Facile Semisynthesis of Ubiquitylated Peptides with the Ligation Auxiliary 2-Aminooxyethanethiol.

Caroline E Weller, Champak Chatterjee

Abstract read

In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

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

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

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

2 authors.

Caroline E WellerDepartment of Chemistry, University of Washington, Seattle, WA, USA.

Champak ChatterjeeDepartment of Chemistry, University of Washington, Seattle, WA, USA. chatterjee@chem.washington.edu.

Funding

Chemical Strategies to Investigate Gene Regulation By Histone SumoylationR01GM110430 · NIGMS · UNIVERSITY OF WASHINGTON · PI CHATTERJEE, CHAMPAK · 2014 to 2022

$2.5M

NIGMS NIH HHS R01 GM110430

6 · The paper itself

Abstract

The posttranslational modification of cellular proteins by ubiquitin (Ub), called ubiquitylation, is indispensable for the normal growth and development of eukaryotic organisms. In order to conduct studies that elucidate the precise mechanistic roles for Ub, access to site-specifically and homogenously ubiquitylated proteins and peptides is critical. However, the low abundance, heterogeneity, and dynamic nature of protein ubiquitylation are significant limitations toward such studies. Here we provide a facile expressed protein ligation method that does not require specialized apparatus and permits the rapid semisynthesis of ubiquitylated peptides by using the atom-efficient ligation auxiliary 2-aminooxyethanethiol.

Indexed as

UbiquitinationCysteineEscherichia coliEstersGene ExpressionHydroxylaminesImidesInteinsMagnetic Resonance SpectroscopyPeptidesRecombinant ProteinsSolid-Phase Synthesis TechniquesSulfhydryl CompoundsUbiquitinUbiquitinated ProteinsUbiquitinsCysteineEstersHydroxylaminesImidesPeptidesRecombinant ProteinsSulfhydryl CompoundsSUMO3 protein, humanUbiquitinUbiquitinated ProteinsUbiquitinsZincAuxiliaryLigationPeptideSemisynthesisSumoylationUbiquitinUbiquitylation

Identifiers

PMID32144673

DOI10.1007/978-1-0716-0434-2_14

PMCPMC7604904

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.