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PMC1820774_F1_9987.jpg | What is the principal component of this image? | Photograph of intraoperative measurement set up. Rostral is to the left, caudal to the right. Three electrodes can be seen inserted through the convex annulus of three adjacent discs. The pressure transducer is seen inserted into the middle disc. |
PMC1820774_F2_9989.jpg | What is the focal point of this photograph? | Part of intraoperative representative radiograph showing electrodes and pressure transducer inserted from the convex side of the scoliotic curve (same patient as figure 1). |
PMC1820780_F3_9993.jpg | Describe the main subject of this image. | Conditional loss of Notch1 in the cerebellar primordium results in severe hypoplasia and loss of Purkinje cell precursors. (a, b) Sagittal whole mount view of E16.5 floxNotch1 (a) and En1-cre; floxNotch1 (b) brains. The arrows in (a, b) indicate the position of the cerebellum. (c-f) Sagittal cryosections of floxNotch1 (c, e) and En1-cre; floxNotch1 (d, f) cerebella stained by hematoxylin and eosin histochemistry (c, d) or by immunohistochemistry for calbindin (e, f). Boxes in (c, d) indicate the approximate photographic fields in (e, f). Dashed box in (f) delineates the residual cerebellum in the mutant embryo. Scale bars in (e, f) represent 300 μm. |
PMC1820780_F3_9994.jpg | What object or scene is depicted here? | Conditional loss of Notch1 in the cerebellar primordium results in severe hypoplasia and loss of Purkinje cell precursors. (a, b) Sagittal whole mount view of E16.5 floxNotch1 (a) and En1-cre; floxNotch1 (b) brains. The arrows in (a, b) indicate the position of the cerebellum. (c-f) Sagittal cryosections of floxNotch1 (c, e) and En1-cre; floxNotch1 (d, f) cerebella stained by hematoxylin and eosin histochemistry (c, d) or by immunohistochemistry for calbindin (e, f). Boxes in (c, d) indicate the approximate photographic fields in (e, f). Dashed box in (f) delineates the residual cerebellum in the mutant embryo. Scale bars in (e, f) represent 300 μm. |
PMC1820780_F3_9996.jpg | What is shown in this image? | Conditional loss of Notch1 in the cerebellar primordium results in severe hypoplasia and loss of Purkinje cell precursors. (a, b) Sagittal whole mount view of E16.5 floxNotch1 (a) and En1-cre; floxNotch1 (b) brains. The arrows in (a, b) indicate the position of the cerebellum. (c-f) Sagittal cryosections of floxNotch1 (c, e) and En1-cre; floxNotch1 (d, f) cerebella stained by hematoxylin and eosin histochemistry (c, d) or by immunohistochemistry for calbindin (e, f). Boxes in (c, d) indicate the approximate photographic fields in (e, f). Dashed box in (f) delineates the residual cerebellum in the mutant embryo. Scale bars in (e, f) represent 300 μm. |
PMC1820783_F3_10002.jpg | What key item or scene is captured in this photo? | IHC results. 3A. Tumor cells displaying positive immunoreactivity for CK7. DAB × 400. 3B. Tumor cells displaying strong membranous positivity for EMA. DAB × 200. 3C. Tumor cells showing intra cytoplasmic dot-like expression for desmin. DAB × 400. 3D. Strong, diffuse, membranous positivity for CD34. DAB × 400. Positive internal control in the vascular endothelial cells noted. |
PMC1820783_F3_10000.jpg | What is the dominant medical problem in this image? | IHC results. 3A. Tumor cells displaying positive immunoreactivity for CK7. DAB × 400. 3B. Tumor cells displaying strong membranous positivity for EMA. DAB × 200. 3C. Tumor cells showing intra cytoplasmic dot-like expression for desmin. DAB × 400. 3D. Strong, diffuse, membranous positivity for CD34. DAB × 400. Positive internal control in the vascular endothelial cells noted. |
PMC1820783_F3_10003.jpg | What is the principal component of this image? | IHC results. 3A. Tumor cells displaying positive immunoreactivity for CK7. DAB × 400. 3B. Tumor cells displaying strong membranous positivity for EMA. DAB × 200. 3C. Tumor cells showing intra cytoplasmic dot-like expression for desmin. DAB × 400. 3D. Strong, diffuse, membranous positivity for CD34. DAB × 400. Positive internal control in the vascular endothelial cells noted. |
PMC1820784_F1_9997.jpg | What is the central feature of this picture? | Contrast-enhanced axial orbital computed tomography showing a well-circumscirbed mass at lateral aspect of the left orbit without bone involvement. |
PMC1820784_F2_9999.jpg | What does this image primarily show? | Hematoxylin-eosin staining (100× magnification) showing poorly differentiated adenocarcinoma, suggesting malignant carcinomatous changes in the recurrent pleomorphic adenoma. Nuclear atypia and prominent mitosis are noted. |
PMC1820789_F12_10005.jpg | What is the main focus of this visual representation? | Image fusion of CT and scintigraphic data showing diffuse Octreotide uptake in the lower limbs of a patient with TAO. Octreotide uptake represents inflammatory activity. Taken from [49]. Each reconstruction plane is labeled in the upper left corner of the image. The right lower image is an anatomical reconstruction of the surface of the leg. |
PMC1820789_F12_10006.jpg | What key item or scene is captured in this photo? | Image fusion of CT and scintigraphic data showing diffuse Octreotide uptake in the lower limbs of a patient with TAO. Octreotide uptake represents inflammatory activity. Taken from [49]. Each reconstruction plane is labeled in the upper left corner of the image. The right lower image is an anatomical reconstruction of the surface of the leg. |
PMC1820789_F16_10008.jpg | What is the dominant medical problem in this image? | Metabolic imaging using 18F-Fluorodeoxyglucose (18F-FDG) showing metabolic activity in the lateral abdomen (dark areas). These areas are located around the Dai mai point which has been evaluated in our study. The accompanying CT images shows a clear deviation of the body axis at the level of the trunk. The images are reproduced with kind permission of the Society of Nuclear Medicine [166]. |
PMC1820829_pbio-0050068-g005_10015.jpg | What is the focal point of this photograph? | N and p50-U1 Associate In Vivo(A) The BiFC assay was used to demonstrate the ability of N and p50-U1 to associate in living tissue. gN-YN (column 1) alone and p50-U1-YC (column 2) alone do not produce fluorescence in N. benthamiana tissue. Co-expression of gN-YN and p50-U1-YC produces Citrine fluorescence (column 3), demonstrating a close association between N and p50-U1. GUS-YC is used as control for the specificity of associations involving gN-YN (column 4). Citrine fluorescence was imaged with the 514-nm laser line of a 15-mW argon laser. Scale bar represents 20 μm.(B) p50-U1-Ob-YC expressed alone does not produce fluorescence (column 1). Co-expression of gN-YN and the non-eliciting p50-U1-Ob-YC does not produce Citrine fluorescence (column 2), indicating that they do not associate in vivo. Scale bar represents 20 μm. |
PMC1820829_pbio-0050068-g005_10010.jpg | What stands out most in this visual? | N and p50-U1 Associate In Vivo(A) The BiFC assay was used to demonstrate the ability of N and p50-U1 to associate in living tissue. gN-YN (column 1) alone and p50-U1-YC (column 2) alone do not produce fluorescence in N. benthamiana tissue. Co-expression of gN-YN and p50-U1-YC produces Citrine fluorescence (column 3), demonstrating a close association between N and p50-U1. GUS-YC is used as control for the specificity of associations involving gN-YN (column 4). Citrine fluorescence was imaged with the 514-nm laser line of a 15-mW argon laser. Scale bar represents 20 μm.(B) p50-U1-Ob-YC expressed alone does not produce fluorescence (column 1). Co-expression of gN-YN and the non-eliciting p50-U1-Ob-YC does not produce Citrine fluorescence (column 2), indicating that they do not associate in vivo. Scale bar represents 20 μm. |
PMC1820829_pbio-0050068-g005_10016.jpg | Can you identify the primary element in this image? | N and p50-U1 Associate In Vivo(A) The BiFC assay was used to demonstrate the ability of N and p50-U1 to associate in living tissue. gN-YN (column 1) alone and p50-U1-YC (column 2) alone do not produce fluorescence in N. benthamiana tissue. Co-expression of gN-YN and p50-U1-YC produces Citrine fluorescence (column 3), demonstrating a close association between N and p50-U1. GUS-YC is used as control for the specificity of associations involving gN-YN (column 4). Citrine fluorescence was imaged with the 514-nm laser line of a 15-mW argon laser. Scale bar represents 20 μm.(B) p50-U1-Ob-YC expressed alone does not produce fluorescence (column 1). Co-expression of gN-YN and the non-eliciting p50-U1-Ob-YC does not produce Citrine fluorescence (column 2), indicating that they do not associate in vivo. Scale bar represents 20 μm. |
PMC1820829_pbio-0050068-g005_10009.jpg | What's the most prominent thing you notice in this picture? | N and p50-U1 Associate In Vivo(A) The BiFC assay was used to demonstrate the ability of N and p50-U1 to associate in living tissue. gN-YN (column 1) alone and p50-U1-YC (column 2) alone do not produce fluorescence in N. benthamiana tissue. Co-expression of gN-YN and p50-U1-YC produces Citrine fluorescence (column 3), demonstrating a close association between N and p50-U1. GUS-YC is used as control for the specificity of associations involving gN-YN (column 4). Citrine fluorescence was imaged with the 514-nm laser line of a 15-mW argon laser. Scale bar represents 20 μm.(B) p50-U1-Ob-YC expressed alone does not produce fluorescence (column 1). Co-expression of gN-YN and the non-eliciting p50-U1-Ob-YC does not produce Citrine fluorescence (column 2), indicating that they do not associate in vivo. Scale bar represents 20 μm. |
PMC1820829_pbio-0050068-g005_10013.jpg | What is the focal point of this photograph? | N and p50-U1 Associate In Vivo(A) The BiFC assay was used to demonstrate the ability of N and p50-U1 to associate in living tissue. gN-YN (column 1) alone and p50-U1-YC (column 2) alone do not produce fluorescence in N. benthamiana tissue. Co-expression of gN-YN and p50-U1-YC produces Citrine fluorescence (column 3), demonstrating a close association between N and p50-U1. GUS-YC is used as control for the specificity of associations involving gN-YN (column 4). Citrine fluorescence was imaged with the 514-nm laser line of a 15-mW argon laser. Scale bar represents 20 μm.(B) p50-U1-Ob-YC expressed alone does not produce fluorescence (column 1). Co-expression of gN-YN and the non-eliciting p50-U1-Ob-YC does not produce Citrine fluorescence (column 2), indicating that they do not associate in vivo. Scale bar represents 20 μm. |
PMC1820829_pbio-0050068-g005_10017.jpg | What is the central feature of this picture? | N and p50-U1 Associate In Vivo(A) The BiFC assay was used to demonstrate the ability of N and p50-U1 to associate in living tissue. gN-YN (column 1) alone and p50-U1-YC (column 2) alone do not produce fluorescence in N. benthamiana tissue. Co-expression of gN-YN and p50-U1-YC produces Citrine fluorescence (column 3), demonstrating a close association between N and p50-U1. GUS-YC is used as control for the specificity of associations involving gN-YN (column 4). Citrine fluorescence was imaged with the 514-nm laser line of a 15-mW argon laser. Scale bar represents 20 μm.(B) p50-U1-Ob-YC expressed alone does not produce fluorescence (column 1). Co-expression of gN-YN and the non-eliciting p50-U1-Ob-YC does not produce Citrine fluorescence (column 2), indicating that they do not associate in vivo. Scale bar represents 20 μm. |
PMC1820829_pbio-0050068-g005_10014.jpg | What is the dominant medical problem in this image? | N and p50-U1 Associate In Vivo(A) The BiFC assay was used to demonstrate the ability of N and p50-U1 to associate in living tissue. gN-YN (column 1) alone and p50-U1-YC (column 2) alone do not produce fluorescence in N. benthamiana tissue. Co-expression of gN-YN and p50-U1-YC produces Citrine fluorescence (column 3), demonstrating a close association between N and p50-U1. GUS-YC is used as control for the specificity of associations involving gN-YN (column 4). Citrine fluorescence was imaged with the 514-nm laser line of a 15-mW argon laser. Scale bar represents 20 μm.(B) p50-U1-Ob-YC expressed alone does not produce fluorescence (column 1). Co-expression of gN-YN and the non-eliciting p50-U1-Ob-YC does not produce Citrine fluorescence (column 2), indicating that they do not associate in vivo. Scale bar represents 20 μm. |
PMC1820829_pbio-0050068-g005_10018.jpg | What stands out most in this visual? | N and p50-U1 Associate In Vivo(A) The BiFC assay was used to demonstrate the ability of N and p50-U1 to associate in living tissue. gN-YN (column 1) alone and p50-U1-YC (column 2) alone do not produce fluorescence in N. benthamiana tissue. Co-expression of gN-YN and p50-U1-YC produces Citrine fluorescence (column 3), demonstrating a close association between N and p50-U1. GUS-YC is used as control for the specificity of associations involving gN-YN (column 4). Citrine fluorescence was imaged with the 514-nm laser line of a 15-mW argon laser. Scale bar represents 20 μm.(B) p50-U1-Ob-YC expressed alone does not produce fluorescence (column 1). Co-expression of gN-YN and the non-eliciting p50-U1-Ob-YC does not produce Citrine fluorescence (column 2), indicating that they do not associate in vivo. Scale bar represents 20 μm. |
PMC1820829_pbio-0050068-g005_10019.jpg | What is being portrayed in this visual content? | N and p50-U1 Associate In Vivo(A) The BiFC assay was used to demonstrate the ability of N and p50-U1 to associate in living tissue. gN-YN (column 1) alone and p50-U1-YC (column 2) alone do not produce fluorescence in N. benthamiana tissue. Co-expression of gN-YN and p50-U1-YC produces Citrine fluorescence (column 3), demonstrating a close association between N and p50-U1. GUS-YC is used as control for the specificity of associations involving gN-YN (column 4). Citrine fluorescence was imaged with the 514-nm laser line of a 15-mW argon laser. Scale bar represents 20 μm.(B) p50-U1-Ob-YC expressed alone does not produce fluorescence (column 1). Co-expression of gN-YN and the non-eliciting p50-U1-Ob-YC does not produce Citrine fluorescence (column 2), indicating that they do not associate in vivo. Scale bar represents 20 μm. |
PMC1821014_F7_10022.jpg | What is the focal point of this photograph? | Age 13.3. After 22 months in braces and genioplasty. Left: Panoramic radiograph does not reveal root resorption. Teeth 27, 38, and 48 were removed at time of genioplasty. Right: Superimposition of lateral ceph before treatment with the fixed appliance (blue) (age 11.4) and after genioplasty (red) (age 13.3). |
PMC1821014_F10_10024.jpg | What's the most prominent thing you notice in this picture? | Age 13.2. Panoramic x-ray. Congenitally missing tooth 28 and impacted teeth 18, 17, 14, 13, 23, 27, 38, 33, 43 and 48. Because of extreme crowding, impaction, and space discrepancy, extraction of teeth 17, 14, 13, 23, 38, 33, 43, and 48 were considered. Tooth 18 will be left in place because of its malposition. |
PMC1821014_F12_10025.jpg | What is the dominant medical problem in this image? | Age 14.2. After five months in braces. Panographic x-ray and tracing of lateral x-ray. Because of mandibular growth and orthodontic decompensation (the latter is a prerequisite for orthognathic surgery) and insufficient growth of maxillary complex, the open bite and Class III worsened as compared with lateral x-ray at age 10.7 (compare Fig. 10). Tooth 18 will be left in place because of its malposition. |
PMC1821014_F17_10035.jpg | What is the central feature of this picture? | Age 16.4. Situation after 1.2 years in braces in order to parallelize 11 and 22 for later prosthodontic rehabilitation. Teeth 24 and 25 had not been bonded because of idiopathic root resorption (compare panographic x-ray, Fig. 16). Extraorally: With and without thermoplastic retainer for temporary replacement of 21. Intraorally: Teeth 11 and 22 were parallelized. |
PMC1821014_F17_10036.jpg | What is the principal component of this image? | Age 16.4. Situation after 1.2 years in braces in order to parallelize 11 and 22 for later prosthodontic rehabilitation. Teeth 24 and 25 had not been bonded because of idiopathic root resorption (compare panographic x-ray, Fig. 16). Extraorally: With and without thermoplastic retainer for temporary replacement of 21. Intraorally: Teeth 11 and 22 were parallelized. |
PMC1821014_F17_10031.jpg | What is the main focus of this visual representation? | Age 16.4. Situation after 1.2 years in braces in order to parallelize 11 and 22 for later prosthodontic rehabilitation. Teeth 24 and 25 had not been bonded because of idiopathic root resorption (compare panographic x-ray, Fig. 16). Extraorally: With and without thermoplastic retainer for temporary replacement of 21. Intraorally: Teeth 11 and 22 were parallelized. |
PMC1821014_F17_10033.jpg | What stands out most in this visual? | Age 16.4. Situation after 1.2 years in braces in order to parallelize 11 and 22 for later prosthodontic rehabilitation. Teeth 24 and 25 had not been bonded because of idiopathic root resorption (compare panographic x-ray, Fig. 16). Extraorally: With and without thermoplastic retainer for temporary replacement of 21. Intraorally: Teeth 11 and 22 were parallelized. |
PMC1821014_F17_10030.jpg | Describe the main subject of this image. | Age 16.4. Situation after 1.2 years in braces in order to parallelize 11 and 22 for later prosthodontic rehabilitation. Teeth 24 and 25 had not been bonded because of idiopathic root resorption (compare panographic x-ray, Fig. 16). Extraorally: With and without thermoplastic retainer for temporary replacement of 21. Intraorally: Teeth 11 and 22 were parallelized. |
PMC1821014_F17_10034.jpg | What stands out most in this visual? | Age 16.4. Situation after 1.2 years in braces in order to parallelize 11 and 22 for later prosthodontic rehabilitation. Teeth 24 and 25 had not been bonded because of idiopathic root resorption (compare panographic x-ray, Fig. 16). Extraorally: With and without thermoplastic retainer for temporary replacement of 21. Intraorally: Teeth 11 and 22 were parallelized. |
PMC1821014_F17_10028.jpg | Can you identify the primary element in this image? | Age 16.4. Situation after 1.2 years in braces in order to parallelize 11 and 22 for later prosthodontic rehabilitation. Teeth 24 and 25 had not been bonded because of idiopathic root resorption (compare panographic x-ray, Fig. 16). Extraorally: With and without thermoplastic retainer for temporary replacement of 21. Intraorally: Teeth 11 and 22 were parallelized. |
PMC1821014_F18_10027.jpg | What does this image primarily show? | Left: age 18.2. Panographic x-ray 5 months before surgery. Right: age 18.6. Tracing of lateral x-ray before orthognathic surgery. |
PMC1821025_F2_10039.jpg | What key item or scene is captured in this photo? | Endoanal ultrasonography (transverse plain) shows the mass (*) located along the left anterior aspect of the anal canal. |
PMC1821025_F3_10040.jpg | What key item or scene is captured in this photo? | CT scan shows the mass (*) along the left anterior aspect of the anal canal. |
PMC1821026_F1_10041.jpg | Describe the main subject of this image. | CT scan of the abdomen with contrast. A heterogeneously enhancing, solid mass can be identified at the junction of the head and body of the pancreas (arrow). |
PMC1821329_F1_10042.jpg | What is the principal component of this image? | CT scan showing bilateral adrenal enlargement consistent with lung cancer metastases (asterisk). |
PMC1821330_F1_10044.jpg | What stands out most in this visual? | FKBP52 expression in human prostate. Prostate tissue was obtained from adult male surgically treated for benign prostatic hyperplasia. The tissue was fixed, paraffin embedded and sectioned before staining. Sections were immunostained with antibody specific for FKBP52 (A) and a consecutive section was immunostained with only secondary antibody for background detection (B). The strongest staining for FKBP52 is in the cytoplasm of ductal epithelial cells. (Sections photographed at 20× magnification). |
PMC1821330_F2_10045.jpg | What is the main focus of this visual representation? | FKBP52 expression in human pre-pubertal genital skin. Foreskin samples from hypospadia patients and control individuals were obtained from surgery. The tissues were fixed, paraffinembedded and sectioned before staining protocols. The upper panel shows FKBP52 staining in mild hypospadia patient (A), severe hypospadia patient (C) and healthy control (E). The background controls for these samples using only the secondary antibody are seen in (B, D and F). The FKBP52 expression is predominantly cytoplasmic, localized in the epidermal region of the foreskin. Similar pattern and intensity are observed in healthy individuals and in hypospadia patients. (Sections photographed at 20× magnification). |
PMC1821330_F2_10048.jpg | What can you see in this picture? | FKBP52 expression in human pre-pubertal genital skin. Foreskin samples from hypospadia patients and control individuals were obtained from surgery. The tissues were fixed, paraffinembedded and sectioned before staining protocols. The upper panel shows FKBP52 staining in mild hypospadia patient (A), severe hypospadia patient (C) and healthy control (E). The background controls for these samples using only the secondary antibody are seen in (B, D and F). The FKBP52 expression is predominantly cytoplasmic, localized in the epidermal region of the foreskin. Similar pattern and intensity are observed in healthy individuals and in hypospadia patients. (Sections photographed at 20× magnification). |
PMC1821330_F2_10050.jpg | What is being portrayed in this visual content? | FKBP52 expression in human pre-pubertal genital skin. Foreskin samples from hypospadia patients and control individuals were obtained from surgery. The tissues were fixed, paraffinembedded and sectioned before staining protocols. The upper panel shows FKBP52 staining in mild hypospadia patient (A), severe hypospadia patient (C) and healthy control (E). The background controls for these samples using only the secondary antibody are seen in (B, D and F). The FKBP52 expression is predominantly cytoplasmic, localized in the epidermal region of the foreskin. Similar pattern and intensity are observed in healthy individuals and in hypospadia patients. (Sections photographed at 20× magnification). |
PMC1821330_F2_10047.jpg | What is shown in this image? | FKBP52 expression in human pre-pubertal genital skin. Foreskin samples from hypospadia patients and control individuals were obtained from surgery. The tissues were fixed, paraffinembedded and sectioned before staining protocols. The upper panel shows FKBP52 staining in mild hypospadia patient (A), severe hypospadia patient (C) and healthy control (E). The background controls for these samples using only the secondary antibody are seen in (B, D and F). The FKBP52 expression is predominantly cytoplasmic, localized in the epidermal region of the foreskin. Similar pattern and intensity are observed in healthy individuals and in hypospadia patients. (Sections photographed at 20× magnification). |
PMC1821330_F2_10046.jpg | What's the most prominent thing you notice in this picture? | FKBP52 expression in human pre-pubertal genital skin. Foreskin samples from hypospadia patients and control individuals were obtained from surgery. The tissues were fixed, paraffinembedded and sectioned before staining protocols. The upper panel shows FKBP52 staining in mild hypospadia patient (A), severe hypospadia patient (C) and healthy control (E). The background controls for these samples using only the secondary antibody are seen in (B, D and F). The FKBP52 expression is predominantly cytoplasmic, localized in the epidermal region of the foreskin. Similar pattern and intensity are observed in healthy individuals and in hypospadia patients. (Sections photographed at 20× magnification). |
PMC1821330_F2_10049.jpg | What is the focal point of this photograph? | FKBP52 expression in human pre-pubertal genital skin. Foreskin samples from hypospadia patients and control individuals were obtained from surgery. The tissues were fixed, paraffinembedded and sectioned before staining protocols. The upper panel shows FKBP52 staining in mild hypospadia patient (A), severe hypospadia patient (C) and healthy control (E). The background controls for these samples using only the secondary antibody are seen in (B, D and F). The FKBP52 expression is predominantly cytoplasmic, localized in the epidermal region of the foreskin. Similar pattern and intensity are observed in healthy individuals and in hypospadia patients. (Sections photographed at 20× magnification). |
PMC1828036_F1_10056.jpg | What is the main focus of this visual representation? | Confocal scanning laser microscopic analysis of human osteoblastic cells after oxandrolone treatment. (a) Confocal scanning laser microscopy depicting AR nuclear fluorescence of human osteoblastic cells not stimulated with oxandrolone, (b) confocal scanning laser microscopy depicting the increased AR nuclear fluorescence of human osteoblastic cells stimulated with oxandrolone 30 μg/mL, (c) confocal scanning laser microscopy depicting cytoplasmic fluorescence of type I collagen in human osteoblastic cells not stimulated with oxandrolone, (d) confocal scanning laser microscopy depicting increased cytoplasmic fluorescence of type I collagen in human osteoblastic cells stimulated with oxandrolone 30 μg/mL, (e) internal negative control for primary antibodies of AR and type I collagen, (f) confocal scanning laser microscopy depicting increased cytoplasmic fluorescence of type I collagen in human osteoblastic cells stimulated with oxandrolone 15 μg/mL. Compare to Figures 1c and 1d. |
PMC1828036_F1_10052.jpg | What stands out most in this visual? | Confocal scanning laser microscopic analysis of human osteoblastic cells after oxandrolone treatment. (a) Confocal scanning laser microscopy depicting AR nuclear fluorescence of human osteoblastic cells not stimulated with oxandrolone, (b) confocal scanning laser microscopy depicting the increased AR nuclear fluorescence of human osteoblastic cells stimulated with oxandrolone 30 μg/mL, (c) confocal scanning laser microscopy depicting cytoplasmic fluorescence of type I collagen in human osteoblastic cells not stimulated with oxandrolone, (d) confocal scanning laser microscopy depicting increased cytoplasmic fluorescence of type I collagen in human osteoblastic cells stimulated with oxandrolone 30 μg/mL, (e) internal negative control for primary antibodies of AR and type I collagen, (f) confocal scanning laser microscopy depicting increased cytoplasmic fluorescence of type I collagen in human osteoblastic cells stimulated with oxandrolone 15 μg/mL. Compare to Figures 1c and 1d. |
PMC1828036_F1_10054.jpg | What is being portrayed in this visual content? | Confocal scanning laser microscopic analysis of human osteoblastic cells after oxandrolone treatment. (a) Confocal scanning laser microscopy depicting AR nuclear fluorescence of human osteoblastic cells not stimulated with oxandrolone, (b) confocal scanning laser microscopy depicting the increased AR nuclear fluorescence of human osteoblastic cells stimulated with oxandrolone 30 μg/mL, (c) confocal scanning laser microscopy depicting cytoplasmic fluorescence of type I collagen in human osteoblastic cells not stimulated with oxandrolone, (d) confocal scanning laser microscopy depicting increased cytoplasmic fluorescence of type I collagen in human osteoblastic cells stimulated with oxandrolone 30 μg/mL, (e) internal negative control for primary antibodies of AR and type I collagen, (f) confocal scanning laser microscopy depicting increased cytoplasmic fluorescence of type I collagen in human osteoblastic cells stimulated with oxandrolone 15 μg/mL. Compare to Figures 1c and 1d. |
PMC1828036_F1_10053.jpg | What is the dominant medical problem in this image? | Confocal scanning laser microscopic analysis of human osteoblastic cells after oxandrolone treatment. (a) Confocal scanning laser microscopy depicting AR nuclear fluorescence of human osteoblastic cells not stimulated with oxandrolone, (b) confocal scanning laser microscopy depicting the increased AR nuclear fluorescence of human osteoblastic cells stimulated with oxandrolone 30 μg/mL, (c) confocal scanning laser microscopy depicting cytoplasmic fluorescence of type I collagen in human osteoblastic cells not stimulated with oxandrolone, (d) confocal scanning laser microscopy depicting increased cytoplasmic fluorescence of type I collagen in human osteoblastic cells stimulated with oxandrolone 30 μg/mL, (e) internal negative control for primary antibodies of AR and type I collagen, (f) confocal scanning laser microscopy depicting increased cytoplasmic fluorescence of type I collagen in human osteoblastic cells stimulated with oxandrolone 15 μg/mL. Compare to Figures 1c and 1d. |
PMC1828036_F1_10055.jpg | What key item or scene is captured in this photo? | Confocal scanning laser microscopic analysis of human osteoblastic cells after oxandrolone treatment. (a) Confocal scanning laser microscopy depicting AR nuclear fluorescence of human osteoblastic cells not stimulated with oxandrolone, (b) confocal scanning laser microscopy depicting the increased AR nuclear fluorescence of human osteoblastic cells stimulated with oxandrolone 30 μg/mL, (c) confocal scanning laser microscopy depicting cytoplasmic fluorescence of type I collagen in human osteoblastic cells not stimulated with oxandrolone, (d) confocal scanning laser microscopy depicting increased cytoplasmic fluorescence of type I collagen in human osteoblastic cells stimulated with oxandrolone 30 μg/mL, (e) internal negative control for primary antibodies of AR and type I collagen, (f) confocal scanning laser microscopy depicting increased cytoplasmic fluorescence of type I collagen in human osteoblastic cells stimulated with oxandrolone 15 μg/mL. Compare to Figures 1c and 1d. |
PMC1828067_F5_10064.jpg | What is the central feature of this picture? | Immunostaining analysis of the effect of BP on the surface interaction of CD44 and MMP-9 in PC3 cell lines. Confocal microscopy analysis of distribution of CD44 (red) and MMP-9 (green) in PC3 cell lines treated with (+, A' to C') or without (-, A-C) pamidronate is shown. Yellow color indicates colocalization of proteins on the cell surface. The results represent one of three experiments performed. Scale Bar-50 μm. |
PMC1828067_F5_10063.jpg | What key item or scene is captured in this photo? | Immunostaining analysis of the effect of BP on the surface interaction of CD44 and MMP-9 in PC3 cell lines. Confocal microscopy analysis of distribution of CD44 (red) and MMP-9 (green) in PC3 cell lines treated with (+, A' to C') or without (-, A-C) pamidronate is shown. Yellow color indicates colocalization of proteins on the cell surface. The results represent one of three experiments performed. Scale Bar-50 μm. |
PMC1828067_F5_10067.jpg | What key item or scene is captured in this photo? | Immunostaining analysis of the effect of BP on the surface interaction of CD44 and MMP-9 in PC3 cell lines. Confocal microscopy analysis of distribution of CD44 (red) and MMP-9 (green) in PC3 cell lines treated with (+, A' to C') or without (-, A-C) pamidronate is shown. Yellow color indicates colocalization of proteins on the cell surface. The results represent one of three experiments performed. Scale Bar-50 μm. |
PMC1828067_F5_10066.jpg | What is being portrayed in this visual content? | Immunostaining analysis of the effect of BP on the surface interaction of CD44 and MMP-9 in PC3 cell lines. Confocal microscopy analysis of distribution of CD44 (red) and MMP-9 (green) in PC3 cell lines treated with (+, A' to C') or without (-, A-C) pamidronate is shown. Yellow color indicates colocalization of proteins on the cell surface. The results represent one of three experiments performed. Scale Bar-50 μm. |
PMC1828067_F5_10065.jpg | What is the dominant medical problem in this image? | Immunostaining analysis of the effect of BP on the surface interaction of CD44 and MMP-9 in PC3 cell lines. Confocal microscopy analysis of distribution of CD44 (red) and MMP-9 (green) in PC3 cell lines treated with (+, A' to C') or without (-, A-C) pamidronate is shown. Yellow color indicates colocalization of proteins on the cell surface. The results represent one of three experiments performed. Scale Bar-50 μm. |
PMC1828067_F6_10058.jpg | What is the focal point of this photograph? | Analysis of the effects of OPN over expression on cell morphology and RANKL expression in PC3 cell lines. A. Indicated PC3 cell lines were photographed using a phase contrast microscope. An increase in multinucleated giant cells was observed in PC3/OPN cells (magnification × 200). B. Immunoblotting analysis of RANKL expression in PC3 cell lines Immunoblotting analysis in protein lysates made from the indicated cell lines was performed with an antibody to RANKL. PC3/OPN cells express greater level of RANKL that PC3 cells. Results shown are a representation of three independent experiments. Bottom panel shows normalization with GAPDH. |
PMC1828067_F6_10060.jpg | What stands out most in this visual? | Analysis of the effects of OPN over expression on cell morphology and RANKL expression in PC3 cell lines. A. Indicated PC3 cell lines were photographed using a phase contrast microscope. An increase in multinucleated giant cells was observed in PC3/OPN cells (magnification × 200). B. Immunoblotting analysis of RANKL expression in PC3 cell lines Immunoblotting analysis in protein lysates made from the indicated cell lines was performed with an antibody to RANKL. PC3/OPN cells express greater level of RANKL that PC3 cells. Results shown are a representation of three independent experiments. Bottom panel shows normalization with GAPDH. |
PMC1828067_F6_10057.jpg | What object or scene is depicted here? | Analysis of the effects of OPN over expression on cell morphology and RANKL expression in PC3 cell lines. A. Indicated PC3 cell lines were photographed using a phase contrast microscope. An increase in multinucleated giant cells was observed in PC3/OPN cells (magnification × 200). B. Immunoblotting analysis of RANKL expression in PC3 cell lines Immunoblotting analysis in protein lysates made from the indicated cell lines was performed with an antibody to RANKL. PC3/OPN cells express greater level of RANKL that PC3 cells. Results shown are a representation of three independent experiments. Bottom panel shows normalization with GAPDH. |
PMC1828067_F6_10059.jpg | What is the main focus of this visual representation? | Analysis of the effects of OPN over expression on cell morphology and RANKL expression in PC3 cell lines. A. Indicated PC3 cell lines were photographed using a phase contrast microscope. An increase in multinucleated giant cells was observed in PC3/OPN cells (magnification × 200). B. Immunoblotting analysis of RANKL expression in PC3 cell lines Immunoblotting analysis in protein lysates made from the indicated cell lines was performed with an antibody to RANKL. PC3/OPN cells express greater level of RANKL that PC3 cells. Results shown are a representation of three independent experiments. Bottom panel shows normalization with GAPDH. |
PMC1828150_F1_10069.jpg | What can you see in this picture? | Sagittal reconstruction from a CT scan upon patient arrival shows mild prominence of the prevertebral soft tissues, without clinically significant hematoma or encroachment on the airway (large white arrow). |
PMC1828150_F5_10071.jpg | Describe the main subject of this image. | After surgical decompression, hematoma size is demonstrably reduced (arrow) in this sagittal MRI. |
PMC1828611_fig4_10078.jpg | What is the main focus of this visual representation? | Tumour-Suppressor Function of dRASSF(A–C, E, and F) Scanning Electron Micrographs of Drosophila heads from control animals (A), animals bearing hpo42–47 clones (B), hpo42–48 clones (C), hpo42–47 clones in a dRASSF loss-of-function background (E), or hpo42–48 clones in a dRASSF loss-of-function background (F). The overgrowth phenotype elicited by the loss of hpo is enhanced by the removal of dRASSF. See Supplemental Experimental Procedures for genotypes.(D) Schematic representation of Hpo protein showing the different mutations used. The hpo42–47 allele causes a deletion of six amino acids in the kinase domain, and this deletion probably inhibits Hpo-ATP binding. The hpo42–48 allele is a deletion of 20 bp and gives rise to a premature stop codon. hpoKC203 changes G to A at the 5′ splicing site and the translation run into a stop codon in the intron.(G–H″) dRASSF rescues Ras1 loss of function. (G–G″) Ras1c40b clones (marked by a lack of GFP) are small. (H–H″) Rasc40b dRASSFX36 clones (marked by a lack of GFP) are larger than Rasc40b clones. dRASSF staining is in red (G′ and H′). |
PMC1828611_fig4_10075.jpg | What key item or scene is captured in this photo? | Tumour-Suppressor Function of dRASSF(A–C, E, and F) Scanning Electron Micrographs of Drosophila heads from control animals (A), animals bearing hpo42–47 clones (B), hpo42–48 clones (C), hpo42–47 clones in a dRASSF loss-of-function background (E), or hpo42–48 clones in a dRASSF loss-of-function background (F). The overgrowth phenotype elicited by the loss of hpo is enhanced by the removal of dRASSF. See Supplemental Experimental Procedures for genotypes.(D) Schematic representation of Hpo protein showing the different mutations used. The hpo42–47 allele causes a deletion of six amino acids in the kinase domain, and this deletion probably inhibits Hpo-ATP binding. The hpo42–48 allele is a deletion of 20 bp and gives rise to a premature stop codon. hpoKC203 changes G to A at the 5′ splicing site and the translation run into a stop codon in the intron.(G–H″) dRASSF rescues Ras1 loss of function. (G–G″) Ras1c40b clones (marked by a lack of GFP) are small. (H–H″) Rasc40b dRASSFX36 clones (marked by a lack of GFP) are larger than Rasc40b clones. dRASSF staining is in red (G′ and H′). |
PMC1828611_fig4_10080.jpg | What is the principal component of this image? | Tumour-Suppressor Function of dRASSF(A–C, E, and F) Scanning Electron Micrographs of Drosophila heads from control animals (A), animals bearing hpo42–47 clones (B), hpo42–48 clones (C), hpo42–47 clones in a dRASSF loss-of-function background (E), or hpo42–48 clones in a dRASSF loss-of-function background (F). The overgrowth phenotype elicited by the loss of hpo is enhanced by the removal of dRASSF. See Supplemental Experimental Procedures for genotypes.(D) Schematic representation of Hpo protein showing the different mutations used. The hpo42–47 allele causes a deletion of six amino acids in the kinase domain, and this deletion probably inhibits Hpo-ATP binding. The hpo42–48 allele is a deletion of 20 bp and gives rise to a premature stop codon. hpoKC203 changes G to A at the 5′ splicing site and the translation run into a stop codon in the intron.(G–H″) dRASSF rescues Ras1 loss of function. (G–G″) Ras1c40b clones (marked by a lack of GFP) are small. (H–H″) Rasc40b dRASSFX36 clones (marked by a lack of GFP) are larger than Rasc40b clones. dRASSF staining is in red (G′ and H′). |
PMC1828611_fig4_10077.jpg | What does this image primarily show? | Tumour-Suppressor Function of dRASSF(A–C, E, and F) Scanning Electron Micrographs of Drosophila heads from control animals (A), animals bearing hpo42–47 clones (B), hpo42–48 clones (C), hpo42–47 clones in a dRASSF loss-of-function background (E), or hpo42–48 clones in a dRASSF loss-of-function background (F). The overgrowth phenotype elicited by the loss of hpo is enhanced by the removal of dRASSF. See Supplemental Experimental Procedures for genotypes.(D) Schematic representation of Hpo protein showing the different mutations used. The hpo42–47 allele causes a deletion of six amino acids in the kinase domain, and this deletion probably inhibits Hpo-ATP binding. The hpo42–48 allele is a deletion of 20 bp and gives rise to a premature stop codon. hpoKC203 changes G to A at the 5′ splicing site and the translation run into a stop codon in the intron.(G–H″) dRASSF rescues Ras1 loss of function. (G–G″) Ras1c40b clones (marked by a lack of GFP) are small. (H–H″) Rasc40b dRASSFX36 clones (marked by a lack of GFP) are larger than Rasc40b clones. dRASSF staining is in red (G′ and H′). |
PMC1828611_fig4_10081.jpg | What object or scene is depicted here? | Tumour-Suppressor Function of dRASSF(A–C, E, and F) Scanning Electron Micrographs of Drosophila heads from control animals (A), animals bearing hpo42–47 clones (B), hpo42–48 clones (C), hpo42–47 clones in a dRASSF loss-of-function background (E), or hpo42–48 clones in a dRASSF loss-of-function background (F). The overgrowth phenotype elicited by the loss of hpo is enhanced by the removal of dRASSF. See Supplemental Experimental Procedures for genotypes.(D) Schematic representation of Hpo protein showing the different mutations used. The hpo42–47 allele causes a deletion of six amino acids in the kinase domain, and this deletion probably inhibits Hpo-ATP binding. The hpo42–48 allele is a deletion of 20 bp and gives rise to a premature stop codon. hpoKC203 changes G to A at the 5′ splicing site and the translation run into a stop codon in the intron.(G–H″) dRASSF rescues Ras1 loss of function. (G–G″) Ras1c40b clones (marked by a lack of GFP) are small. (H–H″) Rasc40b dRASSFX36 clones (marked by a lack of GFP) are larger than Rasc40b clones. dRASSF staining is in red (G′ and H′). |
PMC1828611_fig4_10083.jpg | What object or scene is depicted here? | Tumour-Suppressor Function of dRASSF(A–C, E, and F) Scanning Electron Micrographs of Drosophila heads from control animals (A), animals bearing hpo42–47 clones (B), hpo42–48 clones (C), hpo42–47 clones in a dRASSF loss-of-function background (E), or hpo42–48 clones in a dRASSF loss-of-function background (F). The overgrowth phenotype elicited by the loss of hpo is enhanced by the removal of dRASSF. See Supplemental Experimental Procedures for genotypes.(D) Schematic representation of Hpo protein showing the different mutations used. The hpo42–47 allele causes a deletion of six amino acids in the kinase domain, and this deletion probably inhibits Hpo-ATP binding. The hpo42–48 allele is a deletion of 20 bp and gives rise to a premature stop codon. hpoKC203 changes G to A at the 5′ splicing site and the translation run into a stop codon in the intron.(G–H″) dRASSF rescues Ras1 loss of function. (G–G″) Ras1c40b clones (marked by a lack of GFP) are small. (H–H″) Rasc40b dRASSFX36 clones (marked by a lack of GFP) are larger than Rasc40b clones. dRASSF staining is in red (G′ and H′). |
PMC1828611_fig4_10076.jpg | What is the principal component of this image? | Tumour-Suppressor Function of dRASSF(A–C, E, and F) Scanning Electron Micrographs of Drosophila heads from control animals (A), animals bearing hpo42–47 clones (B), hpo42–48 clones (C), hpo42–47 clones in a dRASSF loss-of-function background (E), or hpo42–48 clones in a dRASSF loss-of-function background (F). The overgrowth phenotype elicited by the loss of hpo is enhanced by the removal of dRASSF. See Supplemental Experimental Procedures for genotypes.(D) Schematic representation of Hpo protein showing the different mutations used. The hpo42–47 allele causes a deletion of six amino acids in the kinase domain, and this deletion probably inhibits Hpo-ATP binding. The hpo42–48 allele is a deletion of 20 bp and gives rise to a premature stop codon. hpoKC203 changes G to A at the 5′ splicing site and the translation run into a stop codon in the intron.(G–H″) dRASSF rescues Ras1 loss of function. (G–G″) Ras1c40b clones (marked by a lack of GFP) are small. (H–H″) Rasc40b dRASSFX36 clones (marked by a lack of GFP) are larger than Rasc40b clones. dRASSF staining is in red (G′ and H′). |
PMC1828611_fig4_10079.jpg | What does this image primarily show? | Tumour-Suppressor Function of dRASSF(A–C, E, and F) Scanning Electron Micrographs of Drosophila heads from control animals (A), animals bearing hpo42–47 clones (B), hpo42–48 clones (C), hpo42–47 clones in a dRASSF loss-of-function background (E), or hpo42–48 clones in a dRASSF loss-of-function background (F). The overgrowth phenotype elicited by the loss of hpo is enhanced by the removal of dRASSF. See Supplemental Experimental Procedures for genotypes.(D) Schematic representation of Hpo protein showing the different mutations used. The hpo42–47 allele causes a deletion of six amino acids in the kinase domain, and this deletion probably inhibits Hpo-ATP binding. The hpo42–48 allele is a deletion of 20 bp and gives rise to a premature stop codon. hpoKC203 changes G to A at the 5′ splicing site and the translation run into a stop codon in the intron.(G–H″) dRASSF rescues Ras1 loss of function. (G–G″) Ras1c40b clones (marked by a lack of GFP) are small. (H–H″) Rasc40b dRASSFX36 clones (marked by a lack of GFP) are larger than Rasc40b clones. dRASSF staining is in red (G′ and H′). |
PMC1828611_fig4_10073.jpg | Can you identify the primary element in this image? | Tumour-Suppressor Function of dRASSF(A–C, E, and F) Scanning Electron Micrographs of Drosophila heads from control animals (A), animals bearing hpo42–47 clones (B), hpo42–48 clones (C), hpo42–47 clones in a dRASSF loss-of-function background (E), or hpo42–48 clones in a dRASSF loss-of-function background (F). The overgrowth phenotype elicited by the loss of hpo is enhanced by the removal of dRASSF. See Supplemental Experimental Procedures for genotypes.(D) Schematic representation of Hpo protein showing the different mutations used. The hpo42–47 allele causes a deletion of six amino acids in the kinase domain, and this deletion probably inhibits Hpo-ATP binding. The hpo42–48 allele is a deletion of 20 bp and gives rise to a premature stop codon. hpoKC203 changes G to A at the 5′ splicing site and the translation run into a stop codon in the intron.(G–H″) dRASSF rescues Ras1 loss of function. (G–G″) Ras1c40b clones (marked by a lack of GFP) are small. (H–H″) Rasc40b dRASSFX36 clones (marked by a lack of GFP) are larger than Rasc40b clones. dRASSF staining is in red (G′ and H′). |
PMC1828611_fig4_10072.jpg | What is being portrayed in this visual content? | Tumour-Suppressor Function of dRASSF(A–C, E, and F) Scanning Electron Micrographs of Drosophila heads from control animals (A), animals bearing hpo42–47 clones (B), hpo42–48 clones (C), hpo42–47 clones in a dRASSF loss-of-function background (E), or hpo42–48 clones in a dRASSF loss-of-function background (F). The overgrowth phenotype elicited by the loss of hpo is enhanced by the removal of dRASSF. See Supplemental Experimental Procedures for genotypes.(D) Schematic representation of Hpo protein showing the different mutations used. The hpo42–47 allele causes a deletion of six amino acids in the kinase domain, and this deletion probably inhibits Hpo-ATP binding. The hpo42–48 allele is a deletion of 20 bp and gives rise to a premature stop codon. hpoKC203 changes G to A at the 5′ splicing site and the translation run into a stop codon in the intron.(G–H″) dRASSF rescues Ras1 loss of function. (G–G″) Ras1c40b clones (marked by a lack of GFP) are small. (H–H″) Rasc40b dRASSFX36 clones (marked by a lack of GFP) are larger than Rasc40b clones. dRASSF staining is in red (G′ and H′). |
PMC1828621_pone-0000328-g004_10092.jpg | What key item or scene is captured in this photo? | Mimivirus infectious cycle.
Mimivirus infected A. polyphaga were stained with DAPI at different times points p.i. and representative pictures are shown. A, B : non infected amoebae; C, D: 0 h p.i. Mimivirus particles inside the cytoplasm and near the cell nucleus could be seen; E, F: 4 h p.i. The heterogeneous structure of the VF appeared near the cell nucleus. No viral particles were detectable in the cytoplasm; G, H : 8 h p.i. The intensively stained VF appeared as an homogeneous structure and neosynthesized viral particles accumulated around the VF; I, J : 18 h p.i. The VF was still intensely stained with quite a different structure, whereas the cell cytoplasm was completely filled with new viral particles. Fluorescence (left column) and DIC (right column) images of the same slide field were taken with a 63×/1.4 oil lens. Fluorescence pictures were taken with an exposure time of 1 sec (A) and 64 msec with gain 2 (C, E, G, I). Inset pictures corresponded to the same as E, G and I taken at a different exposure time 64 msec (E, G) and 16 msec respectively (I). |
PMC1828621_pone-0000328-g004_10087.jpg | What object or scene is depicted here? | Mimivirus infectious cycle.
Mimivirus infected A. polyphaga were stained with DAPI at different times points p.i. and representative pictures are shown. A, B : non infected amoebae; C, D: 0 h p.i. Mimivirus particles inside the cytoplasm and near the cell nucleus could be seen; E, F: 4 h p.i. The heterogeneous structure of the VF appeared near the cell nucleus. No viral particles were detectable in the cytoplasm; G, H : 8 h p.i. The intensively stained VF appeared as an homogeneous structure and neosynthesized viral particles accumulated around the VF; I, J : 18 h p.i. The VF was still intensely stained with quite a different structure, whereas the cell cytoplasm was completely filled with new viral particles. Fluorescence (left column) and DIC (right column) images of the same slide field were taken with a 63×/1.4 oil lens. Fluorescence pictures were taken with an exposure time of 1 sec (A) and 64 msec with gain 2 (C, E, G, I). Inset pictures corresponded to the same as E, G and I taken at a different exposure time 64 msec (E, G) and 16 msec respectively (I). |
PMC1828621_pone-0000328-g004_10091.jpg | What's the most prominent thing you notice in this picture? | Mimivirus infectious cycle.
Mimivirus infected A. polyphaga were stained with DAPI at different times points p.i. and representative pictures are shown. A, B : non infected amoebae; C, D: 0 h p.i. Mimivirus particles inside the cytoplasm and near the cell nucleus could be seen; E, F: 4 h p.i. The heterogeneous structure of the VF appeared near the cell nucleus. No viral particles were detectable in the cytoplasm; G, H : 8 h p.i. The intensively stained VF appeared as an homogeneous structure and neosynthesized viral particles accumulated around the VF; I, J : 18 h p.i. The VF was still intensely stained with quite a different structure, whereas the cell cytoplasm was completely filled with new viral particles. Fluorescence (left column) and DIC (right column) images of the same slide field were taken with a 63×/1.4 oil lens. Fluorescence pictures were taken with an exposure time of 1 sec (A) and 64 msec with gain 2 (C, E, G, I). Inset pictures corresponded to the same as E, G and I taken at a different exposure time 64 msec (E, G) and 16 msec respectively (I). |
PMC1828621_pone-0000328-g004_10093.jpg | What key item or scene is captured in this photo? | Mimivirus infectious cycle.
Mimivirus infected A. polyphaga were stained with DAPI at different times points p.i. and representative pictures are shown. A, B : non infected amoebae; C, D: 0 h p.i. Mimivirus particles inside the cytoplasm and near the cell nucleus could be seen; E, F: 4 h p.i. The heterogeneous structure of the VF appeared near the cell nucleus. No viral particles were detectable in the cytoplasm; G, H : 8 h p.i. The intensively stained VF appeared as an homogeneous structure and neosynthesized viral particles accumulated around the VF; I, J : 18 h p.i. The VF was still intensely stained with quite a different structure, whereas the cell cytoplasm was completely filled with new viral particles. Fluorescence (left column) and DIC (right column) images of the same slide field were taken with a 63×/1.4 oil lens. Fluorescence pictures were taken with an exposure time of 1 sec (A) and 64 msec with gain 2 (C, E, G, I). Inset pictures corresponded to the same as E, G and I taken at a different exposure time 64 msec (E, G) and 16 msec respectively (I). |
PMC1828621_pone-0000328-g004_10084.jpg | What stands out most in this visual? | Mimivirus infectious cycle.
Mimivirus infected A. polyphaga were stained with DAPI at different times points p.i. and representative pictures are shown. A, B : non infected amoebae; C, D: 0 h p.i. Mimivirus particles inside the cytoplasm and near the cell nucleus could be seen; E, F: 4 h p.i. The heterogeneous structure of the VF appeared near the cell nucleus. No viral particles were detectable in the cytoplasm; G, H : 8 h p.i. The intensively stained VF appeared as an homogeneous structure and neosynthesized viral particles accumulated around the VF; I, J : 18 h p.i. The VF was still intensely stained with quite a different structure, whereas the cell cytoplasm was completely filled with new viral particles. Fluorescence (left column) and DIC (right column) images of the same slide field were taken with a 63×/1.4 oil lens. Fluorescence pictures were taken with an exposure time of 1 sec (A) and 64 msec with gain 2 (C, E, G, I). Inset pictures corresponded to the same as E, G and I taken at a different exposure time 64 msec (E, G) and 16 msec respectively (I). |
PMC1828696_ppat-0030032-g003_10096.jpg | What is the core subject represented in this visual? | Export of Sp1 from Lysosomes to the Cell Membrane in MHCII-GFP–Positive Tubular Structures in Live DCs(A) iDCs transfected with MHCII-GFP were treated for 30 min with Sp1-Alexa 594 (500 μg/ml) and then analyzed by live cell imaging using confocal microscopy. In merged fluorescence images, Sp1 co-localizes extensively with MHCII in lysosomes. No MHCII is found on the cell surface.(B) iDCs transfected with MHCII-GFP were pre-incubated for 30 min with Sp1-Alexa 594 (500 μg/ml) and then treated with LPS for 4 h. Merged fluorescence live cell images of confocal microscopy demonstrate that Sp1/MHCII-positive tubular structures emanate from lysosomes in a perinuclear region and transit to the cell membrane. A single translocation Sp1/MHCII-positive tubule is labeled with white arrows (see Video S1).(C) iDCs previously transfected with MHCII-GFP and pre-incubated for 30 min with Sp1-Alexa 594 (500 μg/ml) were stimulated for 4 h with LPS. Combined TIR-FM/EPI microscopy reveals exit of Sp1-containing tubules from lysosomes (red) and their association with the plasma membrane (bright yellow). Tubules are labeled with white arrows (see Video S2). Scale bar, 10 μm.(D) After treatment with Sp1-biotin for 30 min, iDCs were incubated for various time intervals with LPS, and their cell surface was stained with FITC-conjugated streptavidin. Presentation of Sp1-biotin on the DC surface was quantified by flow cytometry. |
PMC1828696_ppat-0030032-g003_10095.jpg | What is the central feature of this picture? | Export of Sp1 from Lysosomes to the Cell Membrane in MHCII-GFP–Positive Tubular Structures in Live DCs(A) iDCs transfected with MHCII-GFP were treated for 30 min with Sp1-Alexa 594 (500 μg/ml) and then analyzed by live cell imaging using confocal microscopy. In merged fluorescence images, Sp1 co-localizes extensively with MHCII in lysosomes. No MHCII is found on the cell surface.(B) iDCs transfected with MHCII-GFP were pre-incubated for 30 min with Sp1-Alexa 594 (500 μg/ml) and then treated with LPS for 4 h. Merged fluorescence live cell images of confocal microscopy demonstrate that Sp1/MHCII-positive tubular structures emanate from lysosomes in a perinuclear region and transit to the cell membrane. A single translocation Sp1/MHCII-positive tubule is labeled with white arrows (see Video S1).(C) iDCs previously transfected with MHCII-GFP and pre-incubated for 30 min with Sp1-Alexa 594 (500 μg/ml) were stimulated for 4 h with LPS. Combined TIR-FM/EPI microscopy reveals exit of Sp1-containing tubules from lysosomes (red) and their association with the plasma membrane (bright yellow). Tubules are labeled with white arrows (see Video S2). Scale bar, 10 μm.(D) After treatment with Sp1-biotin for 30 min, iDCs were incubated for various time intervals with LPS, and their cell surface was stained with FITC-conjugated streptavidin. Presentation of Sp1-biotin on the DC surface was quantified by flow cytometry. |
PMC1828696_ppat-0030032-g003_10094.jpg | What can you see in this picture? | Export of Sp1 from Lysosomes to the Cell Membrane in MHCII-GFP–Positive Tubular Structures in Live DCs(A) iDCs transfected with MHCII-GFP were treated for 30 min with Sp1-Alexa 594 (500 μg/ml) and then analyzed by live cell imaging using confocal microscopy. In merged fluorescence images, Sp1 co-localizes extensively with MHCII in lysosomes. No MHCII is found on the cell surface.(B) iDCs transfected with MHCII-GFP were pre-incubated for 30 min with Sp1-Alexa 594 (500 μg/ml) and then treated with LPS for 4 h. Merged fluorescence live cell images of confocal microscopy demonstrate that Sp1/MHCII-positive tubular structures emanate from lysosomes in a perinuclear region and transit to the cell membrane. A single translocation Sp1/MHCII-positive tubule is labeled with white arrows (see Video S1).(C) iDCs previously transfected with MHCII-GFP and pre-incubated for 30 min with Sp1-Alexa 594 (500 μg/ml) were stimulated for 4 h with LPS. Combined TIR-FM/EPI microscopy reveals exit of Sp1-containing tubules from lysosomes (red) and their association with the plasma membrane (bright yellow). Tubules are labeled with white arrows (see Video S2). Scale bar, 10 μm.(D) After treatment with Sp1-biotin for 30 min, iDCs were incubated for various time intervals with LPS, and their cell surface was stained with FITC-conjugated streptavidin. Presentation of Sp1-biotin on the DC surface was quantified by flow cytometry. |
PMC1828698_ppat-0030035-g006_10101.jpg | What is the principal component of this image? | Dynorphin Binds to P. aeruginosa In Vitro, and Enters the Bacterial Cell Cytoplasm(A–C) Binding of dynorphin to P. aeruginosa; (A) negative control demonstrating no dynorphin staining when cells were not incubated with dynorphin; (B) negative control demonstrating no dynorphin staining when cell were incubated with dynorphin but primary anti-dynorphin antibodies were omitted from staining procedure; and (C) positive staining (brown color) of P. aeruginosa incubated with dynorphin followed by whole procedure of immunostaining.(D) Immunoelectron microscopy of P. aeruginosa PAO1 cells incubated with dynorphin, 100 μM. Black arrows show 10-nm gold spots indicating the presence of dynorphin. |
PMC1828698_ppat-0030035-g006_10098.jpg | What object or scene is depicted here? | Dynorphin Binds to P. aeruginosa In Vitro, and Enters the Bacterial Cell Cytoplasm(A–C) Binding of dynorphin to P. aeruginosa; (A) negative control demonstrating no dynorphin staining when cells were not incubated with dynorphin; (B) negative control demonstrating no dynorphin staining when cell were incubated with dynorphin but primary anti-dynorphin antibodies were omitted from staining procedure; and (C) positive staining (brown color) of P. aeruginosa incubated with dynorphin followed by whole procedure of immunostaining.(D) Immunoelectron microscopy of P. aeruginosa PAO1 cells incubated with dynorphin, 100 μM. Black arrows show 10-nm gold spots indicating the presence of dynorphin. |
PMC1828733_F2_10103.jpg | What's the most prominent thing you notice in this picture? | CT scan of the abdomen/pelvis at 4 months post op showing a normal-looking bladder with right double J stent in place. |
PMC1828734_F1_10105.jpg | What can you see in this picture? | Immunohistochemical staining of tissue microarray cores with MUC1 and MUC3 antibodies. A & B show cores from tumour demonstrating positive (A) and negative (B) MUC1 staining. C & D show cores of tumour demonstrating strong (C) and weak MUC 3 staining. All are at × 100 magnification. |
PMC1828734_F1_10104.jpg | What is being portrayed in this visual content? | Immunohistochemical staining of tissue microarray cores with MUC1 and MUC3 antibodies. A & B show cores from tumour demonstrating positive (A) and negative (B) MUC1 staining. C & D show cores of tumour demonstrating strong (C) and weak MUC 3 staining. All are at × 100 magnification. |
PMC1828734_F1_10106.jpg | What is the dominant medical problem in this image? | Immunohistochemical staining of tissue microarray cores with MUC1 and MUC3 antibodies. A & B show cores from tumour demonstrating positive (A) and negative (B) MUC1 staining. C & D show cores of tumour demonstrating strong (C) and weak MUC 3 staining. All are at × 100 magnification. |
PMC1828734_F1_10107.jpg | What stands out most in this visual? | Immunohistochemical staining of tissue microarray cores with MUC1 and MUC3 antibodies. A & B show cores from tumour demonstrating positive (A) and negative (B) MUC1 staining. C & D show cores of tumour demonstrating strong (C) and weak MUC 3 staining. All are at × 100 magnification. |
PMC1829163_F1_10110.jpg | Describe the main subject of this image. | CD10 and CD13 prostate cancer cell types. Positive staining is indicated by the brown chromogen deposit. Non-cancer glands are generally positive for both CD10 and CD13. In the left and middle cases the tumors consist of small crowded glands in the left half of the field. Most of the cancer glands are CD10- and CD13+, although a few isolated CD10+ cancer glands can be seen. In the right case, a subpopulation of CD13+ cancer cells are present in the larger population of CD10-/CD13- cancer cells. This tumor shows no glandular morphology. Magnification is 20×. |
PMC1829163_F1_10108.jpg | What is the central feature of this picture? | CD10 and CD13 prostate cancer cell types. Positive staining is indicated by the brown chromogen deposit. Non-cancer glands are generally positive for both CD10 and CD13. In the left and middle cases the tumors consist of small crowded glands in the left half of the field. Most of the cancer glands are CD10- and CD13+, although a few isolated CD10+ cancer glands can be seen. In the right case, a subpopulation of CD13+ cancer cells are present in the larger population of CD10-/CD13- cancer cells. This tumor shows no glandular morphology. Magnification is 20×. |
PMC1829163_F1_10109.jpg | What stands out most in this visual? | CD10 and CD13 prostate cancer cell types. Positive staining is indicated by the brown chromogen deposit. Non-cancer glands are generally positive for both CD10 and CD13. In the left and middle cases the tumors consist of small crowded glands in the left half of the field. Most of the cancer glands are CD10- and CD13+, although a few isolated CD10+ cancer glands can be seen. In the right case, a subpopulation of CD13+ cancer cells are present in the larger population of CD10-/CD13- cancer cells. This tumor shows no glandular morphology. Magnification is 20×. |
PMC1829163_F7_10112.jpg | Can you identify the primary element in this image? | CD10 immunohistochemistry of prostate cancer lymph node metastasis. Positive staining is indicated by the brown chromogen deposit. Magnification is 40×. |
PMC1829406_ppat-0030028-g001_10115.jpg | What stands out most in this visual? | Visualization of Bioluminescent Bacteria Inside Live, Anesthetized Animals Shows the Induction of Otitis Media(A–B) Six- to eight-week-old female Balb/cJ mice (Jackson Laboratory, http://www.jax.org) were colonized intranasally with 1 × 105 CFU of type 19F S. pneumoniae strain ST16219F suspended in 100 μl of sterile PBS, then seven days later either (A) infected intranasally in a volume of 100 μl of sterile PBS with 100 TCID50 (doses of virus infectious for 50% of tissue culture wells) of the Mount Sinai strain of influenza virus A/Puerto Rico/8/34 (H1N1), or (B) mock-infected with sterile PBS. Mice were imaged for 60 seconds daily using an IVIS Lumina Imaging System (Xenogen, http://www.xenogen.com), and images were analyzed using Living Image software (version 2.50.1, Xenogen). (A) Pneumococcal load in the nose of a representative mouse colonized with pneumococcus remained the same after mock-infection with PBS, while (B) a representative mouse infected with influenza virus developed otitis media in the left ear.(C) Although colonization of mice on day 7 did not differ between the groups (p = 0.56), significantly more mice infected with influenza developed otitis media than did mock-infected animals (p = 0.00053). An asterisk indicates a significant difference between the groups using a 2-tailed Fisher's Exact test. |
PMC1829407_ppat-0030036-g002_10121.jpg | What's the most prominent thing you notice in this picture? | RR Staining of Uninfected MDM Reveals a Complex Plasma Membrane OrganizationMDM were fed with BSA-gold and fixed in the presence of RR.(A) A cell profile at low magnification contacting a neighboring cell. The smooth left side was previously attached to the substrate (indicated as “bottom”); the right side displaying many RR-positive protrusions is the side facing the extracellular medium (“top”). Seemingly intracellular structures also appear RR-positive. At the tight-fitting contact zones between two cells (arrows) the stain appears more electron-dense than on single lipid bilayers.(B) Higher magnification of the boxed area in (A) showing the collection of vacuolar-like invaginations stained with RR.(C) Higher magnification of the boxed area in (B) showing a RR-positive structure next to a BSA-gold-filled endosome (arrowhead).(D) Comparison of RR-positive cell surface protrusions and similar RR-positive protrusions, which appeared intracellular in this section. Arrowheads indicate gold-filled endosomes. The inset in (D) shows an enlargement of a BSA-gold-filled endosome in the boxed area.(E) Two identical looking structures with stacked protrusions; in the upper one the membranes are not RR-stained, indicating that not all vacuolar structures are accessible to the stain.(F) A collection of BSA-gold-filled endosomes (arrowheads) next to RR-stained vacuolar structures to emphasize the differences in size and morphology. The inset in (F) shows an enlargement of a BSA-gold-filled endosome in the boxed area. Nu, nucleus. Bars, 2 μm (A and B) and 500 nm (C–F). |
PMC1829407_ppat-0030036-g002_10119.jpg | What's the most prominent thing you notice in this picture? | RR Staining of Uninfected MDM Reveals a Complex Plasma Membrane OrganizationMDM were fed with BSA-gold and fixed in the presence of RR.(A) A cell profile at low magnification contacting a neighboring cell. The smooth left side was previously attached to the substrate (indicated as “bottom”); the right side displaying many RR-positive protrusions is the side facing the extracellular medium (“top”). Seemingly intracellular structures also appear RR-positive. At the tight-fitting contact zones between two cells (arrows) the stain appears more electron-dense than on single lipid bilayers.(B) Higher magnification of the boxed area in (A) showing the collection of vacuolar-like invaginations stained with RR.(C) Higher magnification of the boxed area in (B) showing a RR-positive structure next to a BSA-gold-filled endosome (arrowhead).(D) Comparison of RR-positive cell surface protrusions and similar RR-positive protrusions, which appeared intracellular in this section. Arrowheads indicate gold-filled endosomes. The inset in (D) shows an enlargement of a BSA-gold-filled endosome in the boxed area.(E) Two identical looking structures with stacked protrusions; in the upper one the membranes are not RR-stained, indicating that not all vacuolar structures are accessible to the stain.(F) A collection of BSA-gold-filled endosomes (arrowheads) next to RR-stained vacuolar structures to emphasize the differences in size and morphology. The inset in (F) shows an enlargement of a BSA-gold-filled endosome in the boxed area. Nu, nucleus. Bars, 2 μm (A and B) and 500 nm (C–F). |
PMC1829407_ppat-0030036-g002_10120.jpg | What object or scene is depicted here? | RR Staining of Uninfected MDM Reveals a Complex Plasma Membrane OrganizationMDM were fed with BSA-gold and fixed in the presence of RR.(A) A cell profile at low magnification contacting a neighboring cell. The smooth left side was previously attached to the substrate (indicated as “bottom”); the right side displaying many RR-positive protrusions is the side facing the extracellular medium (“top”). Seemingly intracellular structures also appear RR-positive. At the tight-fitting contact zones between two cells (arrows) the stain appears more electron-dense than on single lipid bilayers.(B) Higher magnification of the boxed area in (A) showing the collection of vacuolar-like invaginations stained with RR.(C) Higher magnification of the boxed area in (B) showing a RR-positive structure next to a BSA-gold-filled endosome (arrowhead).(D) Comparison of RR-positive cell surface protrusions and similar RR-positive protrusions, which appeared intracellular in this section. Arrowheads indicate gold-filled endosomes. The inset in (D) shows an enlargement of a BSA-gold-filled endosome in the boxed area.(E) Two identical looking structures with stacked protrusions; in the upper one the membranes are not RR-stained, indicating that not all vacuolar structures are accessible to the stain.(F) A collection of BSA-gold-filled endosomes (arrowheads) next to RR-stained vacuolar structures to emphasize the differences in size and morphology. The inset in (F) shows an enlargement of a BSA-gold-filled endosome in the boxed area. Nu, nucleus. Bars, 2 μm (A and B) and 500 nm (C–F). |
PMC1829407_ppat-0030036-g002_10117.jpg | What's the most prominent thing you notice in this picture? | RR Staining of Uninfected MDM Reveals a Complex Plasma Membrane OrganizationMDM were fed with BSA-gold and fixed in the presence of RR.(A) A cell profile at low magnification contacting a neighboring cell. The smooth left side was previously attached to the substrate (indicated as “bottom”); the right side displaying many RR-positive protrusions is the side facing the extracellular medium (“top”). Seemingly intracellular structures also appear RR-positive. At the tight-fitting contact zones between two cells (arrows) the stain appears more electron-dense than on single lipid bilayers.(B) Higher magnification of the boxed area in (A) showing the collection of vacuolar-like invaginations stained with RR.(C) Higher magnification of the boxed area in (B) showing a RR-positive structure next to a BSA-gold-filled endosome (arrowhead).(D) Comparison of RR-positive cell surface protrusions and similar RR-positive protrusions, which appeared intracellular in this section. Arrowheads indicate gold-filled endosomes. The inset in (D) shows an enlargement of a BSA-gold-filled endosome in the boxed area.(E) Two identical looking structures with stacked protrusions; in the upper one the membranes are not RR-stained, indicating that not all vacuolar structures are accessible to the stain.(F) A collection of BSA-gold-filled endosomes (arrowheads) next to RR-stained vacuolar structures to emphasize the differences in size and morphology. The inset in (F) shows an enlargement of a BSA-gold-filled endosome in the boxed area. Nu, nucleus. Bars, 2 μm (A and B) and 500 nm (C–F). |
PMC1829407_ppat-0030036-g002_10122.jpg | What's the most prominent thing you notice in this picture? | RR Staining of Uninfected MDM Reveals a Complex Plasma Membrane OrganizationMDM were fed with BSA-gold and fixed in the presence of RR.(A) A cell profile at low magnification contacting a neighboring cell. The smooth left side was previously attached to the substrate (indicated as “bottom”); the right side displaying many RR-positive protrusions is the side facing the extracellular medium (“top”). Seemingly intracellular structures also appear RR-positive. At the tight-fitting contact zones between two cells (arrows) the stain appears more electron-dense than on single lipid bilayers.(B) Higher magnification of the boxed area in (A) showing the collection of vacuolar-like invaginations stained with RR.(C) Higher magnification of the boxed area in (B) showing a RR-positive structure next to a BSA-gold-filled endosome (arrowhead).(D) Comparison of RR-positive cell surface protrusions and similar RR-positive protrusions, which appeared intracellular in this section. Arrowheads indicate gold-filled endosomes. The inset in (D) shows an enlargement of a BSA-gold-filled endosome in the boxed area.(E) Two identical looking structures with stacked protrusions; in the upper one the membranes are not RR-stained, indicating that not all vacuolar structures are accessible to the stain.(F) A collection of BSA-gold-filled endosomes (arrowheads) next to RR-stained vacuolar structures to emphasize the differences in size and morphology. The inset in (F) shows an enlargement of a BSA-gold-filled endosome in the boxed area. Nu, nucleus. Bars, 2 μm (A and B) and 500 nm (C–F). |
PMC1831740_pmed-0040108-g005_10128.jpg | What is shown in this image? |
OLIG1 Immunohistochemistry on a Lung Tissue Array
OLIG1 immunohistochemistry on (A and E) tumor-free lung, (B) an OLIG1 negative adenocarcinoma, and (F) an OLIG1 negative SCC; (C) a low OLIG1 expressing adenocarcinoma and (G) a low OLIG1 expressing SCC are shown; (D) a high OLIG1 expressing adenocarcinoma and (H) a high OLIG1 expressing SCC are shown. All images were acquired at 400× magnification. |
PMC1831740_pmed-0040108-g005_10132.jpg | What can you see in this picture? |
OLIG1 Immunohistochemistry on a Lung Tissue Array
OLIG1 immunohistochemistry on (A and E) tumor-free lung, (B) an OLIG1 negative adenocarcinoma, and (F) an OLIG1 negative SCC; (C) a low OLIG1 expressing adenocarcinoma and (G) a low OLIG1 expressing SCC are shown; (D) a high OLIG1 expressing adenocarcinoma and (H) a high OLIG1 expressing SCC are shown. All images were acquired at 400× magnification. |
PMC1831740_pmed-0040108-g005_10129.jpg | What object or scene is depicted here? |
OLIG1 Immunohistochemistry on a Lung Tissue Array
OLIG1 immunohistochemistry on (A and E) tumor-free lung, (B) an OLIG1 negative adenocarcinoma, and (F) an OLIG1 negative SCC; (C) a low OLIG1 expressing adenocarcinoma and (G) a low OLIG1 expressing SCC are shown; (D) a high OLIG1 expressing adenocarcinoma and (H) a high OLIG1 expressing SCC are shown. All images were acquired at 400× magnification. |
PMC1831740_pmed-0040108-g005_10127.jpg | What is being portrayed in this visual content? |
OLIG1 Immunohistochemistry on a Lung Tissue Array
OLIG1 immunohistochemistry on (A and E) tumor-free lung, (B) an OLIG1 negative adenocarcinoma, and (F) an OLIG1 negative SCC; (C) a low OLIG1 expressing adenocarcinoma and (G) a low OLIG1 expressing SCC are shown; (D) a high OLIG1 expressing adenocarcinoma and (H) a high OLIG1 expressing SCC are shown. All images were acquired at 400× magnification. |
PMC1831740_pmed-0040108-g005_10126.jpg | What is the core subject represented in this visual? |
OLIG1 Immunohistochemistry on a Lung Tissue Array
OLIG1 immunohistochemistry on (A and E) tumor-free lung, (B) an OLIG1 negative adenocarcinoma, and (F) an OLIG1 negative SCC; (C) a low OLIG1 expressing adenocarcinoma and (G) a low OLIG1 expressing SCC are shown; (D) a high OLIG1 expressing adenocarcinoma and (H) a high OLIG1 expressing SCC are shown. All images were acquired at 400× magnification. |
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