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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Updated: Apr 21, 2026

Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations
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Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations

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Urinary proteins with post-translational modifications.

Liu Liu1, Xuejiao Liu

  • 1Key Laboratory of Medical Molecular Biology, Department of Pathophysiology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences/School of Basic Medicine, 5 Dong Dan San Tiao, Beijing, China, emma891021@hotmail.com.

Advances in Experimental Medicine and Biology
|October 31, 2014
PubMed
Summary
This summary is machine-generated.

This study introduces a new method for identifying posttranslational modifications (PTMs) in human urine without enrichment. This approach simplifies urine proteomics and aids in discovering PTM biomarkers for diseases.

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Area of Science:

  • Biochemistry
  • Proteomics
  • Biomarker Discovery

Background:

  • Human urine proteome research is crucial for identifying disease biomarkers.
  • Posttranslational modifications (PTMs) significantly influence protein biomarker function.
  • Current methods for PTM identification in urine proteomics can be complex and require enrichment steps.

Purpose of the Study:

  • To develop a simplified method for identifying PTMs in the human urine proteome.
  • To facilitate the discovery of novel PTM biomarkers for various diseases.
  • To establish a foundational dataset for future PTM biomarker research.

Main Methods:

  • Utilized a novel software capable of unrestrictive identification of PTMs.
  • Applied the method to human urine samples for proteomic analysis.
  • Did not require enrichment steps, simplifying the conventional procedure.

Main Results:

  • Successfully identified various PTMs in the human urine proteome, including methylation, dehydration, oxidation, hydroxylation, phosphorylation, and dihydroxylation.
  • Demonstrated that PTM identification can be performed without additional enrichment steps.
  • Generated valuable data for future PTM biomarker discovery.

Conclusions:

  • The developed method offers a streamlined approach to urine proteomics for PTM identification.
  • This technique enhances the potential for discovering new PTM biomarkers associated with diseases.
  • The generated data serve as a critical reference for advancing PTM biomarker research.