Evidence map›Paper›PMID 37692919›Full record

ArticlePeptide science (Hoboken, N.J.)2023

Development of Convergent Hybrid Phase Ligation for Efficient and Convenient Total Synthesis of Proteins.

Ziyong Z Hong, Ruixuan R Yu, Xiaoyu Zhang, Allison M Webb, Nathaniel L Burge, Michael G Poirier, Jennifer J Ottesen

Open access · hybridAbstract read
In one paragraph

Article in Peptide science (Hoboken, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.5field-weighted citation impact, top 33% of its field
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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. Review on the o-Aminoaniline Moiety in Peptide and Protein Chemistry.Chembiochem : a European journal of chemical biology · 2025
    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

7 authors at 1 institution in 1 country.

Ziyong Z HongDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio, 43210.
Ruixuan R YuOhio State Biochemistry Graduate Program, The Ohio State University, Columbus, Ohio, 43210.
Xiaoyu ZhangDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio, 43210.
Allison M WebbDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio, 43210.
Nathaniel L BurgeOhio State Biochemistry Graduate Program, The Ohio State University, Columbus, Ohio, 43210.
Michael G PoirierOhio State Biochemistry Graduate Program, The Ohio State University, Columbus, Ohio, 43210.
Jennifer J OttesenDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio, 43210.
The Ohio State University · US

Funding

Mechanisms of chromatin regulation of transcriptionR35GM139564 · NIGMS · OHIO STATE UNIVERSITY · PI POIRIER, MICHAEL GUY · 2021 to 2025
$3.6M
Cellular, molecular, and biochemical sciences training grantT32GM141955 · NIGMS · OHIO STATE UNIVERSITY · PI Jane Elizabeth Jackman, JESSE J KWIEK · 2021 to 2026
$2.2M
Regulatory Mechanisms of Linker Histones and Their Post-Translational ModificationsR01GM121966 · NIGMS · OHIO STATE UNIVERSITY · PI POIRIER, MICHAEL GUY · 2017 to 2020
$1.2M
NIGMS NIH HHS R01 GM121966NIGMS NIH HHS R35 GM139564NIGMS NIH HHS T32 GM141955
6 · The paper itself

Abstract

Simple and efficient total synthesis of homogeneous and chemically modified protein samples remains a significant challenge. Here, we report development of a convergent hybrid phase native chemical ligation (CHP-NCL) strategy for facile preparation of proteins. In this strategy, proteins are split into ~100-residue blocks, and each block is assembled on solid support from synthetically accessible peptide fragments before ligated together into full-length protein in solution. With the new method, we increase the yield of CENP-A synthesis by 2.5-fold compared to the previous hybrid phase ligation approach. We further extend the new strategy to the total chemical synthesis of 212-residue linker histone H1.2 in unmodified, phosphorylated, and citrullinated forms, each from eight peptide segments with only one single purification. We demonstrate that fully synthetic H1.2 replicates the binding interactions of linker histones to intact mononucleosomes, as a proxy for the essential function of linker histones in the formation and regulation of higher order chromatin structure.

Identifiers

PMID37692919
PMCPMC10488053
OpenAlexW4378213700

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.