Evidence map›Paper›PMID 32403216›Full record

ReviewBiomolecules2020

Targeting Intrinsically Disordered Proteins through Dynamic Interactions.

Jianlin Chen, Xiaorong Liu, Jianhan Chen

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

32 citing papers in PubMed, 51 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Intrinsic disorder may drive the interaction of PROS1 and MERTK in uveal melanoma.International journal of biological macromolecules · 2023
    Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. 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

3 authors at 1 institution in 2 countries.

Jianlin ChenDepartment of Hematology, Taizhou Central Hospital (Taizhou University Hospital), Taizhou 318000, Zhejiang, China.
Xiaorong LiuDepartment of Chemistry, University of Massachusetts, Amherst, MA 01003, USA.
Jianhan ChenDepartment of Chemistry, University of Massachusetts, Amherst, MA 01003, USA.ORCID 0000-0002-5281-1150
University of Massachusetts Amherst · US

Funding

Multi-scale enhanced sampling of disordered proteins: Admin Supplement InstrumentationR01GM114300 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI CHEN, JIANHAN · 2016 to 2020
$1.5M
NIGMS NIH HHS R01 GM114300
6 · The paper itself

Abstract

Intrinsically disordered proteins (IDPs) are over-represented in major disease pathways and have attracted significant interest in understanding if and how they may be targeted using small molecules for therapeutic purposes. While most existing studies have focused on extending the traditional structure-centric drug design strategies and emphasized exploring pre-existing structure features of IDPs for specific binding, several examples have also emerged to suggest that small molecules could achieve specificity in binding IDPs and affect their function through dynamic and transient interactions. These dynamic interactions can modulate the disordered conformational ensemble and often lead to modest compaction to shield functionally important interaction sites. Much work remains to be done on further elucidation of the molecular basis of the dynamic small molecule-IDP interaction and determining how it can be exploited for targeting IDPs in practice. These efforts will rely critically on an integrated experimental and computational framework for disordered protein ensemble characterization. In particular, exciting advances have been made in recent years in enhanced sampling techniques, Graphic Processing Unit (GPU)-computing, and protein force field optimization, which have now allowed rigorous physics-based atomistic simulations to generate reliable structure ensembles for nontrivial IDPs of modest sizes. Such de novo atomistic simulations will play crucial roles in exploring the exciting opportunity of targeting IDPs through dynamic interactions.

Indexed as

HumansIntrinsically Disordered ProteinsMagnetic Resonance SpectroscopyMolecular Dynamics SimulationProtein AggregatesProtein BindingProtein Structure, SecondaryIntrinsically Disordered ProteinsProtein Aggregatesaggregationcancerdisordered ensembledrug designenhanced samplingGPU computingmolecular dynamicsneurodegenerative diseasesp53protein force fields

Identifiers

PMID32403216
PMCPMC7277182
OpenAlexW3021765302

What OpenQuestion holds

Textmetadata
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.