Evidence map›Paper›PMID 24929364›Full record

ArticleBiomolecular NMR assignments2015

(1)H, (13)C, and (15)N backbone and sidechain chemical shift assignments for the HEAT2 domain of human eIF4GI.

Katherine A Edmonds, Gerhard Wagner

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biomolecular NMR assignments, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Katherine A EdmondsDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, 02115, USA.
Gerhard Wagner
Harvard University · US

Funding

T CELL SPECIFIC TRANSCRIPTION COMPLEXESP01GM047467 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 1992 to 2017
$28.6M
OverallP41EB002026 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2018
$17.9M
Acquisition of a 900 MHz NMR SpectrometerP41GM066360 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2002 to 2006
$6.7M
STRUCTURAL BASIS OF TRANSLATION INITIATION BY EIF-4ER01CA068262 · NCI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 1996 to 2015
$3.6M
800 MHz Triple Resonance Observe (TXO) Detection CryoProbeS10RR026417 · NCRR · HARVARD MEDICAL SCHOOL · PI WAGNER, GERHARD · 2010 to 2010
$359k
NCI NIH HHS CA68262NCI NIH HHS R01 CA068262NCRR NIH HHS 1S10RR10219015NCRR NIH HHS S10 RR026417NIBIB NIH HHS EB002026NIBIB NIH HHS P41 EB002026NIGMS NIH HHS GM047467NIGMS NIH HHS GM066360NIGMS NIH HHS P01 GM047467NIGMS NIH HHS P41 GM066360
6 · The paper itself

Abstract

The translation initiation factor eIF4G is required for the translation of many eukaryotic messenger RNAs. Its interaction with the ATP-dependent RNA helicase eIF4A plays an important role in the regulation of translation initiation. eIF4G in humans and other higher eukaryotes contains three HEAT domains, of which HEAT1 and HEAT2 contain binding sites for eIF4A. Here we report the near complete NMR resonance assignment of the 192-residue HEAT2 domain of the human translation initiation factor eIF4GI. The chemical shift data constitute the basis for NMR structural studies aimed at expanding understanding of the role of interactions between the initiation factor eIF4A and eIF4G in translation initiation.

Indexed as

Nuclear Magnetic Resonance, BiomolecularEukaryotic Initiation Factor-4GHumansModels, MolecularProtein Structure, TertiaryEIF4G1 protein, humanEukaryotic Initiation Factor-4G

Identifiers

PMID24929364
PMCPMC4268090
OpenAlexW2014184994

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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.