Evidence map›Paper›PMID 20095971›Full record

ReviewEssays in biochemistry2009

Design of polyamine-based therapeutic agents: new targets and new directions.

M D Thulani Senanayake, Hemali Amunugama, Tracey D Boncher, Robert A Casero, Patrick M Woster

Abstract readReview
In one paragraph

Review in Essays in biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

8 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Current status of the polyamine research field.Methods in molecular biology (Clifton, N.J.) · 2011
    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 3 institutions in 1 country.

M D Thulani SenanayakeDepartment of Pharmaceutical Sciences, Eugene Applebaum College of Pharmacy and Health Sciences, Wayne State University, Detroit, MI 48202, USA. pwoster@wayne.edu
Hemali Amunugama
Tracey D Boncher
Robert A Casero
Patrick M Woster
Eugene Applebaum College of Pharmacy and Health Sciences · USFerris State University · USJohns Hopkins University · US

Funding

Spermine N1-Acetylase Induction in Lung CancersR01CA051085 · NCI · JOHNS HOPKINS UNIVERSITY · PI CASERO, ROBERT A. · 1990 to 2013
$4.7M
The Role of Polyamine Oxidase in Antitumor Drug ResponseR01CA098454 · NCI · JOHNS HOPKINS UNIVERSITY · PI CASERO, ROBERT A. · 2003 to 2013
$2.9M
ANTINEOPLASTIC POLYAMINE ANALOGUESR01CA085509 · NCI · WAYNE STATE UNIVERSITY · PI WOSTER, PATRICK M · 2000 to 2004
$1.2M
NCI NIH HHS R01 CA051085NCI NIH HHS R01 CA085509NCI NIH HHS R01 CA098454
6 · The paper itself

Abstract

Enzymes in the biosynthetic and catabolic polyamine pathway have long been considered targets for drug development, and early drug discovery efforts in the polyamine area focused on the design and development of specific inhibitors of the biosynthetic pathway, or polyamine analogues that specifically bind DNA. More recently, it has become clear that the natural polyamines are involved in numerous known and unknown cellular processes, and disruption of polyamine functions at their effector sites can potentially produce beneficial therapeutic effects. As new targets for polyamine drug discovery continue to evolve, the rational design of polyamine analogues will result in more structurally diverse agents. In addition, the physical linkage of polyamine-like structures to putative drug molecules can have beneficial effects resulting from increases in DNA affinity and selective cellular uptake. The present chapter will summarize recent advances in the development of alkylpolyamine analogues as antitumour agents, and describe subsequent advances that have resulted from incorporating polyamine character into more diverse drug molecules. Specifically, new polyamine analogues, and the role of polyamine fragments in the design of antiparasitic agents, antitumour metal complexes, histone deacetylase inhibitors and lysine-specific demethylase 1 inhibitors, will be described.

Indexed as

AnimalsAntiparasitic AgentsChemistry, PharmaceuticalDNADrug DesignHistone Deacetylase InhibitorsHumansInhibitory Concentration 50MetalsModels, BiologicalModels, ChemicalPolyaminesProtein IsoformsAntiparasitic AgentsDNAHistone Deacetylase InhibitorsMetalsPolyaminesProtein Isoforms

Identifiers

PMID20095971
PMCPMC3564240
OpenAlexW2092770524

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.