imaging algorithms Search Results


90
TOMTEC IMAGING SYSTEMS GMBH tomtec software, arena tta2
Tomtec Software, Arena Tta2, supplied by TOMTEC IMAGING SYSTEMS GMBH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/imaging+algorithms/tomtec+arena++tta2+30+algorithm/pm36357131-62-12-14
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tomtec software, arena tta2 - by Bioz Stars, 2026-10
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90
universal imaging inc particle-tracking image analysis algorithm
Organization of PBD binding sites relative to actin localization during FcγR-mediated phagocytosis. (A) Time series showing phase-contrast and Ratio images of a macrophage internalizing an IgG-opsonized erythrocyte. The color bar indicates the molar ratio (YFP/CFP). YFP-PBD was recruited to the forming phagosome (1.5–4.5 min) to a much greater extent during closure (5.0–7.5 min) and was cleared from the closed phagosome (8.5 min). (B) Particle-tracking analysis of YFP-actin (open circles) and YFP-PBD (closed circles) indicated that actin was recruited to the phagosome after particle binding (0–1 min) and during extension (1–5 min), and YFP-PBD was recruited throughout phagocytosis, with a pronounced increase in recruitment during closure (5.0–8 min). Data are mean ± SEM for 10 <t>phagocytic</t> events; no more than three events were taken from any one cell, and at least five different cells made up the 10 traces. (C) Simultaneous imaging of YFP-PBD and CFP-actin indicated that actin and the majority of PBD binding sites formed a discrete interface during constriction of the opsonized erythrocyte (constriction is inferred from the deformation of the erythrocyte; see arrow). CFP-actin was recruited to the forming phagosome, moved as a concentrated band over the particle during the extension phase (1.5–6.0 min), and condensed at the point of closure (6–7.5 min). YFP-PBD accumulated significantly on the base of the phagosome as constriction of the particle began (4.5–5.0 min), closely followed the moving band of actin during closure (5.5–7.5 min) and then rapidly dissipated (7.5–8.5 min). Bars, 3 μm. Also see Movie 1.
Particle Tracking Image Analysis Algorithm, supplied by universal imaging inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/imaging+algorithms/particle+tracking+image+analysis+algorithm/pmc00491814-160-6-18
Average 90 stars, based on 1 article reviews
particle-tracking image analysis algorithm - by Bioz Stars, 2026-10
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90
Kapelan Bio Imaging GmbH genetic algorithms
Organization of PBD binding sites relative to actin localization during FcγR-mediated phagocytosis. (A) Time series showing phase-contrast and Ratio images of a macrophage internalizing an IgG-opsonized erythrocyte. The color bar indicates the molar ratio (YFP/CFP). YFP-PBD was recruited to the forming phagosome (1.5–4.5 min) to a much greater extent during closure (5.0–7.5 min) and was cleared from the closed phagosome (8.5 min). (B) Particle-tracking analysis of YFP-actin (open circles) and YFP-PBD (closed circles) indicated that actin was recruited to the phagosome after particle binding (0–1 min) and during extension (1–5 min), and YFP-PBD was recruited throughout phagocytosis, with a pronounced increase in recruitment during closure (5.0–8 min). Data are mean ± SEM for 10 <t>phagocytic</t> events; no more than three events were taken from any one cell, and at least five different cells made up the 10 traces. (C) Simultaneous imaging of YFP-PBD and CFP-actin indicated that actin and the majority of PBD binding sites formed a discrete interface during constriction of the opsonized erythrocyte (constriction is inferred from the deformation of the erythrocyte; see arrow). CFP-actin was recruited to the forming phagosome, moved as a concentrated band over the particle during the extension phase (1.5–6.0 min), and condensed at the point of closure (6–7.5 min). YFP-PBD accumulated significantly on the base of the phagosome as constriction of the particle began (4.5–5.0 min), closely followed the moving band of actin during closure (5.5–7.5 min) and then rapidly dissipated (7.5–8.5 min). Bars, 3 μm. Also see Movie 1.
Genetic Algorithms, supplied by Kapelan Bio Imaging GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/imaging+algorithms/genetic+algorithms/ppr0666397-235-22-9
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genetic algorithms - by Bioz Stars, 2026-10
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90
Optik GmbH a practical algorithm for the determination of phase from image and diffraction plane pictures
Organization of PBD binding sites relative to actin localization during FcγR-mediated phagocytosis. (A) Time series showing phase-contrast and Ratio images of a macrophage internalizing an IgG-opsonized erythrocyte. The color bar indicates the molar ratio (YFP/CFP). YFP-PBD was recruited to the forming phagosome (1.5–4.5 min) to a much greater extent during closure (5.0–7.5 min) and was cleared from the closed phagosome (8.5 min). (B) Particle-tracking analysis of YFP-actin (open circles) and YFP-PBD (closed circles) indicated that actin was recruited to the phagosome after particle binding (0–1 min) and during extension (1–5 min), and YFP-PBD was recruited throughout phagocytosis, with a pronounced increase in recruitment during closure (5.0–8 min). Data are mean ± SEM for 10 <t>phagocytic</t> events; no more than three events were taken from any one cell, and at least five different cells made up the 10 traces. (C) Simultaneous imaging of YFP-PBD and CFP-actin indicated that actin and the majority of PBD binding sites formed a discrete interface during constriction of the opsonized erythrocyte (constriction is inferred from the deformation of the erythrocyte; see arrow). CFP-actin was recruited to the forming phagosome, moved as a concentrated band over the particle during the extension phase (1.5–6.0 min), and condensed at the point of closure (6–7.5 min). YFP-PBD accumulated significantly on the base of the phagosome as constriction of the particle began (4.5–5.0 min), closely followed the moving band of actin during closure (5.5–7.5 min) and then rapidly dissipated (7.5–8.5 min). Bars, 3 μm. Also see Movie 1.
A Practical Algorithm For The Determination Of Phase From Image And Diffraction Plane Pictures, supplied by Optik GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/imaging+algorithms/a+practical+algorithm+for+the+determination+of+phase+from+image+and+diffraction+plane+pictures/us11075463-419-3-20
Average 90 stars, based on 1 article reviews
a practical algorithm for the determination of phase from image and diffraction plane pictures - by Bioz Stars, 2026-10
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90
Visage Imaging GmbH ordered subsets-expectation maximization algorithm
Organization of PBD binding sites relative to actin localization during FcγR-mediated phagocytosis. (A) Time series showing phase-contrast and Ratio images of a macrophage internalizing an IgG-opsonized erythrocyte. The color bar indicates the molar ratio (YFP/CFP). YFP-PBD was recruited to the forming phagosome (1.5–4.5 min) to a much greater extent during closure (5.0–7.5 min) and was cleared from the closed phagosome (8.5 min). (B) Particle-tracking analysis of YFP-actin (open circles) and YFP-PBD (closed circles) indicated that actin was recruited to the phagosome after particle binding (0–1 min) and during extension (1–5 min), and YFP-PBD was recruited throughout phagocytosis, with a pronounced increase in recruitment during closure (5.0–8 min). Data are mean ± SEM for 10 <t>phagocytic</t> events; no more than three events were taken from any one cell, and at least five different cells made up the 10 traces. (C) Simultaneous imaging of YFP-PBD and CFP-actin indicated that actin and the majority of PBD binding sites formed a discrete interface during constriction of the opsonized erythrocyte (constriction is inferred from the deformation of the erythrocyte; see arrow). CFP-actin was recruited to the forming phagosome, moved as a concentrated band over the particle during the extension phase (1.5–6.0 min), and condensed at the point of closure (6–7.5 min). YFP-PBD accumulated significantly on the base of the phagosome as constriction of the particle began (4.5–5.0 min), closely followed the moving band of actin during closure (5.5–7.5 min) and then rapidly dissipated (7.5–8.5 min). Bars, 3 μm. Also see Movie 1.
Ordered Subsets Expectation Maximization Algorithm, supplied by Visage Imaging GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/imaging+algorithms/ordered+subsets+expectation+maximization+algorithm/pmc04891115-204-6-22
Average 90 stars, based on 1 article reviews
ordered subsets-expectation maximization algorithm - by Bioz Stars, 2026-10
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90
Hellige GMBH sirt based image reconstruction algorithm
Organization of PBD binding sites relative to actin localization during FcγR-mediated phagocytosis. (A) Time series showing phase-contrast and Ratio images of a macrophage internalizing an IgG-opsonized erythrocyte. The color bar indicates the molar ratio (YFP/CFP). YFP-PBD was recruited to the forming phagosome (1.5–4.5 min) to a much greater extent during closure (5.0–7.5 min) and was cleared from the closed phagosome (8.5 min). (B) Particle-tracking analysis of YFP-actin (open circles) and YFP-PBD (closed circles) indicated that actin was recruited to the phagosome after particle binding (0–1 min) and during extension (1–5 min), and YFP-PBD was recruited throughout phagocytosis, with a pronounced increase in recruitment during closure (5.0–8 min). Data are mean ± SEM for 10 <t>phagocytic</t> events; no more than three events were taken from any one cell, and at least five different cells made up the 10 traces. (C) Simultaneous imaging of YFP-PBD and CFP-actin indicated that actin and the majority of PBD binding sites formed a discrete interface during constriction of the opsonized erythrocyte (constriction is inferred from the deformation of the erythrocyte; see arrow). CFP-actin was recruited to the forming phagosome, moved as a concentrated band over the particle during the extension phase (1.5–6.0 min), and condensed at the point of closure (6–7.5 min). YFP-PBD accumulated significantly on the base of the phagosome as constriction of the particle began (4.5–5.0 min), closely followed the moving band of actin during closure (5.5–7.5 min) and then rapidly dissipated (7.5–8.5 min). Bars, 3 μm. Also see Movie 1.
Sirt Based Image Reconstruction Algorithm, supplied by Hellige GMBH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/imaging+algorithms/sirt+based+image+reconstruction+algorithm/10__1515_slash_bmt__2010__713-1074-15-10
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sirt based image reconstruction algorithm - by Bioz Stars, 2026-10
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90
Imaging Biometrics LLC dt1 algorithm
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Dt1 Algorithm, supplied by Imaging Biometrics LLC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/imaging+algorithms/dt1+algorithm/pmc11198967-123-31-41
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dt1 algorithm - by Bioz Stars, 2026-10
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90
Visiopharm AS automated image analysis algorithms
Patient Demographics
Automated Image Analysis Algorithms, supplied by Visiopharm AS, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/imaging+algorithms/automated+image+analysis+algorithms/pmc09026790-106-30-14
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automated image analysis algorithms - by Bioz Stars, 2026-10
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TOMTEC IMAGING SYSTEMS GMBH offline commercial feature-tracking software
Patient Demographics
Offline Commercial Feature Tracking Software, supplied by TOMTEC IMAGING SYSTEMS GMBH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/imaging+algorithms/rv+algorithm+wall+motion+tracking+software/pmc11137213-100-6-10
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offline commercial feature-tracking software - by Bioz Stars, 2026-10
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90
Lawrence Livermore National Security LLC locally optimized combination of images (loci) algorithm
Preliminary results from <t>Lawrence</t> <t>Livermore</t> National Laboratory. Five planets are visible in the median-subtracted image, only three of which appear within the <t>LOCI</t> search area.
Locally Optimized Combination Of Images (Loci) Algorithm, supplied by Lawrence Livermore National Security LLC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/imaging+algorithms/locally+optimized+combination+of+images++loci++algorithm/pmc04558925-294-18-6
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90
Xerox Corporation image recognition algorithms in gvt
Preliminary results from <t>Lawrence</t> <t>Livermore</t> National Laboratory. Five planets are visible in the median-subtracted image, only three of which appear within the <t>LOCI</t> search area.
Image Recognition Algorithms In Gvt, supplied by Xerox Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/imaging+algorithms/image+recognition+algorithms+in+gvt/us09176694-48-20-43
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Verlag GmbH digital image processing—concepts, algorithms, and scientific applications
Preliminary results from <t>Lawrence</t> <t>Livermore</t> National Laboratory. Five planets are visible in the median-subtracted image, only three of which appear within the <t>LOCI</t> search area.
Digital Image Processing—Concepts, Algorithms, And Scientific Applications, supplied by Verlag GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/imaging+algorithms/digital+image+processing+concepts++algorithms++and+scientific+applications/us08712185-442-3-12
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digital image processing—concepts, algorithms, and scientific applications - by Bioz Stars, 2026-10
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Image Search Results


Organization of PBD binding sites relative to actin localization during FcγR-mediated phagocytosis. (A) Time series showing phase-contrast and Ratio images of a macrophage internalizing an IgG-opsonized erythrocyte. The color bar indicates the molar ratio (YFP/CFP). YFP-PBD was recruited to the forming phagosome (1.5–4.5 min) to a much greater extent during closure (5.0–7.5 min) and was cleared from the closed phagosome (8.5 min). (B) Particle-tracking analysis of YFP-actin (open circles) and YFP-PBD (closed circles) indicated that actin was recruited to the phagosome after particle binding (0–1 min) and during extension (1–5 min), and YFP-PBD was recruited throughout phagocytosis, with a pronounced increase in recruitment during closure (5.0–8 min). Data are mean ± SEM for 10 phagocytic events; no more than three events were taken from any one cell, and at least five different cells made up the 10 traces. (C) Simultaneous imaging of YFP-PBD and CFP-actin indicated that actin and the majority of PBD binding sites formed a discrete interface during constriction of the opsonized erythrocyte (constriction is inferred from the deformation of the erythrocyte; see arrow). CFP-actin was recruited to the forming phagosome, moved as a concentrated band over the particle during the extension phase (1.5–6.0 min), and condensed at the point of closure (6–7.5 min). YFP-PBD accumulated significantly on the base of the phagosome as constriction of the particle began (4.5–5.0 min), closely followed the moving band of actin during closure (5.5–7.5 min) and then rapidly dissipated (7.5–8.5 min). Bars, 3 μm. Also see Movie 1.

Journal:

Article Title: Cdc42, Rac1, and Rac2 Display Distinct Patterns of Activation during Phagocytosis V⃞

doi: 10.1091/mbc.E03-11-0847

Figure Lengend Snippet: Organization of PBD binding sites relative to actin localization during FcγR-mediated phagocytosis. (A) Time series showing phase-contrast and Ratio images of a macrophage internalizing an IgG-opsonized erythrocyte. The color bar indicates the molar ratio (YFP/CFP). YFP-PBD was recruited to the forming phagosome (1.5–4.5 min) to a much greater extent during closure (5.0–7.5 min) and was cleared from the closed phagosome (8.5 min). (B) Particle-tracking analysis of YFP-actin (open circles) and YFP-PBD (closed circles) indicated that actin was recruited to the phagosome after particle binding (0–1 min) and during extension (1–5 min), and YFP-PBD was recruited throughout phagocytosis, with a pronounced increase in recruitment during closure (5.0–8 min). Data are mean ± SEM for 10 phagocytic events; no more than three events were taken from any one cell, and at least five different cells made up the 10 traces. (C) Simultaneous imaging of YFP-PBD and CFP-actin indicated that actin and the majority of PBD binding sites formed a discrete interface during constriction of the opsonized erythrocyte (constriction is inferred from the deformation of the erythrocyte; see arrow). CFP-actin was recruited to the forming phagosome, moved as a concentrated band over the particle during the extension phase (1.5–6.0 min), and condensed at the point of closure (6–7.5 min). YFP-PBD accumulated significantly on the base of the phagosome as constriction of the particle began (4.5–5.0 min), closely followed the moving band of actin during closure (5.5–7.5 min) and then rapidly dissipated (7.5–8.5 min). Bars, 3 μm. Also see Movie 1.

Article Snippet: To quantify signaling events from multiple phagocytic events, a particle-tracking image analysis algorithm was developed in MetaMorph software (Universal Imaging).

Techniques: Binding Assay, Imaging

Ratiometric imaging and tracking analysis of YFP-Cdc42, YFP-Rac1, YFP-Rac2, and YFP-AtkPH domain relative to CFP during phagocytosis. (A, C, E, and G) Phase-contrast, YFP, and Ratio image time series of RAW macrophages phagocytosing IgG-coated erythrocytes. Color bars indicate the ranges of the Ratio values. (B, D, F, and H) Plots of RP/RC indicating the dynamics of YFP-chimera localization to phagosomes, averaged for 10 phagocytic events each. Error bars are the SE of the mean. (A) YFP-Cdc42 was present at the site of binding (0.5 min), localized to the tips of the advancing pseudopod (1.5–4.5 min) and then remained on the phagosome during and following closure (5.5–8.5 min). (B) Tracking analysis indicated the enhancement of YFP-Cdc42 on multiple phagosomes, but it did not indicate a significant change in localization. (C) YFP-Rac1 was present on plasma membranes before phagocytosis as seen by the Ratio image (0.5 min). The ratio increased as membrane extended around the particle (1.5–4.5 min) and then diminished somewhat during internalization (5.5–8.5 min). (D) Cumulative tracking data indicated that the association of YFP-Rac1 with the phagosome was variable, decreased until closure (>8.0 min) and then remained slightly elevated. (E) YFP-Rac2 localized to the base of the phagosome during extension and closure. (F) Tracking analysis showed YFP-Rac2 slightly increased on the phagosome. (G) The YFP-AktPH domain localized rapidly to the site of particle contact (0.5–1.5 min), continually increased (1.5–4.5 min), and then was cleared from the plasma membrane after closure (5.5–8.5 min). (H) YFP-AktPH was localized to phagosomes throughout formation and closure and then was cleared slowly. Bar, 3 μm.

Journal:

Article Title: Cdc42, Rac1, and Rac2 Display Distinct Patterns of Activation during Phagocytosis V⃞

doi: 10.1091/mbc.E03-11-0847

Figure Lengend Snippet: Ratiometric imaging and tracking analysis of YFP-Cdc42, YFP-Rac1, YFP-Rac2, and YFP-AtkPH domain relative to CFP during phagocytosis. (A, C, E, and G) Phase-contrast, YFP, and Ratio image time series of RAW macrophages phagocytosing IgG-coated erythrocytes. Color bars indicate the ranges of the Ratio values. (B, D, F, and H) Plots of RP/RC indicating the dynamics of YFP-chimera localization to phagosomes, averaged for 10 phagocytic events each. Error bars are the SE of the mean. (A) YFP-Cdc42 was present at the site of binding (0.5 min), localized to the tips of the advancing pseudopod (1.5–4.5 min) and then remained on the phagosome during and following closure (5.5–8.5 min). (B) Tracking analysis indicated the enhancement of YFP-Cdc42 on multiple phagosomes, but it did not indicate a significant change in localization. (C) YFP-Rac1 was present on plasma membranes before phagocytosis as seen by the Ratio image (0.5 min). The ratio increased as membrane extended around the particle (1.5–4.5 min) and then diminished somewhat during internalization (5.5–8.5 min). (D) Cumulative tracking data indicated that the association of YFP-Rac1 with the phagosome was variable, decreased until closure (>8.0 min) and then remained slightly elevated. (E) YFP-Rac2 localized to the base of the phagosome during extension and closure. (F) Tracking analysis showed YFP-Rac2 slightly increased on the phagosome. (G) The YFP-AktPH domain localized rapidly to the site of particle contact (0.5–1.5 min), continually increased (1.5–4.5 min), and then was cleared from the plasma membrane after closure (5.5–8.5 min). (H) YFP-AktPH was localized to phagosomes throughout formation and closure and then was cleared slowly. Bar, 3 μm.

Article Snippet: To quantify signaling events from multiple phagocytic events, a particle-tracking image analysis algorithm was developed in MetaMorph software (Universal Imaging).

Techniques: Imaging, Binding Assay, Clinical Proteomics, Membrane

FRET stoichiometric imaging of YFP-Cdc42, YFP-Rac1, and YFP-Rac2 activation during phagocytosis of E-IgG. (A) Phase-contrast and EA images for cells expressing YFP-Cdc42 and CFP-PBD. YFP-Cdc42 produced an EA signal as soon as the erythrocyte contacted the macrophage. The high EA was restricted to the advancing tip of the pseudopod as it moved over the particle (1.5–5.5 min) and diminished during the closure phase (5.5–8.5 min). (B) Tracking analysis indicated the rapid association of YFP-Cdc42 with CFP-PBD and persistent FRET throughout pseudopod extension. (C and D) FRET microscopy and stoichiometry of macrophages expressing YFP-Rac1 and CFP-PBD. YFP-Rac1 interacted with CFP-PBD shortly after particle binding and throughout the pseudopod during extension (1.5–5.5 min). The quantity of YFP-Rac1 in complex with CFP-PBD increased transiently on the base of the pseudopod during the closure phase (5.5–7.5 min) and was deactivated on the closed phagosome (8.5 min). (D) This response was consistent when averaged over multiple phagocytic events. (E and F) FRET microscopy of cells expressing YFP-Rac2 and CFP-PBD indicated that Rac2 activation was delayed until closure. (G) Control cell expressing YFP-Cdc42 and CFP showed a uniform value of EA = 0 throughout phagocytosis. (H) Averaged traces from control cells expressing CFP plus YFP-Cdc42 (red), YFP-Rac1 (blue), or YFP-Rac2 (green) never indicated FRET. Bar, 3 μm. Also see Movies 2–4.

Journal:

Article Title: Cdc42, Rac1, and Rac2 Display Distinct Patterns of Activation during Phagocytosis V⃞

doi: 10.1091/mbc.E03-11-0847

Figure Lengend Snippet: FRET stoichiometric imaging of YFP-Cdc42, YFP-Rac1, and YFP-Rac2 activation during phagocytosis of E-IgG. (A) Phase-contrast and EA images for cells expressing YFP-Cdc42 and CFP-PBD. YFP-Cdc42 produced an EA signal as soon as the erythrocyte contacted the macrophage. The high EA was restricted to the advancing tip of the pseudopod as it moved over the particle (1.5–5.5 min) and diminished during the closure phase (5.5–8.5 min). (B) Tracking analysis indicated the rapid association of YFP-Cdc42 with CFP-PBD and persistent FRET throughout pseudopod extension. (C and D) FRET microscopy and stoichiometry of macrophages expressing YFP-Rac1 and CFP-PBD. YFP-Rac1 interacted with CFP-PBD shortly after particle binding and throughout the pseudopod during extension (1.5–5.5 min). The quantity of YFP-Rac1 in complex with CFP-PBD increased transiently on the base of the pseudopod during the closure phase (5.5–7.5 min) and was deactivated on the closed phagosome (8.5 min). (D) This response was consistent when averaged over multiple phagocytic events. (E and F) FRET microscopy of cells expressing YFP-Rac2 and CFP-PBD indicated that Rac2 activation was delayed until closure. (G) Control cell expressing YFP-Cdc42 and CFP showed a uniform value of EA = 0 throughout phagocytosis. (H) Averaged traces from control cells expressing CFP plus YFP-Cdc42 (red), YFP-Rac1 (blue), or YFP-Rac2 (green) never indicated FRET. Bar, 3 μm. Also see Movies 2–4.

Article Snippet: To quantify signaling events from multiple phagocytic events, a particle-tracking image analysis algorithm was developed in MetaMorph software (Universal Imaging).

Techniques: Imaging, Activation Assay, Expressing, Produced, Microscopy, Binding Assay, Control

Patient Demographics

Journal: Neurosurgery practice

Article Title: Application of Delta T1 maps for quantitative and objective assessment of extent of resection and survival prediction in glioblastoma

doi:

Figure Lengend Snippet: Patient Demographics

Article Snippet: The calibrated pre-contrast and calibrated post-contrast T1 images are then registered and subtracted creating the quantitative delta T1 (dT1) image. (Each of the previous steps can be automatically performed using the dT1 algorithm made available within the IB DeltaSuite TM software (Imaging Biometrics LLC, Elm Grove, Wisconsin)).

Techniques: Methylation

from a 72 y male with IDH1-wild type glioblastoma, obtained 4 days before (A-C) and 1 day after (D-F) tumor resection (ie pre/post-op). Despite the bright signal on both pre-contrast (C) and the post-contrast T1w images (D) the post-resection dT1 (F) shows minimal residual enhancement enabling the dT1-determined EOR of 92.64%, and a RTV of 3.64 cm3 for all slices (all slices not shown).

Journal: Neurosurgery practice

Article Title: Application of Delta T1 maps for quantitative and objective assessment of extent of resection and survival prediction in glioblastoma

doi:

Figure Lengend Snippet: from a 72 y male with IDH1-wild type glioblastoma, obtained 4 days before (A-C) and 1 day after (D-F) tumor resection (ie pre/post-op). Despite the bright signal on both pre-contrast (C) and the post-contrast T1w images (D) the post-resection dT1 (F) shows minimal residual enhancement enabling the dT1-determined EOR of 92.64%, and a RTV of 3.64 cm3 for all slices (all slices not shown).

Article Snippet: The calibrated pre-contrast and calibrated post-contrast T1 images are then registered and subtracted creating the quantitative delta T1 (dT1) image. (Each of the previous steps can be automatically performed using the dT1 algorithm made available within the IB DeltaSuite TM software (Imaging Biometrics LLC, Elm Grove, Wisconsin)).

Techniques:

Patient Demographics for Resection Groups

Journal: Neurosurgery practice

Article Title: Application of Delta T1 maps for quantitative and objective assessment of extent of resection and survival prediction in glioblastoma

doi:

Figure Lengend Snippet: Patient Demographics for Resection Groups

Article Snippet: The calibrated pre-contrast and calibrated post-contrast T1 images are then registered and subtracted creating the quantitative delta T1 (dT1) image. (Each of the previous steps can be automatically performed using the dT1 algorithm made available within the IB DeltaSuite TM software (Imaging Biometrics LLC, Elm Grove, Wisconsin)).

Techniques:

based on (A) dT1-determined extent of resection (EOR), (B) dT1-determined residual tumor volume (RTV) and (C) the radiologist’s impression as gross total resection (GTR) or subtotal resection (STR). All but one patient had an EOR that was categorized as either subtotal resection (STR) or partial total resection (PTR) with a significant difference in overall survival between these groups. One patient’s EOR was categorized as near-total resection (NTR), which was not included in the survival analysis. Using an RTV threshold of 5cm3 a statistically significant difference in survival was observed. No difference in survival, based on the radiologist’s impression, was observed.

Journal: Neurosurgery practice

Article Title: Application of Delta T1 maps for quantitative and objective assessment of extent of resection and survival prediction in glioblastoma

doi:

Figure Lengend Snippet: based on (A) dT1-determined extent of resection (EOR), (B) dT1-determined residual tumor volume (RTV) and (C) the radiologist’s impression as gross total resection (GTR) or subtotal resection (STR). All but one patient had an EOR that was categorized as either subtotal resection (STR) or partial total resection (PTR) with a significant difference in overall survival between these groups. One patient’s EOR was categorized as near-total resection (NTR), which was not included in the survival analysis. Using an RTV threshold of 5cm3 a statistically significant difference in survival was observed. No difference in survival, based on the radiologist’s impression, was observed.

Article Snippet: The calibrated pre-contrast and calibrated post-contrast T1 images are then registered and subtracted creating the quantitative delta T1 (dT1) image. (Each of the previous steps can be automatically performed using the dT1 algorithm made available within the IB DeltaSuite TM software (Imaging Biometrics LLC, Elm Grove, Wisconsin)).

Techniques:

Multivariate Cox Proportionality Hazards Regression Results

Journal: Neurosurgery practice

Article Title: Application of Delta T1 maps for quantitative and objective assessment of extent of resection and survival prediction in glioblastoma

doi:

Figure Lengend Snippet: Multivariate Cox Proportionality Hazards Regression Results

Article Snippet: The calibrated pre-contrast and calibrated post-contrast T1 images are then registered and subtracted creating the quantitative delta T1 (dT1) image. (Each of the previous steps can be automatically performed using the dT1 algorithm made available within the IB DeltaSuite TM software (Imaging Biometrics LLC, Elm Grove, Wisconsin)).

Techniques:

Preliminary results from Lawrence Livermore National Laboratory. Five planets are visible in the median-subtracted image, only three of which appear within the LOCI search area.

Journal: Proceedings of SPIE--the International Society for Optical Engineering

Article Title: On Advanced Estimation Techniques for Exoplanet Detection and Characterization Using Ground-based Coronagraphs

doi: 10.1117/12.925099

Figure Lengend Snippet: Preliminary results from Lawrence Livermore National Laboratory. Five planets are visible in the median-subtracted image, only three of which appear within the LOCI search area.

Article Snippet: 4.2 Preliminary Results: Poyneer and Savransky (Lawrence Livermore National Laboratory) Our implementation of the Locally Optimized Combination of Images (LOCI) algorithm is based on the original description presented by Lafreniére 6 wherein we seek to minimize the residuals between a target image and a linear combination of a set of reference images.

Techniques: