Evidence map›Paper›PMID 31033289›Full record

ArticleJournal of medicinal chemistry2019

Consideration of Binding Kinetics in the Design of Stapled Peptide Mimics of the Disordered Proteins Eukaryotic Translation Initiation Factor 4E-Binding Protein 1 and Eukaryotic Translation Initiation Factor 4G.

Erin E Gallagher, James M Song, Arya Menon, Lauren D Mishra, Alyah F Chmiel, Amanda L Garner

Open access · greenAbstract read
In one paragraph

Article in Journal of medicinal chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

13 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
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  6. Ribosome biogenesis in disease: new players and therapeutic targets.Signal transduction and targeted therapy · 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

6 authors at 2 institutions in 1 country.

Erin E GallagherDepartment of Medicinal Chemistry, College of Pharmacy , University of Michigan , 1600 Huron Parkway, NCRC B520 , Ann Arbor , Michigan 48109 , United States.
James M SongProgram in Chemical Biology , University of Michigan , 210 Washtenaw Avenue , Ann Arbor , Michigan 48109 , United States.
Arya MenonDepartment of Medicinal Chemistry, College of Pharmacy , University of Michigan , 1600 Huron Parkway, NCRC B520 , Ann Arbor , Michigan 48109 , United States.
Lauren D MishraDepartment of Medicinal Chemistry, College of Pharmacy , University of Michigan , 1600 Huron Parkway, NCRC B520 , Ann Arbor , Michigan 48109 , United States.
Alyah F ChmielDepartment of Medicinal Chemistry, College of Pharmacy , University of Michigan , 1600 Huron Parkway, NCRC B520 , Ann Arbor , Michigan 48109 , United States.
Amanda L GarnerDepartment of Medicinal Chemistry, College of Pharmacy , University of Michigan , 1600 Huron Parkway, NCRC B520 , Ann Arbor , Michigan 48109 , United States.ORCID 0000-0002-0870-3347
University of Michigan · USWashtenaw Community College · US

Funding

Research Training in BiogerontologyT32AG000114 · NIA · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SCOTT PLETCHER · 1985 to 2026
$12.4M
INTERDEPARTMENTAL TRAINING IN PHARMACOLOGICAL SCIENCEST32GM007767 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ISOM, LORI L. · 1985 to 2019
$10.2M
Cellular Biotechnology Training Program (CBTP)T32GM008353 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SCHWENDEMAN, ANNA · 1991 to 2021
$9.3M
Cellular Biotechnology Training Program (CBTP) - Years 31-35T32GM145304 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Guizhi Zhu · 2022 to 2026
$2.6M
4E-BP Mimetics as Chemical Probes for Studying Translational Control in CancerR01CA202018 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI GARNER, AMANDA · 2016 to 2020
$1.8M
NCI NIH HHS R01 CA202018NIA NIH HHS T32 AG000114NIGMS NIH HHS T32 GM007767NIGMS NIH HHS T32 GM008353NIGMS NIH HHS T32 GM145304
6 · The paper itself

Abstract

Protein disorder plays a crucial role in signal transduction and is key for many cellular processes including transcription, translation, and cell cycle. Within the intrinsically disordered protein interactome, the α-helix is commonly used for binding, which is induced via a disorder-to-order transition. Because the targeting of protein-protein interactions (PPIs) remains an important challenge in medicinal chemistry, efforts have been made to mimic this secondary structure for rational inhibitor design through the use of stapled peptides. Cap-dependent mRNA translation is regulated by two disordered proteins, 4E-BP1 and eIF4G, that inhibit or stimulate the activity of the m

Indexed as

Drug DesignAdaptor Proteins, Signal TransducingAmino Acid SequenceCell Cycle ProteinsCell Line, TumorCell ProliferationCell SurvivalEukaryotic Initiation Factor-4EEukaryotic Initiation Factor-4GHumansInhibitory Concentration 50KineticsPeptide FragmentsPlasmidsProtein BindingAdaptor Proteins, Signal TransducingCell Cycle ProteinsEIF4EBP1 protein, humanEIF4E protein, humanEIF4G1 protein, humanEukaryotic Initiation Factor-4EEukaryotic Initiation Factor-4GPeptide Fragments

Identifiers

PMID31033289
PMCPMC6679956
OpenAlexW2942721876

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.