Evidence map›Paper›PMID 28801573›Full record

ArticleScientific reports2017

A structural and mechanistic study of π-clamp-mediated cysteine perfluoroarylation.

Peng Dai, Jonathan K Williams, Chi Zhang, Matthew Welborn, James J Shepherd, Tianyu Zhu, Troy Van Voorhis, Mei Hong, Bradley L Pentelute

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

9 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Recent Advances in Bioorthogonal Ligation and Bioconjugation.Topics in current chemistry (Cham) · 2023
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. A reactive peptide interface for site-selective cysteine bioconjugation.Chemical communications (Cambridge, England) · 2021
    Article
  8. Arylation Chemistry for Bioconjugation.Angewandte Chemie (International ed. in English) · 2019
    Review
  9. Site-Selective Cysteine-Cyclooctyne Conjugation.Angewandte Chemie (International ed. in English) · 2018
    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

9 authors at 1 institution in 1 country.

Peng DaiDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, United States.
Jonathan K WilliamsDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, United States.
Chi ZhangDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, United States.
Matthew WelbornDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, United States.
James J ShepherdDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, United States.
Tianyu ZhuDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, United States.
Troy Van VoorhisDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, United States.
Mei HongDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, United States.
Bradley L PenteluteDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, United States. blp@mit.edu.
Massachusetts Institute of Technology · US

Funding

Structures and Dynamics of Proton and Cation-Dependent Channels and TransportersR01GM088204 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI HONG, MEI · 2009 to 2024
$4.8M
Cysteine ArylationR01GM110535 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI PENTELUTE, BRADLEY LETHER · 2014 to 2018
$1.5M
NIGMS NIH HHS R01 GM088204NIGMS NIH HHS R01 GM110535
6 · The paper itself

Abstract

Natural enzymes use local environments to tune the reactivity of amino acid side chains. In searching for small peptides with similar properties, we discovered a four-residue π-clamp motif (Phe-Cys-Pro-Phe) for regio- and chemoselective arylation of cysteine in ribosomally produced proteins. Here we report mutational, computational, and structural findings directed toward elucidating the molecular factors that drive π-clamp-mediated arylation. We show the significance of a trans conformation prolyl amide bond for the π-clamp reactivity. The π-clamp cysteine arylation reaction enthalpy of activation (ΔH

Indexed as

Amino Acid MotifsCalorimetryCysteineMagnetic Resonance SpectroscopyModels, MolecularMutationProtein ConformationProteinsThermodynamicsCysteineProteins

Identifiers

PMID28801573
PMCPMC5554146
OpenAlexW2743892428

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.