Evidence map›Paper›PMID 37277637›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2023

Site-Specific Incorporation of Sulfotyrosine into Proteins in Mammalian Cells.

Xinyuan He, Yan Chen, Jiantao Guo, Wei Niu

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2023. 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 84% 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 1 institution in 1 country.

Xinyuan HeDepartment of Chemical & Biomolecular Engineering, University of Nebraska-Lincoln, Lincoln, NE, USA.
Yan ChenDepartment of Chemistry, University of Nebraska-Lincoln, Lincoln, NE, USA.
Jiantao GuoDepartment of Chemistry, University of Nebraska-Lincoln, Lincoln, NE, USA. jguo4@unl.edu.
Wei NiuDepartment of Chemical & Biomolecular Engineering, University of Nebraska-Lincoln, Lincoln, NE, USA. wniu2@unl.edu.
University of Nebraska–Lincoln · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein tyrosine O-sulfation (PTS) plays a crucial role in numerous extracellular protein-protein interactions. It is involved in diverse physiological processes and the development of human diseases, including AIDS and cancer. To facilitate the study of PTS in live mammalian cells, an approach for the site-specific synthesis of tyrosine-sulfated proteins (sulfoproteins) was developed. This approach takes advantage of an evolved Escherichia coli tyrosyl-tRNA synthetase to genetically encode sulfotyrosine (sTyr) into any proteins of interest (POI) in response to a UAG stop codon. Here, we give a step-by-step account of the incorporation of sTyr in HEK293T cells using the enhanced green fluorescent protein as an example. This method can be widely applied to incorporating sTyr into any POI to investigate the biological functions of PTS in mammalian cells.

Indexed as

Escherichia coliTyrosineAnimalsCodon, TerminatorHEK293 CellsHumansMammalsCodon, TerminatorTyrosinetyrosine O-sulfateAmber suppressionGenetic code expansionGreen fluorescent proteinMammalian cellsProtein tyrosine O-sulfation (PTS)Sulfotyrosine incorporation

Identifiers

PMID37277637
OpenAlexW4379472259

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.