as·pa·rag·i·nyl (N, N),

The aminoacyl radical of asparagine.
Farlex Partner Medical Dictionary © Farlex 2012
References in periodicals archive ?
Succinimide formation from aspartyl and asparaginyl peptides as a model for the spontaneous degradation of proteins.
Legumain (LGMN) also known as asparaginyl endopeptidase (AEP) is implicated in various cancer such as prostrate, breast, colon, lung, ovarian, central nervous system (CNS) related cancers, melanoma and lymphoma (1).
The most common is Jo-1 (histidyl) (15%-30% prevalence), followed by PL-7 (threonyl) and PL-12 (alanyl), with a prevalence of 5% to 10%, followed by EJ (glycyl), OJ (isoleucyl), KS (asparaginyl), Zo (phenylalanyl), and YRS (tyrosyl) (all with prevalences of 1%-5%).
Schachner, "The asparaginyl endopeptidase legumain is essential for functional recovery after spinal cord injury in adult zebrafish," PLoS One, vol.
LGMN, legumain, has a strict specificity for hydrolysis of asparaginyl bonds required for normal lysosomal protein degradation in renal proximal tubules and plays a role in the regulation of cell proliferation via its role in EGFR degradation; VDR, vitamin D (1,25-dihydroxyvitamin D3), is a nuclear receptor that mediates the action of vitamin D3 by controlling the expression of hormone-sensitive genes and plays a central role in calcium homeostasis; HP, haptoglobin, captures and combines with free plasma hemoglobin to allow hepatic recycling of heme iron and to prevent kidney damage.
Morgenstern et al., "A radiolabeled fully human antibody to human aspartyl (asparaginyl) jhydroxylase is a promising agent for imaging and therapy of metastatic breast cancer," Cancer Biotherapy & Radiopharmaceuticals, vol.
Houk, "Neighboring side chain effects on asparaginyl and aspartyl degradation: an Ab initio study of the relationship between peptide conformation and backbone NH acidity," Journal of the American Chemical Society, vol.
Kinetics of deamidation of an asparaginyl residue in a model hexapeptide." Pharmaceutical Research 7, (1990): 703-711
Deamidation of glutaminyl and asparaginyl residues in peptides and proteins.
Proteomics-based identification of novel factor inhibiting hypoxia-inducible factor (FIH) substrates indicates widespread asparaginyl hydroxylation of ankyrin repeat domain-containing proteins.
Transient metal ions like nickel and cobalt are known to mimic cellular hypoxia mainly due to the inhibition of prolyl hydrolases (PDHs) and asparaginyl hydrolase (factor-inhibiting HIF (FIH)).

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