Evidence map›Paper›PMID 36029222›Full record

ReviewThe journal of physical chemistry. B2022

Evolving Experimental Techniques for Structure-Based Drug Design.

Cody Aplin, Shawn K Milano, Kara A Zielinski, Lois Pollack, Richard A Cerione

Open access · greenAbstract readReview
In one paragraph

Review in The journal of physical chemistry. B, 2022. 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
2.4field-weighted citation impact, top 10% 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, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Prediction of enzyme inhibition (ICJournal of molecular modeling · 2025
    Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Cryo-electron microscopy-based drug design.Frontiers in molecular biosciences · 2024
    Review
  15. Article
  16. Article
  17. Article
  18. Review
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 at 1 institution in 1 country.

Cody AplinDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, United States.ORCID 0000-0002-0211-8016
Shawn K MilanoDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, United States.
Kara A ZielinskiSchool of Applied and Engineering Physics, Cornell University, Ithaca, New York 14853, United States.ORCID 0000-0002-9907-5058
Lois PollackSchool of Applied and Engineering Physics, Cornell University, Ithaca, New York 14853, United States.ORCID 0000-0002-9366-4396
Richard A CerioneDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, United States.ORCID 0000-0003-4512-5897
Cornell University · US

Funding

Training and OutreachP30GM124166 · NIGMS · CORNELL UNIVERSITY · PI RICHARD A. CERIONE · 2019 to 2026
$28.3M
The unique roles of the GTP-binding/protein crosslinking enzyme transglutaminase-2 and signaling partners in aggressive cancersR01CA201402 · NCI · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2016 to 2024
$4.3M
New frontiers in extracellular signalingR35GM122575 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2017 to 2021
$3.0M
NCI NIH HHS R01 CA201402NIGMS NIH HHS P30 GM124166NIGMS NIH HHS R35 GM122575
6 · The paper itself

Abstract

Structure-based drug design (SBDD) is a prominent method in rational drug development and has traditionally benefitted from the atomic models of protein targets obtained using X-ray crystallography at cryogenic temperatures. In this perspective, we highlight recent advances in the development of structural techniques that are capable of probing dynamic information about protein targets. First, we discuss advances in the field of X-ray crystallography including serial room-temperature crystallography as a method for obtaining high-resolution conformational dynamics of protein-inhibitor complexes. Next, we look at cryogenic electron microscopy (cryoEM), another high-resolution technique that has recently been used to study proteins and protein complexes that are too difficult to crystallize. Finally, we present small-angle X-ray scattering (SAXS) as a potential high-throughput screening tool to identify inhibitors that target protein complexes and protein oligomerization.

Indexed as

Drug DesignProteinsCrystallography, X-RayScattering, Small AngleX-Ray DiffractionProteins

Identifiers

PMID36029222
PMCPMC10161966
OpenAlexW4293364222

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.