lipidation

lipidation

See Protein lipidation.
McGraw-Hill Concise Dictionary of Modern Medicine. © 2002 by The McGraw-Hill Companies, Inc.
References in periodicals archive ?
Some of the functions of these blood-brain barriers are as follows: Protecting brain health by preventing pathogens (most common infectious bacteria and viruses and other pathogens) from entering the brain Excluding and metabolizing neurotoxic compounds (drugs, antibodies and plasma proteins) and neurotransmitters from brain and blood Safeguarding neurons' ion balances Some of the major approaches in solving the blood-brain barrier (BBB) problems are lipidation, craniotomy-based drug delivery, BBB disruption, and cationic import peptides.
ARFRP1 (GO:0005525, 0007264, 0034067, 0043001, 0042147, 0007369, 0005802, 0016020, 0005829) is required for the lipidation of chylomicrons in the intestine and required for very low density lipoprotein (VLDL) lipidation in the liver [25], TNFRSF6B might have role in response to lipopolysaccharide according to one of the GO annotations (GO:0032496).
Pre[[beta].sub.1]-HDL is the first product of lipidation of minimally lipidated apoA-I and a likely acceptor of cellular cholesterol.
Approximately one-third of all proteins synthesized in the cell travel across the ER where they are folded into their proper three-dimensional structures with posttranslational modifications including disulfide bond formation, glycosylation, hydroxylation, and lipidation. Protein folding in the ER is subject to numerous insults such as increased mRNA translation, elevated demand of protein secretion, genetic mutations of client proteins, deficiency of ER chaperones or foldases, ER redox or calcium perturbations, bacterial and viral infection, ATP depletion, nutrient deficiency, and pharmacological and toxicological insults.
Smith, "ABCA1 mediates unfolding of apolipoprotein AI N terminus on the cell surface before lipidation and release of nascent high-density lipoprotein," Arteriosclerosis, Thrombosis, and Vascular Biology, vol.
APOE adjusts the combination of A[beta] through lipidation [43], and it combines with A[beta] in the form of a molecular chaperone to influence the elimination of A[beta].
Takao et al., "A ubiquitin-like system mediates protein lipidation," Nature, vol.
In addition, proteins can be modified by the covalent attachment of different lipid moieties such as GPI, myristate, palmitate, and stearate (i.e., protein lipidation).
LC3-postive structures include double-membrane autophagosome, autophagosome-like structure, noncanonical LC3 lipidation, and LC3-associated phagocytosis [42].
Many other types of PTMs (such as phosphorylation, glycosylation, ubiquitination, methylation, acetylation, and lipidation) play important roles in the regulation of gene function (Cain et al., 2014), protein degradation (Geiss-Friedlander and Melchior, 2007), cellular differentiation (Grotenbreg and Ploegh, 2007), and signaling (Morrison et al., 2002; Jensen, 2004).
This event involves the formation of an Atg7-dependent conjugated system (Atg12-Atg5), which is responsible for LC3 lipidation by phosphatidylethanolamine.
Jeppesen et al., "Role of AMPK in regulation of LC3 lipidation as a marker of autophagy in skeletal muscle," Cellular Signalling, vol.