Evidence map›Paper›PMID 25392746›Full record

ArticleOpen journal of biophysics2013

Prospective Development of Small Molecule Targets to Oncogenic Ras Proteins.

Reena Chandrashekar, Paul D Adams

Open access · diamondAbstract read
In one paragraph

Article in Open journal of biophysics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-weighted citation impact, top 31% 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

3 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Review
  3. 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

2 authors at 1 institution in 1 country.

Reena ChandrashekarDepartment of Chemistry and Biochemistry, The University of Arkansas, Fayetteville, USA.
Paul D AdamsDepartment of Chemistry and Biochemistry, The University of Arkansas, Fayetteville, USA.
University of Arkansas at Fayetteville · US

Funding

Biophysical studies of oncogenic Cdc42Hs constructsK01CA113753 · NCI · UNIVERSITY OF ARKANSAS AT FAYETTEVILLE · PI ADAMS, PAUL DAMIEN · 2007 to 2011
$769k
NCI NIH HHS K01 CA113753
6 · The paper itself

Abstract

Abnormal expression or mutations in Ras proteins has been found in up to 30% of cancer cell types, making them excellent protein models to probe structure-function relationships of cell-signaling processes that mediate cell transformtion. Yet, there has been very little development of therapies to help tackle Ras-related diseased states. The development of small molecules to target Ras proteins to potentially inhibit abnormal Ras-stimulated cell signaling has been conceptualized and some progress has been made over the last 16 or so years. Here, we briefly review studies characterizing Ras protein-small molecule interactions to show the importance and potential that these small molecules may have for Ras-related drug discovery. We summarize recent results, highlighting small molecules that can be directly targeted to Ras using Structure-Based Drug Design (SBDD) and Fragment-Based Lead Discovery (FBLD) methods. The inactivation of Ras oncogenic signaling

Indexed as

Fragment-Based Drug DesignGTP HydrolysisGuanine Nucleotide Exchange Factors [GEF]Ras [Rat Sarcoma]Small Molecule TargetStructure-Based Drug Design

Identifiers

PMID25392746
PMCPMC4226270
OpenAlexW2077757986

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.