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. 2011 Dec 29;7(12):e1002285. doi: 10.1371/journal.pcbi.1002285

Table 5. Comparative studies for occupied and non-occupied N-glycan sites.

Description Reference
Influence of proline residue neighboring the Asn-x-Ser and the Asn-x-Thr sequons over N-glycosylation in the yeast invertase protein. [43]
Relevance of certain amino acid substitutions at the position +1 in the Asn-x-Ser sequon for N-glycosylation efficiency in the rabies virus glycoprotein. [44]
Relevance of certain amino acid substitutions at the position +1 in the Asn-x-Ser and the Asn-x-Thr sequons for N-glycosylation efficiency using different variants of rabies virus glycoprotein. [45]
Influence of the 20 amino acids at the position following the Asn-x-Ser and Asn-x-Thr sequons for N-glycosylation efficiency using different variants of rabies virus glycoprotein. [46]
Occurrence frequency analysis of some amino acid residues at position +1 in the Asn-x-Ser and Asn-x-Thr sequons studying glycoproteins from the PDB database [47]. [48]
Influence of the 20 amino acids flanking the upstream and downstream of Asn-x-Ser and Asn-x-Thr sequons, using glycoproteins from the UniProtKB/Swiss-Prot database [11]. [19]
Primary, secondary, and tertiary structures statistical analysis of occupied and non-occupied N-glycosylation sites using glycoproteins from the PDB database [47]. [49]