Evidence map›Paper›PMID 29459028›Full record

ReviewAdvances in protein chemistry and structural biology2018

Homo- and Heterodimerization of Proteins in Cell Signaling: Inhibition and Drug Design.

Sitanshu S Singh, Seetharama D Jois

Open access · greenAbstract readReview
In one paragraph

Review in Advances in protein chemistry and structural biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed, 1 pooled it
3.5field-weighted citation impact, top 6% 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

14 citing papers in PubMed, 1 synthesis or guideline pooled it, 23 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Variants inFrontiers in pediatrics · 2024
    Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Embracing nanomaterials' interactions with the innate immune system.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2021
    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

2 authors at 1 institution in 1 country.

Sitanshu S SinghBasic Pharmaceutical Sciences, School of Pharmacy, University of Louisiana at Monroe, Monroe, LA, United States.
Seetharama D JoisBasic Pharmaceutical Sciences, School of Pharmacy, University of Louisiana at Monroe, Monroe, LA, United States. Electronic address: jois@ulm.edu.
University of Louisiana at Monroe · US

Funding

Molecular mechanism of EGFR heterodimerization: inhibition by a peptidomimeticR15CA188225 · NCI · UNIVERSITY OF LOUISIANA AT MONROE · PI JOIS, SEETHARAMA D · 2015 to 2015
$394k
NCI NIH HHS R15 CA188225
6 · The paper itself

Abstract

Protein dimerization controls many physiological processes in the body. Proteins form homo-, hetero-, or oligomerization in the cellular environment to regulate the cellular processes. Any deregulation of these processes may result in a disease state. Protein-protein interactions (PPIs) can be inhibited by antibodies, small molecules, or peptides, and inhibition of PPI has therapeutic value. PPI drug discovery research has steadily increased in the last decade, and a few PPI inhibitors have already reached the pharmaceutical market. Several PPI inhibitors are in clinical trials. With advancements in structural and molecular biology methods, several methods are now available to study protein homo- and heterodimerization and their inhibition by drug-like molecules. Recently developed methods to study PPI such as proximity ligation assay and enzyme-fragment complementation assay that detect the PPI in the cellular environment are described with examples. At present, the methods used to design PPI inhibitors can be classified into three major groups: (1) structure-based drug design, (2) high-throughput screening, and (3) fragment-based drug design. In this chapter, we have described some of the experimental methods to study PPIs and their inhibition. Examples of homo- and heterodimers of proteins, their structural and functional aspects, and some of the inhibitors that have clinical importance are discussed. The design of PPI inhibitors of epidermal growth factor receptor heterodimers and CD2-CD58 is discussed in detail.

Indexed as

Drug DesignHumansProteinsSignal TransductionProteinsCD2–CD58EGFRHeterodimerizationPD-1–PD-L1PPI inhibitionProtein–protein interaction

Identifiers

PMID29459028
PMCPMC6203451
OpenAlexW2762601412

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.