Evidence map›Paper›PMID 31310394›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2019

A Chemical Proteomic Analysis of Illudin-Interacting Proteins.

Philipp Le, Matthew B Nodwell, Jürgen Eirich, Stephan A Sieber

Abstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Phomoxanthone A Targets ATP Synthase.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022
    Article
  5. Article
  6. Article
  7. A Chemical Proteomic Analysis of Illudin-Interacting Proteins.Chemistry (Weinheim an der Bergstrasse, Germany) · 2019
    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

4 authors.

Philipp LeDepartment Chemie, Center for Integrated Protein Science (CIPSM), Technische Universität München, Lichtenbergstraße 4, 85748, Garching, Germany.
Matthew B NodwellDepartment Chemie, Center for Integrated Protein Science (CIPSM), Technische Universität München, Lichtenbergstraße 4, 85748, Garching, Germany.
Jürgen EirichDepartment Chemie, Center for Integrated Protein Science (CIPSM), Technische Universität München, Lichtenbergstraße 4, 85748, Garching, Germany.
Stephan A SieberDepartment Chemie, Center for Integrated Protein Science (CIPSM), Technische Universität München, Lichtenbergstraße 4, 85748, Garching, Germany.ORCID http://orcid.org/0000-0002-9400-906X

Funding

Deutsche Forschungsgemeinschaft SFB749Deutsche Forschungsgemeinschaft SI1096/6-1
6 · The paper itself

Abstract

The illudin natural product family are fungal secondary metabolites with a characteristic spirocyclopropyl-substituted fused 6,5-bicyclic ring system. They have been extensively studied for their cytotoxicity in various tumor cell types, and semisynthetic derivatives with improved therapeutic characteristics have progressed to clinical trials. Although it is believed that this potent alkylating compound class acts mainly through DNA modification, little is known about its binding to protein sites in a cellular context. To reveal putative protein targets of the illudin family in live cancer cells, we employed a semisynthetic strategy to access a series of illudin-based probes for activity-based protein profiling (ABPP). While the probes largely retained potent cytotoxicity, proteomic profiling studies unraveled multiple protein hits, suggesting that illudins exert their mode of action not from addressing a specific protein target but rather from DNA modification and unselective protein binding.

Indexed as

A549 CellsAlkylationAntineoplastic AgentsBinding SitesCell SurvivalHumansProtein BindingProteinsProteomeSecondary MetabolismSesquiterpenesSpiro CompoundsAntineoplastic AgentsProteinsProteomeSesquiterpenesSpiro Compoundsantitumor agentsdrug discoverynatural productsprotein bindingproteomics

Identifiers

PMID31310394
PMCPMC6900183

What OpenQuestion holds

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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.