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Post-translational Translocation of Proteins to the RER01:27

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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
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Initiation of Translation02:33

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Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
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The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
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Related Experiment Video

Updated: Jan 28, 2026

Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations
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Precision Profiling of the Cardiovascular Post-Translationally Modified Proteome.

Thakorn Pruktanakul1,2, Konstantinos Theofilatos1

  • 1King's British Heart Foundation Centre, King's College London, London SE5 9NU, UK.

Journal of Cardiovascular Development and Disease
|January 27, 2026
PubMed
Summary
This summary is machine-generated.

This review explores proteoform diversity, arising from gene expression and post-translational modifications (PTMs). It highlights mass spectrometry methods for analyzing PTMs in cardiovascular disease (CVD) research.

Keywords:
bioinformaticscardiovascular diseasemass spectrometrypost-translational modificationsproteoformsproteomics

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Proteins exist as diverse proteoforms, crucial for physiological and pathological signaling.
  • Proteoform diversity stems from alternative splicing, translation, and post-translational modifications (PTMs).
  • This complexity significantly impacts biological systems and disease mechanisms.

Purpose of the Study:

  • To provide an overview of proteoform generation mechanisms.
  • To highlight mass spectrometry (MS)-based proteomics strategies for proteoform analysis.
  • To focus on PTMs in cardiovascular disease (CVD) and their study methodologies.

Main Methods:

  • Mass spectrometry (MS)-based proteomics.
  • Bioinformatics analysis.
  • Review of existing literature on PTMs and CVD.

Main Results:

  • Detailed mechanisms of proteoform generation are outlined.
  • MS-based workflows for analyzing proteoforms, including PTMs, are presented.
  • Recent findings linking PTMs to cardiovascular disease are discussed.

Conclusions:

  • Understanding proteoform diversity is key to deciphering biological complexity.
  • MS-based proteomics offers powerful tools for studying PTMs in CVD.
  • This review equips researchers with knowledge to explore PTMs in cardiovascular physiology.