posttranslational


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post·trans·la·tion·al

 (pōst′trăns-lā′shə-nəl, -trănz-)
adj.
Of or relating to a substance or process, such as the addition of sugar groups to form a glycoprotein, that occurs or is formed after translation of protein: a posttranslational modification.

post•trans•la•tion•al

(ˌpoʊst trænsˈleɪ ʃə nl, -trænz-)

adj.
occurring after amino acids have begun to form polypeptide chains in protein synthesis.
[1970–75]
References in periodicals archive ?
Catalysis leads to posttranslational inactivation of the type 1 deiodinase and alters its conformation.
Study Selection: Literature search was based on the following keywords: Alzheimer's disease, tau protein, biomarker, cerebrospinal fluid (CSF), therapeutics, plasma, imaging, propagation, spreading, seeding, prion, conformational templating, and posttranslational modification.
Protein tyrosine phosphorylation is a posttranslational modification that is important for the regulation and coordination of various cell proliferations, divisions, growths, and differentiations in normal and cancer cells (Hunter & Cooper, 1985; Hunter, 1987; Hanks et al.
Although functional analysis exhibit miscellaneous posttranslational deformities, which lead to, gain of glycosylation and loss of ubiquitination at some peculiar amino acid residues.
In turn, protein function is regulated by small molecular change known as posttranslational modifications, which cannot be detected in the DNA or RNA.
Objective: Posttranslational modification (PTM) of proteins by ubiquitin family proteins is of fundamental importance for cellular function, regulation and development.
This posttranslational modification reflects average glucose concentrations over the previous 14-21 days (equivalent to the half-life of albumin).
found that daily topical application of 5% L-ascorbic acid enhanced the levels of procollagen types I and III, their posttranslational maturation enzymes, and tissue inhibitor of matrix metalloproteinase.
By inhibiting HMG-CoA reductase, statins lower production of farnesyl pyrophosphate and geranylgeranyl pyrophosphate, which are needed for posttranslational activation of Ras, Rho, and other proteins that are overexpressed in CRC and that have been linked to tumor invasion.
At the beginning a basic protein structure is translated from a DNA sequence followed by changes in the structure of basic protein called posttranslational modifications.
It addresses the chemistry and cellular localization of polyamines; mechanisms of biosynthesis, their interconversion, and degradation in fungi, in comparison with animal and plant cells; polyamine distribution in the fungal kingdom as compared to other eukaryotic organisms; regulatory mechanisms of polyamine metabolism at the transcriptional, translational, and posttranslational levels in fungi and other organisms; general functions of polyamines, their possible modes of action, and their role in cell differentiation and morphogenesis in fungi and other organisms; and polyamine metabolism as a target for disease.
It was found that posttranslational modifications of these proteins by ROS/RNS are responsible for the development of CVD [41,42].
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