Evidence map›Paper›PMID 40875116›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2025

Synthesizing Defined Ubiquitin-Modified SUMO Dimers.

Kai-Yu Hsu, Yane-Shih Wang

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2025. 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.

Kai-Yu HsuInstitute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.
Yane-Shih WangInstitute of Biological Chemistry, Academia Sinica, Taipei, Taiwan. yaneshihwang@gate.sinica.edu.tw.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitination and SUMOylation interactions between proteins play a critical role in various biological processes and the progression of diseases. To investigate the biological functions of the direct crosstalk between protein ubiquitination and SUMOylation biochemically, we have developed a method for synthesizing Ub-tagged SUMO2 dimers using an expanding genetic code approach. In this description, we outline the procedures for creating Ub-SUMO heterodimers through the incorporation of defined noncanonical amino acids (ncAAs) and biorthogonal functional group-guided conjugation techniques. These homogeneous Ub-SUMO heterodimers will serve as valuable tools for studying the mechanisms of Ub-SUMO chain elongation, degradation, topology, and other related protein-protein interactions.

Indexed as

Protein MultimerizationSmall Ubiquitin-Related Modifier ProteinsUbiquitinHumansSumoylationUbiquitinationSmall Ubiquitin-Related Modifier ProteinsSUMO2 protein, humanUbiquitinMichael reactionNoncanonical amino acidSUMO2UbiquitinUb-SUMO heterodimer synthesis

Identifiers

What OpenQuestion holds

Textmetadata
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.