Performance analysis of steady-state harmonic elastography
- 1. Thayer School of Engineering, Dartmouth College, Hanover, NH 03755 (United States)
Description
Shear modulus estimation can be confounded by the ill-posed nature of the inverse elasticity problem. In this paper, we report the results of experiments conducted on simulated and gelatin phantoms to investigate the effect of various parameters (i.e., regularization, spatial filtering and the subzone generation process) associated with shear modulus reconstruction on the statistical accuracy (mean squared error), and image quality (i.e., contrast and spatial resolution) of the recovered mechanical properties. The results indicate several interesting observations. Firstly, the intrinsic spatial resolution of magnetic resonance elastography (MRE) is dependent on both regularization and spatial filtering. Secondly, the elastographic contrast-to-noise ratio (CNRe) increases with increasing regularization and spatial filtering, but it was not affected by the zoning parameters (i.e., the subzones and the extent of the overlap). Thirdly, the statistical accuracy (MSE) of the recovered property improved with increasing regularization, and spatial filtering weight, but the size of the subdomains and their overlap had no significant effect
Additional details
Identifiers
- DOI
- 10.1088/0031-9155/52/10/002;
- PII
- S0031-9155(07)35210-X;
Publishing Information
- Journal Title
- Physics in Medicine and Biology
- Journal Volume
- 52
- Journal Issue
- 10
- Journal Page Range
- p. 2657-2674
- ISSN
- 0031-9155
- CODEN
- PHMBA7
INIS
- Country of Publication
- United Kingdom
- Country of Input or Organization
- International Atomic Energy Agency (IAEA)
- INIS RN
- 38068948
- Subject category
- S62: RADIOLOGY AND NUCLEAR MEDICINE;
- Descriptors DEI
- ACCURACY; ELASTICITY; ERRORS; GELATIN; IMAGES; LAND USE; MAGNETIC RESONANCE; PERFORMANCE; PHANTOMS; SPATIAL RESOLUTION; STEADY-STATE CONDITIONS
- Descriptors DEC
- COLLOIDS; DISPERSIONS; MECHANICAL PROPERTIES; MOCKUP; ORGANIC COMPOUNDS; PROTEINS; RESOLUTION; RESONANCE; STRUCTURAL MODELS