Protein posttranslational modifications: the chemistry of proteome diversifications.

By C. Walsh, S. Garneau‐Tsodikova, G. Gatto. Angewandte Chemie, 2005

1,484 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/0cf9253826ab6883fc5e93589532845f1b8373c9

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In Molecular Biology

1. Xuan Xiao
2. Jianhua Jia
3. Zi Liu
4. Bingxiang Liu
5. Kuo-Chen Chou
6. Yingming Zhao
7. Yi Tang
8. Yue Chen

In Oncology

1. Yingming Zhao
2. Yi Tang
3. Yue Chen
4. W. Gu
5. E. Verdin
6. Kuo-Chen Chou
7. S. J. Serrano-Gomez
8. S. Alahari

In Spectroscopy

1. Kuo-Chen Chou

Citations in the corpus

• Lysine Propionylation and Butyrylation Are Novel Post-translational Modifications in Histones*S (2007, background): “lysine, one of the 15 ribosomally coded amino acid residues known to be modified (1).”
• The roles of conditional disorder in redox proteins (2013, background): “These changes can be tightly regulated and are generally faster and energetically less expensive than transcription or translational means of regulation [2].”
• PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse (2011, methodology): “The cellular regulation of post-translational modification [PTMs; (1)] is complex and plays a fundamental role at all levels of biological regulation.”
• pSuc-Lys: Predict lysine succinylation sites in proteins with PseAAC and ensemble random forest approach. (2016, background): “Keywords: Lysine succinylation; Sequence-coupling model; General PseAAC; Random downsampling; Ensemble random forest; pSuc-Lys web-server I. INTRODUCTION In vivo, one of the most efficient biological mechanisms for expanding the genetic code and for regulating cellular physiology is protein post-tra”
• Regulation of epithelial-mesenchymal transition through epigenetic and post-translational modifications (2016, background): “Post translational modifications are covalent modifications that occur after transcript has been translated into protein [23].”
• The Kinome of Pacific Oyster Crassostrea gigas, Its Expression during Development and in Response to Environmental Factors (2016, positive): “Among these processes, posttranslational modifications (PTM) have been described as one of the most important mechanisms for activating, modifying or suppressing protein functions and for increasing the proteome functional diversity [6].”
• The First Identification of Lysine Malonylation Substrates and Its Regulatory Enzyme* (2011, background): “Proteomes in eukaryotic cells consist of over a million molecular species of proteins, easily orders of magnitude more complex than the corresponding genomes (1, 2).”
• The Roles of Post-translational Modifications in the Context of Protein Interaction Networks (2015, background): “The functional significance of specific PTM-types and the respective proteins carrying them has been amply investigated [26, 32, 36, 37].”