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Relevant bibliographies by topics / Ursodeoxycholic Acid Conjugates

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Academic literature on the topic 'Ursodeoxycholic Acid Conjugates'

Author: Grafiati

Published: 7 June 2025

Last updated: 2 August 2025

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Journal articles on the topic "Ursodeoxycholic Acid Conjugates"

1

Maeda, Yorinobu, and Teruo Murakami. "Diagnosis by Microbial Culture, Breath Tests and Urinary Excretion Tests, and Treatments of Small Intestinal Bacterial Overgrowth." Antibiotics 12, no. 2 (2023): 263. http://dx.doi.org/10.3390/antibiotics12020263.

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Small intestinal bacterial overgrowth (SIBO) is characterized as the increase in the number and/or alteration in the type of bacteria in the upper gastrointestinal tract and accompanies various bowel symptoms such as abdominal pain, bloating, gases, diarrhea, and so on. Clinically, SIBO is diagnosed by microbial culture in duodenum/jejunum fluid aspirates and/or the breath tests (BT) of hydrogen/methane gases after ingestion of carbohydrates such as glucose. The cultural analysis of aspirates is regarded as the golden standard for the diagnosis of SIBO; however, this is invasive and is not wit

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2

Wang, Rui, Jiaquan Wu, David Kin Jin та ін. "Structure of NADP+-bound 7β-hydroxysteroid dehydrogenase reveals two cofactor-binding modes". Acta Crystallographica Section F Structural Biology Communications 73, № 5 (2017): 246–52. http://dx.doi.org/10.1107/s2053230x17004460.

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In mammals, bile acids/salts and their glycine and taurine conjugates are effectively recycled through enterohepatic circulation. 7β-Hydroxysteroid dehydrogenases (7β-HSDHs; EC 1.1.1.201), including that from the intestinal microbeCollinsella aerofaciens, catalyse the NADPH-dependent reversible oxidation of secondary bile-acid products to avoid potential toxicity. Here, the first structure of NADP+bound to dimeric 7β-HSDH is presented. In one active site, NADP+adopts a conventional binding mode similar to that displayed in related enzyme structures. However, in the other active site a unique b

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3

Marchesi, Elena, Rita Cortesi, Lorenzo Preti, et al. "Antisense Oligonucleotides Conjugated with Lipophilic Compounds: Synthesis and In Vitro Evaluation of Exon Skipping in Duchenne Muscular Dystrophy." International Journal of Molecular Sciences 23, no. 8 (2022): 4270. http://dx.doi.org/10.3390/ijms23084270.

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Our groups previously reported that conjugation at 3′-end with ursodeoxycholic acid (UDCA) significantly enhanced in vitro exon skipping properties of ASO 51 oligonucleotide targeting the human DMD exon 51. In this study, we designed a series of lipophilic conjugates of ASO 51, to explore the influence of the lipophilic moiety on exon skipping efficiency. To this end, three bile acids and two fatty acids have been derivatized and/or modified and conjugated to ASO 51 by automatized solid phase synthesis. We measured the melting temperature (Tm) of lipophilic conjugates to evaluate their ability

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4

Bouscarel, B., S. Ceryak, T. W. Gettys, H. Fromm, and F. Noonan. "Alteration of cAMP-mediated hormonal responsiveness by bile acids in cells of nonhepatic origin." American Journal of Physiology-Gastrointestinal and Liver Physiology 268, no. 6 (1995): G908—G916. http://dx.doi.org/10.1152/ajpgi.1995.268.6.g908.

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The present study was undertaken to determine whether bile acids could inhibit hormone-induced adenosine 3',5'-cyclic monophosphate (cAMP) production in cells of nonhepatic origin, as previously reported in the liver [Bouscarel et al., Am. J. Physiol. 268 (Gastrointest. Liver Physiol. 31): G300-G310, 1995]. The bile acids, ursodeoxycholic acid (UDCA), chenodeoxycholic acid, and deoxycholic acid inhibited prostaglandin E1 (PGE1)- and isoproterenol-induced cAMP production by 40-60% in human skin fibroblasts and human umbilical vein endothelial cells, respectively, to a similar extent as that obs

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5

Maevskay, M. V. "Ursodeoxycholic acid: unique properties and clinical applications." Meditsinskiy sovet = Medical Council, no. 8 (May 25, 2023): 96–105. http://dx.doi.org/10.21518/ms2023-136.

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Ursodeoxycholic acid (UDCA) is a natural hydrophilic bile acid, which is present in humans as a small fraction of the total amount of bile acids (5%). Its unique properties underlie its use in a number of liver diseases as a first-line therapy. The ability of UDCA to reduce the secretion of cholesterol into bile, form mixed micelles (liquid crystals) with cholesterol molecules and interact with multifunctional nuclear receptors, are actively used in the treatment and prevention of cholelithiasis. UDCA has the ability to stimulate hepatobiliary secretion, promotes the secretion of bicarbonate b

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6

Odermatt, Alex, Thierry Da Cunha, Carlos A. Penno та ін. "Hepatic reduction of the secondary bile acid 7-oxolithocholic acid is mediated by 11β-hydroxysteroid dehydrogenase 1". Biochemical Journal 436, № 3 (2011): 621–29. http://dx.doi.org/10.1042/bj20110022.

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The oxidized bile acid 7-oxoLCA (7-oxolithocholic acid), formed primarily by gut micro-organisms, is reduced in human liver to CDCA (chenodeoxycholic acid) and, to a lesser extent, UDCA (ursodeoxycholic acid). The enzyme(s) responsible remained unknown. Using human liver microsomes, we observed enhanced 7-oxoLCA reduction in the presence of detergent. The reaction was dependent on NADPH and stimulated by glucose 6-phosphate, suggesting localization of the enzyme in the ER (endoplasmic reticulum) and dependence on NADPH-generating H6PDH (hexose-6-phosphate dehydrogenase). Using recombinant huma

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7

Bouscarel, B., H. Fromm, S. Ceryak, and M. M. Cassidy. "Ursodeoxycholic acid increases low-density lipoprotein binding, uptake and degradation in isolated hamster hepatocytes." Biochemical Journal 280, no. 3 (1991): 589–98. http://dx.doi.org/10.1042/bj2800589.

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Ursodeoxycholic acid (UDCA), in contrast to both chenodeoxycholic acid (CDCA), its 7 alpha-epimer, and lithocholic acid, enhanced receptor-dependent low-density lipoprotein (LDL) uptake and degradation in isolated hamster hepatocytes. The increase in cell-associated LDL was time- and concentration-dependent, with a maximum effect observed at approx. 60 min with 1 mM-UDCA. This increase was not associated with a detergent effect of UDCA, as no significant modifications were observed either in the cellular release of lactate dehydrogenase or in Trypan Blue exclusion. The effect of UDCA was not d

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8

Iwaki, Tomomichi, Norio Miyazawa, Hiromi Hasegawa, Hirao Sakakuta, Norio Hirabayashi, and Hiroshi Kasai. "The choleretic effect of N-acetylglucosamine conjugates of Ursodeoxycholic acid (UDCA) in bile fistura rats." Japanese Journal of Pharmacology 73 (1997): 219. http://dx.doi.org/10.1016/s0021-5198(19)45378-x.

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9

Hata, Soichiro, Pijun Wang, Nicole Eftychiou, et al. "Substrate specificities of rat oatp1 and ntcp: implications for hepatic organic anion uptake." American Journal of Physiology-Gastrointestinal and Liver Physiology 285, no. 5 (2003): G829—G839. http://dx.doi.org/10.1152/ajpgi.00352.2002.

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Transport of a series of3H-radiolabeled C23, C24, and C27bile acid derivatives was compared and contrasted in HeLa cell lines stably transfected with rat Na+/taurocholate cotransporting polypeptide (ntcp) or organic anion transporting polypeptide 1 (oatp1) in which expression was under regulation of a zinc-inducible promoter. Similar uptake patterns were observed for both ntcp and oatp1, except that unconjugated hyodeoxycholate was a substrate of oatp1 but not ntcp. Conjugated bile acids were transported better than nonconjugated bile acids, and the configuration of the hydroxyl groups (α or β

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10

Bouscarel, B., H. Fromm, and R. Nussbaum. "Ursodeoxycholate mobilizes intracellular Ca2+ and activates phosphorylase a in isolated hepatocytes." American Journal of Physiology-Gastrointestinal and Liver Physiology 264, no. 2 (1993): G243—G251. http://dx.doi.org/10.1152/ajpgi.1993.264.2.g243.

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In isolated hamster hepatocytes, ursodeoxycholic acid (UDCA) mobilized intracellular free calcium ([Ca2+]i) and activated phosphorylase a with a half-maximally effective concentration of 188 and 9 microM, respectively. Addition of ethylene glycol-bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid (EGTA) did not affect the maximum [Ca2+]i mobilized by UDCA; however, [Ca2+]i returned to basal levels in 4-5 min compared with > 10 min in the absence of EGTA. Both UDCA and vasopressin activated phosphorylase a to the same extent in the presence and absence of extracellular Ca2+, and the effec

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