Evidence map›Paper›PMID 21635152›Full record

ReviewExpert opinion on therapeutic patents2011

Inhibition of Akt with small molecules and biologics: historical perspective and current status of the patent landscape.

Margrith E Mattmann, Sydney L Stoops, Craig W Lindsley

Abstract readReview
In one paragraph

Review in Expert opinion on therapeutic patents, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 1 pooled it
2.9field-weighted citation impact, top 9% 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

21 citing papers in PubMed, 1 synthesis or guideline pooled it, 63 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Phospho-Form Specific Substrates of Protein Kinase B (AKT1).Frontiers in bioengineering and biotechnology · 2020
    Article
  14. Article
  15. The Akt pathway in oncology therapy and beyond (Review).International journal of oncology · 2018
    Review
  16. Review
  17. Article
  18. Article
  19. Review
  20. Disruption of PH-kinase domain interactions leads to oncogenic activation of AKT in human cancers.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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 at 2 institutions in 1 country.

Margrith E MattmannVanderbilt University, Vanderbilt Medical Center, Vanderbilt Program in Drug Discovery, Department of Pharmacology , Department of Chemistry , Nashville, TN 37232 , USA.
Sydney L Stoops
Craig W Lindsley
Vanderbilt University Medical Center · USVanderbilt University · US

Funding

Postdoctoral Training in CNS Drug Discovery ResearchT32MH093366 · NIMH · VANDERBILT UNIVERSITY · PI CONN, P JEFFREY · 2011 to 2015
$1.0M
NIMH NIH HHS T32 MH093366
6 · The paper itself

Abstract

introductionAkt plays a pivotal role in cell survival and proliferation through a number of downstream effectors; unregulated activation of the PI3K/PTEN/Akt pathway is a prominent feature of many human cancers. Akt is considered an attractive target for cancer therapy by the inhibition of Akt alone or in combination with standard cancer chemotherapeutics. Both preclinical animal studies and clinical trials in humans have validated Akt as an important target of cancer drug discovery. AREA COVERED: A historical perspective of Akt inhibitors, including PI analogs, ATP-competitive and allosteric Akt inhibitors, along with other inhibitory mechanisms are reviewed in this paper with a focus on issued patents, patent applications and a summary of clinical trial updates since the last review in 2007. EXPERT OPINION: A vast diversity of inhibitors of Akt, both small molecule and biologic, have been developed in the past 5 years, with over a dozen in various phases of clinical development, and several displaying efficacy in humans. While it is not yet clear which mechanism of Akt inhibition will be optimal in humans, or which Akt isoforms to inhibit, or whether a small molecule or biologic agent will be best, data to all of these points will be available in the near future.

Indexed as

Adenosine TriphosphateAnimalsAntineoplastic AgentsBinding, CompetitiveBiological ProductsBiotransformationCentral Nervous System DiseasesHumansNeoplasmsOncogene Protein v-aktPatents as TopicSmall Molecule LibrariesAdenosine TriphosphateAntineoplastic AgentsBiological ProductsOncogene Protein v-aktSmall Molecule Libraries

Identifiers

PMID21635152
PMCPMC4279453
OpenAlexW1967412891

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.