Evidence map›Paper›PMID 26295307›Full record

ReviewOncotarget2015

The 26S proteasome is a multifaceted target for anti-cancer therapies.

Tatyana A Grigoreva, Vyacheslav G Tribulovich, Alexander V Garabadzhiu, Gerry Melino, Nickolai A Barlev

Open access · diamondAbstract readReview
In one paragraph

Review in Oncotarget, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed, 2 pooled it
6.8field-weighted citation impact, top 2% 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

47 citing papers in PubMed, 2 syntheses or guidelines pooled it, 79 citations in OpenAlex.

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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 2 institutions in 2 countries.

Tatyana A GrigorevaSt. Petersburg State Technological Institute (Technical University), St. Petersburg, Russia.
Vyacheslav G TribulovichSt. Petersburg State Technological Institute (Technical University), St. Petersburg, Russia.
Alexander V GarabadzhiuSt. Petersburg State Technological Institute (Technical University), St. Petersburg, Russia.
Gerry MelinoSt. Petersburg State Technological Institute (Technical University), St. Petersburg, Russia.
Nickolai A BarlevInstitute of Cytology RAS, St. Petersburg, Russia.
St. Petersburg State Technological Institute · RUInstitute of Cytology · RU

Funding

Medical Research Council MC_U132670600
6 · The paper itself

Abstract

Proteasomes play a critical role in the fate of proteins that are involved in major cellular processes, including signal transduction, gene expression, cell cycle, replication, differentiation, immune response, cellular response to stress, etc. In contrast to non-specific degradation by lysosomes, proteasomes are highly selective and destroy only the proteins that are covalently labelled with small proteins, called ubiquitins. Importantly, many diseases, including neurodegenerative diseases and cancers, are intimately connected to the activity of proteasomes making them an important pharmacological target. Currently, the vast majority of inhibitors are aimed at blunting the proteolytic activities of proteasomes. However, recent achievements in solving structures of proteasomes at very high resolution provided opportunities to design new classes of small molecules that target other physiologically-important enzymatic activities of proteasomes, including the de-ubiquitinating one. This review attempts to catalog the information available to date about novel classes of proteasome inhibitors that may have important pharmacological ramifications.

Indexed as

AnimalsAntineoplastic AgentsAntineoplastic Combined Chemotherapy ProtocolsDrug DesignHumansMolecular StructureMolecular Targeted TherapyNeoplasmsProteasome Endopeptidase ComplexProteasome InhibitorsProteolysisStructure-Activity RelationshipUbiquitinationAntineoplastic AgentsATP dependent 26S proteaseProteasome Endopeptidase ComplexProteasome Inhibitorscombined anti-cancer therapyproteasomeproteasome inhibitorsubiquitin-dependent proteolysis

Identifiers

PMID26295307
PMCPMC4694792
OpenAlexW1918838535

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.