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Misincorporation Proteomics Technologies: A Review
 
 
Correction to Proteomes 2021, 9(1), 2.
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Correction

Correction: Steele et al. Misincorporation Proteomics Technologies: A Review. Proteomes 2021, 9, 2

1
Proteomics Core Facility and School of Life Sciences, The University of Technology Sydney, Ultimo, NSW 2007, Australia
2
Neurotoxin Research Group, School of Life Sciences, The University of Technology Sydney, Ultimo, NSW 2007, Australia
*
Author to whom correspondence should be addressed.
Proteomes 2022, 10(2), 22; https://doi.org/10.3390/proteomes10020022
Submission received: 12 May 2022 / Accepted: 16 May 2022 / Published: 16 June 2022
(This article belongs to the Special Issue Proteomics: Technologies and Their Applications)

Error in Table

In the original publication, there was a mistake in Table 2 as published [1]. There were spelling/typographical errors that led to incorrect information to align to the wrong amino acid. Therefore, unfortunately the assignments are incorrect. We have restored the correct assignments and ensured the fidelity of the table. The core idea behind the table is unchanged by the correction, as it was only used to provide examples of PTMs that are found on amino acids; as such, the correct reformatting does not impact the concepts/ideas/message provided by this review in any way. The corrected Table 2 appears below.
The authors apologize for any inconvenience caused and state that the scientific conclusions are unaffected. The original publication has also been updated.

Reference

  1. Steele, J.R.; Italiano, C.J.; Phillips, C.R.; Violi, J.P.; Pu, L.; Rodgers, K.J.; Padula, M.P. Misincorporation Proteomics Technologies: A Review. Proteomes 2021, 9, 2. [Google Scholar] [CrossRef]
Table 2. Amino acids and their biological post-translational modifications.
Table 2. Amino acids and their biological post-translational modifications.
Site of ModificationLetter SymbolModification
AlanineACarbonylation
ArginineRHydroxylation, Phosphorylation, Methylation, ADP-ribosylation, Citrullination, Carbonylation
AsparagineNHydroxylation, Methylation, N-linked glycosylation
Aspartic acidDHydroxylation, Phosphorylation, Methylation
Cysteine CHydroxylation, Phosphorylation, Methylation, Sulfation, Myristoylation, ADP-ribosylation, Nitrosylation
Glutamic acid EPhosphorylation, Methylation, ADP-ribosylation
GlutamineQMethylation, Carbonylation
GlycineGMyristoylation
HistidineHPhosphorylation, Methylation
IsoleucineIMethylation, Carbonylation
LeucineLMethylation
LysineKHydroxylation, Phosphorylation, Methylation, Ubiquitination, Myristoylation, ADP-ribosylation, Carbonylation, Malonylation, Succinylation, Glutarylation, Biotinylation
MethionineMHydroxylation
PhenylalanineFHydroxylation
ProlinePHydroxylation
Serine SPhosphorylation, Methylation, Sulfation, O-linked glycosylation, Carbonylation, Decanoylation
SelenocysteineUHydroxylation
ThreonineTPhosphorylation, Methylation, Sulfation, O-linked glycosylation, Decanoylation
TryptophanWGlycosylation, Bromination, Quinone
Tyrosine YHydroxylation, Phosphorylation, Sulfation, O-linked glycosylation, Quinone
ValineVHydroxylation, Carbonylation
The table provides context for how a misincorporation at a particular site could have large biological impacts on cell function [58].
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MDPI and ACS Style

Steele, J.R.; Italiano, C.J.; Phillips, C.R.; Violi, J.P.; Pu, L.; Rodgers, K.J.; Padula, M.P. Correction: Steele et al. Misincorporation Proteomics Technologies: A Review. Proteomes 2021, 9, 2. Proteomes 2022, 10, 22. https://doi.org/10.3390/proteomes10020022

AMA Style

Steele JR, Italiano CJ, Phillips CR, Violi JP, Pu L, Rodgers KJ, Padula MP. Correction: Steele et al. Misincorporation Proteomics Technologies: A Review. Proteomes 2021, 9, 2. Proteomes. 2022; 10(2):22. https://doi.org/10.3390/proteomes10020022

Chicago/Turabian Style

Steele, Joel R., Carly J. Italiano, Connor R. Phillips, Jake P. Violi, Lisa Pu, Kenneth J. Rodgers, and Matthew P. Padula. 2022. "Correction: Steele et al. Misincorporation Proteomics Technologies: A Review. Proteomes 2021, 9, 2" Proteomes 10, no. 2: 22. https://doi.org/10.3390/proteomes10020022

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