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192 results for “glycosylation”
Senegenin Modulates O-GlcNAc Glycosylation to Thwart Hepatocellular Carcinoma Progression
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Fig. 5. C2C12 in Insulin-mimetic activity of 23-glycosyl oleanane triterpenoids isolated from Gymnema latifolium
Fig. 5. C2C12 myotube cells were exposed to compounds 2 and 4 (5 μM and 20 μM, respectively) and incubated for 1 h. The phosphorylation of the protein AMPK in the cells was assessed by Western blot analysis. Fold expression was calculated as p-AMPK/AMPK and normalized to the protein level of β-actin. Values are expressed as the mean ± SD (n = 3).
Fig. 2. Key 1H–1H in Insulin-mimetic activity of 23-glycosyl oleanane triterpenoids isolated from Gymnema latifolium
Fig. 2. Key 1H–1H COSY (bold) and HMBC (1H → 13C, green arrows) correlations for compounds 1, 2, 5, and 7. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 4 in Insulin-mimetic activity of 23-glycosyl oleanane triterpenoids isolated from Gymnema latifolium
Fig. 4. Stimulatory effects of compounds 1⎯9 on glucose uptake in 3T3-L1 adipocytes using the fluorescent glucose derivative 2-NBDG. (A) Differentiated adipocytes were treated with isolated compounds (1–9) at a concentration of 20 μM and insulin (100 nM) as a positive control. After 1 h of incubation with or without 2-NBDG, images were captured by fluorescence microscopy. (B) The fluorescence signal in the adipocytes was measured and analyzed. After the cells were incubated for 1 h with or without 2-NBDG, the fluorescence signals were measured at Ex/Em = 450/535 nm. The results are presented as the mean ± SD (n = 3) of experiments performed in triplicate; *p <0.05, **p <0.01, and ***p <0.001, compared to the vehicle group. (C) Differentiated 3T3-L1 adipocytes were treated with compounds 2 and 4 at concentrations of 1, 5, and 20 μM or insulin at 100 nM. After 1 h of incubation, the fluorescence intensities were measured using a fluorescence microscope. (D) The concentration–response effects on glucose uptake in 3T3-L1 adipocytes. Cells were exposed to compounds at various concentrations (5, 10, and 20 μM) and incubated for 1 h. The cells were lysed, and the fluorescence signals were measured at Ex/Em =450/535 nm. Data are expressed as the mean ±SD (n =3) of experiments performed in triplicate; *p <0.05, **p <0.01, and ***p <0.001, compared to the negative control.
Mimicry of the Proton Wire Mechanism of Enzymes Inside a Supramolecular Capsule Enables β-Selective O-Glycosylations
<p>Data underlying the figures in the publication “Mimicry of the proton wire mechanism of enzymes inside a supramolecular capsule enables β-selective O-glycosylations”, published in <em>Nature Chemistry</em>.</p> <p>Table of contents:</p> <p><strong>1. Figure 1</strong>: An editable chemdraw graphic of <em>Figure 1</em>.</p> <p><strong>2. Figure 2</strong>: .zip archive containing an editable chemdraw graphic of <em>Figure 2</em>, and NMR spectra of compounds 7 and 9.</p> <p><strong>3. Figure 3</strong>: .zip archive containing an editable chemdraw graphic of <em>Figure 3</em>, and source data underlying <em>Figures 3a</em>, <em>3c</em> and <em>3d</em>.</p> <p><strong>4. Figure 4</strong>: .zip archive containing an editable chemdraw graphic of <em>Figure 4</em>, NMR spectra of <em>Figure 4c</em> and source data underlying <em>Figures 4d</em> and <em>4e</em>.</p> <p><strong>5. Figure 5</strong>: .zip archive containing an editable chemdraw graphic of <em>Figure 5</em>, and NMR spectra of compounds 26-31, S8 and S9.</p> <p><strong>6. Table 1</strong>: .zip archive containing an editable chemdraw graphic of <em>Table 1</em>, and NMR spectra of all compounds shown in <em>Table 1</em>.</p>
Self-assembling peptide nanofiber HIV vaccine elicits robust vaccine-induced antibody functions and modulates Fc glycosylation.
<p>To develop vaccines for certain key global pathogens such as HIV, it is crucial to elicit both neutralizing and non-neutralizing Fc-mediated effector antibody functions. Clinical evidence indicates that non-neutralizing antibody functions including antibody-dependent cellular cytotoxicity (ADCC) and antibody-dependent cellular phagocytosis (ADCP) contribute to protection against several pathogens. In this study, we demonstrated that conjugation of HIV Envelop (Env) antigen gp120 to a self-assembling nanofiber material named Q11 induced antibodies with higher breadth and functionality when compared to soluble gp120. Immunization with Q11-conjugated gp120 vaccine (gp120-Q11) demonstrated higher tier 1 neutralization, ADCP and ADCC as compared to soluble gp120. Moreover, Q11 conjugation altered the Fc N-glycosylation profile of antigen-specific antibodies, leading to a phenotype associated with increased ADCC in animals immunized with gp120-Q11. Thus, this nanomaterial vaccine strategy can enhance non-neutralizing antibody functions possibly through modulation of IgG Fc N-glycosylation.</p>
Exploring the Chemical Space of Glycosylation in Noncovalent Protein Complexes: an Expedition along Different Structural Levels of Human Chorionic Gonadotropin Employing Mass Spectrometry
<p><strong>Supplementary files for "Exploring the Chemical Space of Glycosylation in Noncovalent Protein Complexes: an Expedition along Different Structural Levels of Human Chorionic Gonadotropin Employing Mass Spectrometry"</strong></p> <p><strong>Introduction</strong></p> <p>This data repository contains all previously unpublished raw data files for the manuscript “Exploring the Chemical Space of Glycosylation in Noncovalent Protein Complexes: an Expedition along Different Structural Levels of Human Chorionic Gonadotropin Employing Mass Spectrometry” by Maximilian Lebede<sup>||</sup>, Fiammetta Di Marco<sup>||</sup>, Wolfgang Esser-Skala, René Hennig, Therese Wohlschlager, Christian G. Huber.</p> <p><strong>Files</strong></p> <p>This repository contains 9 files:</p> <ul> <li><strong>Dimer Raw Files.zip</strong> folder containing 4 files of native-MS data (*.raw, Thermo RAW file format) of two batches of the drug product Ovitrelle® at native dimer level. </li> <li><strong>H11M9 Ovitrelle BA056714 Glycopeptide R1 230920_07.zip</strong> folder containing 1 file of HPLC-MS/MS glycopeptide data (*.raw, Thermo RAW file format) of one batch of the drug product Ovitrelle®.</li> <li><strong>H11M9 Ovitrelle BA056714 Glycopeptide R2 230920_08.zip</strong> folder containing 1 file of HPLC-MS/MS glycopeptide data (*.raw, Thermo RAW file format) of one batch of the drug product Ovitrelle®.</li> <li><strong>H11M9 Ovitrelle BA056714 Glycopeptide R3 230920_09.zip</strong> folder containing 1 file of HPLC-MS/MS glycopeptide data (*.raw, Thermo RAW file format) of one batch of the drug product Ovitrelle®.</li> <li><strong>H11M9 Ovitrelle BA059433 Glycopeptide R1 240920_15.zip</strong> folder containing 1 file of HPLC-MS/MS glycopeptide data (*.raw, Thermo RAW file format) of one batch of the drug product Ovitrelle®.</li> <li><strong>H11M9 Ovitrelle BA059433 Glycopeptide R2 240920_16.zip</strong> folder containing 1 file of HPLC-MS/MS glycopeptide data (*.raw, Thermo RAW file format) of one batch of the drug product Ovitrelle®.</li> <li><strong>H11M9 Ovitrelle BA059433 Glycopeptide R3 240920_17.zip</strong> folder containing 1 file of HPLC-MS/MS glycopeptide data (*.raw, Thermo RAW file format) of one batch of the drug product Ovitrelle®.</li> <li><strong>MoFi Settings.zip</strong> folder containing 12 files of MoFi settings (*.xml) to annotate deconvoluted spectra of hCG subunits and dimer of two Ovitrelle® batches, untreated and after desialylation. A typical MoFi setting file is build from protein sequence (*.FASTA), monosaccharide and frequent modification atomic composition (*.csv), glycan or glycoform library (*.csv) and deconvoluted spectrum in centroid (*.csv). Files are named as following: Settings_Ovitrelle_Batch number (BA056714 or BA059433)_Structural level (Alpha, Beta or Dimer)_Enzymatic treatement (Untreated or Sialidase).</li> <li><strong>Subunit Raw Files.zip</strong> folder containing 8 files of HPLC-MS data (*.raw, Thermo RAW file format) of two batches of the drug product Ovitrelle® at intact subunit level. </li> </ul> <p>Raw files are named as following: Instrument, Drug product (Ovitrelle), Batch number (BA056714 or BA059433), Structural level (Dimer, Subunits or Glycopeptides), Enzymatic treatment (untreated, Sialidase, PNGase F or PNGase F + Sialidase) and date. Glycopeptide data includes 3 replicates (R1-3).</p> <p><strong>License</strong></p> <p>This work is licensed under the Creative Commons Attribution 4.0 International License. To view a copy of this license, visit <a href="http://creativecommons.org/licenses/by/4.0/">http://creativecommons.org/licenses/by/4.0/</a> .</p> <p> </p>
Supplementary Data for: "Molecular basis for bacterial N-glycosylation by a soluble HMW1C-like N-glycosyltransferase"
<p>This data set contains files related to the article "<strong>Molecular basis for bacterial <em>N</em>-glycosylation by a soluble HMW1C-like <em>N</em>-glycosyltransferase</strong>" by Beatriz Piniello, Javier Macías-León, Shun Miyazaki, Ana García-García, Ismael Compañón, Mattia Ghirardello, Víctor Taleb, Billy Veloz, Francisco Corzana, Atsushi Miyagawa, Carme Rovira and Ramón Hurtado-Guerrero.</p> <p>Description of the files:</p> <p><strong>Simulation data:</strong></p> <p>- <strong>classical_md_simulations.zip: </strong>includes the inputs and initial and final structures of the classical MD simulation of AaNGT in complex with UDP-Glc and peptide, for both Asn3 in amide and imidic acid form.</p> <p>- <strong>qmmm_simulations.zip</strong>: includes the inputs for equilibration and metadynamics, and the initial structure extracted from the classical MD. Other relevant structures included in the directories of the pertinent figures (see below). Also includes plots of the CVs for each of the metadynamics.</p> <p><strong>Data related to the figures in the manuscript (data from the plots is in the Source Data file included with the manuscript):</strong></p> <p><strong>- Figure_4.zip: </strong>PDB file of the structure shown.</p> <p>- <strong>Figure_5.zip</strong>: PDB files of the structures shown (MC, TS and P, (already uploaded in v1) and FES file.</p> <p>- <strong>Figure_S6.zip: </strong>PDB files of the structures shown (MC, TS and P).</p> <p>- <strong>Figure_S7.zip: </strong>PDB files of the structures shown (MC, TS and P) for both simulations, and their respective FES files.</p> <p>- <strong>Figure_S9.zip</strong>: PDB file of the structure shown (computational only). It is the same as the structure shown in <strong>Figure 8</strong>.</p> <p>- <strong>Figure_S11.zip</strong>: PDB file of the structure shown.</p> <p>- <strong>Table_S3.zip: </strong>Excel file with the data to obtain the table. TS is given as a single structure in the table and thus not included in the file.</p> <p> </p> <p>More data can be made available upon reasonable request.</p>
Fig. 5. Total ubiquinone-9 in 3-O-glycosylation of kaempferol restricts the supply of the benzenoid precursor of ubiquinone (Coenzyme Q) in Arabidopsis thaliana
Fig. 5. Total ubiquinone-9 content in the rosette leaves of wild-type, ugt78d2, f3′h, and f3′h/ugt78d2 plants. Plants were grown on soil in 16-h days (110 μE m 2 s 1) at 22 ◦C for 3 weeks. Data represent the means of 7–8 biological replicates ±SE. P values from an analysis of variance between each mutant and the wild-type reference are indicated above the bars. The asterisk indicates significant differences from the wild type as determined by variance analysis (P <α = 0.1).
Fig. 4. 4 in 3-O-glycosylation of kaempferol restricts the supply of the benzenoid precursor of ubiquinone (Coenzyme Q) in Arabidopsis thaliana
Fig. 4. 4-hydroxybenzoate content in A. thaliana roots and rosette leaves. Roots were harvested from 17-day-old axenic cultures, while rosette leaves were harvested from 3-week-old plants grown on soil. Samples were processed with and without acidic hydrolysis, and 4-hydroxybenzoate was quantified by HPLCspectrophotometry. Data represent the means of 3–4 biological replicates ± SE. P values from an analysis of variance between the ugt78d1/ugt78d2 knockout and the wild-type reference are indicated above the bars. Threshold for statistically significant differences between ugt78d1/ugt78d2 and wild-type data as determined by variance analysis was P <α = 0.1. n.d.: not detected.
Fig. 1 in 3-O-glycosylation of kaempferol restricts the supply of the benzenoid precursor of ubiquinone (Coenzyme Q) in Arabidopsis thaliana
Fig. 1. Metabolic origins of 4-hydroxybenzoate for ubiquinone biosynthesis in plant cells. Note that chemical modeling of the peroxidative cleavage of kaempferol predicts that peroxidases do not act on kaempferol itself, but on its α-diketone tautomer. The formation of the latter is contingent on the presence of a double bond between C-2 and C-3 and a free C-3- OH on the C-ring. Dashed arrows indicate unknown and/or multiple steps. Ara, arabinosyl; Glu, glucosyl; Rha, Rhamnosyl; UGT78D1, flavonol 3-O-rhamnosyltransferase; UGT78D2, flavonol 3-O-glucosyltransferase; UGT78D3, flavonol 3-O- arabinosyltransferase.
Fig. 3 in 3-O-glycosylation of kaempferol restricts the supply of the benzenoid precursor of ubiquinone (Coenzyme Q) in Arabidopsis thaliana
Fig. 3. Total ubiquinone content and rate of de novo ubiquinone biosynthesis in A. thaliana. A) Total ubiquinone-9 content in the rosette leaves of 3-week-old wild-type, ugt78d1, ugt78d2, ugt78d3 and ugt78d1/ugt78d2 plants grown on soil. B) Relative ubiquinone-9- [Ring-13C] labeling in the leaves of axenically 6 grown wild-type, ugt78d1, ugt78d2, ugt78d3 and ugt78d1/ugt78d2 plants fed for 3h with 250 μM of phenylalanine-[Ring- 13C]. Data represent the means of 4–6 6 biological replicates ± SE. P values from an analysis of variance between each mutant and the wild-type reference are indicated above the bars. Asterisks indicate significant differences from the wild type as determined by variance analysis (P <α = 0.1).
Fig. 2 in Glycosylated constituents isolated from the trunk of Abies holophylla and their anti-inflammatory and neurotrophic activity
Fig. 2. Key COSY (blue bold), HMBC (red arrow), and NOESY (green dashed arrow) correlations of previously undescribed compounds 1–11. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
Fig. 5 in Glycosylated constituents isolated from the trunk of Abies holophylla and their anti-inflammatory and neurotrophic activity
Fig. 5. Stereochemical assignment of C-2 in 9 and 10 via two different empirical rules. (A) 13C NMR chemical shifts values of C-1, C-2, C-3, and C-1′ in 9 and 10 (top), and (R)- and (S)-PG (bottom) and their differences [δ(R–S)]. (B) 1H NMR chemical shift value of H-1 in 9 and 10 (left) and (R)- and (S)-OG and (R)- and (S)-EG (right).
Fig. 3 in Glycosylated constituents isolated from the trunk of Abies holophylla and their anti-inflammatory and neurotrophic activity
Fig. 3. Extracted ion chromatograms (EICs) of chiral derivatized monosaccharides purchased or obtained by hydrolysis of isolated compounds. (A) D- and L-allopyranose (m/z 447.1260). (B) D- and L-apiofuranose (m/z 417.1154). (C) L- and D-rhamnopyranose (m/z 431.1311). (D) D- and L-glucopyranose (m/z 447.1260). (E) L- and D-arabinopyranose (m/z 417.1154). All, allopyranose. Api, apiofuranose. Rha, rhamnopyranose. Glc, glucopyranose. Ara, arabinopyranose. See the Materials and methods section below for detailed derivatization procedures.
Fig. 1 in Molecular networking-driven isolation of 8 -Glycosylated biscoumarins from Cruciata articulata
Fig. 1. Molecular network of Cluster G1. Red: Parent ions of isolated new biscoumarins (1–4); Yellow: Parent ions for proposed structures. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
Fig. 3 in Antioxidant activity and mechanism of dihydrochalcone C-glycosides: Effects of C-glycosylation and hydroxyl groups
Fig. 3. The distribution and energy (in eV) of HOMO and LUMO for the studied dihydrochalcones at the B3LYP/6-31G(d,p) level in the gas phase.
Study of Hemostasis in Patients With Congenital Disorder of Glycosylation
ClinicalTrials.gov study NCT03560570. IPD Sharing: NO. Countries: 1. Publications: 0.
Follicle Stimulating Hormone (FSH) Glycosylation in Women: Effect of Estradiol
ClinicalTrials.gov study NCT03868202. IPD Sharing: NO. Countries: 1. Publications: 13.
"Incidence and Consequences of Disorders of Glycosylation in Patients With Conotruncal and Septal Heart Defects"
ClinicalTrials.gov study NCT02503267. IPD Sharing: Not stated. Countries: 1. Publications: 9.
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Allen Brain Atlas
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