Evidence map›Paper›PMID 21548783›Full record

ReviewAnnual review of biochemistry2011

Transmembrane communication: general principles and lessons from the structure and function of the M2 proton channel, K⁺ channels, and integrin receptors.

Gevorg Grigoryan, David T Moore, William F DeGrado

Abstract readReview
In one paragraph

Review in Annual review of biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

23 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. A Designed ZnJournal of the American Chemical Society · 2025
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  17. Life at the border: adaptation of proteins to anisotropic membrane environment.Protein science : a publication of the Protein Society · 2014
    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

3 authors at 1 institution in 1 country.

Gevorg GrigoryanDepartment of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA. gevorg@alum.mit.edu
David T Moore
William F DeGrado
University of Pennsylvania · US

Funding

Development of drugs that target the M2 proton channel from the influenza A VirusU01AI074571 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 2008 to 2012
$7.5M
Structure of M2 Proton Channel from Influenza A VirusR01GM056423 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1997 to 2016
$4.5M
De novo design of alpha-helical bundlesR37GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 2004 to 2013
$3.6M
DE NOVO DESIGN OF ALPHA HELICAL BUNDLESR01GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1996 to 2016
$2.4M
Understanding transmembrane helix interaction on the structural levelF32GM084631 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GRIGORYAN, GEVORG · 2009 to 2010
$72k
NIAID NIH HHS AI74571NIAID NIH HHS U01 AI074571NIGMS NIH HHS 5F32GM084631NIGMS NIH HHS F32 GM084631NIGMS NIH HHS GM54616NIGMS NIH HHS GM56432NIGMS NIH HHS R01 GM054616NIGMS NIH HHS R01 GM056423NIGMS NIH HHS R37 GM054616
6 · The paper itself

Abstract

Signal transduction across biological membranes is central to life. This process generally happens through communication between different domains and hierarchical coupling of information. Here, we review structural and thermodynamic principles behind transmembrane (TM) signal transduction and discuss common themes. Communication between signaling domains can be understood in terms of thermodynamic and kinetic principles, and complex signaling patterns can arise from simple wiring of thermodynamically coupled domains. We relate this to functions of several signal transduction systems: the M2 proton channel from influenza A virus, potassium channels, integrin receptors, and bacterial kinases. We also discuss key features in the structural rearrangements responsible for signal transduction in these systems.

Indexed as

IntegrinsPotassium ChannelsViral Matrix ProteinsCell CommunicationCell MembraneIonsLigandsModels, MolecularProtein ConformationSignal TransductionThermodynamicsViroporin ProteinsIntegrinsIonsLigandsM2 protein, Influenza A virusPotassium ChannelsViral Matrix ProteinsViroporin Proteins

Identifiers

PMID21548783
PMCPMC3767166
OpenAlexW2135187069

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.