Evidence map›Paper›PMID 25635379›Full record

ReviewMolecules (Basel, Switzerland)2015

Tyrosine sulfation as a protein post-translational modification.

Yuh-Shyong Yang, Chen-Chu Wang, Bo-Han Chen, You-Hua Hou, Kuo-Sheng Hung, Yi-Chih Mao

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed, 1 pooled it
5.5field-weighted citation impact, top 4% 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

64 citing papers in PubMed, 1 synthesis or guideline pooled it, 133 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
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  16. Late-stageChemical science · 2024
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  18. Article
  19. Review
  20. Review

4 more citing papers are in PubMed but not listed here.

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

6 authors at 2 institutions in 1 country.

Yuh-Shyong YangDepartment of Biological Science and Technology, National Chiao Tung University, 75 Po-Ai Street, Hsinchu 30068, Taiwan. ysyang@mail.nctu.edu.tw.
Chen-Chu WangDepartment of Biological Science and Technology, National Chiao Tung University, 75 Po-Ai Street, Hsinchu 30068, Taiwan. no13123.bt99g@nctu.edu.tw.
Bo-Han ChenDepartment of Biological Science and Technology, National Chiao Tung University, 75 Po-Ai Street, Hsinchu 30068, Taiwan. J730703@yahoo.com.tw.
You-Hua HouDepartment of Biological Science and Technology, National Chiao Tung University, 75 Po-Ai Street, Hsinchu 30068, Taiwan. E01252001@gmail.com.
Kuo-Sheng HungDepartment of Neurosurgery, Center of Excellence for Clinical Trial and Research, Taipei Medical University-Wan Fang Medical Center, Taipei 11696, Taiwan. kshung25@gmail.com.
Yi-Chih MaoDepartment of Biological Science and Technology, National Chiao Tung University, 75 Po-Ai Street, Hsinchu 30068, Taiwan. mugokimo@gmail.com.
National Yang Ming Chiao Tung University · TWTaipei Medical University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Integration of inorganic sulfate into biological molecules plays an important role in biological systems and is directly involved in the instigation of diseases. Protein tyrosine sulfation (PTS) is a common post-translational modification that was first reported in the literature fifty years ago. However, the significance of PTS under physiological conditions and its link to diseases have just begun to be appreciated in recent years. PTS is catalyzed by tyrosylprotein sulfotransferase (TPST) through transfer of an activated sulfate from 3'-phosphoadenosine-5'-phosphosulfate to tyrosine in a variety of proteins and peptides. Currently, only a small fraction of sulfated proteins is known and the understanding of the biological sulfation mechanisms is still in progress. In this review, we give an introductory and selective brief review of PTS and then summarize the basic biochemical information including the activity and the preparation of TPST, methods for the determination of PTS, and kinetics and reaction mechanism of TPST. This information is fundamental for the further exploration of the function of PTS that induces protein-protein interactions and the subsequent biochemical and physiological reactions.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceAnimalsEnzyme AssaysHumansKineticsMolecular Sequence DataSulfotransferasesTyrosineprotein-tyrosine sulfotransferaseSulfotransferasesTyrosinetyrosine O-sulfate

Identifiers

PMID25635379
PMCPMC6272617
OpenAlexW2014949148

What OpenQuestion holds

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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.