Evidence map›Paper›PMID 29397684›Full record

ArticleACS chemical biology2018

Cardiovascular Small Heat Shock Protein HSPB7 Is a Kinetically Privileged Reactive Electrophilic Species (RES) Sensor.

Sanjna L Surya, Marcus J C Long, Daniel A Urul, Yi Zhao, Emily J Mercer, Islam M EIsaid, Todd Evans, Yimon Aye

Abstract read
In one paragraph

Article in ACS chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

14 citing papers in PubMed, 35 citations in OpenAlex.

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  14. Getting the Message? Native Reactive Electrophiles Pass Two Out of Three Thresholds to be Bona Fide Signaling Mediators.BioEssays : news and reviews in molecular, cellular and developmental biology · 2018
    Review
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

8 authors at 1 institution in 1 country.

Sanjna L SuryaDepartment of Chemistry and Chemical Biology , Cornell University , Ithaca , New York 14853 , United States.
Marcus J C LongDepartment of Chemistry and Chemical Biology , Cornell University , Ithaca , New York 14853 , United States.
Daniel A UrulDepartment of Chemistry and Chemical Biology , Cornell University , Ithaca , New York 14853 , United States.
Yi ZhaoDepartment of Chemistry and Chemical Biology , Cornell University , Ithaca , New York 14853 , United States.
Emily J Mercer
Islam M EIsaidDepartment of Chemistry and Chemical Biology , Cornell University , Ithaca , New York 14853 , United States.
Todd Evans
Yimon AyeDepartment of Chemistry and Chemical Biology , Cornell University , Ithaca , New York 14853 , United States.ORCID 0000-0002-1256-4159
Cornell University · US

Funding

A Gata456 Pipeline of DiscoveryR35HL135778 · NHLBI · WEILL MEDICAL COLL OF CORNELL UNIV · PI EVANS, TODD R · 2017 to 2023
$5.7M
Deconvoluting Redox Biology with Targeted ChemistryDP2GM114850 · NIGMS · CORNELL UNIVERSITY · PI AYE, YIMON · 2014 to 2014
$2.3M
Zeiss LSM710 Confocal Microscope for Shared Imaging FacilityS10RR025502 · NCRR · CORNELL UNIVERSITY · PI WILLIAMS, REBECCA M · 2009 to 2009
$500k
NCRR NIH HHS S10 RR025502NHLBI NIH HHS R35 HL135778NIGMS NIH HHS DP2 GM114850
6 · The paper itself

Abstract

Small heat shock protein (sHSP)-B7 (HSPB7) is a muscle-specific member of the non-ATP-dependent sHSPs. The precise role of HSPB7 is enigmatic. Here, we disclose that zebrafish Hspb7 is a kinetically privileged sensor that is able to react rapidly with native reactive electrophilic species (RES), when only substoichiometric amounts of RES are available in proximity to Hspb7 expressed in living cells. Among the two Hspb7-cysteines, this RES sensing is fulfilled by a single cysteine (C117). Purification and characterizations in vitro reveal that the rate for RES adduction is among the most efficient reported for protein-cysteines with native carbonyl-based RES. Covalent-ligand binding is accompanied by structural changes (increase in β-sheet-content), based on circular dichroism analysis. Among the two cysteines, only C117 is conserved across vertebrates; we show that the human ortholog is also capable of RES sensing in cells. Furthermore, a cancer-relevant missense mutation reduces this RES-sensing property. This evolutionarily conserved cysteine-biosensor may play a redox-regulatory role in cardioprotection.

Indexed as

AldehydesAlkylationAnimalsCell Line, TumorCysteineHEK293 CellsHSP27 Heat-Shock ProteinsHumansKineticsMutagenesisProtein Structure, SecondarySequence Homology, Amino AcidZebrafish4-hydroxy-2-nonenalAldehydesCysteineHSP27 Heat-Shock ProteinsHSPB7 protein, human

Identifiers

PMID29397684
PMCPMC6260788
OpenAlexW2787318526

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Registered trials

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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.