Evidence map›Paper›PMID 28983186›Full record

ArticleNew journal of chemistry = Nouveau journal de chimie2017

Solution-phase and solid-phase sequential, selective modification of side chains in KDYWEC and KDYWE as models for usage in single-molecule protein sequencing.

Erik T Hernandez, Jagannath Swaminathan, Edward M Marcotte, Eric V Anslyn

Abstract read
In one paragraph

Article in New journal of chemistry = Nouveau journal de chimie, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Single-molecule fluorescence methods for protein biomarker analysis.Analytical and bioanalytical chemistry · 2023
    Review
  5. Article
  6. Protein Sequencing, One Molecule at a Time.Annual review of biophysics · 2022
    Review
  7. Review
  8. Studies of Surface Preparation for the Fluorosequencing of Peptides.Langmuir : the ACS journal of surfaces and colloids · 2021
    Article
  9. Photoredox-Catalyzed DecarboxylativeACS chemical biology · 2021
    Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Erik T HernandezDepartment of Chemistry, University of Texas at Austin, Austin, TX, 78712-1224, USA.
Jagannath SwaminathanCenter for Systems and Synthetic Biology, Department of Molecular Biosciences, Institute for Cellular and Molecular Biology, University of Texas at Austin.
Edward M MarcotteCenter for Systems and Synthetic Biology, Department of Molecular Biosciences, Institute for Cellular and Molecular Biology, University of Texas at Austin.
Eric V AnslynDepartment of Chemistry, University of Texas at Austin, Austin, TX, 78712-1224, USA.

Funding

Proteomics and model organism humanization to decode human geneticsR35GM122480 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI EDWARD M MARCOTTE · 2017 to 2026
$5.4M
Next-Generation Proteomics: Massively Parallel Single-Molecule Protein IdentificaDP1GM106408 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI MARCOTTE, EDWARD M · 2012 to 2016
$3.8M
NIGMS NIH HHS DP1 GM106408NIGMS NIH HHS R35 GM122480
6 · The paper itself

Abstract

Single-molecule protein sequencing is regarded as a promising new method in the field of proteomics. It potentially offers orders of magnitude improvements in sensitivitiy and throughput for protein detection when compared to mass spectrometry. However, the development of such a technology faces significant barriers, especially in the need to chemically derivatize specific amino-acid types with unique labels. For example, fluorescent dyes would be suitable for single-molecule microscopy or nanopore-based sequencing. These emerging single-molecule protein-sequencing technologies suggests a need to develop an amino acid side chain-selective modification scheme that could target several side chains of interest. Current work for modifying residues focuses mainly on one or two side chains. The need to label many side chains, as recent computational modeling suggests, is required for high protein, sequencing coverage of the human proteome. Herein, we report our stragety for modifying two model peptides KYDWEC and KDYWE containing the most reactive residues, using highly opitmized mass labels in a sequential and selective fashion both using solution-phase and solid-phase chemistries, respectively. This will serve as a step towards a modification scheme appropriate for single-molecule studies.

Identifiers

PMID28983186
PMCPMC5624723

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.