Evidence map›Paper›PMID 20227292›Full record

ArticleJournal of the American Society for Mass Spectrometry2010

Shape changes induced by N-terminal platination of ubiquitin by cisplatin.

Jonathan P Williams, Hazel I A Phillips, Iain Campuzano, Peter J Sadler

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Top-down mass spectrometry reveals multiple interactions of an acetylsalicylic acid bearing Zeise's salt derivative with peptides.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
    Article
  2. PTEN-Induced Putative Kinase 1 (PINK1)/Parkin-Mediated Mitophagy Protects PC12 Cells Against Cisplatin-Induced Neurotoxicity.Medical science monitor : international medical journal of experimental and clinical research · 2019
    Article
  3. Article
  4. Review
  5. Under-Reported Aspects of Platinum Drug Pharmacology.Molecules (Basel, Switzerland) · 2017
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Mass-spectrometric characterization of cisplatin binding sites on native and denatured ubiquitin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011
    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.

Jonathan P WilliamsDepartment of Chemistry, University of Warwick, Coventry, United Kingdom. Jonathan_Williams@waters.com
Hazel I A Phillips
Iain Campuzano
Peter J Sadler

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The three-dimensional conformation of a protein is an important property and plays a key role in its biological activity. We show here that ion mobility-mass spectrometry (IM-MS) can be used to detect conformational changes in the protein ubiquitin in the gas phase induced by reaction with the anticancer drug cisplatin. The primary adduct was ubiquitin-{Pt(NH(3))(2)} under denaturing conditions. Up to three different conformations appear to be generated upon platination depending on the charge state. The collision cross-sections (Omega) for each conformation indicate that the conformations of the platinated protein are contracted in size compared with unmodified ubiquitin with generally smaller Omega values. Ion mobility-tandem MS allowed determination of the platinum binding site without a requirement for prior chromatographic separation. A rapid 30-min digestion of cisplatin-modified ubiquitin with trypsin allowed the platination site to be identified as the N-terminal methionine following low-energy collision-induced dissociation (CID) studies of the modified peptide. The data were generated using a Traveling-Wave based ion mobility-MS approach. Such cisplatin-induced shape changes may have a significant effect on its function in vivo. This work highlights the usefulness of the ion-mobility mass spectrometry technique for shedding new light on such protein interactions.

Indexed as

UbiquitinAnimalsCattleCisplatinErythrocytesIonsPeptide FragmentsProtein ConformationSpectrometry, Mass, Electrospray IonizationTandem Mass SpectrometryTrypsinCisplatinIonsPeptide FragmentsTrypsinUbiquitin

Identifiers

What OpenQuestion holds

Textmetadata
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.