Evidence map›Paper›PMID 24010710›Full record

ReviewStructure (London, England : 1993)2013

Allosteric conformational barcodes direct signaling in the cell.

Ruth Nussinov, Buyong Ma, Chung-Jung Tsai, Peter Csermely

Open access · bronzeAbstract readReview
In one paragraph

Review in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

26 citing papers in PubMed, 55 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. AlphaFold, Artificial Intelligence (AI), and Allostery.The journal of physical chemistry. B · 2022
    Review
  5. Article
  6. Protein ensembles link genotype to phenotype.PLoS computational biology · 2019
    Review
  7. Review
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Oligomerization and nanocluster organization render specificity.Biological reviews of the Cambridge Philosophical Society · 2015
    Review
  16. Article
  17. Article
  18. Review
  19. Principles of allosteric interactions in cell signaling.Journal of the American Chemical Society · 2014
    Review
  20. Article
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

4 authors at 3 institutions in 3 countries.

Ruth NussinovBasic Science Program, SAIC-Frederick, Inc., Cancer and Inflammation Program, National Cancer Institute, Frederick, MD 21702, USA; Sackler Institute of Molecular Medicine, Department of Human Genetics and Molecular Medicine, Sackler School of Medicine, Tel Aviv University, Tel Aviv 69978, Israel. Electronic address: nussinor@helix.nih.gov.
Buyong Ma
Chung-Jung Tsai
Peter Csermely
National Cancer Institute · USSemmelweis University · HUTel Aviv University · IL

Funding

Biomolecular Recognition and Binding MechanismsZIABC010441 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NUSSINOV, RUTH · 2009 to 2025
$9.4M
CCR NIH HHS HHSN261200800001CIntramural NIH HHSNCI NIH HHS HHSN261200800001E
6 · The paper itself

Abstract

The cellular network is highly interconnected. Pathways merge and diverge. They proceed through shared proteins and may change directions. How are cellular pathways controlled and their directions decided, coded, and read? These questions become particularly acute when we consider that a small number of pathways, such as signaling pathways that regulate cell fates, cell proliferation, and cell death in development, are extensively exploited. This review focuses on these signaling questions from the structural standpoint and discusses the literature in this light. All co-occurring allosteric events (including posttranslational modifications, pathogen binding, and gain-of-function mutations) collectively tag the protein functional site with a unique barcode. The barcode shape is read by an interacting molecule, which transmits the signal. A conformational barcode provides an intracellular address label, which selectively favors binding to one partner and quenches binding to others, and, in this way, determines the pathway direction, and, eventually, the cell's response and fate.

Indexed as

Signal TransductionAllosteric RegulationAnimalsCatalytic DomainExtracellular Signal-Regulated MAP KinasesHumansIntracellular Signaling Peptides and ProteinsModels, MolecularPhosphorylationProtein Interaction MapsProtein Processing, Post-TranslationalExtracellular Signal-Regulated MAP KinasesIntracellular Signaling Peptides and Proteins

Identifiers

PMID24010710
PMCPMC6361540
OpenAlexW1966693725

What OpenQuestion holds

Textmetadata
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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.