PubMed Health⌕ Search

PubMed · 10862071

Nonlinear smoothing for reduction of systematic and random errors in diffusion tensor imaging.

Abstract

Calculation and sorting of the eigenvectors of diffusion using diffusion tensor imaging has previously been shown to be sensitive to noise levels in the acquired data. This sensitivity manifests as random and systematic errors in the diffusion eigenvalues and derived parameters such as indices of anisotropy. An optimized application of nonlinear smoothing techniques to diffusion data prior to calculation of the diffusion tensor is shown to reduce both random and systematic errors, while causing little blurring of anatomical structures. Conversely, filtering applied to calculated images of fractional anisotropy is shown to fail in reducing systematic errors and in recovering anatomical detail. Using both real and simulated brain data sets, it is demonstrated that this approach has the potential to allow acquisition of data that would otherwise be too noisy to be of use.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

G J Parker, J A Schnabel, M R Symms, D J Werring, G J Barker. 2000. Nonlinear smoothing for reduction of systematic and random errors in diffusion tensor imaging.. https://doi.org/10.1002/1522-2586(200006)11%3A6%3C702%3A%3Aaid-jmri18%3E3.0.co%3B2-a

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Analysis of peptide rotational diffusion by homonuclear NMR.

The analysis of the rotational diffusion of a molecule using homonuclear NMR is investigated. The homonuclear longitudinal and transverse cross-relaxation rates, which can be quantitatively measured using off-Resonance Rotating frame nuclear Overhauser Effect Spectroscopy (ROESY), are used to build a distribution, which exhibits a solid-state-like pattern characteristic of the diffusion tensor. The distributions of the antimicrobial peptide ranalexin in water and in 30% of trifluoracetic acid (TFE) are compared, and the peptide rotational diffusion is shown to be more isotropic in water than in 30% TFE. This difference is further supported by the analysis of NMR ranalexin conformers in 30% TFE, and by the analysis of a molecular dynamics simulation of peptide in water.

Anisotropy↗

CheW binding interactions with CheA and Tar. Importance for chemotaxis signaling in Escherichia coli.

The initial signaling events underlying the chemotactic response of Escherichia coli to aspartic acid occur within a ternary complex that includes Tar (an aspartate receptor), CheA (a protein kinase), and CheW. Because CheW can bind to CheA and to Tar, it is thought to serve as an adapter protein in this complex. The functional importance of CheW binding interactions, however, has not been investigated. To better define the role of CheW and its binding interactions, we performed biochemical characterization of six mutant variants of CheW. We examined the ability of the purified mutant CheW proteins to bind to CheA and Tar, to promote formation of active ternary complexes, and to support chemotaxis in vivo. Our results indicate that mutations which eliminate CheW binding to Tar (V36M) or to CheA (G57D) result in a complete inability to form active ternary complexes in vitro and render the CheW protein incapable of mediating chemotaxis in vivo. The in vivo signaling pathway can, however, tolerate moderate changes in CheW-Tar and CheW-CheA affinities observed with several of the mutants (G133E, G41D, and 154ocr). One mutant (R62H) provided surprising results that may indicate a role for CheW in addition to binding CheA/receptors and promoting ternary complex formation.

Anisotropy↗

Determination of calpha chemical shift tensor orientation in peptides by dipolar-modulated chemical shift recoupling NMR spectroscopy.

We present a new method for determining the orientation of chemical shift tensors in polycrystalline solids with site resolution and demonstrate its application to the determination of the Calpha chemical shift tensor orientation in a model peptide with beta-sheet torsion angles. The tensor orientation is obtained under magic angle spinning by modulating a recoupled chemical shift anisotropy (CSA) pattern with various dipolar couplings. These dipolar-modulated chemical shift patterns constitute the indirect dimension of a 2D spectrum and are resolved according to the isotropic chemical shifts of different sites in the direct dimension. These dipolar-modulated CSA spectra are equivalent to the projection of a 2D static separated-local-field spectrum onto its chemical shift dimension, except that its dipolar dimension is multiplied with a modulation function. Both (13)C-(1)H and (13)C-(15)N dipolar couplings can modulate the CSA spectra of the Calpha site in an amino acid and yield the relative orientations of the chemical shift principal axes to the C-H and C-N bonds. We demonstrate the C-H and C-N modulated CSA experiments on methylmalonic acid and N-tBoc-glycine, respectively. The MAS results agree well with the results of the 2D separated-local-field spectra, thus confirming the validity of this MAS dipolar-modulation approach. Using this technique, we measured the Val Calpha tensor orientation in N-acetylvaline, which has beta-sheet torsion angles. The sigma(11) axis is oriented at 158 degrees (or 22 degrees) from the C-H bond, while the sigma(22) axis is tilted by 144 degrees (or 36 degrees) from the C-N bond. Both the orientations and the magnitude of this chemical shift tensor are in excellent agreement with quantum chemical calculations.

Anisotropy↗