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420 Treffer

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  1. Detailansicht für Treffer 1 öffnen
    Built-In Self-Test of High-Density and Realistic ILV Layouts in Monolithic 3-D ICs
    Chaudhuri, Arjun ; Banerjee, Sanmitra ; et al.
    In: IEEE Transactions on Very Large Scale Integration (VLSI) Systems ; volume 31, issue 3, page 296-309 ; ISSN 1063-8210 1557-9999, 2023
    Online academicJournal
    Zugriff:
    Volltext
    Volltext
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  2. Detailansicht für Treffer 2 öffnen
    Yield gains from improved lentil varieties (ILVs) based on data from experimental stations.
    Yigezu Atnafe Yigezu (11999227) ; M. Wakilur Rahman (11999230) ; et al.
    2022
    unknown
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  3. Detailansicht für Treffer 3 öffnen
    Tumor control following ILV immunization is mediated by IL12.
    Jardin A. Leleux (11785205) ; Tina C. Albershardt (11785208) ; et al.
    2021
    Bild
    Wie komme ich dran?
  4. Detailansicht für Treffer 4 öffnen
    Tumor control following ILV immunization is mediated by IL12.
    Jardin A. Leleux (11785205) ; Tina C. Albershardt (11785208) ; et al.
    2021
    Bild
    Wie komme ich dran?
  5. Detailansicht für Treffer 5 öffnen
    Pairing ILVs for testing monolithic 3D integrated circuits
    Gupta, Vivek Kumar ; Roy, Surajit Kumar ; et al.
    In: 2018 International Symposium on Devices, Circuits and Systems (ISDCS, 2018
    Online Konferenz
    Zugriff:
    Volltext
    Wie komme ich dran?
  6. Detailansicht für Treffer 6 öffnen
    Solution State NMR Chemical Shift Assignments for Yeast Peroxiredoxin Tsa1 mutated S78D - Backbone 1H, 13C, and 15N and ILV methyl groups ...
    Troussicot, Laura ; Vallet, Alicia ; et al.
    2023
    unknown
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  7. Detailansicht für Treffer 7 öffnen
    Die innerbetriebliche Leistungsverrechnung (ILV) der Radiologie des Klinikums der Ludwig-Maximilians-Universität München
    Biniok, Maximilian
    2019
    Online academicJournal
    Zugriff:
    Volltext
    Volltext
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  8. Detailansicht für Treffer 8 öffnen
    Figure 2—figure supplement 3. Correlation between the experimental and predicted RDC measurements of the NRD-TAD structural ensemble. ; Plots show comparison between experimental and average predicted RDC values with a goodness of fit given by R2 value (a value of 1 indicates perfect fit) and Q factor (Cornilescu et al., 1998). The average predicted RDC values of the structural ensemble were calculated using Rosetta with the SVD (singular value decomposition) fit method for the residues 63–66, 69, 72–78, 80–99, 101–111, 113–114 (human sequence numbering). (A) Correlation of NH RDC values, which were used in the structure calculation. (B) Correlation of NCO RDC values. The NCO RDCs were not used in the structure calculation, so the correlation is an independent validation of the structural model. Note that the NH RDC values were measured using the ILV sample with (alanine mutations) but the NCO RDC values were calculated using the sample without alanine mutations (see Materials and methods and Figure 2—figure supplement 1).
    2019
    unknown
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  9. Detailansicht für Treffer 9 öffnen
    Figure 1—figure supplement 2. URY, URX, URA and BAG endings. ; TEM cross-sections through two right labial sensilla (I., III.) and process bundles (II., IV.) of P. pacificus (specimen 107) (seen from anterior). (I) Right ventral lip, 3.8 µm from the tip of the nose. The membranous extension of a URYV branch (blue) wraps halfway round the ILV sensillum. It terminates further distally in the tip of the ventral lip. (II) Right dorsal lip, 7.8 µm from the tip of the nose. This more posterior section shows that the dendrites of all three UR neurons are part of the dorsal labial process bundle. The URYD process is found next to CEPshD, URX next to ILshD and OLQshD, and URAD next to CEPD and OLQD. (III) Right lateral lip, 3.6 µm from the tip of the nose, showing branches of URYD, URYV and the URX dendrite extending into the lateral labial process bundle. URYV is associated with ILsh, and URYD with ILsh, OLLsh and OLLso. URX and BAG endings are found apposed to ILso. For more anterior sections showing the elaborate URX and BAG extensions, see Figure 1L. (IV.) Right lateral lip, 7.05 µm from the tip of the nose. Lateral labial processes, branches of URYD and URYV, and the BAG dendrite are located directly ventral of the amphid sensillum. URYD shows many prominent singlet microtubules (see inset) but appears to be unciliated. URX will join the bundle more anteriorly.
    2019
    unknown
    Wie komme ich dran?
  11. Detailansicht für Treffer 11 öffnen
    Figure 4. NMR and mutagenesis identify the nucleosome acidic patch as the binding interface for RNF169(UDM2). ; (A) Superimposed 1H-13C HMQC spectra of ILV-methyl labeled H2A (left panel) and ILV-methyl labeled H2B (right panel) in the context of the H2AK13Cub-NCP without (black) and with (yellow, left; red, right) wild-type RNF169(UDM2), respectively. RNF169(UDM2) was added at 2.5-fold excess relative to ubiquitin. Arrows indicate peak movement. Data collected at 14.1 T, 45°C. (B) Chemical shift perturbations (CSPs) in ILV-methyl labeled H2A (yellow, top panel) and ILV methyl-labeled H2B (red, bottom panel) H2AK13Cub-NCPs. Residues with CSP values 1σ above the average are indicated (black line). CSPs were calculated as described in Materials and Methods. (C) Location of residues with significant CSPs in H2A (yellow) and H2B (red) shown in space filling representation and indicated with arrows on nucleosome crystal structure (2PYO) (Clapier et al., 2008a). Acidic patch residues are shown in stick representation and coloured black. H2A: light yellow, H2B: salmon, H3: light blue and H4: light green. (D) Selected isoleucine regions of 1H-13C HMQC spectra of free (black) and 2.5-fold excess RNF169(UDM2) bound (red) ILV-methyl labeled ub H2AK13Cub-NCP. Spectra of acidic patch mutant NCPs, H2AK13C(D89A/E91A)ub-NCP (purple, left panel) and H2AK13C(E60A/E63A)ub-NCP (teal, right panel), with 5-fold excess RNF169(UDM2) to ubiquitin are overlaid and highlight the resulting binding deficiency. All data are recorded at 14.1 T, 45°C.
    2017
    unknown
    Wie komme ich dran?
  13. Detailansicht für Treffer 13 öffnen
    Figure 7. Visualization of Ypq1-FKBP ILVs. ; (A–B) EM images of the vacuole in pep12Δpep4Δvma4Δatg9Δ cells (pep12Δ) with or without Hse1DUB (No Rapamycin treatment). (C) EM image of the vacuole in cells expressing Hse1DUB after rapamycin treatment (2 hr) at 26°C. Arrows indicate representative vesicles formed following rapamycin-induced Ypq1 sorting. (D) EM images of the vacuole in pep4Δvma4Δatg9Δ cells (PEP12) without Hse1DUB (No Rapamycin treatment). ‘V’ in the figures (7A~D) is abbreviated for vacuole. (E) Average number of ILVs (per cell per section) calculated by counting ILVs within vacuoles of cells (pep12Δ) without Hse1DUB, with Hse1DUB, and with both Hse1DUB and rapamycin treatment. The mean value of ILVs formed in vacuole lumen was quantified and error bars are standard deviation. Two-tail t-test was performed between pep12Δ(Hse1DUB-/Rap-) and pep12Δ(Hse1DUB+/Rap-), and between pep12Δ(Hse1DUB+/Rap-) and pep12Δ(Hse1DUB+/Rap+). α = 0.025 (Bonferroni correction), p-value0.05 (n.s., non-significant), N = 64 vesicles for each condition. (G) Cartoon model depicting Ypq1 sorting from the vacuole membrane into the vacuole lumen. After lysine withdrawal, Ypq1 is ubiquitinated by the Ssh4/Rsp5 E3-ligase complex. Ubiquitinated Ypq1 and PtdIns(3)P recruit ESCRT-0 to the vacuole membrane. ESCRT-0 sorts Ypq1 and recruits downstream ESCRTs to the vacuole membrane. The ESCRTs internalize Ypq1 directly into the vacuole lumen for degradation.
    2017
    unknown
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  14. Detailansicht für Treffer 14 öffnen
    Figure 6. The MVB pathway supplies sterol for induction of microautophagy. ; (A) The vacuolar content of ncr1△npc2△ after nitrogen starvation for 5 hr. ILVs, seen as small rugged structures (arrows), and microautophagic vesicles labeled for PtdIns(3)P in the cytoplasmic leaflet (*) were observed. Bars: 0.2 µm. (B) The density of ILVs in the vacuolar lumen after nitrogen starvation was significantly higher in ncr1△npc2△ than in WT. Mean ± SD are represented (n = 3; >30 vacuoles were counted in each experiment). **p
    2017
    unknown
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  15. Detailansicht für Treffer 15 öffnen
    Figure 2. Correlative light microscopy and electron tomography of perivacuolar MVBs. ; Yeast cells expressing Vps4-eGFP or Vps4-mNeonGreen were cryo-fixed and sections subjected to correlative light microscopy and electron tomography. (a–d) Representative images from epifluorescence microscopy of 300 nm thick sections, highlighting the presence of Vps4-eGFP perivacuolar fluorescent spots (green). TetraSpeck beads (white) were used to align the light microscopy and electron tomographic images. Scale bar = 1 µm. The highlighted Vps4-eGFP containing objects (1-5) were contained in the sections used to obtain electron tomographic images; the examples illustrate the appearance of endosomes containing ILV (gray spots) and ILV buds (arrowheads). Scale bar = 100 nm. (e) 3D model of MVBs imaged by electron tomography corresponding to panel (c) showing the MVB limiting membrane (yellow), ILVs (red) and vacuole (blue). Scale bar = 100 nm. (f) Histogram distribution indicating the content of ILV buds per MVB determined from the electron tomographic reconstructions from 35 yeast cells with 12 Vps4-eGFP and 26 Vps4-mNeonGreen fluorescent spots. See Supplementary file 1 for details.
    2017
    unknown
    Wie komme ich dran?
  16. Detailansicht für Treffer 16 öffnen
    Figure 3. Thermodynamics and kinetics of the RNF169(UDM2)-H2AK13C ub-NCP interaction. ; (A) Selected regions of 1H-13C HMQC spectra of ILV-methyl labeled ubiquitin in H2AK13Cub-NCPs with increasing amounts of unlabeled RNF169(UDM2). Arrows indicate direction of peak movement. Data collected at 14.1 T, 45°C. (B) Chemical shift derived binding curves for selected residues in ILV-methyl labeled ubiquitin in H2AK13Cub-NCPs (left panel) and free ILV-methyl labeled ubiquitin (right panel) upon addition of unlabeled RNF169(UDM2) (circles), with best fits (solid lines) shown. Ratio of RNF169(UDM2) to ubiquitin indicated on horizontal axis. (C) Fitted line shapes for I44δ1 (extracted from 1H-13C correlation spectra by taking traces along the 13C-dimension). Experimental data in black, with simulated line shapes in red. Ratio of ubiquitin to RNF169(UDM2) indicated in each panel and vertical grey dashed lines denote the resonance positions of I44δ1 in the absence (free) and presence (bound) of saturating amounts of RNF169(UDM2). The extracted kinetic parameters for the RNF169, ub-NCP binding reaction are shown above the traces.
    2017
    unknown
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  17. Detailansicht für Treffer 17 öffnen
    Figure 5. Acute cytosolic depletion of Vps4 blocks endosomal traffic to the vacuole and changes the structure of perivacuolar MVBs. ; Rapid depletion of cytosolic Vps4-eGFP-FRB was achieved by its capture on the cytosolic surface of the plasma membrane induced by rapamycin-mediated heterodimerization with Pma1-FKBP12. (a) Phase contrast and live cell epifluorescence microscopy of yeast cells expressing Vps4-eGFP-FRB (green) and the cargo Mup1-mRuby2 (red) before (panel 1) or 60 min after addition of methionine (panels 2–4), used to activate endocytosis of Mup1 and its transport into the vacuole. Rapamycin was added to deplete Vps4-eGFP-FRB (panel 3, 4), and untagged Vps4 was co-expressed to rescue the anchor-away effect (panel 4). The locations of the plasma membrane (PM), vacuole (V) and class E compartment (E) are indicated. Scale bar = 5 µm. (b) SDS-PAGE and western blot analysis with the indicated antibodies of samples from equal volumes of membrane and cytosolic fractions of Vps4-eGFP cells, vps4Δ mutants and Vps4-eGFP-FRB cells in the absence and presence of rapamycin. (c) Live cell epifluorescence and phase contrast microscopy of yeast cells expressing a mixture of Snf7 and Snf7-eGFP together with Vps4-FRB before or after the addition of rapamycin. Scale bar = 5 µm. (d) 3D model (top) and 2D slices (bottom) of tomographic reconstructions obtained from 400 nm slices of yeast cells before and after addition of rapamycin. The images show typical examples of MVBs containing ILVs (red) surrounded by the limiting membrane (yellow), endosomes lacking ILVs and an example of class E-like compartment (green); arrowheads point to ILV buds. To facilitate the imaging, MBVs were clustered in one region by overexpression of Vps21 (TDH3-VPS21) (Adell et al., 2014). Scale bar = 100 nm. The outcome of the morphological analysis of all MVBs (fully or only partially present in the section) is shown.
    2017
    unknown
    Wie komme ich dran?
  18. Detailansicht für Treffer 18 öffnen
    Figure 6. Proposal of a model for the mechanism of ESCRT-mediated intraluminal vesicle formation. ; The figure shows a schematic representation for possible stages during the budding and scission of ILVs in MVBs. ESCRT-0-II (not shown) bind cargo proteins and nucleate rapid assembly of several ESCRT-III filaments. These ESCRT-III assemblies grow and shrink stochastically and recruit Vps4. ESCRT-III dynamics occur continuously throughout the formation of ILVs and do not require Vps4. When recruited, Vps4 hexamers, docked by MIT-MIM association on one filament, exerts ATP-dependent force on another filament by pulling the C-terminus of an ESCRT-III subunit into the hexamer pore; as the cycling process ensues, the filament movement drives crowding of the membrane-anchored cargo. The crowding forces membrane invagination, to create the surface area needed to accommodate the cargo molecules. The forces exerted by the interactions between ESCRT-III and Vps4 hexamers also generate the neck of the nascent bud, lead to membrane constriction and ultimately to vesicle fission and final release of the ESCRT machinery.
    2017
    unknown
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  19. Detailansicht für Treffer 19 öffnen
    Figure 5—figure supplement 1. Effects of the acute depletion of the cytosolic Vps4 pool. ; (a) Schematic representation of the anchor away approach used to acutely deplete the amount of cytosolic Vps4-FRB (OFF). Addition of rapamycin (RAP) results in the association of Vps4-FRB with the highly abundant Pma1-FKBP12 stable located at the plasma membrane. (b) Live cell phase contrast and epifluorescence microscopy of yeast cells expressing Vps4-eGFP-FRB alone or with Vps4-mCherry before or after exposure to 1 µg/ml rapamycin for less than one minute or 30 min. It shows the rapid effect of the anchor away approach as reflected by the stable accumulation of Vps4 at the plasma membrane and its depletion from intracellular endosomal carriers. (c) Live cell confocal microscopy fluorescence recovery after photo-bleaching (FRAP) of Vps4-eGFP-FRB before and 10 min after the addition of 1 µg/ml rapamycin. The images in the top show typical examples of FRAP results for perivacuolar endosomes located next to the vacuole labeled with internalized FM4-64 dye. The images in the bottom show an overview of the selected cells and the photobleached area (arrow). Scale bar = 5 µm. The plots show the fluorescence traces and the fitted FRAP pattern for cells expressing Vps4-FRB-eGFP before (n = 21) or after rapamycin addition (n = 28), for cells expressing Vps4-eGFP (n = 34) and for cells expressing Vps4E233Q-eGFP (n = 26). Their distribution of fitted time constants is shown in the histogram. The box plot shows median, 25th, and 75th percentiles and outermost data points of the fitted time constants. The permutation test for differences between the means of the time constants was not significant. (d) The top panels (a–d) are low magnification views of MBVs highlighting the region (dotted squares) used for the tomographic reconstructions depicted in Figure 5d. Panel E corresponds to another example observed after 120 min incubation with rapamycin; it also shows the accumulation of nearly empty perivacuolar endosomes mostly lacking buds located in proximity to the class E compartment. Enlarged views of the selected regions 1–3 are shown. Limiting MVB membrane (yellow), ILVs (red) and class E-like structures (green) are indicated; arrowheads point to ILV buds. Scale bar = 100 nm (a–e) and 20 nm (1, 2, 3).
    2017
    unknown
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  20. Detailansicht für Treffer 20 öffnen
    Figure 5. Retrogradely transported TrkA+ endosomes within cell bodies evolve from MVBs into simple, single-membrane vesicle structures. ; (a) Schematic of the pulse-block assay. The Flag-TrkA assay is performed in Ntrk1Flag sympathetic neurons cultured in compartmentalized microfluidic chambers as in Figure 1—figure supplement 1A using pre-conjugated anti-Flag antibody and Protein A-5 nm gold. Nocodazole is applied to distal axons 25 min post-NGF application to block retrograde transport. Neurons are fixed at indicated time points and processed for EM. (b) The Flag-TrkA assay was performed in WT neurons, Ntrk1Flag neurons treated with either DMSO or nocodazole in distal axons (25 min post NGF). Cells were fixed at indicated time points and processed for EM. The number of gold particles per section per cell was quantified (n = 3, Results were pooled from over 150 Flag-gold particles). (c) The pulse-block assay was performed as in (a), and membrane topology of the Flag epitope was assessed. A schematic of the inner- or outer-leaflet position for membrane of ILVs, the limiting membrane and SVs is shown on the right. (d,e) The pulse-block assay was performed and the distribution of retrogradely transported Flag-TrkA gold particles in MVBs, single-membrane vesicle structures (SVs) and lysosomes within the cell body over time was assessed (e) Results were pooled from over 150 Flag-gold particles from four samples for each time point. Representative images of retrograde Flag-TrkA in each of the three membrane compartments are shown in (d). (f) Sympathetic neurons in compartmentalized cultures were incubated with transferrin-gold (6 nm) in distal axons and the pulse-block assay was performed. The distribution of retrograde transferrin-gold in MVBs, SVs and lysosomes was assessed by EM. For (d–f), over 150 endosomes were counted for each condition at each time point in four independent experiments. Scale bar: 100 nm. Data are represented as mean ± SEM. ***p
    2018
    unknown
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