SpSrtA-Catalyzed Isopeptide Ligation on Lysine Residues.

Jiajia Wu, Tianyu Chu, Jian Hao, Liang Lin

Open access · goldAbstract read

In one paragraph

Article in Microorganisms, 2024. 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, top 99% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

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

4 authors at 3 institutions in 1 country.

Jiajia WuDepartment of Chemistry, Shanghai University, Shanghai 200444, China.ORCID 0009-0006-1608-6162

Tianyu ChuCollege of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China.ORCID 0009-0002-2904-7323

Jian HaoDepartment of Chemistry, Shanghai University, Shanghai 200444, China.

Liang LinState Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 200032, China.

Shanghai University · CNChinese Academy of Sciences · CNPeking University · CN

Funding

National Natural Science Foundation of China 22177126

6 · The paper itself

Abstract

Sortase-mediated ligation (SML) is widely used for protein bioconjugation. However, the sortase used in this strategy typically recognizes only the N-terminal oligoglycine, which is absent in most natural proteins. To broaden the spectrum of substrates compatible with SML, we focus on a novel sortase, sortase A from

Indexed as

isopeptide ligationsortase Ayeast display

Identifiers

PMID38258005

DOI10.3390/microorganisms12010179

PMCPMC10818881

OpenAlexW4390948219

What OpenQuestion holds

Textmetadata

LicenceCC BY

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.