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ProteomicsPerserverence of protein homeostasis despite mistranslation of glycine codons with alanine
By physically linking amino acids to their codon assignments, transfer RNAs (tRNAs) are essential for protein synthesis and translation fidelity. Some natural human tRNA variants cause amino acid mis-incorporation at a codon or set of codons. Recent work showed a naturally occurring tRNASer variant ...
ORGANISM(S): Mus musculus (Mouse) 
2024-05-21 | PXD034180 | Pride
Trna Amino acid misincorporation Mistranslation 
ProteomicsRepeat length of the C9orf72-associated glycine-alanine polypeptides affects their toxicity
G4C2 hexanucleotide repeat expansions in a non-coding region of the C9orf72 gene are the most common cause of familial amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). G4C2 insertion length is variable, and patients can carry up to several thousand repeats. Dipeptide repeat pro...
ORGANISM(S): Drosophila melanogaster (Fruit fly) 
2023-09-12 | PXD038900 | Pride
Toxicity Repeat length Drosophila C9orf72 Glycine-alanine 
UnknownConformational entropy of alanine versus glycine in protein denatured states.
Not available
S-EPMC1815238 | biostudies-literature
Unknownald of Mycobacterium tuberculosis encodes both the alanine dehydrogenase and the putative glycine dehydrogenase.
Not available
S-EPMC3294785 | biostudies-literature
UnknownDegradation of glycine and alanine on irradiated quartz.
Not available
S-EPMC3676737 | biostudies-literature
ProteomicsInclusion bodies formed by polyglutamine and poly(glycine-alanine) are enriched with distinct proteomes but converge in proteins that are risk factors for disease and involved in protein degradation
Poly(glycine-alanine) (polyGA) is one of the dipolypeptides expressed in Motor Neuron Disease caused by C9ORF72 mutations and accumulates as inclusion bodies in the brain of patients. Superficially these inclusions are similar to those formed by polyglutamine (polyQ) in Huntington’s disease and both...
ORGANISM(S): Mus musculus (Mouse) 
2020-08-18 | PXD018824 | Pride
Huntington Aggregates C9prf72 Polyga 
ProteomicsInclusion bodies formed by polyglutamine and poly(glycine-alanine) are enriched with distinct proteomes but converge in proteins that are risk factors for disease and involved in protein degradation
Poly(glycine-alanine) (polyGA) is one of the dipolypeptides expressed in Motor Neuron Disease caused by C9ORF72 mutations and accumulates as inclusion bodies in the brain of patients. Superficially these inclusions are similar to those formed by polyglutamine (polyQ) in Huntington’s disease and bot...
ORGANISM(S): Mus musculus (Mouse) 
2020-08-18 | PXD018505 | Pride
Huntington C9orf72 Chaperones Proteosome Inclusions 
UnknownLow-Molecular-Weight Fish Collagen Peptide (Valine-Glycine-Proline-Hydroxyproline-Glycine-Proline-Alanine-Glycine) Prevents Osteoarthritis Symptoms in Chondrocytes and Monoiodoacetate-Injected Rats.
Not available
S-EPMC10744650 | biostudies-literature
UnknownMelting properties of peptides and their solubility in water. Part 1: dipeptides based on glycine or alanine.
Not available
S-EPMC9073158 | biostudies-literature
UnknownGlycine-alanine repeats impair proper substrate unfolding by the proteasome.
Not available
S-EPMC1440830 | biostudies-literature
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