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B Hemdal,
I Andersson,
A Grahn, M Håkansson,
M Ruschin,
A Thilander-Klang,
M Båth,
S Börjesson,
J Medin,
A Tingberg,
L G Månsson,
S Mattsson
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ABSTRACT: There is a need for tools that in a simple way can be used for the evaluation of image quality related to clinical requirements in mammography. The aim of this work was to adjust the present European image quality criteria to be relevant also for digital mammography images, and to use as simple and as few criteria as possible. A pilot evaluation of the new set of criteria was made with mammograms of 28 women from a General Electric Senographe 2000D full-field digital mammography system. One breast was exposed using the standard automatic exposure mode, the other using about half of that absorbed dose. Three experienced radiologists evaluated the images using visual grading analysis technique. The results indicate that the new quality criteria can be used for the evaluation of image quality related to clinical requirements in digital mammography in a simple way. The results also suggest that absorbed doses for the mammography system used may be substantially reduced.
Radiation Protection Dosimetry 02/2005; 114(1-3):383-8. · 0.82 Impact Factor
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A Grahn,
B Hemdal,
I Andersson,
M Ruschin,
A Thilander-Klang,
S Börjesson,
A Tingberg,
S Mattsson, M Håkansson,
M Båth,
L G Månsson,
J Medin,
F Wanninger,
W Panzer
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ABSTRACT: The European Commission (EC) quality criteria for screen-film mammography are used as a tool to assess image quality. A new set of criteria was developed and initially tested in a previous study. In the present study, these criteria are further evaluated using screen-film mammograms that have been digitised, manipulated to simulate different image quality levels and reprinted on film. Expert radiologists have evaluated these manipulated images using both the original (EC) and the new criteria. A comparison of three different simulated dose levels reveals that the new criteria yield a larger separation of image criteria scores than the old ones. These results indicate that the new set of image quality criteria has a higher discriminative power than the old set and thus seems to be more suitable for evaluation of image quality in mammography.
Radiation Protection Dosimetry 02/2005; 114(1-3):389-94. · 0.82 Impact Factor
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ABSTRACT: In this study a set of structures has been simulated to represent a range of clinically relevant breast cancer mammographic lesions including solid tumours and microcalcifications. All structures have been created using simple random-based mathematical functions and have been inserted into a subset of digital mammography images at appropriate contrast levels into various regions of the breast, including dense fibroglandular and adipose tissue. These structures and their appearance in these clinical images were evaluated in terms of how realistic they looked. They will be used as the input to a large-scale clinical trial designed to examine the effect of significant dose reduction in digital mammography by comparing the detectability of such structures in images acquired at full and quarter automatic exposure control (AEC) dose level and in images with simulated noise levels in between.
Radiation Protection Dosimetry 02/2005; 114(1-3):424-31. · 0.82 Impact Factor
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ABSTRACT: The effect of pixel size on shape determination in screening digital mammography systems was studied using a shape identification task as the measured outcome. Ten microcalcifications on screen-films were digitised to a range of pixel sizes (2.5-200 microm) and extracted from computed radiography (CR) images (50 microm) acquired under equivalent imaging conditions. Fifteen observers attempted to identify the shape of each microcalcification at each pixel size. The results were collated to provide a fraction of correct responses vs. pixel size curve for each microcalcification. Averaging over all shapes, pixel values >100 microm lead to a significant decrease in shape determination ability (p < 0.01) for digitised screen-film. For CR images, half the shapes were not properly identified. Hence, although 20-100 microm was sufficient for microcalcification shape determination for digitised screen-film images, 50 microm was only borderline sufficient for the CR digital images.
Radiation Protection Dosimetry 01/2005; 114(1-3):415-23. · 0.82 Impact Factor
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ABSTRACT: The structure of a mutant form of staphylococcal enterotoxin A (SEA) has been determined to 2.1 A resolution. The studied SEA substitution H187-->A187 (SEAH187A) leads to an almost 10-fold reduction of the binding to major histocompatibility complex (MHC) class II. H187 is important for this interaction since it coordinates Zn2+. The zinc ion is thought to hold MHC class II and SEA together in a complex. Interestingly, only one of two molecules in the asymmetric unit binds Zn2+. H225, D227, a water molecule, and H44 from a symmetry-related molecule ligate Zn2+. The symmetry-related histidine is necessary for this substituted Zn2+ site to bind to Zn2+ at low zinc concentration (no Zn2+ added). Since a water molecule replaces the missing H187, H44 binds Zn2+ at the position where betaH81 from MHC class II probably will bind. Dynamic light scattering analysis reveals that in solution as well as in the crystal lattice the SEA(H187A) mutant forms aggregates. The substitution per se does not cause aggregation since wild-type SEA also forms aggregates. Addition of EDTA reduces the size of the aggregates, indicating a cross-linking function of Zn2+. In agreement with the biological function, the aggregation is weak (i.e. not revealed by gel filtration) and non-specific.
JBIC Journal of Biological Inorganic Chemistry 10/2001; 6(8):757-62. · 3.29 Impact Factor
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ABSTRACT: Water molecules are found to complete the Ca2+ coordination sphere when a protein fails to provide enough ligating oxygens. Hydrogen bonding of these water molecules to the protein backbone or side chains may contribute favorably to the Ca2+ affinity, as suggested in an earlier study of two calbindin D(9k) mutants [E60D and E60Q; Linse et al. (1994) Biochemistry 33, 12478-12486]. To investigate the generality of this conclusion, another side chain, Gln 22, which hydrogen bonds to a Ca2+-coordinating water molecule in calbindin D(9k), was mutated. Two calbindin D(9k) mutants, (Q22E+P43M) and (Q22N+P43M), were constructed to examine the interaction between Gln 22 and the water molecule in the C-terminal calcium binding site II. Shortening of the side chain, as in (Q22N+P43M), reduces the affinity of binding two calcium ions by a factor of 18 at low ionic strength, whereas introduction of a negative charge, as in (Q22E+P43M), leads to a 12-fold reduction. In 0.15 M KCl, a 7-fold reduction in affinity was observed for both mutants. The cooperativity of Ca2+ binding increases for (Q22E+P43M), while it decreases for (Q22N+P43M). The rates of Ca2+ dissociation are 5.5-fold higher for the double mutants than for P43M at low ionic strength. For both mutants, reduced strength of hydrogen bonding to calcium-coordinating water molecules is a likely explanation for the observed effects on Ca2+ affinity and dissociation. In the apo forms, the (Q22E+P43M) mutant has lower stability toward urea denaturation than (Q22N+P43M) and P43M. 2D (1)H NMR and crystallographic experiments suggest that the structure of (Q22E+P43M) and (Q22N+P43M) is unchanged relative to P43M, except for local perturbations in the loop regions.
Biochemistry 09/2001; 40(33):9887-95. · 3.42 Impact Factor
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ABSTRACT: The three-dimensional structure of a bacterial superantigen, Staphylococcus aureus enterotoxin H (SEH), bound to human major histocompatibility complex (MHC) class II (HLA-DR1) has been determined by X-ray crystallography to 2.6 A resolution (1HXY). The superantigen binds on top of HLA-DR1 in a completely different way from earlier co-crystallized superantigens from S.aureus. SEH interacts with high affinity through a zinc ion with the beta1 chain of HLA-DR1 and also with the peptide presented by HLA-DR1. The structure suggests that all superantigens interacting with MHC class II in a zinc-dependent manner present the superantigen in a common way. This suggests a new model for ternary complex formation with the T-cell receptor (TCR), in which a contact between the TCR and the MHC class II is unlikely.
The EMBO Journal 08/2001; 20(13):3306-12. · 9.20 Impact Factor
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ABSTRACT: The structure of calbindin D(9k) with two substitutions was determined by X-ray crystallography at 1.8-A resolution. Unlike wild-type calbindin D(9k), which is a monomeric protein with two EF-hands, the structure of the mutated calbindin D(9k) reveals an intertwined dimer. In the dimer, two EF-hands of the monomers have exchanged places, and thus a 3D domain-swapped dimer has been formed. EF-hand I of molecule A is packed toward EF-hand II of molecule B and vice versa. The formation of a hydrophobic cluster, in a region linking the EF-hands, promotes the conversion of monomers to 3D domain-swapped dimers. We propose a mechanism by which domain swapping takes place via the apo form of calbindin D(9k). Once formed, the calbindin D(9k) dimers are remarkably stable, as with even larger misfolded aggregates like amyloids. Thus calbindin D(9k) dimers cannot be converted to monomers by dilution. However, heating can be used for conversion, indicating high energy barriers separating monomers from dimers.
Protein Science 06/2001; 10(5):927-33. · 2.80 Impact Factor
