Sentence examples for mutation of aspartic from inspiring English sources

Mutation of aspartic acid 187 to asparagine (D187N) or tyrosine (D187Y) in domain 2 of the actin-modulating protein gelsolin causes the neurodegenerative disease familial amyloidosis of Finnish type (FAF).

Thus, the mutation of aspartic acid 469 to a glycine residue allows Chk1 to respond to UV irradiation and CPT treatment to maintain checkpoint function.

Activating mutations in rolled, the fly ortholog of ERK, were initially identified from fly screens of EGFR mutants and subsequently shown to result from a mutation of aspartic acid to asparagine at amino acid 334 (Brunner et al., 1994).

However, mutation of aspartic acid 139 to glutamate and alanine shows a moderate impairment of iron binding, corresponding to an approximate 4-fold increase in Kd for D139E and a 6-fold increase in Kd for D139A.

The substantial changes we observed in kcat as a result of mutation of aspartic acid 139 in cPAH raised the possibility that destabilization of iron binding in the active site could be contributing to the reduction in enzymatic activity.

However, it was also clear that a contiguous stretch of MED-associated mutations were present in both the N- and C-type motifs of the T34 repeat and of the 33 mutations in nine codons, 27 were reported to have caused MED, whereas the mutation of aspartic acid at residue 376 was associated with MED in three cases and a single PSACH patient.

In conclusion, we have shown that the mutations of aspartic acid 139 in the second coordination sphere of cPAH do not affect the enzyme's ability to bind its substrate, phenylalanine, but instead influence both iron and cofactor binding.

These data clearly show that mutation of the aspartic acid residues that are seen to interact with the ribose moiety of AXPs and NADH do not lead to the ablation of ligand binding.

However, mutation of the aspartic acid residue at position 54 to a glutamic acid (MNV/SVD2/D54E) resulted in increased cleavage at the NS5NS6 boundary, yielding mature NS6 to levels similar to that observed in the double domain swap chimaeric construct (11±5% compared with 10±7% for MNV/DV2D/D54E and MNV/SVD2, respectively).

Conversely, S18 de-phosphorylation may increase Hausp Cry1 association because mutation of S18 to the non-phosphorylatable amino acid alanine (S18A) increases interaction and mutation to aspartic acid, which is chemically similar to phospho-serine, decreases the interaction.

Furthermore, the triple mutation to aspartic acid (DDD) caused a 95% reduction in the 5HT uptake capacity of SERT (Fig. 5A), possibly indicating a synergistic relationship between these three positions.