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Protein Modifications in the RER01:26

Protein Modifications in the RER

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
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A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes
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Recent Progress in Predicting Posttranslational Modification Sites in Proteins.

Yan Xu1, Kuo-Chen Chou

  • 1Department of Information and Computer Science, University of Science and Technology Beijing, Beijing 100083, P.R. China. yxu@gordonlifescience.org.

Current Topics in Medicinal Chemistry
|August 20, 2015
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Summary
This summary is machine-generated.

Post-translational modifications (PTMs) alter protein functions and are crucial for biological processes and diseases like cancer. Identifying PTM sites is vital for research and drug development.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Bioinformatics

Background:

  • Post-translational modifications (PTMs) are critical protein biosynthesis steps that alter protein properties.
  • PTMs play roles in essential biological processes and are implicated in major diseases, including cancer.
  • Accurate identification of PTM sites is crucial for advancing biological research and drug discovery.

Purpose of the Study:

  • To review recent advancements in identifying protein post-translational modification sites.
  • To focus on predictors utilizing the pseudo amino acid composition (PseAAC) approach.
  • To highlight PTM prediction tools with publicly accessible web servers.

Main Methods:

  • Review of computational methods for PTM site prediction.
  • Emphasis on the pseudo amino acid composition (PseAAC) approach.
  • Assessment of web servers for PTM prediction accessibility.

Main Results:

  • Summarized recent progress in PTM site identification.
  • Highlighted PseAAC-based predictors with established web servers.
  • Provided an overview of available tools for PTM analysis.

Conclusions:

  • Computational tools, particularly those using PseAAC, have advanced PTM site identification.
  • Accessible web servers facilitate the application of these predictors in research and drug development.
  • Continued development is needed to address future challenges in PTM site prediction.