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Image Search Results
Journal: Science Advances
Article Title: Label-free quantitation of glycated hemoglobin in single red blood cells by transient absorption microscopy and phasor analysis
doi: 10.1126/sciadv.aav0561
Figure Lengend Snippet: ( A and B ) Protein structure of the glycation site of HbA1c, and normal Hb, respectively. The crystal structure of HbA1c (3B75) and Hb (1LFZ) are from Protein Data Bank. Cyan sphere, water molecule; red sphere, oxygen atom; green sphere, carbon atom; blue sphere, nitrogen atom. In (A), the polar force between glucose and heme and surrounding water is highlighted by blue dashed lines. Regions of interest (ROIs) are highlighted by red dashed circles. ( C and D ) Zoom-in view of the interaction between glucose and porphyrin ring from glycated Hb (C) and normal Hb (D).
Article Snippet: Transient absorption imaging of whole blood study was achieved by measuring the
Techniques:
Journal: Science Advances
Article Title: Label-free quantitation of glycated hemoglobin in single red blood cells by transient absorption microscopy and phasor analysis
doi: 10.1126/sciadv.aav0561
Figure Lengend Snippet: ( A and B ) Fluorescence spectra of Hb (0.025 mg/ml) (A) along with HbA1c (0.025 mg/ml) (B), respectively. Excitation wavelength, 447 nm; integration time, 1000 s; band-pass filter, 488 ± 10 nm; power on the sample, 150 μW. 20× air objective. ( C and D ) Time-resolved photoluminescence (PL) measurements of Hb (0.025 mg/ml) (C) and HbA1c (0.025 mg/ml) (D), respectively. a.u., arbitrary units. ( E and F ) Absorption spectra (normalized) of Hb (E) and HbA1c (F), respectively.
Article Snippet: Transient absorption imaging of whole blood study was achieved by measuring the
Techniques: Fluorescence
Journal: Science Advances
Article Title: Label-free quantitation of glycated hemoglobin in single red blood cells by transient absorption microscopy and phasor analysis
doi: 10.1126/sciadv.aav0561
Figure Lengend Snippet: ( A and B ) Time-resolved decay curves (normalized) of Hb (A) and HbA1c (B), respectively. int., intensity. ( C ) Merged time-resolved curves (normalized) of Hb and HbA1c. ( D and E ) Time-resolved decay curves (normalized) of oxyHb (D) and oxyHbA1c (E), respectively. ( F ) Merged time-resolved curves (normalized) of oxyHb and oxyHbA1c. ( G ) Proposed excited-state dynamic pathway of Hb when pumped at 520 nm and probed at 780 nm.
Article Snippet: Transient absorption imaging of whole blood study was achieved by measuring the
Techniques:
Journal: Science Advances
Article Title: Label-free quantitation of glycated hemoglobin in single red blood cells by transient absorption microscopy and phasor analysis
doi: 10.1126/sciadv.aav0561
Figure Lengend Snippet: ( A ) Time-resolved decay curves (normalized) of standard HbA1c solutions (human whole blood based) at different concentrations. ( B ) Zoom-in view of (A) from delay time of 1 to 4 ps. ( C ) Component s versus different ω from 0 to 2π THz for pure HbA1c and Hb. ( D ) Phasor plot of standard HbA1c solutions of different concentrations when ω = 0.8π THz. ( E ) Calibration curve of standard HbA1c solution at different concentrations (component s versus HbA1c%).
Article Snippet: Transient absorption imaging of whole blood study was achieved by measuring the
Techniques:
Journal: Science Advances
Article Title: Label-free quantitation of glycated hemoglobin in single red blood cells by transient absorption microscopy and phasor analysis
doi: 10.1126/sciadv.aav0561
Figure Lengend Snippet: ( A ) Pseudocolor transient absorption images (delay time, 0 ps) of single RBCs with ROIs are highlighted by blue dashed circles. Scale bar, 10 μm. Pump: 520 nm, 2 mW on the sample; probe: 780 nm, 10 mW on the sample. int., intensity. ( B and C ) Time-resolved decay curves (normalized) of ROIs shown in (A). ( D to F ) HbA1c fraction (in single RBCs) distribution along with the fitted glucose concentration from three diabetic whole blood samples. ( G to I ) HbA1c fraction (in single RBCs) distribution along with the derived glucose concentration from three healthy whole blood samples. Curve fitted by .
Article Snippet: Transient absorption imaging of whole blood study was achieved by measuring the
Techniques: Concentration Assay, Derivative Assay
Journal: Cells
Article Title: Type 1 Diabetes-Associated Autoantibodies, Sera and T-Cell Receptor Sequences Recognize Myelin Basic Protein: A Novel Peripheral Diabetic Neuropathy–Multiple Sclerosis Connection
doi: 10.3390/cells15151384
Figure Lengend Snippet: Selection of T1D TCR that mimic MS TCR. Note that many of the MS TCR are identified as being MBP specific. A complete listing of all the T1D–MS TCR matches found is supplied in the . The titles of the TCR (e.g., T1D DIA 11) refer to the identities of the TCR sequences provided in and are followed by the TCR sequence. The underlined codes are the UNIPROT KB identification numbers of the MS TCR sequences.
Article Snippet: Disease State Supplier Our ID Sample ID Age Sex Race HbA1c % Serum Treatment T1D Lee Biosolutions LEE 01 09E5731 A1c-50.11 39 M Caucasian 11.5 EDTA T1D Lee Biosolutions LEE 02 09E5731 A1c-50.12 36 F
Techniques: Selection, Sequencing
Journal: Cells
Article Title: Type 1 Diabetes-Associated Autoantibodies, Sera and T-Cell Receptor Sequences Recognize Myelin Basic Protein: A Novel Peripheral Diabetic Neuropathy–Multiple Sclerosis Connection
doi: 10.3390/cells15151384
Figure Lengend Snippet: Ultraviolet spectroscopy experiment evaluating the binding of type 1 diabetic T cell receptor sequences (DIA TCR) to human myelin basic protein (hMBP). Binding constants can be approximated by finding the concentration of TCR peptide at the inflection point of each curve. However, because these experiments were run in solution, while actual TCR-MBP binding would involve cell-cell interactions, the calculated affinities probably significantly underestimate the actual affinity of the TCR for MBP in vivo. The TCR labels refer to the sequences listed in and . TCR4,8,9 is a consensus sequence derived from DIA4, DIA8, and DIA9.
Article Snippet: Disease State Supplier Our ID Sample ID Age Sex Race HbA1c % Serum Treatment T1D Lee Biosolutions LEE 01 09E5731 A1c-50.11 39 M Caucasian 11.5 EDTA T1D Lee Biosolutions LEE 02 09E5731 A1c-50.12 36 F
Techniques: Spectroscopy, Binding Assay, Concentration Assay, In Vivo, Sequencing, Derivative Assay
Journal: Cells
Article Title: Type 1 Diabetes-Associated Autoantibodies, Sera and T-Cell Receptor Sequences Recognize Myelin Basic Protein: A Novel Peripheral Diabetic Neuropathy–Multiple Sclerosis Connection
doi: 10.3390/cells15151384
Figure Lengend Snippet: Results of enzyme-linked immunoadsorption assays involving sera from type 1 diabetes mellitus patients (T1D) or healthy controls binding to human myelin basic protein (hMBP). DIA 1, DIA 2, etc. refer to the sera codes (see Materials and Methods). Only some of the experimental curves are provided so that the differences in the curves can be seen clearly. In particular, most of the negative results (flat lines) were omitted because they overlay each other to such an extent that they cannot be differentiated. This omitted data and the resulting binding constants are shown in .
Article Snippet: Disease State Supplier Our ID Sample ID Age Sex Race HbA1c % Serum Treatment T1D Lee Biosolutions LEE 01 09E5731 A1c-50.11 39 M Caucasian 11.5 EDTA T1D Lee Biosolutions LEE 02 09E5731 A1c-50.12 36 F
Techniques: Binding Assay
Journal: Cellular and Molecular Life Sciences
Article Title: Low glycemic index diet restrains epileptogenesis in a gender-specific fashion
doi: 10.1007/s00018-023-04988-1
Figure Lengend Snippet: Experimental plan and parameters analyzed during the administration of the two diets. A StD and LGID were delivered ad libitum to SynIIKO pregnant females starting from mating and continuing during pregnancy and lactation. Mice were maintained with LGID also after weaning and for the entire lifespan. Starting from the day of weaning, all mice were weekly checked for two months for body weight ( B ), food intake ( C ) and water consumption ( D ). Parameters analyzed in the two experimental groups revealed that LGID mice increased food consumption, although no differences appeared in body weight and water consumption ( n = 30 KO StD; n = 32 KO LGID). Five months after birth all mice were subjected to blood analysis for the evaluation of glycemia ( E , F ) and glycated hemoglobin ( G ) levels. E For the analyses of blood glucose, mice were fasted for 24 h. Glycemia was measured immediately after the fasting period and 1 h after food administration. Glycemia levels showed a increase after food consumption in StD and LGID-fed mice ( n = 12 for both StD and LGID). F Percentage increase of glycaemia observed 1 h after food administration ( n = 12 for both StD and LGID). G Glycated hemoglobin levels were higher in StD-fed mice when compared with animals treated with LGID ( n = 8 for both StD and LGID). Data are expressed as means ± sem. * p < 0.05, ** p < 0.01; two-way repeated-measures ANOVA ( B – D ), paired Student’s t -test ( E ), unpaired Student's t -test ( F ), unpaired Mann–Whitney U -test ( G )
Article Snippet: Glycated
Techniques: MANN-WHITNEY