C‐terminomics: Targeted analysis of natural and posttranslationally modified protein and peptide C‐termini

Tanco, Sebastián; Gevaert, Kris; Damme, Petra Van

doi:10.1002/pmic.201400301

Cited by 53 publications

(57 citation statements)

References 98 publications

(136 reference statements)

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“…93 For a detailed description and comparison of these approaches, please refer to the recent review by Tanco et al (2015). 41 Despite these advances problems remain. After trypsin digestion, protein C-terminal peptides are rarely identified by LC-MS/MS as they inherently lack basic residues.…”

Section: Enrichment Of Protein C-terminimentioning

confidence: 99%

Protein Termini and Their Modifications Revealed by Positional Proteomics

2015

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A myriad of co- and post-translational modifications occur at protein N- and C-termini, resulting in an extra layer of proteome complexity and an additional source of protein regulation. Here, we review N- and C-terminal modifications and the contemporary positional proteomics techniques used to isolate protein terminal peptides from complex protein mixtures and characterize their diversity and occurrence in biological systems. Furthermore, these degradomics strategies--often referred to as N- and C-terminomics--represent dedicated high-throughput techniques to study proteolysis in dynamic living systems. Over the past decade, terminomics studies have provided indispensable information on the functional states of individual proteins, cell types, tissues, and biological processes and delivered fundamental new data for the Human Proteome Project, including high confidence identifications of many so-called "missing proteins", which had not been identified by traditional proteomics analyses.

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Section: Enrichment Of Protein C-terminimentioning

confidence: 99%

Protein Termini and Their Modifications Revealed by Positional Proteomics

2015

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“…In this case, the primary amines of C‐terminal peptides are modified by N ‐hydroxysuccinimide ester of butyrate, which enables the separation of the N‐ and C‐terminal peptides with an additional HPLC step . While other approaches to the MS analysis of proteolytic C‐termini have also been reported, poor detection limits and complex methodologies composed of several steps of chemical manipulations remain significant limitations to the application of C‐terminal degradomics …”

Section: Discovery Of Protease Substratesmentioning

confidence: 99%

Degradomics in Biomarker Discovery

Grozdanić

Vidmar

Vizovišek

et al. 2019

Proteomics Clinical Apps

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The upregulation of protease expression and proteolytic activity is implicated in numerous pathological conditions such as neurodegeneration, cancer, cardiovascular and autoimmune diseases, and bone degeneration. During disease progression, various proteases form characteristic patterns of cleaved proteins and peptides, which can affect disease severity and course of progression. It has been shown that qualitative and quantitative monitoring of cleaved protease substrates can provide relevant prognostic, diagnostic, and therapeutic information. As proteolytic fragments and peptides generated in the affected tissue are commonly translocated to blood, urine, and other proximal fluids, their possible application as biomarkers is the subject of ongoing research. The field of degradomics has been established to enable the global identification of proteolytic events on the organism level, utilizing proteomic approaches and sample preparation techniques that facilitate the detection of proteolytic processing of protease substrates in complex biological samples. In this review, some of the latest developments in degradomic methodologies used for the identification and validation of biologically relevant proteolytic events and their application in the search for clinically relevant biomarker candidates are presented. The current state of degradomics in clinics is discussed and the future perspectives of the field are outlined.

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“…The α‐carboxyl group is known to exhibit lower chemical reactivity and therefore it is less amenable to selective modification in aqueous solution . The methods to enrich C‐termini include modified versions of TAILS and COFRADIC.…”

Section: Proteomics Approachmentioning

confidence: 99%

“…The α-carboxyl group is known to exhibit lower chemical reactivity and therefore it is less amenable to selective modification in aqueous solution. [120] The methods to enrich C-termini include modified versions of TAILS and COFRADIC. In carboxyterminal amine-based isotope labeling of substrates (C-TAILS), all the primary amines are blocked by dimethylation and the carboxyl groups are blocked with an ethanolamine, 1-ethyl-3-(3-(dimethylamino)propyl) carbodiimide (EDAC).…”

Section: Positive Enrichment Of C-terminal Peptidesmentioning

confidence: 99%

Proteolysis to Identify Protease Substrates: Cleave to Decipher

2018

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Proteolysis is an irreversible post-translational modification process, characterized by highly precise yet stable cleavage of proteins. Downstream events in signaling processes are reliant on proteolysis triggered by the protease activity. Studies indicate that abnormal proteolytic activity may lead to the manifestation of diseased conditions. Therefore, characterization of proteases may provide clues to understand their role in fundamental cellular processes like cellular growth, differentiation, apoptosis, and survival. The relevance of proteases and their substrates as clinical targets are being studied. Understanding the mechanism of proteolytic activity, the identity, and the role of repertoire of its substrates in a physiological pathway has opened avenues for novel drug designing. However, only a limited knowledge of protease substrates is currently available. In this review, the authors recapitulate the library screening, proteomics, and bioinformatics based approaches that have been employed for the identification of protease substrates.

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C‐terminomics: Targeted analysis of natural and posttranslationally modified protein and peptide C‐termini

Cited by 53 publications

References 98 publications

Protein Termini and Their Modifications Revealed by Positional Proteomics

Protein Termini and Their Modifications Revealed by Positional Proteomics

Degradomics in Biomarker Discovery

Proteolysis to Identify Protease Substrates: Cleave to Decipher

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