Native Chemical Ligation to Install Chemical Protein Modifications.

Eldon R Hard, Afraah Javed, Matthew R Pratt

Abstract read

In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing 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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

3 authors.

Eldon R HardDepartment of Chemistry, University of Southern California, Los Angeles, CA 90089, USA.

Afraah JavedDepartment of Chemistry, University of Southern California, Los Angeles, CA 90089, USA.

Matthew R PrattDepartment of Chemistry, University of Southern California, Los Angeles, CA 90089, USA. matthew.pratt@usc.edu.

Funding

Functional Analysis of O-GlcNAc using Synthetic Protein ChemistryR01GM114537 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI PRATT, MATTHEW ROBERT · 2015 to 2024

$3.1M

Chemistry-enabled glycoscienceR35GM158201 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI Matthew Robert Pratt · 2025 to 2026

$965k

NIGMS NIH HHS R01 GM114537NIGMS NIH HHS R35 GM158201

6 · The paper itself

Abstract

Native chemical ligation is utilized for the generation of homogenous samples of full-length proteins with site-specific chemical modifications. It is commonly used for the site-specific installation of post-translational modifications, in particular those that to-date cannot be readily incorporated by other means. Here, we describe the assembly of recombinantly expressed and/or chemically synthesized protein fragments via this chemoselective bioconjugation reaction. Derivative ligation methods are also discussed to enable the greatest amount of flexibility for the generation of a desired protein.

Indexed as

Protein EngineeringProtein Processing, Post-TranslationalProteinsMaleimidesRecombinant ProteinsMaleimidesProteinsRecombinant ProteinsDiselenide-selenoester ligation (DSL)Expressed protein ligation (EPL)Expressed protein selenoester ligation (EPSL)Maleimide protection/deprotectionNative chemical ligation (NCL)Post-translational modifications (PTMs)Protein semisynthesis

Identifiers

PMID42542481

DOI10.1021/jacs.0c07663

PMCPMC13551872

What OpenQuestion holds

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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.