(e502), and sma‐3(wk20) mutants. **P 0.01. 500 young adult animals were collected for analysis. Error bars indicate s.d. from three experiments.
(A) Co-immunoprecipitation data showed that PLCγ1 did not interact with the DCC receptor (n = 2, N = 3).
C. GAA activity in tissues from the Gaa KO mouse after treatment with rhGAA alone (black bars) (n of mice = 10) and with co-dosing of rhGAA and 2 gr/Kg/day NAC (n of mice =7, dark grey bars). Data presented as mean ± SD. Values obtained in tissues treated with rhGAA alone for each treatment are taken as 100. A Student's t-test was applied to compare the results in each of the tissues. D. GAA activity in tissues from the Gaa KO mouse after treatment with rhGAA alone (black bars) (n of mice =4) and with co-dosing of rhGAA and 100 mg/Kg/day IDE (n of mice =6, light grey bars). Data presented as mean ± SD. Values obtained in tissues treated with rhGAA alone for each treatment are taken as 100. A Student's t-test was applied to compare the results in each of the tissues. E
A. F4L5.13 prevents BRB defects and restores vascular morphogenesis in Tspan12-/- mice. 10 mg/kg F4L5.13 or isotype control antibody was injected i.p. every 48h from P5 to P20. Multiple images acquired at 10x magnification were stitched together to create a high-resolution image of a representative part of the retinal flat mounts. Scale bar 500 µm.
C The colocalization analysis of K63-Ub (Red), Flag-NLRP3 (Purple) and GFP- CCDC50 in HeLa cells; scale bars, 5 μM.
TNF-dependent induction of cleavage of PARP and Caspase 3 in primary Hoip+/+ or HoipK778R/K778R MEFs determined by immunoblotting. Total cell extracts of MEFs treated with hTNF (100ng/ml) and CHX (1µg/ml) for the indicated times subjected to SDS-PAGE followed by immunoblotting using antibodies as indicated. Anti-α-Tubulin antibody used to monitor loading amount. Representative data of two independent experiments.
A. Expression validation of mESC-specific SATS isoforms and their corresponding common isoforms by RT-PCR. The left panel shows the schematic structures of each isoform, with the first exons of the common isoforms and SATS isoforms named 1 and 1a (and 1b when multiple mESC-specific SATS isoforms were identified), respectively. Other exons are numbered according to their orders in the common isoforms. Due to space limitation, some canonical exons presented in both the common and SATS isoforms are omitted and represented by "//". The sites of forward primers (red) and reverse primers (blue) are marked at corresponding exons. mESC1 and mESC2 represent two different mESC lines; ADSC, adipose derived stem cells; NSC, neural stem cells; MEF, mouse embryonic fibroblasts; TTF, tail tip fibroblasts; NC represents PCR negative control without template. Numbers in parenthesis represent the abundance rank of SATS isoforms.
(G) Same assay as shown in (F) but using an anti‐Ape1 antiserum for western blotting.
(F) Immunofluorescence and IHC staining of Nfatc1 and Sirt7 in HFs of 15-month-old Sirt7+/+ and Sirt7-/- mice. The white/black dashed line indicates bulge (Bu) of hair follicle.
(C) Wild‐type MEFs were transfected with control or cortactin siRNA, treated MG132 2.5 μM for 18 h, and subjected to filter‐trap assay using a ubiquitin antibody. The knockdown level of endogenous cortactin was confirmed by immunoblotting using an antibody against cortactin and GAPDH in the right panel.
Heat map indicating the relative expression levels of DDR and cell cycle-related gene transcripts in MEFs from indicated genotypes (Data are extracted from RNAseq datasets).
(B) Detailed interactions between residues from the RBD (green) and scFD20 involve VH CDR3 (magenta), VL CDR1 (orange), and VL CDR2 (cyan). FD20 residues are labeled black and RBD residues are labeled grey. A prime symbol indicates residues from VL CDRs.
(C) Mock treated or Sept2 depleted Drp1 -/- MEF cells were labeled with mitotracker orange (red), treated for the indicated amount of time with 2µM FCCP and stained for actin with phalloidin (green). Insets are enlarged twofold.
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.
TIGAR regulates intracellular ROS levels in response to nutrient starvation or metabolic stress. (A) ROS levels in U2OS cells stably over-expressing Flag-tagged-TIGAR (clones TIGAR#5 and TIGAR#7) or control cells (clones Cont#1 and Cont#3) left untreated, after 6 h of nutrient starvation or 24 h of metabolic stress. ROS levels were measured by flow cytometry after DCF treatment. The results are expressed as the mean DCF fluorescence (and standard deviation), from three independent experiments.
G. Quantification of GFAP immunostaining in control virus-positive cells and Daam2 overexpressing cells. Data is presented as mean ± SEM. n= 22 images from N=3 mice per genotype. Relative fluorescent intensity was quantified, and Student's t-test was used, **** p<0.0001.
A-L Double immunolabelling of CETN3 (green) and SYCP3 (red) on squashed WT mouse spermatocytes at (A) leptotene, (B) zygotene, (C) pachytene, (D) metaphase I, (E) telophase I, (F) early interkinesis (F), late interkinesis (G), prophase II (H), metaphase II (I), telophase II (J), round spermatid (K), and elongated spermatid (L). Amplifications at 300% magnification for the centrosomic CETN3 signals are presented for each image. Chromatin has been stained with DAPI (blue). Scale bar in L represents 10 μm.
Cideb deficiency impairs the packaging of SCAP/SREBP into COPII vesicles. Protein present in the vesicle or microsome fractions obtained from WT or Cideb-/- liver were detected by IB. Quantification of IB data from 3 independent experiments. Data information: Data represent the Mean ± SEM; NS: not significant, *: p < 0.05, **: p < 0.01, ***: p < 0.001, by 2-tailed Student's t test.
Numbers of weaned mice of the indicated genotypes from crosses of Hoip+/K778R; Sharpin+/cpdm mice.
E, F AUCell scores for the 'αβ and γδ TCR shared' signature (left panel) and for the 'γδ TCR only' signature (right panel) among the UMAP plot of cells corresponding to Datasets 1 (E) and 2 (F).
(B) Representative immunofluorescence images of HeLa cells in various mitotic stages. Cells were extracted, fixed, and co-stained for Cyclin B2 (green), ACA (red), and DNA (blue). Scale bar, 10 µm.
Analytical ultracentrifugation (AUC) of PTPIP51_TPR and PTPIP51_ΔTM. The molecular weights of recombinant PTPIP51 calculated and estimated in AUC experiments are shown. All fusion tags were removed from the respective recombinant proteins for the AUC experiments.
F: Pie chart showing the number of genomic regions co-bound by NANOG and OCT4 in EsrrbHi E-GFPd1 ESCs that lose binding of NANOG and OCT4 (Class I) or that lose binding of NANOG but retain OCT4 (Class II) during transition to EsrrbNeg. A few regions keep NANOG binding but lose OCT4 (n = 16) or keep binding of both (n = 60).