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323 results for “glutamine”

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zenodo44/100

Dataset for the TGM2 (Protein-glutamine gamma-glutamyltransferase 2) antibody screening study

<p><strong>This antibody characterization dataset is related to the F1000 research article openly available at F1000Research.</strong></p> <p><em>This project contains the following underlying data included in a study aimed at characterizing seventeen commercial antibodies against Protein-glutamine gamma-glutamyltransferase 2 (TGM2) protein, encoded by TGM2 gene. The original study is also available on the Zenodo YCharOS community (<a href="https://doi.org/10.5281/zenodo.10819348">https://doi.org/10.5281/zenodo.10819348</a>).</em></p>

opencc-by-4.0Apr 2024View details →
zenodo40/100

Figure 6 in Oral glutamine dipeptide or oral glutamine free amino acid reduces burned injury progression in rats

Figure 6. Graphical representation of Glutathione (ΜM) in the seven days after injury in G1-Control, G2-Dip, and G3-Free AA. G2-Dip presented a larger amount concerning the G1-Control *(P&lt;0.05).

opencc-by-4.0Jun 2024View details →
zenodo40/100

Figure 4 in Oral glutamine dipeptide or oral glutamine free amino acid reduces burned injury progression in rats

Figure 4. Graphical representation of interspace (stasis) regions length (mm) in the seven days after injury in G1-Control,G2-Dip, and G3-FreeAA.G1-Control presented smaller interspaces in 666 relation to the treated groups G2-Dip (P&lt;0.01) and G3-FreeAA *(P&lt;0.01).

opencc-by-4.0Jun 2024View details →
zenodo40/100

Figure 5 in Oral glutamine dipeptide or oral glutamine free amino acid reduces burned injury progression in rats

Figure 5. Graphical representation of fibroblast counts in three fields of the interspace dermis among in the seven days after injury in G1-Control, G2-Dip, and G3-FreeAA. G1-Control presented less amount of fibroblast concerning the treated groups G2-Dip (P&lt;0.01) and G3-Free AA *(P&lt;0.01).

opencc-by-4.0Jun 2024View details →
zenodo40/100

Figure 3 in Oral glutamine dipeptide or oral glutamine free amino acid reduces burned injury progression in rats

Figure 3. Histopathology study of the necrotic areas: (A) Photomicrograph of G2-Dip animal, with necrosis presence in the dermis (superior arrows) just below the epidermis (E) and in the hypodermis (arrows below in the right). Hair follicle (HF). Masson's trichrome; 100x; (B) Photomicrograph of G1-Control animal, hemorrhagic foci are observed in both dermis and hypodermis (arrows). Central blood vessel (BV). Masson's trichrome; 400x; (C) Photomicrograph of G3-FreeAA animal, with a large area of edema in both dermis and hypodermis (arrows). Hair follicle (HF). Masson's trichrome; 100x; (D) Photomicrograph of G1-Control animal: hemorrhagic focus can be observed in the hypodermis and many neutrophils (minor arrows) in a blood vessel (BV) lumen, some in diapedesis through its wall (larger arrow). The thinner arrows show a small intercellular inflammatory infiltrate. Giemsa; 400x.

opencc-by-4.0Jun 2024View details →
zenodo40/100

Figure 2 in Oral glutamine dipeptide or oral glutamine free amino acid reduces burned injury progression in rats

Figure 2. Graphical representation of necrosis percentage evolution obtained by photographic analysis in the burn interspace, two and seven days after injury in G1-Control, G2-Dip and G3-FreeAA. In the G3-FreeAA there was a significant reduction of necrosis between two and seven days *(P&lt;0.05).

opencc-by-4.0Jun 2024View details →
zenodo40/100

Figure 1 in Oral glutamine dipeptide or oral glutamine free amino acid reduces burned injury progression in rats

Figure 1. Rat comb burn model: (A) Comb metal plate; (B) Comb burn injury, with four rectangular full-thickness burn areas separated by three unburned interspaces (stasis zone); (C) rectangular burned full thickness areas just after the injury; (D) animal from treated group 7 days after injury showing interspaces (stasis zone) without necrosis.

opencc-by-4.0Jun 2024View details →
zenodo40/100

Figure 1 in Characterization of glutamine synthetase from the ammonium-excreting strain HM053 of Azospirillum brasilense

Figure 1. Transferase activity of glutamine synthetase. (A) Transferase activity of wild-type glutamine synthetase in the absence and presence of magnesium as well as with snake venom phosphodiesterase treatment; (B) Transferase activity of P347L glutamine synthetase in the absence and presence of magnesium, and with snake venom phosphodiesterase treatment. The activity of GS is expressed in µmol γ-glutamyl-hydroxamate.min-1.mg protein-1, given that the absorbance of 530 nm of 1 µmolγ-glutamylhydroxamate was 0.054. The total activity was determined in the absence of Mg2+ (-Mg2+) and the non-adenylylated (active) fraction was determined in the presence of 60 mM Mg2+ (+Mg2+). Samples were incubated at 30 ºC for 0, 10, 30 and 60 min before measuring activity. SVP-treated GS samples (+ SVP) were incubated with snake venom phosphodiesterase. GS activity reactions contained 3 µg of protein.

opencc-by-4.0Dec 2022View details →
zenodo40/100

Figure 3 in Characterization of glutamine synthetase from the ammonium-excreting strain HM053 of Azospirillum brasilense

Figure 3. Prediction of the structure of glutamine synthetase from the mutant P347L. (A) Prediction of the P347L-GS structure. The amino acid marked in pink corresponds to leucine in strain HM053; (B) b1) Prediction structure of wild-type GS from amino acid 346 to 361. b2) Prediction structure of P347L-GS from amino acid 346 to 361. b3) Alignment of prediction structures of wildtype GS and P347L GS from amino acid 346 to 361. The amino acid marked in blue corresponds to the proline that is mutated in strain HM053. The amino acid marked in pink is leucine that replaced proline in the mutated amino acid in strain HM053.

opencc-by-4.0Dec 2022View details →
zenodo40/100

Figure 2 in Characterization of glutamine synthetase from the ammonium-excreting strain HM053 of Azospirillum brasilense

Figure 2. Western blot assays of glutamine synthetase after treatment with snake venom phosphodiesterase. Samples (~ 0.3 µg GS protein) were separated by SDS‐PAGE followed by Western blotting with an anti‐GS antibody. A) Wild-type glutamine synthetase; B) P347L glutamine synthetase. Lane 1: GS after 0 min of incubation at 30 ºC without any treatment; lanes 2 to 5: GS after 0, 10, 30 and 60 min incubation at 30 ºC with snake venom phosphodiesterase. Lane 6: GS after 60 min incubation at 30 ºC without treatment.

opencc-by-4.0Dec 2022View details →
zenodo36/100

Experimental data from Dietler et al. (2022) "Signal Transduction in Light-Oxygen-Voltage Receptors Lacking the Active-Site Glutamine"

<p>This .xlsx file contains the experimental data underpinning the research reported in Dietler et al. (2022) &quot;Signal Transduction in Light-Oxygen-Voltage Receptors Lacking the Active-Site Glutamine&quot;</p>

opencc-by-4.0Mar 2022View details →
zenodo36/100

Impact of low pH on glutamine incorporation in CD8+ T cells

<p>OT-I CTLs were cultured for 4 hours with <sup><span>13</span></sup><span>C</span>-glutamine in the presence, or absence, of IL-2 at pH7.4 or pH6.6. Metabolites that incorporated isotopic glutamine were identified by HILIC-HRMS.</p>

opencc-by-4.0Jun 2024View details →
zenodo36/100

Glutamine sensing licenses cholesterol synthesis.

<p>The uploaded metabolomic dataset contains liquid-chromatography-mass spectrometry (LC-MS) data associated to a publication of Bruna Martins Garcia et al. from the Lena Pernas laboratory.</p> <p>The title olf the article is: <strong>Glutamine sensing licenses cholesterol synthesis.</strong></p> <p>This article is to be published 2024 in the EMBO Journal-</p> <p>Abstract of the article: The mevalonate pathway produces essential metabolites such as cholesterol. Although this pathway is negatively regulated by metabolic intermediates, little is known of the metabolites that positively regulate its activity.<em> </em>We found that the amino acid glutamine is required to activate the mevalonate pathway. Glutamine starvation inhibited cholesterol synthesis and blocked transcription of the mevalonate pathway&mdash;even in the presence of glutamine derivatives such as ammonia and a-ketoglutarate. We pinpointed this glutamine-dependent effect to a loss in the ER-to-Golgi trafficking of SCAP that licenses the activation of SREBP2, the major transcriptional regulator of cholesterol synthesis. Both enforced Golgi-to-ER retro-translocation and the expression of a nuclear SREBP2 rescued mevalonate pathway activity during glutamine starvation. In a cell model of impaired mitochondrial respiration in which glutamine uptake is enhanced, SREBP2 activation and cellular cholesterol were increased. Thus, the mevalonate pathway senses and is activated by glutamine at a previously uncharacterized step, and the modulation of glutamine synthesis may be a strategy to regulate cholesterol levels in pathophysiological conditions.&nbsp;</p> <p>The associated data in this repository is grouped according to the figures in the the above mentioned article. Each zip folder contains the LC-MS raw files and one or more Excel tables describing the parameters (retention time, observed molecular weight, detected error to expected molecular weight, signal-to-noise and the integrated raw values of the detected compounds. Material and Method utilized for the analysis of the diverse samples is available in the context of the above mentioned article.</p>

opencc-by-4.0Aug 2024View details →
dryad36/100

Data from: Protection of pepper plants from drought by microbacterium sp. 3J1 by modulation of the plant's glutamine and α-ketoglutarate content: a comparative metabolomics approach

<p><span>Desiccation-tolerant plants are able to survive for extended periods of time in the absence of water. The molecular understanding of the mechanisms used by these plants to resist droughts can be of great value for improving drought tolerance in crops. This understanding is especially relevant in an environment that tends to increase the number and intensity of droughts. The combination of certain microorganisms with drought-sensitive plants can improve their tolerance to water scarcity. One of these bacteria is <i>Microbacterium </i>sp. 3J1, an actinobacteria able to protect pepper plants from drought. In this study, we supplemented drought-tolerant and drought-sensitive plant rhizospheres with <i>Microbacterium</i> sp. 3J1 and analyzed their proteomes under drought to investigate the plant-microbe interaction. We also compare this root proteome with the proteome found in desiccation-tolerant plants. In addition, we studied the proteome of <i>Microbacterium</i> sp. 3J1 subjected to drought to analyze its contribution to the plant-microbe interaction. We describe those mechanisms shared by desiccation-tolerant plants and sensitive plants protected by microorganisms focusing on protection against oxidative stress, and production of compatible solutes, plant hormones, and other more specific proteins.</span></p>

opencc-zeroMay 2020View details →
zenodo36/100

Trajectories from "A glutamine-based single ɑ-helix scaffold to target globular proteins" Escobedo et al. 2022

<p>Trajectories from the manuscript &quot;A glutamine-based single ɑ-helix scaffold to target globular proteins&quot; Escobedo et al. 2022.</p> <p>https://www.biorxiv.org/content/10.1101/2022.05.06.490931v1</p>

opencc-by-4.0Oct 2022View details →
zenodo36/100

Supplemental data to "Acute and persistent effects of oral glutamine supplementation on growth, cellular proliferation, and tight junction protein transcript abundance in jejunal tissue of low and normal birthweight pre-weaning piglets"

<p>Supplementary data to&nbsp;&quot;Acute and persistent effects of oral glutamine supplementation on growth, cellular proliferation, and tight junction protein transcript abundance in jejunal tissue of low and normal birthweight pre-weaning piglets&quot;</p>

opencc-by-4.0Oct 2023View details →
ClinicalTrials.gov36/100

Enteral Versus Parenteral Glutamine Supplement

ClinicalTrials.gov study NCT00875797. IPD Sharing: Not stated. Countries: 1. Publications: 1.

restrictedIPD-UNDECIDEDFeb 2026View details →
ClinicalTrials.gov36/100

Glutamine for the Treatment of Patients With Irritable Bowel Syndrome

ClinicalTrials.gov study NCT01414244. IPD Sharing: UNDECIDED. Countries: 1. Publications: 1.

restrictedIPD-UNDECIDEDFeb 2026View details →
ClinicalTrials.gov36/100

Trial of Glutamine and Antioxidant Supplementation in Critically Ill Patients

ClinicalTrials.gov study NCT00133978. IPD Sharing: Not stated. Countries: 5. Publications: 5.

restrictedIPD-UNDECIDEDFeb 2026View details →
ClinicalTrials.gov36/100

A Randomized Double-Blind Control-Comparison Crossover Trial of Oral Glutamine to Suppress Frequently Recurrent Herpes Labialis

ClinicalTrials.gov study NCT00913692. IPD Sharing: Not stated. Countries: 1. Publications: 3.

restrictedIPD-UNDECIDEDFeb 2026View details →

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