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C Elster

Publications and source records attributed to C Elster.

18 recordsLinked to original sources
PubMed2002

MEG-analysis using the Hilbert transform.

Event-related fields (ERFs) measured by magnetoencephalography (MEG) upon visual stimulation are analysed by Hilbert transformation. The Hilbert transform of real-valued measured ERF is an analytic complex signal, represented by phase and amplitude. The temporal behaviour of the derivative of the phase, i.e. the instantaneous frequency, allows to distinguish time intervals containing meaningful signal from noise. On the basis of both phase and amplitude, energies and latencies of single event ERFs can be determined.

Evoked Potentials, Visual↗
PubMed2000

Quantitative MRS: comparison of time domain and time domain frequency domain methods using a novel test procedure.

For quantitative analysis of in vivo MR spectra, a state-of-the-art time domain method was compared with a recently reported time domain frequency domain method which uses wavelets for background characterization. The comparison was made on the basis of results for simulated test problems that were constructed by combining measured and simulated MRS data at different signal-to-noise ratios in order to simultaneously reflect real world difficulties, in particular the overlapping background problem, and to allow for quantitative judgment of a method's accuracy. Incorporating prior knowledge was also considered. The results obtained give insight into the accuracy of the methods when applied to measured MRS data. Due to the improved background characterization, the time domain frequency domain method outperformed the time domain method in some of the test cases. Both methods were also applied to serial brain MR spectra of a healthy volunteer on 10 occasions.

Brain↗
PubMed1997

Influenza virus M1 protein binds to RNA through its nuclear localization signal.

The RNA-binding activity of influenza A virus M1 protein was studied by cross-linking the protein to viral RNA followed by sequence analysis of the oligoribonucleotide bound to the protein as well as sequence analysis of the M1 peptide bound to the RNA. M1 was found to bind to RNA without any RNA sequence specificity, as verified in a series of filter-binding experiments using a large variety of nucleic acids including DNA. The peptide sequence that bound to the RNA was the RKLKR nuclear localization signal of M1. Site-specific mutagenesis of recombinant M1 showed that most of the basic residues in that region had to be mutated in order to inhibit RNA-binding. We also constructed an M1 mutant that no longer bound to RNA but which was still able to inhibit the in vitro transcription activity of isolated viral ribonucleoprotein, albeit to a lower extent. Mutation of the zinc-binding sequence had no effect on RNA-binding or transcription-inhibition activity.

Amino Acid Sequence↗
PubMed1994

Salmonellal splenic abscess in the antibiotic era: a Latin American perspective.

Ten cases of salmonellal splenic abscesses recently documented in various Latin American countries are discussed. All patients were adults; the mean age was 32.6 years, and there was a predominance of males (seven). Predisposing conditions were identified in four cases. All 10 cases were documented by diagnostic imaging techniques; in one case, exploratory diagnostic laparotomy was also performed. Splenectomy was performed on eight patients, while two other patients responded to long courses of intravenous antimicrobial therapy alone. One patient died as the result of perioperative splenic rupture, and two patients underwent second laparotomies because of left subphrenic abscesses. Except for one human immunodeficiency virus-infected individual, all patients were immunocompetent and had large solitary lesions. Salmonella typhi was the predominant organism isolated and was recovered in six of the 10 cases.

Abscess↗
PubMed1994

A small percentage of influenza virus M1 protein contains zinc but zinc does not influence in vitro M1-RNA interaction.

A peptide containing the CCHH motif, the putative zinc-binding sequence of influenza virus M1 protein, was found to bind zinc in a one-to-one complex with the characteristics of a typical zinc-binding peptide. Intact influenza virus also contained zinc and we show that this zinc is bound to the M1 protein in the virus. However, only a small proportion of M1 contained zinc: 4% in virus and 6 to 9% in isolated protein. One strain, B/Yamagata/16/88, consistently contained more zinc: 15 to 20% both in virus and in isolated protein. We also determined the RNA binding and transcription inhibition activities of various M1 proteins and found that the zinc content of M1 had no influence on either activity. We suggest that the zinc in M1 has a structural role in the virion other than nucleic acid binding.

Amino Acid Sequence↗
PubMed1993

Pharmacokinetic model identification and parameter estimation as an ill-posed problem.

For model identification and parameter estimation in the framework of linear pharmacokinetics it is most often assumed that the disposition function is a finite sum of exponential functions with time constants lambda i and associated coefficients Ci. Least-square fitting procedures are used to estimate the coefficients Ci and the corresponding discrete locations lambda i on the lambda-axes. This work presents an alternative approach. It does not assume that the non-zero coefficients are located at sharply defined values of lambda, but that they are represented by a continuous function h(lambda), the spectrum of the disposition function. This turns the non-linear least-square problem into a linear problem, which is known to be as so-called "ill-posed". Regularization methods have been developed in recent years as suitable tools for the treatment of such ill-posed problems. Application of Tikhonov regularization to the case of the bolus kinetics of propofol in 8 volunteers is demonstrated. In 7 of the 8 cases a spectrum with 4 to 5 peaks was found, and in one volunteer there were only 2 peaks. All spectra with more than 2 peaks showed negative values of h(lambda). The method used is described and the results are compared with those of conventional compartment analysis.

Humans↗
PubMed1993

Organization of the genes necessary for hydrogenase expression in Rhodobacter capsulatus. Sequence analysis and identification of two hyp regulatory mutants.

A 25 kbp DNA fragment from the chromosome of Rhodobacter capsulatus B10 carrying hydrogenase (hup) determinants was completely sequenced. Coding regions corresponding to 20 open reading frames were identified. The R. capsulatus hydrogenase-specific gene (hup and hyp) products bear significant structural identity to hydrogenase gene products from Escherichia coli (13), from Rhizobium leguminosarum (16), from Azotobacter vinelandii (10) and from Alcaligenes eutrophus (11). The sequential arrangement of the R. capsulatus genes is: hupR2-hupU-hypF-hupS-hupL-hupM-hu pD-hupF-hupG-hupH-hupJ-hupK-hypA- hypB-hupR1- hypC-hypD-hypE-ORF19-ORF20, all contiguous and transcribed from the same DNA strand. The last two potential genes do not encode products that are related to identified hydrogenase-specific gene products in other species. The sequence of the 12 R. capsulatus genes underlined above is presented. The mutation site in two of the Hup- mutants used in this study, RS13 and RCC12, was identified in the hypF gene (deletion of one G) and in the hypD gene (deletion of 54 bp), respectively. The hypF gene product shares 45% identity with the product of hydA from E. coli and the product of hypF from R. leguminosarum. Those products present at their N-terminus a Cys arrangement typical of zinc-finger proteins. The G deletion in the C-terminal region of hypF in the RS13 mutant prevented the expression of a hupS::lacZ translational fusion from being stimulated by H2 as it is observed in the wild-type strain B10. It is inferred that the HypF protein is a factor involved in H2 stimulation of hydrogenase expression.

Amino Acid Sequence↗