Journal: bioRxiv

Article Title: RGG peptide induces the disassembly of disease-relevant FUS and TDP43 condensates

doi: 10.1101/2025.03.19.643735

Figure Lengend Snippet: (A) Graph representing the distribution of FUS-P525L protein in nucleus and cytoplasm. The fluorescent intensities of the nucleus and cytoplasm were calculated from the experiment as performed in , and the ratio is plotted here. A student-paired t-test was used to calculate the significance value (n=6). (B) Incucyte images (real-time cell death analysis) representing the cellular uptake of propidium iodide (PI) in different conditions in HeLa cells. Scale bar=100um. (C) Graph representing the number of propidium iodide (PI) positive cells (dead cells) from the experiment as performed in B. The time on the x-axis reflects the time-point after transfection in hours. The significance was calculated using 2-way ANOVA with multiple comparisons (n=4). Error bars in all graphs represent mean ±SEM, and the same color points in A depict the data from a single experimental set. *, **, ***, and **** denote p-value≤0.05, ≤0.01, ≤0.001, and ≤0.0001, respectively.

Article Snippet: The cell death analysis was performed using the IncuCyte S3 live-cell analysis instrument (Sartorius), and the change in the number of PI-positive cells (dead cells) in different conditions was plotted in the graph.

Techniques: Transfection

Journal: bioRxiv

Article Title: RGG peptide induces the disassembly of disease-relevant FUS and TDP43 condensates

doi: 10.1101/2025.03.19.643735

Figure Lengend Snippet: Incucyte images representing the cellular uptake of propidium iodide (PI) in different conditions in HeLa cells. Scale bar=100um. The images are part of and .

Article Snippet: The cell death analysis was performed using the IncuCyte S3 live-cell analysis instrument (Sartorius), and the change in the number of PI-positive cells (dead cells) in different conditions was plotted in the graph.

Techniques:

Journal: European journal of biochemistry

Article Title: The N-glycans of jack bean alpha-mannosidase. Structure, topology and function.

doi: 10.1046/j.1432-1327.1999.00598.x

Figure Lengend Snippet: Fig. 1. HPLC profiles of PA-sugar chains from jack bean a-man- nosidase. Panel A: RP-HPLC of PA-derivatives from jack bean a-man- nosidase. The PA-derivatives were applied onto a Cosmosil 5C18-AR (6.0 250 mm) column and eluted as described in the text. The run- through-fraction (around 9 min) contained some PA-derivatives bearing only one GlcNAc residue at their reducing-ends, which are known to be derived from released intact N-glycans as by-products of hydrazinolysis [7,12]. Panel B: Size-fractionation HPLC of the partially purified PA-sugar chains shown in Panel A (Peaks I and II) by RP-HPLC.

Article Snippet: The two glycopeptide fractions [elution volume from 244±292 mL (high-mannose-type glycan) and from 408±500 mL (complex-type glycan)] were concentrated in a rotary evaporator and the former glycopeptide-fraction was applied to a Jasco 880-PU HPLC apparatus with a Poros R1 column (4.6 100 mm).

Techniques: Residue, Derivative Assay, Fractionation, Purification

Journal: European journal of biochemistry

Article Title: The N-glycans of jack bean alpha-mannosidase. Structure, topology and function.

doi: 10.1046/j.1432-1327.1999.00598.x

Figure Lengend Snippet: Fig. 3. RP-HPLC of a lysylendopeptidase digest of alkylated jack bean a-mannosidase. The lysylendopeptidase digest of alkylated jack bean a- mannosidase (100 mg) was applied onto a Vydac C8 column. The column was eluted by a linear gradient of 2±40% acetonitrile in 0.1% trifluoroacetic acid. Panel A: Total ion monitoring chromatogram (TIC). `RT: 28.2 min' indicates the position of glycopeptide (GP) which eluted after 28.2 min. Panel B: Precursor ion (m/z 366.0; Hex-HexNAc) monitoring. Panel C: Precursor ion (m/z 204.1; HexNAc) monitoring. Panel D: ESI-MS spectrum of the glycopeptide GP (complex-type) from Panel A.

Article Snippet: The two glycopeptide fractions [elution volume from 244±292 mL (high-mannose-type glycan) and from 408±500 mL (complex-type glycan)] were concentrated in a rotary evaporator and the former glycopeptide-fraction was applied to a Jasco 880-PU HPLC apparatus with a Poros R1 column (4.6 100 mm).

Techniques: Glycoproteomics

Journal: European journal of biochemistry

Article Title: The N-glycans of jack bean alpha-mannosidase. Structure, topology and function.

doi: 10.1046/j.1432-1327.1999.00598.x

Figure Lengend Snippet: Fig. 5. RP-HPLC of a glycopeptide-fraction obtained by gel-filtration of a lysylendopeptidase-digest of alkylated jack bean a-mannosidase. The glycopeptide fraction obtained by Sephadex G-25 gel-filtration (fraction volume from 244 to 292 mL) was applied onto a Poros R1 column. The column was eluted with 5% acetonitrile in 0.1% trifluoroacetic acid for 5 min, followed by a linear gradient of 5±60% acetonitrile in 0.1% trifluoroacetic acid. Only the peak indicated by an arrow was found to contain neutral sugars. GP (high-mannose-type) indicates a glycopeptide bearing the high-mannose-type N-glycan.

Article Snippet: The two glycopeptide fractions [elution volume from 244±292 mL (high-mannose-type glycan) and from 408±500 mL (complex-type glycan)] were concentrated in a rotary evaporator and the former glycopeptide-fraction was applied to a Jasco 880-PU HPLC apparatus with a Poros R1 column (4.6 100 mm).

Techniques: Glycoproteomics, Filtration