Evidence map›Paper›PMID 29352103›Full record

ArticleThe Journal of biological chemistry2018

Dynamic cycling of t-SNARE acylation regulates platelet exocytosis.

Jinchao Zhang, Yunjie Huang, Jing Chen, Haining Zhu, Sidney W Whiteheart

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.8field-weighted citation impact, top 32% 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

6 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
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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

5 authors at 1 institution in 1 country.

Jinchao ZhangFrom the Department of Molecular and Cellular Biochemistry, University of Kentucky College of Medicine, Lexington, Kentucky 40536.
Yunjie HuangFrom the Department of Molecular and Cellular Biochemistry, University of Kentucky College of Medicine, Lexington, Kentucky 40536.
Jing ChenFrom the Department of Molecular and Cellular Biochemistry, University of Kentucky College of Medicine, Lexington, Kentucky 40536.
Haining ZhuFrom the Department of Molecular and Cellular Biochemistry, University of Kentucky College of Medicine, Lexington, Kentucky 40536.
Sidney W WhiteheartFrom the Department of Molecular and Cellular Biochemistry, University of Kentucky College of Medicine, Lexington, Kentucky 40536 whitehe@uky.edu.
University of Kentucky · US

Funding

Protein CoreP30GM110787 · NIGMS · UNIVERSITY OF KENTUCKY · PI WHITEHEART, SIDNEY WALDO · 2014 to 2018
$5.7M
MOLECULAR MECHANISMS OF PLATELET EXOCYTOSISR01HL056652 · NHLBI · UNIVERSITY OF KENTUCKY · PI WHITEHEART, SIDNEY WALDO · 1996 to 2019
$5.2M
Platelet Endocytosis in Innate ImmunityR01HL138179 · NHLBI · UNIVERSITY OF KENTUCKY · PI WHITEHEART, SIDNEY WALDO · 2017 to 2019
$1.3M
NHLBI NIH HHS R01 HL056652NHLBI NIH HHS R01 HL138179NIGMS NIH HHS P30 GM110787
6 · The paper itself

Abstract

Platelets regulate vascular integrity by secreting a host of molecules that promote hemostasis and its sequelae. Given the importance of platelet exocytosis, it is critical to understand how it is controlled. The t-SNAREs, SNAP-23 and syntaxin-11, lack classical transmembrane domains (TMDs), yet both are associated with platelet membranes and redistributed into cholesterol-dependent lipid rafts when platelets are activated. Using metabolic labeling and hydroxylamine (HA)/HCl treatment, we showed that both contain thioester-linked acyl groups. Mass spectrometry mapping further showed that syntaxin-11 was modified on cysteine 275, 279, 280, 282, 283, and 285, and SNAP-23 was modified on cysteine 79, 80, 83, 85, and 87. Interestingly, metabolic labeling studies showed incorporation of [

Indexed as

ExocytosisProtein Processing, Post-TranslationalAcylationAcyltransferasesBlood PlateletsCysteineEnzyme InhibitorsHumansHydroxylamineMembrane MicrodomainsOxidation-ReductionPalmitic AcidPlatelet ActivationPlatelet AggregationProtein TransportP-SelectinAcyltransferasesCysteineEnzyme InhibitorsHydroxylaminePalmitic AcidP-SelectinQa-SNARE ProteinsQb-SNARE ProteinsQc-SNARE ProteinsReducing AgentsSELP protein, humanSNAP23 protein, humanSTX11 protein, humanThiolester HydrolasesTritiumacyltransferasecardiovascularceruleninlipid raftmembrane fusionpalmostatin Bposttranslational modification (PTM)SNAP-23syntaxinthrombosis

Identifiers

PMID29352103
PMCPMC5846156
OpenAlexW2784150934

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.