Evidence map›Paper›PMID 31797579›Full record

ArticleCurrent protocols in toxicology2019

Analysis of Protein-Protein Interactions by Split Luciferase Complementation Assay.

Yuekun Lang, Zhong Li, Hongmin Li

Abstract read
In one paragraph

Article in Current protocols in toxicology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Acta pharmaceutica Sinica. B · 2022
    Article
  8. Review
  9. Article
  10. Article
  11. 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.

Yuekun LangWadsworth Center, New York State Department of Health, Albany, New York.
Zhong LiWadsworth Center, New York State Department of Health, Albany, New York.
Hongmin LiWadsworth Center, New York State Department of Health, Albany, New York.

Funding

High throughput screening of orthosteric inhibitors of flavivirus proteaseR01AI131669 · NIAID · WADSWORTH CENTER · PI LI, HONGMIN · 2018 to 2022
$2.6M
High throughput screening of the Prp8 intein splicing inhibitors for pathogenic fungiR01AI140726 · NIAID · WADSWORTH CENTER · PI LI, HONGMIN · 2019 to 2022
$2.4M
High throughput screening of orthosteric inhibitors of flavivirus proteaseR56AI131669 · NIAID · WADSWORTH CENTER · PI LI, HONGMIN · 2017 to 2017
$524k
Identification and characterization of allosteric inhibitors of Zika protease by targeting the NS2B conformational changeR21AI140491 · NIAID · WADSWORTH CENTER · PI LEMASTER, DAVID M, LI, HONGMIN · 2018 to 2019
$460k
In vivo efficacy studies of existing drugs re-purposed for flaviviruses in mouse modelsR21AI133219 · NIAID · WADSWORTH CENTER · PI LI, HONGMIN · 2017 to 2018
$452k
New Use of Old Drugs for Zika VirusR21AI134568 · NIAID · WADSWORTH CENTER · PI LI, HONGMIN · 2017 to 2018
$447k
Discovery of therapeutics against Cryptococcosis by Repurposing Pharmaceutical LibrariesR21AI141178 · NIAID · WADSWORTH CENTER · PI LI, HONGMIN · 2019 to 2020
$441k
NIAID NIH HHS R01 AI131669NIAID NIH HHS R01 AI140726NIAID NIH HHS R21 AI133219NIAID NIH HHS R21 AI134568NIAID NIH HHS R21 AI140491NIAID NIH HHS R21 AI141178NIAID NIH HHS R56 AI131669
6 · The paper itself

Abstract

Protein-protein interactions are important in human disease. Developing and refining tools to understand physical contacts between signaling proteins is crucial. This article describes a split luciferase complementation (SLC) method designed to discover inhibitors of protein-protein interaction. Different fusion proteins with split luciferase are constructed, expressed, and purified, and then assessed to determine the best pair that generates the strongest luminescence. SLC specificity and affinity are further confirmed. Step-by-step instructions are provided for performing these assays using the NS2B-NS3 interaction as an example. NS2B is an essential cofactor for flaviviral NS3 protease function. Advantages and disadvantages of these assays are further discussed. © 2019 by John Wiley & Sons, Inc. Basic Protocol 1: Expression and purification of fusion proteins Basic Protocol 2: Analysis of prey/bait pairs by SLC-based NS2B-NS3 interaction assay Support Protocol 1: Interaction specificity assay Support Protocol 2: Competition binding assay: Dose-response inhibition using cold prey or bait Support Protocol 3: Competition binding assay: Inhibition by MBP-NS3 versus irrelevant MBP tag Support Protocol 4: SLC-based NS2B-NS3 interaction assay using NS2B mutations known to disrupt NS2B-NS3 interactions.

Indexed as

Binding, CompetitiveBiological AssayCloning, MolecularDEAD-box RNA HelicasesLuciferases, FireflyLuminescent ProteinsMutationNucleoside-TriphosphataseProtein BindingRecombinant Fusion ProteinsRNA HelicasesSerine EndopeptidasesViral Nonstructural ProteinsViral ProteasesDEAD-box RNA HelicasesLuciferases, FireflyLuminescent ProteinsNS2B protein, flavivirusNS3 protein, flavivirusNucleoside-TriphosphataseRecombinant Fusion ProteinsRNA HelicasesSerine EndopeptidasesViral Nonstructural ProteinsViral Proteasesflaviviral proteaseNS2B-NS3protein-protein interactionsplit luciferase complementation

Identifiers

PMID31797579
PMCPMC7269092

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.