Evidence map›Paper›PMID 35530783›Full record

ArticleRSC advances2019

Structure-based design of nucleoside-derived analogues as sulfotransferase inhibitors.

Neil M Kershaw, Dominic P Byrne, Hollie Parsons, Neil G Berry, David G Fernig, Patrick A Eyers, Richard Cosstick

Open access · goldAbstract read
In one paragraph

Article in RSC advances, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.3field-weighted citation impact, top 46% 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

5 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Searching for Sulfotyrosines (sY) in a HA(pY)STACK.Journal of proteome research · 2025
    Article
  3. Article
  4. Review
  5. Article
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

7 authors at 1 institution in 1 country.

Neil M KershawDepartment of Chemistry, University of Liverpool Liverpool L69 7ZD UK nkershaw@liverpool.ac.uk.ORCID https://orcid.org/0000-0002-4557-1742
Dominic P ByrneDepartment of Biochemistry, Institute of Integrative Biology, University of Liverpool Liverpool L69 7ZB UK.
Hollie ParsonsDepartment of Chemistry, University of Liverpool Liverpool L69 7ZD UK nkershaw@liverpool.ac.uk.
Neil G BerryDepartment of Chemistry, University of Liverpool Liverpool L69 7ZD UK nkershaw@liverpool.ac.uk.
David G FernigDepartment of Biochemistry, Institute of Integrative Biology, University of Liverpool Liverpool L69 7ZB UK.
Patrick A EyersDepartment of Biochemistry, Institute of Integrative Biology, University of Liverpool Liverpool L69 7ZB UK.ORCID https://orcid.org/0000-0002-9220-2966
Richard CosstickDepartment of Chemistry, University of Liverpool Liverpool L69 7ZD UK nkershaw@liverpool.ac.uk.
University of Liverpool · GB

Funding

Biotechnology and Biological Sciences Research Council BB/N021703/1
6 · The paper itself

Abstract

Sulfotransferases (STs) catalyse the transfer of a sulfonyl group ('sulfation') from the enzyme co-factor 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to a variety of biomolecules. Tyrosine sulfation of proteins and carbohydrate sulfation play a crucial role in many protein-protein interactions and cell signalling pathways in the extracellular matrix. This is catalysed by several membrane-bound STs, including tyrosylprotein sulfotransferase 1 (TPST1) and heparan sulfate 2-

Identifiers

PMID35530783
PMCPMC9072872
OpenAlexW2980232077

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.