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Related Concept Videos

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.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
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The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
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The interval estimate of any variable is known as the prediction interval. It helps decide if a point estimate is dependable.
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Purification of Tubulin with Controlled Posttranslational Modifications and Isotypes from Limited Sources by Polymerization-Depolymerization Cycles
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Research progress in protein posttranslational modification site prediction.

Wenying He1, Leyi Wei1, Quan Zou1,2

  • 1School of Computer Science and Technology, Tianjin University, Tianjin, China.

Briefings in Functional Genomics
|December 22, 2018
PubMed
Summary
This summary is machine-generated.

Identifying posttranslational modifications (PTMs) is crucial for understanding cell biology. Machine learning tools offer rapid PTM prediction, aiding research and disease treatment development.

Keywords:
glycosylationmachine learningposttranslational modificationubiquitination

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Area of Science:

  • Biochemistry
  • Bioinformatics
  • Computational Biology

Background:

  • Posttranslational modifications (PTMs) are critical regulators of protein function, impacting nearly all cellular processes.
  • Identifying PTMs is fundamental for understanding cell biology mechanisms and developing disease treatments.

Purpose of the Study:

  • To review bioinformatics tools for PTM prediction published since 2008.
  • To summarize prediction approaches for ubiquitination and glycosylation sites.
  • To discuss current challenges and future directions in PTM bioinformatics.

Main Methods:

  • Manual curation of bioinformatics tools.
  • Review of machine learning approaches for PTM site prediction.
  • Synthesis of information on ubiquitination and glycosylation site prediction.

Main Results:

  • A curated list of PTM bioinformatics tools is presented.
  • Common strategies for predicting ubiquitination and glycosylation sites are summarized.
  • Key challenges and limitations of existing PTM prediction tools are identified.

Conclusions:

  • Bioinformatics tools offer efficient alternatives to experimental PTM identification.
  • Further development is needed to address the challenges in current PTM prediction tools.
  • Future research should focus on improving accuracy and expanding the scope of PTM prediction.