Evidence map›Paper›PMID 32950259›Full record

ReviewTrends in pharmacological sciences2020

Serial Crystallography for Structure-Based Drug Discovery.

Lan Zhu, Xiaoyu Chen, Enrique E Abola, Liang Jing, Wei Liu

Abstract readReview
In one paragraph

Review in Trends in pharmacological sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
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

8 citing papers in PubMed.

  1. Review
  2. Target Engagement Assays in Early Drug Discovery.Journal of medicinal chemistry · 2025
    Review
  3. Review
  4. Guide to serial synchrotron crystallography.Current research in structural biology · 2024
    Review
  5. Article
  6. Review
  7. Review of FRET biosensing and its application in biomolecular detection.American journal of translational research · 2023
    Review
  8. Room-temperature serial synchrotron crystallography of Drosophila cryptochrome.Acta crystallographica. Section D, Structural biology · 2022
    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

5 authors.

Lan ZhuBiodesign Center for Applied Structural Discovery, Biodesign Institute, Arizona State University, Tempe, AZ 85287, USA; School of Molecular Sciences, Arizona State University, Tempe, AZ 85287, USA.
Xiaoyu ChenBiodesign Center for Applied Structural Discovery, Biodesign Institute, Arizona State University, Tempe, AZ 85287, USA; School of Molecular Sciences, Arizona State University, Tempe, AZ 85287, USA.
Enrique E AbolaBiodesign Center for Applied Structural Discovery, Biodesign Institute, Arizona State University, Tempe, AZ 85287, USA; School of Molecular Sciences, Arizona State University, Tempe, AZ 85287, USA.
Liang JingBiodesign Center for Applied Structural Discovery, Biodesign Institute, Arizona State University, Tempe, AZ 85287, USA; School of Molecular Sciences, Arizona State University, Tempe, AZ 85287, USA.
Wei LiuBiodesign Center for Applied Structural Discovery, Biodesign Institute, Arizona State University, Tempe, AZ 85287, USA; School of Molecular Sciences, Arizona State University, Tempe, AZ 85287, USA. Electronic address: w.liu@asu.edu.

Funding

Structure Determination of G Protein-Coupled Receptors by Microcrystal Electron DiffractionR01GM124152 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI NANNENGA, BRENT · 2017 to 2021
$1.6M
Structure and Function of Dopamine ReceptorsR21DA042298 · NIDA · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI LIU, WEI · 2017 to 2018
$404k
NIDA NIH HHS R21 DA042298NIGMS NIH HHS R01 GM124152
6 · The paper itself

Abstract

Rational drug discovery has greatly accelerated the development of safer and more efficacious therapeutics, assisted significantly by insights from experimentally determined 3D structures of ligands in complex with their targets. Serial crystallography (SX) with X-ray free-electron lasers has enabled structural determination using micrometer- or nanometer-size crystals. This technology, applied in the past decade to solve structures of notoriously difficult-to-study drug targets at room temperature, has now been adapted for use in synchrotron radiation facilities. Ultrashort time scales allow time-resolved characterization of dynamic structural changes and pave the road to study the molecular mechanisms by 'molecular movie.' This article summarizes the latest progress in SX technology and deliberates its demanding applications in future structure-based drug discovery.

Indexed as

Crystallography, X-RayDrug DiscoveryHumansLasersProtein ConformationReceptors, G-Protein-CoupledStructure-Activity RelationshipSynchrotronsReceptors, G-Protein-CoupledGPCR ligand swappingserial femtosecond crystallographystructure-based drug discovery (SBDD)synchrotron-based serial crystallographytime-resolved serial crystallographyX-ray free-electron laser (XFEL)

Identifiers

PMID32950259
PMCPMC7572805

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.