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Differential bicodon usage in lowly and highly abundant proteins
(PeerJ, 2017-03)
Degeneracy in the genetic code implies that different codons can encode the same amino acid. Usage preference of synonymous codons has been observed in all domains of life. There is much evidence suggesting that this bias ...
ER chaperones in neurodegenerative disease: Folding and beyond
(2016)
Proteins along the secretory pathway are co-translationally translocated into the lumen of the endoplasmic reticulum (ER) as unfolded polypeptide chains. Afterwards, they are usually modified with N-linked glycans, correctly ...
Bicodon bias can determine the role of synonymous SNPs in human diseases
(BioMed Central, 2017-03)
Background: For a long time synonymous single nucleotide polymorphisms were considered as silent mutations. However, nowadays it is well known that they can affect protein conformation and function, leading to altered ...
ER chaperones in neurodegenerative disease: Folding and beyond
(2016)
Proteins along the secretory pathway are co-translationally translocated into the lumen of the endoplasmic reticulum (ER) as unfolded polypeptide chains. Afterwards, they are usually modified with N-linked glycans, correctly ...
ER chaperones in neurodegenerative disease: Folding and beyond
(Elsevier, 2016)
Proteins along the secretory pathway are co-translationally translocated into the lumen of the endoplasmic reticulum (ER) as unfolded polypeptide chains. Afterwards, they are usually modified with N-linked glycans, correctly ...
Glycoprotein-folding quality control in the endoplasmic reticulum
(De Gruyter, 2012)
Nearly one third of proteins synthesized by eukaryotic cells belong to the secretory pathway, gaining access to the endoplasmic reticulum (ER) either co- or post-translationally. In the ER disulfide bonds are formed, ...