1,721,101 research outputs found
Performances and limitations of a technique for background calibration of capacitor mismatch errors in pipelined A/D converters.
No full textImportin alpha binds to an unusual bipartite nuclear localization signal in the heterogeneous ribonucleoprotein type I
No full textThe heterogeneous nuclear ribonucleoprotein (hnRNP) type I, a modulator of alternative splicing, localizes in the nucleoplasm of mammalian cells and in a discrete perinucleolar structure. HnRNP I contains a novel type of bipartite nuclear localization signal (NLS) at the N-terminus of the protein that we have previously named nuclear determinant localization type I (NLD-I). Recently, a neural counterpart of hnRNP I has been identified that contains a putative NLS with two strings of basic amino acids separated by a spacer of 30 residues. In the present study we show that the neural hnRNP I NLS is necessary and sufficient for nuclear localization and represents a variant of the novel bipartite NLS present in the NLD-I domain. Furthermore, we demonstrate that the NLD-I is transported into the nucleus by cytoplasmic factor(s) with active transport modality. Binding assays using recombinant importin α show an interaction with NLD-I similar to that of SV40 large T antigen NLS. Deletion analysis indicates that both stretches of basic residues are necessary for binding to importin α. The above experimental results lead to the conclusion that importin α acts as cytoplasmic receptor for proteins characterized by a bipartite NLS signal that extends up to 37 residues.The heterogeneous nuclear ribonucleoprotein (hnRNP) type I, a modulator of alternative splicing, localizes in the nucleoplasm of mammalian cells and in a discrete perinucleolar structure. HnRNP I contains a novel type of bipartite nuclear localization signal (NLS) at the N-terminus of the protein that we have previously named nuclear determinant localization type I (NLD-I). Recently, a neural counterpart of hnRNP I has been identified that contains a putative NLS with two strings of basic amino acids separated by a spacer of 30 residues. In the present study we show that the neural hnRNP I NLS is necessary and sufficient for nuclear localization and represents a variant of the novel bipartite NLS present in the NLD-I domain. Furthermore, we demonstrate that the NLD-I is transported into the nucleus by cytoplasmic factor(s) with active transport modality. Binding assays using recombinant importin alpha show an interaction with NLD-I similar to that of SV40 large T antigen NLS. Deletion analysis indicates that both stretches of basic residues are necessary for binding to importin alpha. The above experimental results lead to the conclusion that importin alpha acts as cytoplasmic receptor for proteins characterized by a bipartite NLS signal that extends up to 37 residues
An improved code density test for dynamic characterization of A/D converters
No full textAn improved code density test for flash A/D converters is proposed, revealing some dynamic phenomena (e.g., missing codes) hidden by the conventional approach. Formulas are reported for obtaining, from code density, effective noise estimates fully consistent with those provided by waveform analysis. Finally, it is shown that the variance of noise estimates obtained by time-domain analysis may be unacceptably large if the observation window is not properly chose
Functional simulation of a technique for background calibration of capacitor mismatch errors in pipelined A/D converters
No full textThis paper analyses the performance of a recently proposed background calibration technique with digital cancellation of D/A converter noise, suitable for high-speed, high-resolution, pipelined analog-to-digital converters (ADCs)
About the number of records to be acquired for histogram testing of A/D converters using synchronous sinewave and clock generators
No full text- …
