Evidence map›Paper›PMID 27552080›Full record

ReviewCurrent opinion in structural biology2016

Conformational insight into multi-protein signaling assemblies by hydrogen-deuterium exchange mass spectrometry.

Rane A Harrison, John R Engen

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

30 citing papers in PubMed, 69 citations in OpenAlex.

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  5. GPCR targeting of E3 ubiquitin ligase MDM2 by inactive β-arrestin.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

2 authors at 1 institution in 1 country.

Rane A HarrisonDepartment of Chemistry & Chemical Biology, Northeastern University, Boston, MA 02115, USA.
John R EngenDepartment of Chemistry & Chemical Biology, Northeastern University, Boston, MA 02115, USA. Electronic address: j.engen@northeastern.edu.
Northeastern University · US

Funding

Extending the applications of hydrogen exchange mass spectrometryR01GM101135 · NIGMS · NORTHEASTERN UNIVERSITY · PI ENGEN, JOHN R · 2012 to 2015
$1.2M
NIGMS NIH HHS R01 GM101135
6 · The paper itself

Abstract

Hydrogen-deuterium exchange (HDX) mass spectrometry (MS) can provide information about proteins that can be challenging to obtain by other means. Structure/function relationships, binding interactions, and the effects of modification have all been measured with HDX MS for a diverse and growing array of signaling proteins and multiprotein signaling complexes. As a result of hardware and software improvements, receptors and complexes involved in cellular signaling-including those associated with membranes-can now be studied. The growing body of HDX MS studies of signaling complexes at membranes is particularly exciting. Recent examples are presented to illustrate what can be learned about signaling proteins with this technique.

Indexed as

Signal TransductionAnimalsDetergentsDeuterium Exchange MeasurementHumansMass SpectrometryProtein ConformationProteinsDetergentsProteins

Identifiers

PMID27552080
PMCPMC5154849
OpenAlexW2507820983

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.