Case Study Analysis of Linear Chirp and Multitones (OFDM) Radar Signals Through Simulations and Measurement with HYCAM-Research Test Bench

This paper presents a experimental platform that allows comparing objectively any radar waveforms. This is realized by equating radar characteristics, using the same test-bench HYCAM-Research, the same signal processing and also insuring the reproducibility of the experiments. The experimental measurements on linear chirp and multitones are analyzed through distance and velocity imaging

Case Study Analysis of Linear Chirp and Multitones (OFDM) Radar Signals Through Simulations and Measurement with HYCAM-Research Test Bench

This paper presents a experimental platform that allows comparing objectively any radar waveforms. This is realized by equating radar characteristics, using the same test-bench HYCAM-Research, the same signal processing and also insuring the reproducibility of the experiments. The experimental measurements on linear chirp and multitones are analyzed through distance and velocity imaging

Differential binding regulation of microtubule-associated proteins MAP1A, MAP1B, and MAP2 by tubulin polyglutamylation.

The major neuronal post-translational modification of tubulin, polyglutamylation, can act as a molecular potentiometer to modulate microtubule-associated proteins (MAPs) binding as a function of the polyglutamyl chain length. The relative affinity of Tau, MAP2, and kinesin has been shown to be optimal for tubulin modified by approximately 3 glutamyl units. Using blot overlay assays, we have tested the ability of polyglutamylation to modulate the interaction of two other structural MAPs, MAP1A and MAP1B, with tubulin. MAP1A and MAP2 display distinct behavior in terms of tubulin binding; they do not compete with each other, even when the polyglutamyl chains of tubulin are removed, indicating that they have distinct binding sites on tubulin. Binding of MAP1A and MAP1B to tubulin is also controlled by polyglutamylation and, although the modulation of MAP1B binding resembles that of MAP2, we found that polyglutamylation can exert a different mode of regulation toward MAP1A. Interestingly, although the affinity of the other MAPs tested so far decreases sharply for tubulins carrying long polyglutamyl chains, the affinity of MAP1A for these tubulins is maintained at a significant level. This differential regulation exerted by polyglutamylation toward different MAPs might facilitate their selective recruitment into distinct microtubule populations, hence modulating their functional properties

L-Ilf3 and L-NF90 Traffic to the Nucleolus Granular Component: Alternatively-Spliced Exon 3 Encodes a Nucleolar Localization Motif

Ilf3 and NF90, two proteins containing double-stranded RNA-binding domains, are generated by alternative splicing and involved in several functions. Their heterogeneity results from posttranscriptional and posttranslational modifications. Alternative splicing of exon 3, coding for a 13 aa N-terminal motif, generates for each protein a long and short isoforms. Subcellular fractionation and localization of recombinant proteins showed that this motif acts as a nucleolar localization signal. Deletion and substitution mutants identified four arginines, essential for nucleolar targeting, and three histidines to stabilize the proteins within the nucleolus. The short isoforms are never found in the nucleoli, whereas the long isoforms are present in the nucleoplasm and the nucleoli. For Ilf3, only the posttranslationally-unmodified long isoform is nucleolar, suggesting that this nucleolar targeting is abrogated by posttranslational modifications. Confocal microscopy and FRAP experiments have shown that the long Ilf3 isoform localizes to the granular component of the nucleolus, and that L-Ilf3 and L-NF90 exchange rapidly between nucleoli. The presence of this 13 aminoacid motif, combined with posttranslational modifications, is responsible for the differences in Ilf3 and NF90 isoforms subcellular localizations. The protein polymorphism of Ilf3/NF90 and the various subcellular localizations of their isoforms may partially explain the various functions previously reported for these proteins

Etude structurale et fonctionnelle des facteurs Ilf3 et NF90, deux protéines impliquées dans le routage intracellulaire des ARN messagers

PARIS-BIUSJ-Thèses (751052125) / SudocPARIS-BIUSJ-Physique recherche (751052113) / SudocSudocFranceF

Case study analysis of linear Chirp and multi-tones radar signals through simulations and measurement with HYCAM-Research test bench

National audienceThis paper present a experimental platform that allows comparing objectively any radar waveforms. This is realized by equating radar characteristics, using the same test-bench HYCAM-Research, the same signal processing and also the reproducibility of the experiments. The experimental measurements on linear chirp and multitones are analyzed through distance and velocity imaging

Subcellular localization of GFP fused with the short or long N-terminal sequence of Ilf3/NF90.

<p>Plasmids pEGFP-N1 (Control, left panels), pEGFP-N1-Ilf3/NF90 common N-terminal short sequence (Short-GFP, mid panels) and pEGFP-N1-Ilf3/NF90 common N-terminal long sequence (Long-GFP, right panels) were transfected into HeLa cells. After 24 hours, cells were fixed and co-stained with anti-α-tubulin antibody (α-Tub) and DAPI. GFP or GFP fusion proteins appear in green, α-tubulin in red and DAPI staining in blue. Arrows point to intranuclear foci.</p

Ilf3 and NF90 polymorphism in nuclear fractions purified from P19 cells.

<p>Ilf3 and NF90 from P19 cell nuclear fractions were submitted to 2-D PAGE and immunodetected with polyclonal antibody 78. Arrows positioned in the same coordinates in Ilf3 or NF90 panels indicate the positions of Ilf3 and NF90 long and short isoforms. The faint signal in the middle right panel was detected with a ten fold longer time exposure than that of the other panels.</p

Subcellular distribution of Ilf3 and NF90 in P19 cells.

<p>After subcellular fractionation, proteins from identical percentages of each fraction were submitted to SDS-PAGE, blotted onto nitrocellulose and immunodetected with the serum Ab78 raised against Ilf3 and NF90 (S.E.: short exposure time; L.E.: long exposure time), anti-UBF serum (UBF) or anti-α-tubulin antibody (α-tub.). Molecular weight markers (kDa) are indicated at the right.</p