EMBO/sd-character-level-ner huggingface dataset:
Release of TNFα (6 h pi), IL-6 (48 h pi), IL-1β (48 h pi) detected by Bio-Plex® Multiplex Immunoassay in the supernatant of mock and IAV infected BALO cultures with and without TR-Mac (n=3 biological replicates)
(f) Left, brain sections stained with Fluorojade B in rats injected with saline (n = 6), TAT-GluN2B (n = 5) or TAT-GluN2BCTM (n = 5) after treatment as shown in a. Right, quantification of cellular damage by counting the number of Fluorojade B-positive cells in each 640 × 640 pixel image at 10× magnification. TAT-GluN2BCTM (10 mg per kilogram) displayed more prominent neuroprotection in the cortex (P 0.001) and striatum (P 0.001) as compared to TAT-GluN2B (10 mg per kilogram). Cortex: H(2) = 41.235; P 0.001; striatum: H(2) = 38.808; P 0.001. Kruskal-Wallis ANOVA on ranks with Dunn's post hoc; bars represent relative means ± s.e.m., ***,ΔΔΔP 0.001. n values represent tissue from 3 animals collected from at least 2 litters. Scale bars 1 mm in b,c,e, 20 μm in f. Full-length blots are presented in Supplementary Figure 9.
Simple western analysis (Peggy Sue) of nuclear fractionation shows an increase in nuclear actin, ph-EZH2 and PO2-S2p levels in injured AECs. RNAi-mediated depletion of IPO9 (siIPO9) prevents injury-induced nuclear actin and POL2-S2p.
qPCR quantification of PAX6A and PAX6D gene expression under the treatment of DOX (n=3 biological replicates for each sample).
(B) Kymographs of pole (bottom)-to-cortex (top) line scans of control and CITK-depleted EB3-tdTomatoHeLa cells. The maximum projection of a 20-pixel-wide line (exemplified above) was plotted at 500 ms time intervals from left to right. MT growth results in diagonal lines.
Microglia infiltrating the rd10 retina upregulate IL-1β expression during degeneration. Iba1+ microglia (green) were immunonegative for IL-1β (red) at P18 but become prominently IL-1β immunopositive at P22 (arrows). Scale bars, 25 μm.
A, B ISH of miniature pig canine frontal sections showing expression patterns of RUNX2 at embryonic day 60 (E60) and E90. (A', B') are magnifications of boxed regions in the corresponding figure panels. Data information: Scale bars = 50 µm.
F. Prevention of superoxide release in activated human control and SIGLEC11/16 knockout THP1-macrophages by polySia avDP20. Cultured human THP1-macrophages were stimulated with RPE cell debris or co-stimulated with debris and polySia avDP20. Addition of debris stimulated the production of superoxide. 1.5 µM polySia avDP20 completely prevented the release of superoxide induced by debris challenge. No response to polySia avDP20 was detectable in the knockout macrophages. Data are presented as mean +/- SEM. n=6. p* ≤ 0.05, *** p ≤ 0.001, ANOVA followed by Bonferroni. Untreated WT macrophages vs debris treated WT macrophages p = 0.037, debris treated WT macrophage vs debris plus polySia avDP20 1.5 µM treated WT macrophages p < 0.001, debris plus polySia avDP20 WT macrophages vs KO macrophages p = 0.001,
(B) Single confocal section showing colocalization of Atg5-Atg12/Atg16-eGFP and mCherry-Atg8 on GUVs.
(E) Cumulative distribution plot of the density of AGO2 clusters in the 3'unstralated regions of AGO2 bound mRNAs (AGO2 cluster>0) whose degradation rates were either significantly (n=711, red) or not significantly changed (n=1127, black) between KO and WT cells, based on the 10 minutes pulse estimates. Density of clusters presented in this analysis was estimated based on data from (Leung et al., 2011).
E) Representative images of Miro1 truncation constructs expressed in DKO MEFs. Mitochondria and peroxisomes are stained with Tom20 and catalase, respectively. White arrowheads highlight an area where an isolated peroxisome is situated.F
Flow cytometry sorting scheme for isolation of secretory cells (EpCAM+KDR+) (B) and experimental designs for organoid cultures (C). Secretory cells were isolated from unlabeled Lats1/2 dKO lungs, followed by 3D organoid co-cultures with stromal cells. 3D normal media was changed to experimental media 1 day prior to 4-hydroxytamoxifen (4-OHT) or ethanol (EtOH) treatment. Organoids were analyzed at day 8 post 4-OHT or EtOH treatment.
(B) individual and dual colour kymographs showing GFP-dynein (green in merge) localising to the plus ends of dynamic Alexa568-microtubules (Alexa568-MT, magenta in merge). Protein concentrations were 10 nM GFP-dynein, 20 nM human dynactin, 20 nM EB1 and 17.5 µM Alexa568-tubulin (5% labelling ratio).
Leaf tissues from wild type (WT) and atg7 expressing NBR1-TAP were collected at indicated hours (h) under 45°C and prepared for soluble and insoluble proteins as described in Materials and Methods. Proteins from the first supernatants (S) and last pellets (P) were subjected to SDS-PAGES and probed with a peroxidase-conjugated anti-peroxidase antibody for detection of NBR1-TAP. Protein samples prepared from non-transgenic Col-0 wild-type plants were included as controls.
Western blot analysis of Flag-RNF8 denaturing-IP in HEK293 cells showing K48-linked hyper-ubiquitination of RNF8 after siRNA-mediated p97 depletion.
Fb Act (clone 2) or Fb EV cells were cultured together in 2D with SCC13 cells. After 7 day of culture SCC13 cells were identified by K14 and the number of K14-positive colony area was quantified. N=6.
(A) GFP-p62 or -SNX18 full-length, SH3-LC, or PX-BAR regions were in vitro translated and incubated with GST-LC3B or -GABARAP. The resulting pulldowns were separated by SDS-PAGE. Bound proteins were detected by autoradiography and GST proteins by Coomassie blue staining.
Western blot analysis of FoxO1, PDK4, p-PDHA1 and PDHA1 in GAS muscles of WT and DKO mice. Western blot analysis of FoxO1, PDK4, p-PDHA1 and PDHA1 in C2C12 cells transfected with Ago-183/96 (left) or Ant-183/96 (right).
(c) GST-Beclin-1 (1-85) was subjected to an in vitro ULK1 kinase reaction and analysed by mass spectrometry. Ser 14, Ser 15 in humans (outlined), is the main phosphorylation site identified (for mass spectrometry data, see Supplementary Fig. S2b,c). Mass spectrometry was performed on a single experiment.
B. Class averages of antibody-bound T4SS3-10+D4FLAG. Class averages of the aligned NS-EM images of the T4SS3-10+D4FLAG with 3-4 particles per class. Red circles indicate the position of the antibody.
(E) Western blotting of in vitro ubiquitination assays of eS7A. The reactions were performed with the indicated components including His-tagged ubiquitin. Ribosomes were purified from Hel2Δ cells expressing HA-tagged eS7A. Polyubiquitinated HA-tagged eS7A (eS7A-3HA) was detected by Western blot analysis using an anti-HA antibody. We observed Hel2-mediated polyubiquitination of the monoubiquitinated eS7A.
F Left panel, western blot results showing overexpression of catalase (CAT) in Tsc2-deficient MEFs, and unaffected by exposure to everolimus (independent experiments n = 2). The CAT expression level is indicated by the ratio of the corresponding signal relative to loading control and basal setting (noted as 1(ref)). Right panel, Cat overexpression (log10-fold change) in Tsc2-deficient MEFs. The asterisks indicate significant difference with two-sided t-test (P = 1x10-2; replicates/condition n = 3, and independent experiments n = 2). The bars indicate mean ± SD. Dotted horizontal lines indicate 2-fold (top) and 0.5-fold (bottom).
Representative confocal z-stack images of co-immunostaining for β-galactosidase (green) and CAMKII (red, upper) or GAD67 (magenta, lower) in neurons from the brains of Cdc50a knockout-first allele (Cdc50a lacZ/+) mice. Scale bar, 20 μm.
C. Mutation of Miro1 EF-hands diminishes Miro1 ubiquitination with S65-phosphorylated ubiquitin. HEK cells were transfected with EYFP-Parkin with either myc-Miro1-WT or myc-Miro1-EF with or without PINK1-V5. Cells were treated with either DMSO or A&O (both 10 µM) for 5 hrs with the exception of the PINK1-V5 group. Myc-Miro1 was immunoprecipitated and probes were immunoblotted for Miro1 (red), S65-Phosphoubiquitin and PINK1-V5 (green; the weak bands marked with the asterisk are nonspecific).
Browser representation and independent northern analysis and AGO1-loaded miR165/166.
(A) Expression of +1CGG-nLuc-3xFLAG RAN translation reporters in HEK293T cells treated with 2 μM TG (for stress induction) analyzed by immunoblot (n=3 biological replicates). To evaluate effects of SRPK1 inhibition cells were pre-treated with DMSO or SRPIN340 before reporter transfection. Data information: Error bars represent mean +/- SD. Two-tailed Student's t test with Welch's correction. ∗p < 0.05; ∗∗p < 0.01; ∗∗∗p < 0.001 and ∗∗∗∗p < 0.0001.
Representative IF images showing the average intensity of endogenous BRCA1 at UV-A micro-laser-induced DNA damage tracks in U2OS cells. (Scale bar; 10µm).   Graph represents the quantification of (F). (ns P>0.05, ***P<0.001; unpaired t-test, n=2, mean +SEM, at least 100 nuclei per condition and experiment).
G: USV, Analysis of call type complexity. NexCre cTKOs used simple calls either with similar or reduced frequency (downwards). Note that NexCre cTKOs used complex call types less frequently. Simple call types: Short (Mann Whitney test; ns, p = 0.0747), Flat (Mann Whitney test; ns, p = 0.2172), Upwards (Mann Whitney test; ns, p = 0.2383), Downwards (Unpaired Student's t-test; LM n = 1359 calls, NexCre cTKO n = 1507 calls; **p = 0.0085) and Chevre (Welch's test; ns, p = 0.1281). Complex call types are Two Syllable (Mann Whitney test; ns, p = 0.2380), Frequency-Steps (Mann Whitney test; ns, p = 0.5246), Composite (Unpaired Student's t-test; LM = 2258 calls, NexCre cTKO n = 722 calls; **p = 0.0086), Waves (Welch's test; LM = 403 calls, NexCre cTKO n = 88 calls; **p = 0.0039) and Harmonics (Mann Whitney test; LM = 711 calls, NexCre cTKO n = 197 calls; ****p < 0.0001).
C Tumor growth curves in WT and KO mice treated with either PBS or anti-mouse Ly6g (n=5).
(E) Western blot analyses of DDX5 protein in gastric cancer cells with the enforced expression of lncPSCA.
(B) The effects of α-KG on the HU sensitivity of snf1Δ and other checkpoint mutants. Yeast spot assays were performed as in Fig 2A.
G Embryonic myosin expression revealed by immunostaining along with laminin (green) on transverse cross-sections from limb of WT (n=5), mdx (n=8) and mdx/CD38-/- (n=8) mice. Scale bars: 50 µm. Dot plot showing the relative proportion of embryonic myosin area in limb of WT, mdx and mdx/CD38-/- mice. Data information: Each dot of the graphs represents a mouse. one value/mouse; After normality and variance comparison tests, significance was assessed using: G: Welch's ANOVA followed by Welch's t-tests. Values are expressed as means ± SEM. Significance: *p<0.05, **p<0.01, ***p<0.001.
A Negative stain micrograph of a sheet formed by purified UMOD filaments in 100 mM NaCl (top). Analysis of this material by correlation averaging reveals a periodic pattern (bottom) with a two-fold symmetry axis perpendicular to the plane of the sheet (white symbol). Scale bars: 250 Å (top) and 125 Å (bottom).
K. The cumulative cognitive score calculated for each day on the basis of hippocampal dependent strategies was significantly impaired when comparing WT control mice to APP control mice. Data is normalized to WT control group. Bars and error bars indicate mean ± sem. Number of mice: WT-control, n = 17, male: 9, female: 8; APP-control, n = 8, male: 6, female: 2; APP miR-inhibtor mix, n = 12, male: 8, female: 4. L. Comparison of the number of visits to the platform during probe test. WT-control: 4.76 ± 1.82 (mean ± std. deviation), APP-control: 2.5 ± 2.5 (mean ± std. deviation), APP miR-inhibitor mix: 3.41 ± 2.15 (mean ± std. deviation). Bars and error bars indicate mean ± sem. Number of mice: WT-control, n = 17, male: 9, female: 8; APP-control, n = 8, male: 6, female: 2; APP miR-inhibtor mix, n = 12, male: 8, female: 4.
(d-f) Akt Ser473 phosphorylation measured by flow cytometry (d,e) or immunoblotting (f). FL83B cells (d,e) or WT primary hepatocytes (f) were pretreated with conditioned medium (CM) generated from WT, Pycard−/− (d), Nlrp3−/− or Casp1−/− (e) macrophages for 24 h, then stimulated with insulin. Control medium was obtained from wild-type BMM cultures without stimulation.
A. Patient 1 (older sibling) underwent 3 MRI studies, first and last are shown. Top row: 21 months; Bottom row: 4 years 7 months. The corpus callosum is thin on T1 weighted sagittal images (I, V, VI) with a saber-shape (long arrows). The shape remains consistent over time. The vermis is normal in configuration and size initially (I), but demonstrates volume loss on follow-up (V, VI) examination (short arrows). FLAIR axial image (II) is age appropriate, while (VII) demonstrates periatrial increased signal (arrow). There is delay in myelin maturation present on T1 (III, VIII) and T2 (IV, IX) weighted axial images (long arrows) on initial examination, with further slow myelin development over time. There is deficiency of periatrial white matter volume on both T1 (III, VIII) and T2 (IV, IX) weighted axial images (short arrows). Coronal T2 image (V) demonstrates abnormally increased signal of the dentate nuclei (arrow), unchanged on follow-up image (X). Superior vermian atrophy (short arrows) over time.
F Expression of thermogenic genes and brown adipocyte markers in iBAT of Cdk4+/+ (n=6) and Cdk4-/- (n=6) mice as assessed by RT-PCR.
H) Median distances from the closest pDHS to the closest iDHS grouped according to the fold induction in TM after 2 hours plus PMA/I compared to TM.
(E) RT-qPCR analysis of relative Fancc or Fancl mRNA levels from whole brains from mock- and ZIKV Paraiba infected Ifnar-/- newborn mice. Mean ± SEM of n=3 biological replicates, ***p < 0.001 by Student's t test.
D. Representative staining for P-Smad1/5 in crypts from wild-type and Angptl2-/- mice following DSS treatment for 6 days and then untreated water for 6 more days (DSS) or untreated water for 12 days (Untreated). Dashed lines indicate half of the crypt and arrowheads show P-Smad1/5-positive cells in lower halves of crypts. Scale bar = 50 μm.E. The number of P-Smad1/5-positive cells in the crypt base (n=60) from wild-type and Angptl2-/- mice following DSS treatment for 6 days and then untreated water for 6 more days (DSS) or untreated water for 12 days (Untreated). Multiple areas in 3 mice per genotype were quantified.
Huh-7 cells were first serum-starved and then incubated with oleic acid for the indicated time before staining with Bodipy 493/503, TRAPPC9, Rab18 and γ-COP.A. In the merged images, bodipy 493/503 was pseudocolored in green, TRAPPC9 in red, and ADRP in blue. In the colocalization between TRAPPC9 and ADRP on the right side, the ADRP signal was re-colored to green for easy visualization. Bar = 10μm.
WB analysis of markers of endocytic trafficking and degradative pathway in the dorsal striatum of Tor1a+/- mice. A) The level of β-arrestin 2 (β-Arr2) is not altered (Tor1a+/+ N=11, Tor1a+/- N=12, t test P=0.6796), whereas the level of spinophilin (B) is decreased (Tor1a+/+ N=5, Tor1a+/- N=8, t test *P=0.0151)
(a, b) IB3-1 cells were transfected with either HA-tagged human beclin 1, empty vector, p62 siRNA or scrambled oligonucleotides followed by rosiglitazone (10 μM). (a) Cells were immunostained with anti-HDAC6 (red) and anti-PPAR-γ (green) antibodies. Yellow indicates co-localization. N, nucleus. Scale bar, 10 μm.
200 µg of yeast protein extract in different buffer compositions was processed by R2-P2 followed by DDA-MS peptide analysis. Sample preparation was performed in triplicate. Mean count of unique phosphopeptides are shown for the different conditions (n=3).   Fraction of phosphopeptides with 0, 1 or 2 missed cleavage sites. The mean is displayed (n=3).   Boxplot depicting phosphopeptide MS1 signal intensity distributions.   Boxplot depicting coefficients of variation (CVs) distributions for phosphopeptide MS1 signal intensities (n=3).
(M) Abstracted HF cycling in Sirt7−/−, Sirt7+/+, Sirt7-TG and WT mice mentioned above. The red star indicates anagen entry in Sirt7−/− and Sirt7-TG mice; the black arrows show the date of doxycycline feeding.
D. Average density plot of ChIPseq read counts of H3K27me3 at -/+ 5 kb from the TSS of refseq genes in ESCs treated with siRNA-control or siRNA-Baz2a Q1: first quartile corresponding to sequences with high H3K27me3 content. Q2-4: quartiles 2-4 corresponding to sequences with low H3K27me3 content.
C, D Representative images of γH2AX (green), telomere immuno-FISH (red) in DC cells treated with vehicle or 3 mM NR. White arrows: co-localization of γH2AX foci and telomeric DNA (or TIF). Enlarged views of co-localizing foci are shown at the right panel and in Figure EV1. Percentage of DC and control cells with indicated TIFs per nuclei. ~ 100 cells per condition were scored.
B, C. Representative images of Control and cKO with EYFP and DCX staining three weeks after TAM treatment. Note that the numbers of DCX-positive cells are increased. Boxes indicate magnified regions in C.
Electron microscopy showing two adjacent mitochondria (one intact and one ruptured) in a DM platelet. a. Lower powered view of the single DM platelet. b. The enlarged inset highlights the ruptured mitochondria (with loss of cristae morphology) next to the intact mitochondria. c. Black dash line indicates mitochondria membrane and red dash line indicate phagophore formation. (M- mitochondria)
(B) Lon surveillance of truncated protein variants. As an example, an N-terminal FLAG-tagged derivative of MPN304, which encodes a truncated variant of ArcA (ArcA-Nt), was expressed in the ΔIndLon mutant, and its accumulation monitored over time under non-inducing conditions using anti-FLAG antibodies. Anti-Lon antibodies were used to monitor Lon depletion along the time course experiment (western blot figure on left). MPN304 stability was also assessed by in vivo degradation experiments in Lon depleted mutants (36h of depletion), in which protein expression was blocked with gentamicin (Gm) during the indicated time points after transient induction of Lon for 3h. As control, samples after Gm treatment were also taken from non-induced samples. LC, loading control (western blot figure on right). Immunoblots are representative of two independent experiments. A schematic representation of the arginine deiminase pathway, which is inactive in M. pneumoniae, and the estimated protein copy number of its components are also shown for the ΔIndLon mutant grown in inducing (+) or depleting (-) conditions.
(H) Representative Western blot and densitometric quantification of phospho-AMPK and total AMPK in mouse gastrocnemius (n=6). Data information: For all data, n represents the number of biological replicates. Statistical significance was calculated by unpaired, two-tailed Student's T-test. Data are mean ± SEM. ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001.
(e) Wild-type Parkin colocalization with impaired mitochondria after 2 h of CCCP treatment was analysed (n = 4). (g) Quantification of results from cells in e.
H. The TBK1- and IKKε-activating agonists poly(I:C) and LPS increase mTOR P-S2159 in a BX-795 sensitive manner in cultured macrophages: RAW264.7 macrophages were pre-treated with BX-795 [10 μM] (2 hr.) and stimulated -/+ poly (I:C) [30 μg/ml] or LPS [100 ng/ml] (60 min).
D. VEGF-Ahyper mice have decreased levels of the major antioxidant in the lens, reduced glutathione (μmol/gm lens weight), prior to cataract formation. Lenses with 0 to +1 cataracts from 11-months old mice were used for measurements. ** P-value: 0.0097. N=7/group (2 independent experiments).
A, Quantification of iNOS expression on gated macrophages (CD11b+ F480+) from MC38 and KPC tumours, with representative histograms. Data are presented as mean ± SEM and analysed by Mann-Witney (n=6 mice/group).
E Proportion of mitochondria with 0 to 6 or more MAMs are shown for each cell line, as DX/REL pairs. Data information: n=137-241 mitochondria per cell line
J Tex11-deficient mice produced XY aneuploid spermatozoa. FISH assay of Chr X (green) and Chr Y (red) was performed in Tex11+/Y and Tex11-/Y spermatozoa. Nuclei were stained with DAPI (blue). The arrows indicate the Y chromosome, and the arrowheads indicate the X chromosome.
Expression data dot plots of genes found differentially regulated in cluster C1 between day 23 BALO with (C1+) and without (C1-) microinjected TR-Mac. The circle size illustrates the number of cells expressing a specific gene
Expression of different cytokines and phosphatases in RAW 264.7 cells and PEC infected with Leishmania donovani (Ld) parasites. A scheme of the experiments is shown in panel A.
The identified DEGs separated HO-1-/- and HO-1+/+ ECs by (B) hierarchical clustering and (C) PCA.
(d) Dynamic simulation of AV and CC stresses normalized values in arbitrary units (from Movie EV9 - 40 %; 65 %; 80 % epiboly) represented as in Figure 1a. The AV and CC stresses are equal at the poles, as the epiboly simulation progresses, the CC stress steeps up from animal to vegetal and the difference between CC and AV stresses change sense at the EVL / yolk margin.
C. Effects of LINC00115 knockdown on neuro-like sphere formation (C). Data information: data are representative of three independent experiments. Error bars, ± SD. *, p < 0.05, **, p < 0.01, by One-way ANOVA in
A. Schematic representation of generation of expanded CD4+ T cells and reactivation. CD4+ T cells were sorted from PBMCs of ARVs suppressed HIV-infected individuals and expanded in presence of PHA, IL-2, and autologous feeder PBMCs from healthy donor.
RAB21 is required for endosomal sorting of direct clathrin-independent cargos. RAB21 associates with WASH/retromer subcomplexes at endosomes. RAB21 could either i) recruit WASH/retromer or ii) be recruited by WASH/retromer or iii) be part of a positive feedback loop that would allow WASH/retromer and RAB21 recruitment at endosomes. Endosomal RAB21 would be required for WASH-mediated F-actin polymerization. Although the data does not directly demonstrate a direct link between F-actin generation and cargo sorting, we propose that RAB21-dependent F-actin generation would be required for sorting of a CIE cargo subclass (MCT1, SLC3A2, Basigin and CD44), while it would not be required for other cargos (CI-MPR or Glut1). In RAB21 knockout cells, decreased WASH/retromer endosomal localization is observed, which results in reduced endosomal F-actin and direct CIE cargos misrouting. This ultimately leads to the lysosomal degradation of these misrouted cargos (demonstrated for SLC3A2). Dotted line between VARP and RAB21 indicates that their co-regulation with the retromer is speculative.
(A) Western blot analysis of Caspase 8, FLIP and FADD recruitment to the TRAIL-R2 DISC in A549, HCT116 and DU145 cell lines following incubation with increasing concentrations (1x, 2x, or 4x) of anti-TRAIL-R2 (AMG655)-conjugated magnetic beads for 90 minutes.
C. Viability analysis of patient-derived GICs (TG1, TG16, GBM5, GBM44) and NSCs (NSC24, NSC25, NSC5031, NSC8853) treated with prazosin for 72 h. *P=0.0286, n=4, two-sided Mann-Whitney U-test.
(C and D) Salmonella cfus quantified per gram of stool (C) and per organ (D) at 4 days post-infection are displayed. Data are shown as mean ± SD; ∗∗p ≤ 0.01. Data are representative of at least two independent experiments (n = 9 for WT; n = 7 or 8 for Clec12a−/−).
(G) Normalization of NMDAR-dependent LFS-LTD at synapses of PtenΔC/ΔC mice (16-21 days) by sarcosine treatment (750 µM), as shown by fEPSP slopes. Note that the data for WT-V and ΔC-V are identical to those shown in Fig. 4C because the whole experiments were performed together; we generated independent figures for DCS and sarcosine results for the clear presentation of the data. (n = 14 slices from 6 mice for WT-V, 11 (7) for WT-Sarc, 7(4) for ΔC-V, 9 (6) for ΔC-Sarc, **P < 0.01, ns, not significant, two-way ANOVA with Tukey's multiple comparison). The grey traces represent baseline fEPSP prior to LTD induction. The error bars represent SEM.
(b,c) Likewise, SH-SY5Y cells did not show beclin 1 cleavage on exposure to rotenone (b) or 6-OHDA (c; duplicate lanes). Data are representative of 2-3 independent experiments per toxin.