Evidence map›Paper›PMID 27959494›Full record

ArticleBiochemistry2017

Characterization of Protein Tyrosine Phosphatase 1B Inhibition by Chlorogenic Acid and Cichoric Acid.

James M Lipchock, Heidi P Hendrickson, Bonnie B Douglas, Kelly E Bird, Patrick S Ginther, Ivan Rivalta, Nicholas S Ten, Victor S Batista, J Patrick Loria

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

7 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. The importance of including the C-terminal domain of PTP1BJournal of enzyme inhibition and medicinal chemistry · 2023
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. 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 3 institutions in 2 countries.

James M LipchockDepartment of Chemistry, Washington College , Chestertown, Maryland 21620, United States.
Heidi P HendricksonDepartment of Chemistry, Yale University , New Haven, Connecticut 06511, United States.ORCID http://orcid.org/0000-0002-5012-738X
Bonnie B DouglasDepartment of Chemistry, Washington College , Chestertown, Maryland 21620, United States.
Kelly E BirdDepartment of Chemistry, Washington College , Chestertown, Maryland 21620, United States.
Patrick S GintherDepartment of Chemistry, Washington College , Chestertown, Maryland 21620, United States.
Ivan RivaltaDepartment of Chemistry, Yale University , New Haven, Connecticut 06511, United States.ORCID http://orcid.org/0000-0002-1208-602X
Nicholas S TenDepartment of Chemistry, Yale University , New Haven, Connecticut 06511, United States.
Victor S BatistaDepartment of Chemistry, Yale University , New Haven, Connecticut 06511, United States.
J Patrick LoriaDepartment of Chemistry, Yale University , New Haven, Connecticut 06511, United States.ORCID http://orcid.org/0000-0002-4824-9089
Washington College · USYale University · USUniversité Claude Bernard Lyon 1 · FR

Funding

PREDOCTORAL PROGRAM IN BIOPHYSICST32GM008283 · NIGMS · YALE UNIVERSITY · PI XIONG, YONG · 1988 to 2022
$10.5M
Mechanism of catalytic regulation and active site loop motions in related protein tyrosine phosphatasesR01GM112781 · NIGMS · YALE UNIVERSITY · PI LORIA, JOSEPH P · 2015 to 2024
$2.8M
Computational and Biochemical Studies of Temperature Effects on Allostery in the Imidazole Glycerol Phosphate Synthase (IGPS) from T. maritimaR01GM106121 · NIGMS · YALE UNIVERSITY · PI BATISTA, VICTOR S, LORIA, JOSEPH P · 2014 to 2021
$2.3M
NIGMS NIH HHS R01 GM106121NIGMS NIH HHS R01 GM112781NIGMS NIH HHS T32 GM008283
6 · The paper itself

Abstract

Protein tyrosine phosphatase 1B (PTP1B) is a known regulator of the insulin and leptin signaling pathways and is an active target for the design of inhibitors for the treatment of type II diabetes and obesity. Recently, cichoric acid (CHA) and chlorogenic acid (CGA) were predicted by docking methods to be allosteric inhibitors that bind distal to the active site. However, using a combination of steady-state inhibition kinetics, solution nuclear magnetic resonance experiments, and molecular dynamics simulations, we show that CHA is a competitive inhibitor that binds in the active site of PTP1B. CGA, while a noncompetitive inhibitor, binds in the second aryl phosphate binding site, rather than the predicted benzfuran binding pocket. The molecular dynamics simulations of the apo enzyme and cysteine-phosphoryl intermediate states with and without bound CGA suggest CGA binding inhibits PTP1B by altering hydrogen bonding patterns at the active site. This study provides a mechanistic understanding of the allosteric inhibition of PTP1B.

Indexed as

AlgorithmsAllosteric RegulationBinding, CompetitiveBinding SitesCaffeic AcidsCatalytic DomainChlorogenic AcidEnzyme InhibitorsHumansHydrogen BondingKineticsMagnetic Resonance SpectroscopyMolecular Dynamics SimulationProtein BindingProtein DomainsProtein Tyrosine Phosphatase, Non-Receptor Type 1Caffeic Acidschicoric acidChlorogenic AcidEnzyme InhibitorsProtein Tyrosine Phosphatase, Non-Receptor Type 1PTPN1 protein, humanSuccinates

Identifiers

PMID27959494
PMCPMC5292209
OpenAlexW2563038743

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.