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Image Search Results
Journal: PLoS ONE
Article Title: Increased Phosphorylation of Vimentin in Noninfiltrative Meningiomas
doi: 10.1371/journal.pone.0009238
Figure Lengend Snippet: Tumor extracts were analyzed using SELDI-TOF on Q10 anion-exchange ProteinChip Arrays, as shown in . Signal intensity at the 53-kDa mass level were measured and calculated parameters plotted for (A) infiltrative/invasive tumor samples, (B) noninfiltrative tumor samples. Medians, 25 th and 75 th percentiles are marked with line segments across the boxes and the lowest and highest signal values with bars.
Article Snippet: Sinapinic acid was used as the ionization matrix and
Techniques:
Journal: PLoS ONE
Article Title: Increased Phosphorylation of Vimentin in Noninfiltrative Meningiomas
doi: 10.1371/journal.pone.0009238
Figure Lengend Snippet: After purification by chromatography and electrophoresis, the 53-kDa marker was cleaved by proteases. (A) peptide fingerprint after GluC endoproteinase digestion obtained by SELDI-TOF analysis on NP20 ProteinChip Arrays. Peptides with measured molecular masses matching those of the computed GluC endoproteinase proteolytic peptides of vimentin are indicated with an asterisk. (B) GluC endoproteinase peptides of vimentin identified by SELDI-TOF are listed according to their masses. (C) Mapping of the peptides identified by either peptide mass fingerprinting or nanoLC-MS/MS to the vimentin sequence. Sequences highlighted in grey correspond to GluC endoproteinase peptides identified in B. Underlined sequences correspond to 60 trypsin peptides identified by nanoLC-MS/MS. Phosphorylated peptides (37-50 amino acid and 70-78 amino acid peptides) are underlined with dots.
Article Snippet: Sinapinic acid was used as the ionization matrix and
Techniques: Purification, Chromatography, Electrophoresis, Marker, Peptide Mass Fingerprinting, Tandem Mass Spectroscopy, Sequencing
Journal: PLoS ONE
Article Title: Increased Phosphorylation of Vimentin in Noninfiltrative Meningiomas
doi: 10.1371/journal.pone.0009238
Figure Lengend Snippet: Purified 53-kDa marker from noninfiltrative tissue extracts was treated by alkaline phosphatase and samples were analyzed using SELDI-TOF MS. Analyses were performed on Q10 anion-exchange ProteinChip Arrays (A and B) or hydrophilic NP20 ProteinChip Arrays (C and D). (A and C) Controls with untreated purified 53-kDa marker. (B and D) phosphatase-treated marker.
Article Snippet: Sinapinic acid was used as the ionization matrix and
Techniques: Purification, Marker
Journal: Frontiers in Molecular Neuroscience
Article Title: Sample Pooling and Inflammation Linked to the False Selection of Biomarkers for Neurodegenerative Diseases in Top–Down Proteomics: A Pilot Study
doi: 10.3389/fnmol.2018.00477
Figure Lengend Snippet: Identification of the candidate biomarker in outliers. (A) Four CJD samples with a 10–15 kDa band of different intensity (arrow). (B) Electrophoresis analysis of the purified candidate biomarker. The arrow marks the position of the peak. (C) After passive elution of the band in (B) , the presence of the candidate biomarker was confirmed by SELDI-TOF analysis with a Q10 ProteinChip Array.
Article Snippet: The
Techniques: Biomarker Discovery, Electrophoresis, Purification