Evidence map›Paper›PMID 21686180›Full record

ReviewInternational journal of molecular sciences2011

Novel strategies for drug discovery based on Intrinsically Disordered Proteins (IDPs).

Jihua Wang, Zanxia Cao, Liling Zhao, Shuqiang Li

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

18 citing papers in PubMed, 60 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Intrinsically Disordered Proteins: An Overview.International journal of molecular sciences · 2022
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Protein stability: a crystallographer's perspective.Acta crystallographica. Section F, Structural biology communications · 2016
    Review
  15. Article
  16. Binding cavities and druggability of intrinsically disordered proteins.Protein science : a publication of the Protein Society · 2015
    Article
  17. Article
  18. 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 2 institutions in 2 countries.

Jihua WangShandong Provincial Key Laboratory of Functional Macromolecular Biophysics, Dezhou 253023, China; E-Mails: qiayilai@mail.ustc.edu.cn (Z.C.); zll2008@mail.ustc.edu.cn (L.Z.).
Zanxia Cao
Liling Zhao
Shuqiang Li
Dezhou University · CNHarvard University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intrinsically disordered proteins (IDPs) are proteins that usually do not adopt well-defined native structures when isolated in solution under physiological conditions. Numerous IDPs have close relationships with human diseases such as tumor, Parkinson disease, Alzheimer disease, diabetes, and so on. These disease-associated IDPs commonly play principal roles in the disease-associated protein-protein interaction networks. Most of them in the disease datasets have more interactants and hence the size of the disease-associated IDPs interaction network is simultaneously increased. For example, the tumor suppressor protein p53 is an intrinsically disordered protein and also a hub protein in the p53 interaction network; α-synuclein, an intrinsically disordered protein involved in Parkinson diseases, is also a hub of the protein network. The disease-associated IDPs may provide potential targets for drugs modulating protein-protein interaction networks. Therefore, novel strategies for drug discovery based on IDPs are in the ascendant. It is dependent on the features of IDPs to develop the novel strategies. It is found out that IDPs have unique structural features such as high flexibility and random coil-like conformations which enable them to participate in both the "one to many" and "many to one" interaction. Accordingly, in order to promote novel strategies for drug discovery, it is essential that more and more features of IDPs are revealed by experimental and computing methods.

Indexed as

Amino Acid SequenceDrug DiscoveryIntrinsically Disordered ProteinsProtein Interaction MapsProtein Structure, TertiarySequence Analysis, ProteinIntrinsically Disordered Proteinsdrug-discoveryinteraction networksintrinsically disordered proteinssequence characterizationsstructural characterizations

Identifiers

PMID21686180
PMCPMC3116186
OpenAlexW2164332468

What OpenQuestion holds

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LicenceCC BY
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.