Evidence map›Paper›PMID 30920720›Full record

ArticleChembiochem : a European journal of chemical biology2019

Artificially Linked Ubiquitin Dimers Characterised Structurally and Dynamically by NMR Spectroscopy.

Xiaohui Zhao, Maite Mißun, Tobias Schneider, Franziska Müller, Joachim Lutz, Martin Scheffner, Andreas Marx, Michael Kovermann

Open access · hybridAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

9 citing papers in PubMed, 17 citations in OpenAlex.

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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

8 authors at 1 institution in 1 country.

Xiaohui ZhaoUniversität Konstanz, Chemie, Universitätsstrasse 10, 78457, Konstanz, Germany.
Maite MißunUniversität Konstanz, Chemie, Universitätsstrasse 10, 78457, Konstanz, Germany.
Tobias SchneiderUniversität Konstanz, Chemie, Universitätsstrasse 10, 78457, Konstanz, Germany.
Franziska MüllerUniversität Konstanz, Chemie, Universitätsstrasse 10, 78457, Konstanz, Germany.
Joachim LutzUniversität Konstanz, Chemie, Universitätsstrasse 10, 78457, Konstanz, Germany.
Martin ScheffnerUniversität Konstanz, Chemie, Universitätsstrasse 10, 78457, Konstanz, Germany.ORCID 0000-0003-2229-0128
Andreas MarxUniversität Konstanz, Chemie, Universitätsstrasse 10, 78457, Konstanz, Germany.
Michael KovermannUniversität Konstanz, Chemie, Universitätsstrasse 10, 78457, Konstanz, Germany.ORCID 0000-0002-3357-9843
University of Konstanz · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

As one of the most prevalent post-translational modifications in eukaryotic cells, ubiquitylation plays vital roles in many cellular processes, such as protein degradation, DNA metabolism, and cell differentiation. Substrate proteins can be tagged by distinct types of polymeric ubiquitin (Ub) chains, which determine the eventual fate of the modified protein. A facile, click chemistry based approach for the efficient generation of linkage-defined Ub chains, including Ub dimers, was recently established. Within these chains, individual Ub moieties are connected through a triazole linkage, rather than the natural isopeptide bond. Herein, it is reported that the conformation of an artificially K48-linked Ub dimer resembles that of the natively linked dimer, with respect to structural and dynamic characteristics, as demonstrated by means of high-resolution NMR spectroscopy. Thus, it is proposed that artificially linked Ub dimers, as generated by this approach, represent potent tools for studying the inherently different properties and functions of distinct Ub chains.

Indexed as

AlkynesAzidesClick ChemistryNuclear Magnetic Resonance, BiomolecularPoint MutationProtein Structure, QuaternaryTriazolesUbiquitinAlkynesAzidesTriazolesUbiquitinclick chemistrydimerizationNMR spectroscopyproteinsubiquitylation

Identifiers

PMID30920720
PMCPMC6771822
OpenAlexW2929008202

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.