Evidence map›Paper›PMID 22578832›Full record

ReviewCurrent opinion in pharmacology2012

Therapeutic development in targeting protein-protein interactions with synthetic topological mimetics.

Lun K Tsou, Yao Cheng, Yung-Chi Cheng

Abstract readReview
In one paragraph

Review in Current opinion in pharmacology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. 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

3 authors.

Lun K TsouLaboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, NY 10065, USA.
Yao Cheng
Yung-Chi Cheng

Funding

Clinical Study of PHY906, a Novel Chinese Herbal Medicine, as a Modulator of IrinP01CA154295 · NCI · YALE UNIVERSITY · PI CHENG, YUNG-CHI · 2011 to 2016
$6.4M
BIOCHEMICAL PHARMACOLOGY OF ANTIHIV COMPOUNDSR01AI038204 · NIAID · YALE UNIVERSITY · PI CHENG, YUNG-CHI · 1995 to 2014
$5.2M
NCI NIH HHS P01 CA154295NCI NIH HHS P01CA154295-01A1NIAID NIH HHS AI38204NIAID NIH HHS R01 AI038204NIAID NIH HHS R56 AI038204
6 · The paper itself

Abstract

Protein-protein interactions lie at the heart of cellular signaling pathways and the deregulation of which has frequently led to diseases. In contrast to inhibitors that bind to distinctive enzyme active sites, molecules targeting protein surface topologies have been underexploited in drug development. The challenges in developing protein surface antagonists or agonists originate from the relatively large and flat surface areas that lack well-defined cavities required for sufficient binding affinity. In the past decade, our understanding of protein recognition has served as solid basis for the design of synthetic mimetics to modulate these protein-protein interactions. Herein, we summarize recent successes in the development of synthetic α-helix mimetics, proteomimetics, and biologics with the therapeutic potentials of inhibiting tumorgenesis or cancer-related viral infections.

Indexed as

Antineoplastic AgentsAntiviral AgentsApoptosisBiological ProductsHumansNeoplasmsProtein BindingProteinsReceptor Protein-Tyrosine KinasesReceptors, Death DomainAntineoplastic AgentsAntiviral AgentsBiological ProductsProteinsReceptor Protein-Tyrosine KinasesReceptors, Death Domain

Identifiers

PMID22578832
PMCPMC3660839

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Registered trials

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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.