EMBO/sd-character-level-ner huggingface dataset:
Volcano plots of phosphopeptide median Log2 fold-change (contraction/sham surgery) plotted against the -Log10 p-value in rat contraction (left) or mouse running (right). Colored dots represent significantly-regulated phosphopeptides (p < 0.05, n=5, moderated t-test). Gray dots represent phosphopeptides that were detected but not significantly altered in exercise.
A Yeast two-hybrid assay for the interaction of PknG with UbcH7. Yeast strains were transformed with the indicated plasmids, wherethe TAK1-TAB2 interaction served as a positive control. Left, low stringency. Right, high stringency.
(M-N") NR2F1 (red) and S100β (green, astrocytes) IF on cross-sections of human GW11 and GW14 ONs. Higher magnifications (M'-N") show that most of S100β+ astrocytes co-express NR2F1. Scale bars: 100µm for human sections,
DFL does not affect the cytokine-inducing activities of disulfide HMGB1 (ds-HMGB1). Mouse Bone Marrow Derived Macrophages were activated or not for 3 h with 3 µg/ml ds-HMGB1 (~100 nM) or 10 ng/ml LPS, in the presence of the indicated concentrations of DFL. The data points represent n=3 biological replicates, with avg ± sd, in one representative experiment (of 2 performed in different days). The levels of TNFα mRNA are not significantly different in the presence of increasing concentrations of DFL (one-way ANOVA plus post tests).
HEK-293 cells were transfected with an expression vector containing the murine PD-1, CD28, BTLA, CTLA-4, or ICOS gene and screened for cells stably expressing each gene. The transfected cells were stained with antibodies against the respective PD-1, CD28, BTLA, CTLA-4, or ICOS protein (open histograms) or isotype Ab (shaded histograms). Representative flow cytometric profiles showing the expression of each receptor. PD-1, CD28, BTLA, CTLA-4, or ICOS gene-transfected HEK-293 cells were stained with biotinylated TAPBPL-Ig and control Ig, followed by streptavidin-PE. Representative flow cytometric showing the binding of TAPBPL-Ig (open histograms) or control Ig protein (shaded histogram) to the transfected cells. The data are representative of 3 independent experiments.
Dose-response to EV20/MMAF after 5 days of treatment in BT474 cells resistant to T-DM1 (BT-TDM1R#1 and BT-TDM1R#6).
C Representative confocal images of cleaved caspase 3 positive cells (red) in the transversal tumor sections and viewed with a 20x objective. The stromal compartments were immunolabeled in green with an antibody against vimentin. HBCx-14 (TP53mutant) tumors from the different treated groups were collected at day 18. Scale bar=50 µm. c-cas-3: cleaved caspase 3.
(A) HepG2 cells were stably transfected with vector or FLAG-JFK. Cellular extracts were immunopurified with anti-FLAG immunoafﬁnity resin and eluted with FLAG peptides. The eluates were resolved on SDS-PAGE and silver-stained. The proteins bands were retrieved and analyzed by mass spectrometry.
V. cholerae ΔvrrA ΔmicV strains carrying the indicated reporter plasmids (x-axis) and either an empty vector control (pCtr), the pMicV, or the pVrrA plasmid, were cultivated in M9 and GFP fluorescence was measured. Fluorescence of the control strains was set to 1. The target genes were classified according to regulated only by MicV
Heatmap showing changes in CAGE signal upstream of motif-dependent 21U-RNAs upon ints-11 knockdown in an N2 and a tfiis mutant background. The total cpms corresponding to each nucleotide position upstream to 21U-RNAs are shown as a barplot (top part).
D. Volcano plot depicting the protein-protein binding partners of LSD1 depleting in PeTa cells treated with ORY-1001 versus DMSO. Proteins belonging to the LSD1 complex are marked in red, protein localization in blue and other protein interaction partners in green. FC, fold-change.
H, AltFUS mitochondrial expression in untagged altFUS transfected HEK293 cells following fractionation (representative image from n=3), with Tubulin as a marker of the cytosolic fraction and VDAC as a marker of the mitochondrial fraction (WCL = Whole Cell Lysate, Cyto = Cytosol fraction, Mito = mitochondrial fraction).
(A) O-GalNAc type O-glycosylation pathway. Biosynthesis of Core 1 type structures is shown. (B) Strategy for generation and characterization of GALNT isoform knock outs in HaCaT keratinocytes.
b, Autophagic flux by mCherry-GFP-LC3 puncta quantification upon purmorphamine treatment in MEFs in the presence of serum. Yellow, autophagosomes; red only, autophagolysosomes; total, both compartments. (*P = 0.0323, 40 fields).
A Analysis of Heparan Sulfate (HS) expression by FACS using the 10E4 antibody. Data information histograms representative (left panels) and MFIs from three independent experiments (*p < 0.05 and **p < 0.01; Student's t-test) are shown +/- SEM.
(E) Experimental plan for macrophage depletion setting. Mice were preconditioned for 3 days by i.p. injection with anti-CSF1R antibody (or isotype IgG control) before LLC (CD90.1+) tumor cell injection and then injected 3 times a week until sacrifice. When the tumor reached 80-100 mm3 mice were treated by gavage with vehicle or glufosinate (20mg/kg) for 14 days.
A. Elution profiles and SDS-PAGE for SEC runs on the indicated column of the Cyclin B1:CDK1 complex (blue profile), MBP-MAD1:MAD2 (red), and their combination (green). Note that the same Cyclin B1:CDK1 elution profile and SDS-PAGE is also displayed as reference in panels D and F to improve clarity. For the same reason, the MBP-MAD1:MAD2 elution profile and SDS-PAGE is also displayed in panels 2A-C. B. Elution profiles and SDS-PAGE for SEC runs on the indicated column of CDK1 (blue), MBP-MAD1:MAD2 (red), and their combination (green). C. Elution profiles and SDS-PAGE for SEC runs on the indicated column of Cyclin B1 (blue), MBP-MAD1:MAD2 (red), and their combination (green). D. Elution profiles and SDS-PAGE for SEC runs of the Cyclin B1:CDK1 complex (blue), MBP-MAD1∆93:MAD2 (green), and their combination (red).
C Cumulative probability plots of FOF1 a-mNG jump distances in E. coli WT and fabA(Ts) cells. For an analysis of cell-to-cell heterogeneity of median jump distances of FOF1 a-mNG, see Appendix Fig S13A.
A) A previous structure of SARS PLpro bound to a non-hydrolysable, Lys48-linked diubiquitin probe (pdb 5e6j, (Békés et al, 2016)) explained the noted preference of PLpro for longer Lys48-linked chains. While the proximal ubiquitin unit occupies the S1 site in a highly similar fashion in SARS~Ub and SARS2~Ub structures (see B, Fig 2A, EV2), the second, distal, ubiquitin unit binds to the α2 helix of PLpro, through a common binding mode involving the ubiquitin Ile44 patch. On helix α2, a central Phe70 in SARS PLpro residue is flanked by residues involved in polar contacts.
(D-F) Quantification of amount of MVBs per cell section (D), amount of exosomes per MVB (E), and amount of exosomes per cell section (F), based on TEM analysis.
Genes associated with indicated GO terms plotted by fold change in expression in Mta123∆ ES cells (x-axis) or Mbd3∆ ES cells (y-axis). Genes are coloured if they are differentially expressed (log2 fold-change > 1 and adjusted p-value < 0.05) in either comparison as indicated. The dotted lines show the fold-change cut-off of 2. GO-terms were identified using David v.6.8 using a Benjamini score with a cutoff of 0.05.
(E) Representative confocal microscopy images of immunostaining for CD4, Foxp3 and insulin in islet grafts. Scale bar = 50 µm.
(J) ChIP-qPCR analysis of the association of HIF1A with the promoter of thermogenic genes in 3T3-L1 cells differentiated into beige adipocytes. IgG was used as control. Consensus HIF1A binding sites were obtained from JASPAR database (a database of transcription factor binding profiles). Data information: The data were presented as the mean ± SD of triplicate tests (n = 3). Statistical analyses were performed using Student t‐test. ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001.
Flow cytometry of intracellular Foxp3 staining in CD4+ naïve T cells transduced with control retrovirus (MigRI) or retrovirus encoding C/EBPβ and cultured for 2 d under conditions as indicated. Representative experiments are shown in the left panel and pooled data from 4 (C with mean values are shown on the right. Dot plots are gated for CD4+GFP+ and numbers indicate percent Foxp3+ cells in the gate
A S6 phosphorylation after 6 h in SD‐N was analyzed by immunoblotting with a loading control.
Model of NuRD function during differentiation of pluripotent cells. NuRD facilitates lineage commitment of ES cells after exit from pluripotency (red arrows), allowing cells to form differentiated cell types (Top). In the absence of Mbd3, residual NuRD activity ensures cells retain the appropriate differentiation trajectory, but the cells are unable to reach a differentiated cell fate (dotted red arrows; Middle). In the absence of all three MTA proteins there is no residual NuRD activity and ES cells are unable to either achieve appropriate lineage commitment, or to maintain the proper differentiation trajectory (dotted arrows, Bottom).
(C) Western analysis of EPAC1 and EPAC2 abundance, as well as active GTP-bound RAP1 levels in the indicated early-passage cells during their log-phase growth period (n=3). Actin and total RAP1 were used as loading controls.
(C) Heatmap for the genes that are differentially expressed in kidney between WT ORX and WT ORX + T (q < 0.05; FC > 1.5) and corresponding levels in ARLmon/Y ORX and ARLmon/Y ORX + T.
B. Fraction (1/17th) of a typical field of view. In a microfluidic chamber, actin filaments (yellow) are anchored by their pointed ends and align with the flow.
(H) Recorded PV+ interneurons were filled with biocytin and their dendritic morphology was reconstructed using Imaris software. Scale bars: 30 μm.
(D) FACS assay showing interactions of Mtb H37Rv with different galectins including galectin-3, galectin-8, and galectin-9. The blank control was H37Rv staining with APC-anti-rabbit antibody alone.
(J) CSAG2 Δ37 mutant does not regulate p53 ac-K382 levels. Cells were transfected with the indicated Myc-CSAG2 constructs for 48 hr before being treated with 1 μM doxorubicin/ 0.4 μM TSA. Cell lysates were blotted for the indicated proteins.
G. ThT assays for the inhibition of Aβ aggregation. Fluorescence intensity was normalized to Aβaggregates (100%, day 5).
E Model of the molecular pathway primed by Activin A to safeguard quiescence in adult prostate progenitors.
(A) HT29 cells were infected with Shigella WT, S325, or ospD deletion mutants, and incubated for 8 h. Cell lysates were subjected to immunoblotting.
B, Measurement of lactate secretion from proliferating NSCs, and of NSCs differentiating for 3 days (switch to neurogenesis) or for 7 days (fully differentiated), normalized to cellular protein content (mean±SEM; N=6; *** p<0.001).
(C) Proposed model of Atg8-PE conjugate formation mediated by the Atg12-Atg5‐Atg16 complex. CBB, Coomassie Brilliant Blue staining; GST, glutathione S‐transferase; HA, haemagglutinin; PE, phosphatidylethanolamine; WT, wild‐type.
C) Most of the proteins whose abundance changed significantly over time differed between WT and CKO cells.
Venn diagrams showing the overlap between genes upregulated (FDR ≤ 0.01, Log2FC ≥ 1 and maxTPM ≥ 1) by EZH2i treatment in each cellular state.
F: IL-6 protein release in hEGC cultures upon stimulation with NTPDase inhibitor ARL67156 at indicated concentrations; n=4-6, hEGCs.
(F) WT, Pml-/-, Mk2-/- and Pml-/-Mk2 -/- mice were injected i.v. with TNF (1.5 mg/kg), and survival was monitored for 24 h. Data represent a combination of two independent experiments (n=10). *P < 0.05 for Log-rank (Mantel-Cox) test.
PTPA is an essential factor for PP2A mediated dephosphorylation of Ago2. Expression of PTPA after LPS stimulation in RAW 264.7 cells as well as in PEC isolated from BALB/c mice. β-actin is used as loading control (H).
HeLa cells were transfected with the indicated siRNAs (two control/non-targeting siRNAs and three PRMT1-specific siRNAs). The subcellular localization of p14ARF (exclusively nucleolar or not-exclusively nucleolar but predominantly nucleo-/cytoplasmic) was quantified by cell counting (percentage of cells) for all used siRNAs in (H) and for siControl_1 / siPRMT1_1 from three independent experiments in (I) (mean ± SD, ***: p-value ≤ 0.001 using Welch´s t-test).
A Bacterial two-hybrid analysis with HybA and/or HybB fused chromosomally with the T25 and T18 domains of B. pertussis CyaA, respectively in the absence of endogenous CyaA. Bacteria were grown on LB agar containing 20 µg/ml X-gal at 37°C for 14 hours in the presence/absence of O2. Scale bar, 1 cm.
Quantitation of the BODIPY signal shown as integrated total lipid for the genotypes The box end points are the upper (75%) and lower (25%) quartiles, the whiskers define the maximum 95th percentile and minimum 5th percentile values respectively, the central band is the median and the square is the mean. Data were analysed using the Kruskal Wallis test followed by Dunn's test for post hoc analysis for significance due to unequal sample sizes. ***p<0.001, **p<0.01.
(H) Immunoblotting analysis of Pdia4 and markers in the cytosolic (Cyto), nuclear (Nuc), membrane (Mem), mitochondrial (Mito), and ER compartments of Ming 6 cells using the indicated antibodies. Data information: Data from 3 experiments are presented as the mean ± SD.
(B) Results of the Western blot analysis for RAD21, E-cadherin, and VIM in RAD21KD- MCF7, -T47D, -SNU16, and -SNU620cells are presented.
(A) RAW264.7 cells stably expressing GFP-LC3 were transiently transfected with control or miR-155 mimic and then infected with Texas Red-labeled BCG for 1 h. The co-localization of BCG with LC3 was detected by confocal microscopy. (B) Quantification of the co-localization of BCG with LC3-positive autophagosomes is shown.
C, D RNF123 inhibits the SeV-induced, but not the cGAS and STING-mediated RANTES and IFN-β transcription. The transfection and treatment were as in A. Total RNA was isolated and Q-PCR (D) was performed using the indicated primers.
CO mRNA data in LDs in WT and the pif4;pif5 mutant at 22 and 27°C (WT 22°C data/simulation: as in (B-E); pif4;pif5 22°C data: dashed black lines, open squares; WT 27°C data: red lines, filled circles; pif4;pif5 27°C data: dashed red lines, open circles).
B Hypocotyl length, given as the mean ± SD, of plants grown as in (A) (R8, grey bars) or at 30 µmol.m-2.s-1 660-nm red light (R30, pink bars) showing partial insensitivity of pap8-1 to the PBG overexpression. Measurements are given in source data; in the order of the graph n equals (50, 133, 58, 43, 36, 112, 25, 60) δ-test (comparison of the mean) R8: δPBG/PBGp8-1= 20.38 corresponding to p-value < 10-31 δwt/p8-1= 0.5 < 1.96 not significant at α set to 0.05).
Representative GO terms of genes upregulated in MC1 (WT, red bars) or KMC1 (kit mutant, blue bars) from the uninjured hearts, respectively. Dotted lines indicate P= 0.05.
(A) Influence diagram of the network controlling the phosphorylation of mitotic substrates. The auto-activation of CycB:Cdk1 and PP2A:B55 is controlled by inhibitory phosphorylation and by the Greatwall-ENSA pathway, respectively. CycA:Cdk1 helps CycB:Cdk1 auto-activation and inhibits PP2:B55 activity through Greatwall phosphorylation. Three different classes of mitotic substrates (early, intermediate and late) are distinguished based on their sensitivity to CycA:Cdk1, CycB:Cdk1 and PP2A:B55.
The release of IL-18 (c) from THP-1 cells were measured by enzyme-linked immunosorbent assay (ELISA) following HSV-1 infection.
TRF1 immunofluorescence of the lungs. Notice the absence and presence of TRF1 signal in the carcinomas and surrounding healthy tissue of Trf1Δ/Δ mice, respectively.
C Negative correlation (rs and P are indicated) between histamine levels in LAM plasma and patient FEV1 (% predicted), at the time of blood sample collection. D Similar negative correlation (rs and P are indicated) between histamine and DLCO.
(D) Principal component analysis of tumor-associated myeloid cells vs blood monocytes and microglia from tumor-free mice. (n=3 per condition)
Quantitation of the number of PML-NBs/nucleus from cells treated as described in (D). Statistical significance via 2‐tailed Student's t‐test. Cell number analyzed: 192 - 430; p < 10-10. Automated PML-NB segmentation is based on PML signal. Representative pictures showing that Ubc9-depleted cells cannot efficiently induce the self-assembly of PML-NBs upon treatment with MG132 (10 µM) and OP-puro (25 µM) for 4 h. Scale bars: 10 µm.
C. Representative micrographs of the immunogold-labelled complex His6-TssA1/TssB1C1. The presence of gold particles is indicated with white arrows. Two close-up views of TssB1C1 sheath displaying gold particles at one extremity are shown (inset panels). Scale bars are 2,000 Å and 500 Å for images 1 and 2-6, respectively.
(B) 293 cells were transfected with indicated siRNAs for 48 h followed by real‐time PCR analysis of BAG1 and BAG3 mRNA levels. Depicted is the mean relative expression ratio (log2) ±s.e.m. *P0.05 and ***P0.001 versus nons, n=3.
(K) Co-IF for the proliferation marker Ki67, the mitotic marker phospho-histone H3 (pHH3), and Tbr2 to identify mitotic APs (division at apical surface) and BPs (division in basal VZ or SVZ) in control and DKO E13.5 neocortices. Arrowheads depict pHH3+Tbr2+ cells. (L) Average percentage of Ki67+ APs and BPs that are pHH3+ in control and DKO E13.5 neocortices. Data are means ± SEM (n=4 embryos, 3 litters).
(E) Whole-mount immunostaining images show neurofilament (red), netrin-1 (purple), and DCC (green), respectively. An E11.5 Plcg1f/f;Nes-Cre embryo showed shortened dorsal ramus and opthalmic nerves (white and yellow boxes). Scale bar: 200 μm
E Reaction of GST‐tagged TRAF6 (aa 1-285) with UBE2D3 as in (A). See Supplementary Fig S11E and F for additional TRAF6 reactions.
(D) Quantification of futsch mRNA levels obtained from isolated 3rd instar larvae brains of the indicated genotypes via real-time PCR analysis. Bars show average ± SD of biological triplicates. Bars are labelled with the number of replicates.
E. Substrate-binding pocket mutations Y90A and Y74A/Y90A/T105A/S107K affect the ability of ectopically expressed spMis18fl to rescue the temperature sensitivity of mis18-262 cells to varying degrees. Five-fold serial dilutions of mis18-262 cells transformed with plasmids harbouring the indicated spMis18fl constructs, spotted on PMG - uracil + Phloxine B media supplemented with (repressed) or without (expressed) thiamine, and incubated at the indicated temperatures; dead cells stain dark pink.
(A) XPO1 and STK38 are required for YAP1 nuclear export at high confluence. A549 cells were transiently transfected with the indicated siRNA (control and KPT conditions = siNT) at low or high confluency. 48 hours later, cells were incubated overnight in the presence of XPO1 inhibitors KPT-185 and KPT-330 (final concentration = 1 µM) or with DMSO for all other conditions. The next day, cells were fixed and stained for endogenous YAP1. Quantitative representation of YAP1 nuclear fluorescence intensity (n > 300 cells from 3 independent experiments, mean ± SEM; ***p<0.001, Mann-Whitney test). XPO1 activity inhibition by both KPT-185 and KPT-330 as well as STK38 silencing failed to induce YAP1 nuclear exit at high confluence
Brain transcription of mRNA species for various inflammasome components (n=6 mice per group). Data are expressed as mean ± STDEV, data for each cytokine were tested by unpaired t-test; *P<0.05, **P<0.01, ***P<0.001. Symbols above bars are versus WT
B. Distortion product otoacoustic emissions (DPOAEs) were detected in each ear, whereasC. Auditory brainstem responses (ABR) were lacking, together providing the signature of auditory synaptopathy or neuropathy.
(C) The number of GFP-LC3 dots per GFP-positive cell in (B) was quantified (mean ± s.d.; n = 81).
C, D GST pulldown assays of in vitro transcribed/translated 35S-Myc-CALCOCO1 constructs with indicated recombinant GST-VAPA or GST-VAPB constructs.The scheme is a representation of CALCOCO1 domains and motifs.
C Hypocotyl length of seedlings of (left) AtWT, pifq, pif7-2, ChWT, (middle) 35S:GFP-ΔNt-HFR1 (ΔNtHFR1), hfr1-5 and (right) chfr1-1 and chfr1-2 lines grown at warm temperatures. Hypocotyl lengths are the means ± SE of three biological replicates. Asterisks mark significant differences (Student t-test: * p-value <0.05, ** p-value <0.01) relative to the same genotype grown at 22ºC (left and right graphs, black asterisks), and between the indicated pairs (middle graph, red asterisks).
C, D NTN1 (C) and DAPK1 (D) gene expression in paired breast tissues (normal: green bars, tumor: red bars, RNAseq from TCGA breast cohort, n = 112 and 114, respectively.
B Western blot analysis of proteins renatured with either single-stranded or double-stranded M1x4 or M2x4 DNA oligonucleotides.
(I) HALO proximity histogram depicts the distance (μm) between the indicated cell types for individual mice (n=3).
(G) Scatter plot of codon-specific occupancies for 28 nt RPFs comparing eEF3d to WT cells from libraries prepared with CHX+ANS. Trend line (blue) and its slope are shown. Codons that encode proline and glycine are colored in purple and green, respectively.
B. Quantification of GFP RNA levels associating with RABIF in immunoprecipitation assays from the indicated cell lines. Note that even though RABIF binds several-fold more to RAB13(T22N) (see Figure 7A, B) it binds similarly to the wild-type and T22N RAB13 RNA, indicating that RABIF binds similarly to nascent RAB13. After translation, it is likely displaced upon GTP-loading of wild type RAB13, while it remains more stably bound to the nucleotide-free (T22N) form. N=6. Bars: mean ± s.e.m.. p-values: *<0.05 by analysis of variance with Dunn's multiple comparisons test.
(B) Redistribution of nuclear TDP-43 to the cytoplasm in a poly-GA/poly-GR double-positive cell. Note that nuclei of poly-GA/poly-GR double positive cells are frequently disrupted.
Schematic representation for construction of Rhoj mutant mice. Cre-loxP-mediated genetic recombination of the Rhoj-flox allele generates the Rhoj-KO allele by excising the RhoJ cDNA-polyA cassette inserted into exon 1 of the Rhoj gene.
(a) Each of the compounds induced LC3-II in primary neurons, as determined by western blotting. At 5 μM but not 0.5 μM, the compounds significantly increased LC3-II/GAPDH (b) and LC3-II/LC3-I (c) ratios (nonsignificant (NS), P > 0.05; 0.05 *P 0.01, **P 0.01; F = 13.74 (in b) and 9.74 (in c), one-way ANOVA with Dunnett's post-test). Error bars represent s.e.m. Values were pooled from five independent experiments.
F. The IgG or anti-m6A antibody enrichment of the WT-BZLF1 and mut-BZLF1 mRNAs was measured by RIP-qPCR in the CNE2EBV cell lines. Blank indicates CNE2EBV cells without plasmids transfection. The fold enrichment was determined by calculating the 2-ΔCt of the RIP sample relative to the input sample. The mean value of the m6A enrichment level on WT-BZLF1 mRNA was normalized to 1.
D-E, Quantification of FUS cytoplasmic granules, number (D) and area (μm2) (E) in cells over-expressing the bicistronic (+) or monocistronic (-) construct for FUS, FUS-G156E, FUS-R495x, FUS-K510E, FUS-Q519x, FUS-Q519I-fs527x, FUS-R521C, and FUS-P525L. Statistical comparisons are made between bicistronic and monocistronic versions of each construct (n=3 - biological replicates, mean ± SD, **** = p value < 0.0001, *** = p value < 0.001, ** = p value < 0.01, * = p value < 0.05, n.s. = non-significant, one-way ANOVA test with Sidak's multiple comparison).
MOAP-1 deficiency promotes tumor initiation. measurements of the number, diameter of the largest nodules and total liver weight of the 4.5-month-old WT and MOAP-1 KO mice (n=18 and 23 respectively) injected with a single dose of DEN (25 µg/g body weight) at 15-day-old.
A Illustration of the image analysis process. The inverted "Union Jack" look-up table (LUT) was used to better visualise GFP-Parkin clusters, which were then manually selected as regions of interest (ROIs) and the corresponding mitochondrial fluorescence intensity was measured. Data information: Data are given as mean and SEM, *= p < 0.05, ***= p < 0.001, ****= p < 0.0001. Scale bar = 10 μm.
(A) Four fetuses (named NW-1, NW-2, NW-3 and NW-4) with different eye morphology were retrieved at E44 by caesarean section