Relevant bibliographies by topics / Serotonylation

Academic literature on the topic 'Serotonylation'

Author: Grafiati
Published: 10 December 2022
Last updated: 29 January 2023

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Journal articles on the topic "Serotonylation"

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Williams, Erin R. "Chromatin serotonylation limits differentiation." Science Signaling 12, no. 576 (April 9, 2019): eaau2218. http://dx.doi.org/10.1126/scisignal.aau2218.

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Penumatsa, K. C., and B. L. Fanburg. "Transglutaminase 2-mediated serotonylation in pulmonary hypertension." American Journal of Physiology-Lung Cellular and Molecular Physiology 306, no. 4 (February 15, 2014): L309—L315. http://dx.doi.org/10.1152/ajplung.00321.2013.

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The monoamine serotonin (5-HT) has been previously implicated in pulmonary arterial remodeling and is considered a potential therapeutic target for the disease pulmonary arterial hypertension (PAH). More recently, it has been recognized that the enzyme tissue transglutaminase (TG2) mediates cross-linking of proteins with 5-HT, a posttranslational process of monoaminylation known as “serotonylation.” TG2 activity and serotonylation of protein participate in both smooth muscle proliferation and contraction produced by 5-HT. Indeed, markedly increased TG2 activity has now been identified in lung tissue of an experimental rodent model of pulmonary hypertension, and elevated serotonylation of fibronectin and the signaling molecule Rho, downstream products of transglutamidation, have been found in blood of patients with PAH. The basic mechanism by which TG2 is activated and the potential role(s) of serotonylated proteins in pulmonary hypertension remain a mystery. In the present review we have tried to address the current understanding of 5-HT metabolism in pulmonary hypertension and relate it to what is currently known about the evolving cellular process of serotonylation.
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Abdala-Valencia, Hiam, Sergejs Berdnikovs, Christine A. McCary, Daniela Urick, Riti Mahadevia, Michelle E. Marchese, Kelsey Swartz, Lakiea Wright, Gökhan M. Mutlu, and Joan M. Cook-Mills. "Inhibition of allergic inflammation by supplementation with 5-hydroxytryptophan." American Journal of Physiology-Lung Cellular and Molecular Physiology 303, no. 8 (October 15, 2012): L642—L660. http://dx.doi.org/10.1152/ajplung.00406.2011.

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Clinical reports indicate that patients with allergy/asthma commonly have associated symptoms of anxiety/depression. Anxiety/depression can be reduced by 5-hydroxytryptophan (5-HTP) supplementation. However, it is not known whether 5-HTP reduces allergic inflammation. Therefore, we determined whether 5-HTP supplementation reduces allergic inflammation. We also determined whether 5-HTP decreases passage of leukocytes through the endothelial barrier by regulating endothelial cell function. For these studies, C57BL/6 mice were supplemented with 5-HTP, treated with ovalbumin fraction V (OVA), house dust mite (HDM) extract, or IL-4, and examined for allergic lung inflammation and OVA-induced airway responsiveness. To determine whether 5-HTP reduces leukocyte or eosinophil transendothelial migration, endothelial cells were pretreated with 5-HTP, washed and then used in an in vitro transendothelial migration assay under laminar flow. Interestingly, 5-HTP reduced allergic lung inflammation by 70–90% and reduced antigen-induced airway responsiveness without affecting body weight, blood eosinophils, cytokines, or chemokines. 5-HTP reduced allergen-induced transglutaminase 2 (TG2) expression and serotonylation (serotonin conjugation to proteins) in lung endothelial cells. Consistent with the regulation of endothelial serotonylation in vivo, in vitro pretreatment of endothelial cells with 5-HTP reduced TNF-α-induced endothelial cell serotonylation and reduced leukocyte transendothelial migration. Furthermore, eosinophil and leukocyte transendothelial migration was reduced by inhibitors of transglutaminase and by inhibition of endothelial cell serotonin synthesis, suggesting that endothelial cell serotonylation is key for leukocyte transendothelial migration. In summary, 5-HTP supplementation inhibits endothelial serotonylation, leukocyte recruitment, and allergic inflammation. These data identify novel potential targets for intervention in allergy/asthma.
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Zlotorynski, Eytan. "Histone serotonylation boosts neuronal transcription." Nature Reviews Molecular Cell Biology 20, no. 6 (April 3, 2019): 323. http://dx.doi.org/10.1038/s41580-019-0124-4.

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Muma, Nancy A., and Zhen Mi. "Serotonylation and Transamidation of Other Monoamines." ACS Chemical Neuroscience 6, no. 7 (February 5, 2015): 961–69. http://dx.doi.org/10.1021/cn500329r.

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Watts, Stephanie W., Jessica R. C. Priestley, and Janice M. Thompson. "Serotonylation of Vascular Proteins Important to Contraction." PLoS ONE 4, no. 5 (May 25, 2009): e5682. http://dx.doi.org/10.1371/journal.pone.0005682.

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Anastas, Jamie N., and Yang Shi. "Histone Serotonylation: Can the Brain Have “Happy” Chromatin?" Molecular Cell 74, no. 3 (May 2019): 418–20. http://dx.doi.org/10.1016/j.molcel.2019.04.017.

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Lin, Jason Ching-Yao, Chi-Chi Chou, Zhijay Tu, Lun-Fu Yeh, Shang-Chuen Wu, Kay-Hooi Khoo, and Chun-Hung Lin. "Characterization of Protein Serotonylation via Bioorthogonal Labeling and Enrichment." Journal of Proteome Research 13, no. 8 (July 23, 2014): 3523–29. http://dx.doi.org/10.1021/pr5003438.

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Zhao, Shuai, Kelly N. Chuh, Baichao Zhang, Barbara E. Dul, Robert E. Thompson, Lorna A. Farrelly, Xiaohui Liu, et al. "Histone H3Q5 serotonylation stabilizes H3K4 methylation and potentiates its readout." Proceedings of the National Academy of Sciences 118, no. 6 (February 1, 2021): e2016742118. http://dx.doi.org/10.1073/pnas.2016742118.

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Serotonylation of glutamine 5 on histone H3 (H3Q5ser) was recently identified as a permissive posttranslational modification that coexists with adjacent lysine 4 trimethylation (H3K4me3). While the resulting dual modification, H3K4me3Q5ser, is enriched at regions of active gene expression in serotonergic neurons, the molecular outcome underlying H3K4me3–H3Q5ser crosstalk remains largely unexplored. Herein, we examine the impact of H3Q5ser on the readers, writers, and erasers of H3K4me3. All tested H3K4me3 readers retain binding to the H3K4me3Q5ser dual modification. Of note, the PHD finger of TAF3 favors H3K4me3Q5ser, and this binding preference is dependent on the Q5ser modification regardless of H3K4 methylation states. While the activity of the H3K4 methyltransferase, MLL1, is unaffected by H3Q5ser, the corresponding H3K4me3/2 erasers, KDM5B/C and LSD1, are profoundly inhibited by the presence of the mark. Collectively, this work suggests that adjacent H3Q5ser potentiates H3K4me3 function by either stabilizing H3K4me3 from dynamic turnover or enhancing its physical readout by downstream effectors, thereby potentially providing a mechanism for fine-tuning critical gene expression programs.
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Wang, Han-Ming, Wan-Zhu Liu, Fu-Tian Tang, Hai-Juan Sui, Xing-Jie Zhan, and Hong-Xin Wang. "Cystamine slows but not inverses the progression of monocrotaline-induced pulmonary arterial hypertension in rats." Canadian Journal of Physiology and Pharmacology 96, no. 8 (August 2018): 783–89. http://dx.doi.org/10.1139/cjpp-2017-0720.

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Tissue transglutaminase (TG2) plays an important role in pulmonary arterial hypertension (PAH). Previous research indicate that TG2 and protein serotonylation catalyzed by TG2 are upregulated in PAH. Serotonin transporter inhibitor fluoxetine ameliorates PAH via inhibition of protein serotonylation. It is still unknown whether PAH is inhibited through direct inhibition of TG2. Therefore, the present study aimed to investigate the effects of TG2 inhibitor cystamine on monocrotaline-induced PAH in rats. Rats were treated with monocrotaline (60 mg·kg−1, i.p.) in combination with or without cystamine (20, 40 mg·kg−1·day−1, p.o.). The results showed that compared with monocrotaline alone, combination of monocrotaline with cystamine (40 mg·kg−1·day−1, p.o.) relieved right ventricle hypertrophy, inhibited pulmonary arteriolar remodeling, and downregulated protein expression of TG2, phosphorylated protein kinase B (Akt), and extracellular regulated protein kinase (ERK) at day 21. However, except for TG2 expression, these changes were not significantly inhibited by cystamine at day 35. In addition, cystamine dose-dependently enhanced the survival rate of rats injected with monocrotaline at day 35. The findings suggest that cystamine slows but not reverses monocrotaline-induced PAH in rats, which was largely associated with the inhibition of TG2 protein expression and Akt and ERK activation.
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Dissertations / Theses on the topic "Serotonylation"

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林清堯. "Characterization of Transglutaminase-Mediated Protein Serotonylation via Click Chemistry." Thesis, 2014. http://ndltd.ncl.edu.tw/handle/2wqztd.

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Book chapters on the topic "Serotonylation"

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Muma, Nancy A., and Khushboo Kapadia. "Serotonylation and neuronal function." In Handbook of Behavioral Neuroscience, 257–65. Elsevier, 2020. http://dx.doi.org/10.1016/b978-0-444-64125-0.00013-x.

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Conference papers on the topic "Serotonylation"

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Wei, Lin, Rod R. Warburton, Suzy A. Comhair, Serpil C. Erzurum, Nicholas S. Hill, and Barry L. Fanburg. "Association Of Serotonylation Of Fibronectin With Pulmonary Hypertension." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a4956.

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Liu, Y., DL Laskin, and BL Fanburg. "Serotonylation of Proteins in Pulmonary Artery Smooth Muscle Cells." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a2481.

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