Evidence map›Paper›PMID 10975572›Full record

ArticleProtein science : a publication of the Protein Society2000

Chemical cross-linking with thiol-cleavable reagents combined with differential mass spectrometric peptide mapping--a novel approach to assess intermolecular protein contacts.

K L Bennett, M Kussmann, P Björk, M Godzwon, M Mikkelsen, P Sørensen, P Roepstorff

Open access · greenAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

45 citing papers in PubMed, 151 citations in OpenAlex.

  1. MS-Based Proteomics Approach in Mapping Protein-Protein Interaction.Advances in experimental medicine and biology · 2026
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  15. Large Scale Chemical Cross-linking Mass Spectrometry Perspectives.Journal of proteomics & bioinformatics · 2013
    Article
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  17. Protein flexibility is key to cisplatin crosslinking in calmodulin.Protein science : a publication of the Protein Society · 2012
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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

7 authors at 2 institutions in 2 countries.

K L BennettDepartment of Molecular Biology, University of Southern Denmark, Odense. bennett@pr-group.sdu.dk
M Kussmann
P Björk
M Godzwon
M Mikkelsen
P Sørensen
P Roepstorff
University of Southern Denmark · DKActive Biotech (Sweden) · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The intermolecular contact regions between monomers of the homodimeric DNA binding protein ParR and the interaction between the glycoproteins CD28 and CD80 were investigated using a strategy that combined chemical cross-linking with differential MALDI-MS analyses. ParR dimers were modified in vitro with the thiol-cleavable cross-linker 3,3'-dithio-bis(succinimidylproprionate) (DTSSP), proteolytically digested with trypsin and analyzed by MALDI-MS peptide mapping. Comparison of the peptide maps obtained from digested cross-linked ParR dimers in the presence and absence of a thiol reagent strongly supported a "head-to-tail" arrangement of the monomers in the dimeric complex. Glycoprotein fusion constructs CD28-IgG and CD80-Fab were cross-linked in vitro by DTSSP, characterized by nonreducing SDS-PAGE, digested in situ with trypsin and analyzed by MALDI-MS peptide mapping (+/- thiol reagent). The data revealed the presence of an intermolecular cross-link between the receptor regions of the glycoprotein constructs, as well as a number of unexpected but nonetheless specific interactions between the fusion domains of CD28-IgG and the receptor domain of CD80-Fab. The strategy of chemical cross-linking combined with differential MALDI-MS peptide mapping (+ thiol reagent) enabled localization of the interface region(s) of the complexes studied and clearly demonstrates the utility of such an approach to obtain structural information on interacting noncovalent complexes.

Indexed as

Bacterial ProteinsAmino Acid SequenceB7-1 AntigenBinding SitesCD28 AntigensCross-Linking ReagentsCysteineDNA-Binding ProteinsElectrophoresis, Polyacrylamide GelLysineMolecular Sequence DataPeptide MappingRepressor ProteinsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationB7-1 AntigenBacterial ProteinsCD28 AntigensCross-Linking ReagentsCysteineDNA-Binding ProteinsLysineParR protein, bacteriaRepressor Proteins

Identifiers

PMID10975572
PMCPMC2144725
OpenAlexW2101522386

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.