Evidence map›Paper›PMID 34827669›Full record

ReviewBiomolecules2021

Inhibitors of Discoidin Domain Receptor (DDR) Kinases for Cancer and Inflammation.

William A Denny, Jack U Flanagan

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

6 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. 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.

William A DennyAuckland Cancer Society Research Centre, Maurice Wilkins Centre, School of Medical Sciences, University of Auckland, Auckland 1142, New Zealand.ORCID 0000-0001-7997-1843
Jack U FlanaganAuckland Cancer Society Research Centre, Maurice Wilkins Centre, School of Medical Sciences, University of Auckland, Auckland 1142, New Zealand.
University of Auckland · NZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The discoidin domain receptor tyrosine kinases DDR1 and DDR2 are distinguished from other kinase enzymes by their extracellular domains, which interact with collagen rather than with peptidic growth factors, before initiating signaling via tyrosine phosphorylation. They share significant sequence and structural homology with both the c-Kit and Bcr-Abl kinases, and so many inhibitors of those kinases are also effective. Nevertheless, there has been an extensive research effort to develop potent and specific DDR inhibitors. A key interaction for many of these compounds is H-bonding to Met-704 in a hydrophobic pocket of the DDR enzyme. The most widespread use of DDR inhibitors has been for cancer therapy, but they have also shown effectiveness in animal models of inflammatory conditions such as Alzheimer's and Parkinson's diseases, and in chronic renal failure and glomerulonephritis.

Indexed as

Discoidin Domain ReceptorsInflammationNeoplasmsProtein Kinase InhibitorsAnimalsDiscoidin Domain Receptor 1Discoidin Domain Receptor 2HumansDiscoidin Domain Receptor 1Discoidin Domain Receptor 2Discoidin Domain ReceptorsProtein Kinase InhibitorsDDR kinase inhibitorsselectivitysmall molecules

Identifiers

PMID34827669
PMCPMC8615839
OpenAlexW3214431145

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.