Evidence map›Paper›PMID 30016585›Full record

ArticleJournal of the American Chemical Society2018

Site-Specific Protein Labeling with N-Hydroxysuccinimide-Esters and the Analysis of Ubiquitin Ligase Mechanisms.

Daniel R Dempsey, Hanjie Jiang, Jay H Kalin, Zan Chen, Philip A Cole

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

29 citing papers in PubMed, 56 citations in OpenAlex.

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  11. Recent Advances in Bioorthogonal Ligation and Bioconjugation.Topics in current chemistry (Cham) · 2023
    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 2 institutions in 1 country.

Daniel R DempseyDivision of Genetics, Departments of Medicine and Biological Chemistry and Molecular Pharmacology , Harvard Medical School and Brigham and Women's Hospital , Boston , Massachusetts 02115 , United States.
Hanjie JiangDepartment of Pharmacology and Molecular Sciences , Johns Hopkins School of Medicine , Baltimore , Maryland 21205 , United States.
Jay H KalinDivision of Genetics, Departments of Medicine and Biological Chemistry and Molecular Pharmacology , Harvard Medical School and Brigham and Women's Hospital , Boston , Massachusetts 02115 , United States.ORCID 0000-0002-8747-6022
Zan ChenDepartment of Pharmacology and Molecular Sciences , Johns Hopkins School of Medicine , Baltimore , Maryland 21205 , United States.
Philip A ColeDivision of Genetics, Departments of Medicine and Biological Chemistry and Molecular Pharmacology , Harvard Medical School and Brigham and Women's Hospital , Boston , Massachusetts 02115 , United States.ORCID 0000-0001-6873-7824
Brigham and Women's Hospital · USJohns Hopkins University · US

Funding

Chemical Approaches to Protein PhosphorylationR01CA074305 · NCI · JOHNS HOPKINS UNIVERSITY · PI COLE, PHILIP A · 2002 to 2025
$8.0M
ENZYMATIC STUDIES ON PROTEIN TYROSINE KINASE CSKR29CA074305 · NCI · ROCKEFELLER UNIVERSITY · PI COLE, PHILIP A · 1997 to 2001
$188k
Structural and Functional Analysis of the Post-translational Modifications of PTEN and MKP-1F32GM120855 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI DEMPSEY, DANIEL R. · 2016 to 2017
$113k
NCI NIH HHS R01 CA074305NCI NIH HHS R29 CA074305NIGMS NIH HHS F32 GM120855
6 · The paper itself

Abstract

N-Hydroxysuccinimide (NHS)-esters are widely used to label proteins nonselectively on free amino groups. Such broad labeling can be disadvantageous because it can interfere with protein structure or function and because stoichiometry is poorly controlled. Here we describe a simple method to transform NHS-esters into site-specific protein labeling on N-terminal Cys residues. MESNA addition converts NHS-esters to chemoselective thioesters for N-Cys modification. This labeling strategy was applied to clarify mechanistic features of the ubiquitin E3 ligase WWP2 including its interaction with one of its substrates, the tumor suppressor PTEN, as well as its autoubiquitination molecularity. We propose that this convenient protein labeling strategy will allow for an expanded application of NHS-esters in biochemical investigation.

Indexed as

AnimalsBiotinCysteineEscherichia coliEstersFluoresceinsFluorescent DyesGlutathione TransferaseHumansProtein BindingPTEN PhosphohydrolaseRhodaminesSaccharomyces cerevisiaeSpodopteraSuccinimidesUbiquitinBiotinCysteineEstersFluoresceinsFluorescent DyesGlutathione TransferasePTEN PhosphohydrolasePTEN protein, humanRhodaminesSuccinimidesUbiquitinUbiquitin-Protein LigasesUracil-DNA GlycosidaseWWP2 protein, human

Identifiers

PMID30016585
PMCPMC6093203
OpenAlexW2884087457

What OpenQuestion holds

Textmetadata
LicenceTDM
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.