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UnknownRepression of p53 function by SIRT5-mediated desuccinylation at Lysine 120 in response to DNA damage.
Not available
S-EPMC8989948 | biostudies-literature
UnknownImprovement mechanism of cellulose nanocrystal in coordination with calcium ions on the thermal gelation of soybean protein amyloid fibrils.
Not available
S-EPMC12663481 | biostudies-literature
MetabolomicsPlasma metabolome alteration in dairy cows with left displaced abomasum before and after surgical correction
Left displaced abomasum (LDA) leads to substantial changes in the metabolism of dairy cows. Surgical correction of LDA can rapidly improve the health of cows; however, changes in metabolism following surgery are rarely described. To investigate the changes of plasma metabolome in cows with LDA befor...
2022-08-17 | MTBLS4126 | MetaboLights
UnknownEffects of Copper Dopants on the Magnetic Property of Lightly Cu-Doped ZnO Nanocrystals.
Not available
S-EPMC7466550 | biostudies-literature
UnknownEGLN1 prolyl hydroxylation of hypoxia-induced transcription factor HIF1α is repressed by SET7-catalyzed lysine methylation.
Not available
S-EPMC9123262 | biostudies-literature
ProteomicsRepression of EGLN1 activity by SET7-catalyzed methylation
Repression of EGLN1 activity by SET7-catalyzed methylation
ORGANISM(S): Homo Sapiens 
2022-03-08 | PXD032126 |
MetabolomicsPu-erh tea and theabrownin ameliorate metabolic syndrome in mice via potential microbiota-gut-liver-brain interactions
Metabolic syndrome (MS) is a common metabolic disorder characterized by obesity, insulin resistance, cardiovascular disease and gut microbiota dysbiosis. Pu-erh tea and its ingredient theabrownin have known functions on the reduction of body weight gain and fat accumulation. However, few studies sys...
2024-09-25 | MTBLS2594 | MetaboLights
UnknownHydrochemical characteristics of surface waters and their relationships to the Kashin-Beck Disease in Longzi County, Tibet.
Not available
S-EPMC9098842 | biostudies-literature
ProteomicsIdentification of IRF3 hydroxylation site
Identification of IRF3 hydroxylation site in cells
ORGANISM(S): Homo Sapiens 
2024-03-12 | PXD050566 |
UnknownA three-level regulatory mechanism of the aldo-keto reductase subfamily AKR12D.
Not available
S-EPMC10923870 | biostudies-literature
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