Different Molecular Consequences of Frameshift Mutations in theANTXR2Gene
نویسندگان
چکیده
منابع مشابه
Molecular misreading: the occurrence of frameshift proteins in different diseases.
Neuronal homoeostasis requires a constant balance between biosynthetic and catabolic processes. Eukaryotic cells primarily use two distinct mechanisms for degradation: the proteasome and autophagy of aggregates by the lysosomes. We focused on the UPS (ubiquitin-proteasome system). As a result of molecular misreading, misframed UBB (ubiquitin B) (UBB+1) is generated. UBB+1 accumulates in the neu...
متن کاملMitochondrial Genomes and Frameshift Mutations: Hidden Stop Codons, their Functional Consequences and Disease Associations
Mitochondria are the power house of the cell. They are present in virtually every cell in body. They play a central role in metabolism, apoptosis, disease and aging. They are the site of oxidative phosphorylation, essential for the production of ATP, as well as for other biochemical functions. Mitochondria have a genome separate from the nuclear genome referred to as mitochondrial DNA (mt DNA)....
متن کاملFunctional divergence of proteins through frameshift mutations.
Frameshift mutations are generally considered to be deleterious and of little importance for the evolution of novel gene functions. However, by screening an exhaustive set of vertebrate gene families, we found that, when a second transcript encoding the original gene product compensates for this mutation, frameshift mutations can be retained for millions of years and enable new gene functions t...
متن کاملReversion of Frameshift Mutations Stimulated by Lesions
Temperature-sensitive (ts) mutants representative of a number of genes of phage T4 were crossed with rII mutants to allow isolation of ts, rII double-mutant recombinants. The rl mutations used were characterized as frameshift mutations primarily on the basis of their revertability by proflavine. For each ts, rII double mutant, the effect of the ts mutation on spontaneous reversion of the rII mu...
متن کاملMolecular pathogenesis of a disease: structural consequences of aspartylglucosaminuria mutations.
A deficiency of functional aspartylglucosaminidase (AGA) causes a lysosomal storage disease, aspartylglucosaminuria (AGU). The recessively inherited disease is enriched in the Finnish population, where 98% of AGU alleles contain one founder mutation, AGU(Fin). Elsewhere in the world, we and others have described 18 different sporadic AGU mutations. Many of these are predicted to interfere with ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Human Mutation
سال: 2013
ISSN: 1059-7794
DOI: 10.1002/humu.22190