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The finding of a functional variant, which alters protein function, would greatly enhance our understanding of the mechanisms of albumin excretion in kidney health and disease.
Nevertheless, mutational studies on at least five different proteins with conserved codon repeats have demonstrated that alteration in amino acid repeat length alters protein function [ 29, 56].
However, regardless of the type or cause of such a mutation, it usually changes the amino acid sequence of the encoded protein and thus alters protein function.
The recombinant EAP-S102L construct is perhaps the first functional binding protein derived from a native enzyme, illustrating how one single mutation tremendously alters protein function.
Lipid electrophile modification of nucleic acids can induce base-pair substitutions, frameshift mutations, and strand breaks, whereas modification of proteins distorts tertiary structure and alters protein function.
Tyrosine nitration, a chemically stable marker of oxidative stress, alters protein function, and is extensively associated with tumor inflammation and neurodegenerative disease.
Similar(47)
Mutation and domain shuffling together with other genetic events can create functional variation and in some cases completely alter protein function.
PTMs alter protein function by introducing structural changes through the addition or removal of covalently-attached functional groups on the amino acid chain.
Most of the FGF17 and IL17RD mutations altered protein function in vitro.
This induces the irreversible formation of advanced glycation end products (AGE), which may alter protein function and protein degradation.
A major challenge is to define how certain reactive intermediates may chemically modify critical proteins and how modification of specific amino acids may alter protein function which in turn may affect cell signalling, regulation, defence, function and viability.
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