Evidence map›Paper›PMID 23426629›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Insights into antiamyloidogenic properties of the green tea extract (-)-epigallocatechin-3-gallate toward metal-associated amyloid-β species.

Suk-Joon Hyung, Alaina S DeToma, Jeffrey R Brender, Sanghyun Lee, Subramanian Vivekanandan, Akiko Kochi, Jung-Suk Choi, Ayyalusamy Ramamoorthy, Brandon T Ruotolo, Mi Hee Lim

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
13.2field-weighted citation impact, top 1% 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

90 citing papers in PubMed, 235 citations in OpenAlex.

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  10. APP-C31: An Intracellular Promoter of Both Metal-Free and Metal-Bound Amyloid-βAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
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  20. A role for bioinorganic chemistry in the reactivation of mutant p53 in cancer.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
    Review

30 more citing papers are in PubMed but not listed here.

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

10 authors at 1 institution in 1 country.

Suk-Joon HyungDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.
Alaina S DeToma
Jeffrey R Brender
Sanghyun Lee
Subramanian Vivekanandan
Akiko Kochi
Jung-Suk Choi
Ayyalusamy Ramamoorthy
Brandon T Ruotolo
Mi Hee Lim
University of Michigan–Ann Arbor · US

Funding

Next-generation Mass Spectrometry Technologies for Integrated Structural Proteomics- RenewalR01GM095832 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RUOTOLO, BRANDON T · 2011 to 2024
$5.8M
Supplement: Investigation of Membrane-Bound Cytochromes-P450-b5 InteractionsR01GM084018 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAMAMOORTHY, AYYALUSAMY · 2009 to 2018
$3.8M
NIGMS NIH HHS GM-084018NIGMS NIH HHS GM-095832NIGMS NIH HHS R01 GM084018NIGMS NIH HHS R01 GM095832
6 · The paper itself

Abstract

Despite the significance of Alzheimer's disease, the link between metal-associated amyloid-β (metal-Aβ) and disease etiology remains unclear. To elucidate this relationship, chemical tools capable of specifically targeting and modulating metal-Aβ species are necessary, along with a fundamental understanding of their mechanism at the molecular level. Herein, we investigated and compared the interactions and reactivities of the green tea extract, (-)-epigallocatechin-3-gallate [(2R,3R)-5,7-dihydroxy-2-(3,4,5-trihydroxyphenyl)-3,4-dihydro-2H-1-benzopyran-3-yl 3,4,5-trihydroxybenzoate; EGCG], with metal [Cu(II) and Zn(II)]-Aβ and metal-free Aβ species. We found that EGCG interacted with metal-Aβ species and formed small, unstructured Aβ aggregates more noticeably than in metal-free conditions in vitro. In addition, upon incubation with EGCG, the toxicity presented by metal-free Aβ and metal-Aβ was mitigated in living cells. To understand this reactivity at the molecular level, structural insights were obtained by ion mobility-mass spectrometry (IM-MS), 2D NMR spectroscopy, and computational methods. These studies indicated that (i) EGCG was bound to Aβ monomers and dimers, generating more compact peptide conformations than those from EGCG-untreated Aβ species; and (ii) ternary EGCG-metal-Aβ complexes were produced. Thus, we demonstrate the distinct antiamyloidogenic reactivity of EGCG toward metal-Aβ species with a structure-based mechanism.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesCamellia sinensisCatechinCopperHumansMetalsModels, MolecularNeuroprotective AgentsNuclear Magnetic Resonance, BiomolecularPeptide FragmentsPlant ExtractsProtein BindingProtein ConformationProtein MultimerizationTandem Mass SpectrometryAmyloid beta-Peptidesamyloid beta-protein (1-40)CatechinCopperepigallocatechin gallateMetalsNeuroprotective AgentsPeptide FragmentsPlant ExtractsZinc

Identifiers

PMID23426629
PMCPMC3593904
OpenAlexW2071692831

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.