Evidence map›Paper›PMID 31640223›Full record

ArticleInternational journal of molecular sciences2019

Combination of SAXS and Protein Painting Discloses the Three-Dimensional Organization of the Bacterial Cysteine Synthase Complex, a Potential Target for Enhancers of Antibiotic Action.

Brenda Rosa, Marialaura Marchetti, Gianluca Paredi, Heinz Amenitsch, Nina Franko, Roberto Benoni, Barbara Giabbai, Maria Giovanna De Marino, Andrea Mozzarelli, Luca Ronda and 3 more

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 36% 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

6 citing papers in PubMed, 16 citations in OpenAlex.

  1. iScience · 2026
    Article
  2. Article
  3. Article
  4. Molecular responses during bacterial filamentation reveal inhibition methods of drug-resistant bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  5. Review
  6. 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

13 authors at 3 institutions in 3 countries.

Brenda RosaDipartimento di Medicina e Chirurgia, Università di Parma, Via Gramsci 14, 43126 Parma, Italy. brenda.rosa@studenti.unipr.it.ORCID 0000-0002-7203-0490
Marialaura MarchettiCentro Interdipartimentale Biopharmanet-TEC, Università di Parma, Parco Area delle Scienze 27/A, 43124 Parma, Italy. marialaura.marchetti@unipr.it.ORCID 0000-0002-4615-6786
Gianluca ParediCentro Interdipartimentale Siteia, Università di Parma, Parco Area delle Scienze 181/A, 43124 Parma, Italy. gianluca.paredi@unipr.it.ORCID 0000-0003-2659-7485
Heinz AmenitschInstitute for Inorganic Chemistry, Graz University of Technology, Stremayrgasse 9, 8010 Graz, Austria. heinz.amenitsch@elettra.eu.ORCID 0000-0002-0788-1336
Nina FrankoDipartimento di Scienze degli Alimenti e del Farmaco, Università di Parma, Parco Area delle Scienze 23/A, 43124 Parma, Italy. nina.franko@studenti.unipr.it.
Roberto BenoniDipartimento di Medicina e Chirurgia, Università di Parma, Via Gramsci 14, 43126 Parma, Italy. roberto.benoni@uochb.cas.cz.
Barbara GiabbaiStructural Biology Laboratory, Elettra Sincrotrone Trieste S.C.p.A., SS 14 km 163,5 in AREA Science Park-Basovizza, 34149 Trieste, Italy. barbara.giabbai@elettra.eu.
Maria Giovanna De MarinoDipartimento di Medicina e Chirurgia, Università di Parma, Via Gramsci 14, 43126 Parma, Italy. mariagiovanna.demarino@studenti.unipr.it.
Andrea MozzarelliDipartimento di Scienze degli Alimenti e del Farmaco, Università di Parma, Parco Area delle Scienze 23/A, 43124 Parma, Italy. andrea.mozzarelli@unipr.it.ORCID 0000-0003-3762-0062
Luca RondaDipartimento di Medicina e Chirurgia, Università di Parma, Via Gramsci 14, 43126 Parma, Italy. luca.ronda@unipr.it.
Paola StoriciStructural Biology Laboratory, Elettra Sincrotrone Trieste S.C.p.A., SS 14 km 163,5 in AREA Science Park-Basovizza, 34149 Trieste, Italy. paola.storici@elettra.eu.ORCID 0000-0002-2590-3332
Barbara CampaniniDipartimento di Scienze degli Alimenti e del Farmaco, Università di Parma, Parco Area delle Scienze 23/A, 43124 Parma, Italy. barbara.campanini@unipr.it.ORCID 0000-0003-0359-0627
Stefano BettatiDipartimento di Medicina e Chirurgia, Università di Parma, Via Gramsci 14, 43126 Parma, Italy. stefano.bettati@unipr.it.ORCID 0000-0001-6787-0594
University of Parma · ITElettra-Sincrotrone Trieste S.C.p.A. · ITGraz University of Technology · AT

Funding

H2020 Marie Skłodowska-Curie Actions 642620University of Parma FIL2016
6 · The paper itself

Abstract

The formation of multienzymatic complexes allows for the fine tuning of many aspects of enzymatic functions, such as efficiency, localization, stability, and moonlighting. Here, we investigated, in solution, the structure of bacterial cysteine synthase (CS) complex. CS is formed by serine acetyltransferase (CysE) and

Indexed as

BacteriaBacterial ProteinsCatalytic DomainCysteine SynthaseIsoenzymesModels, MolecularMultienzyme ComplexesMutagenesis, Site-DirectedProtein Interaction MapsScattering, Small AngleSerine O-AcetyltransferaseX-Ray DiffractionBacterial ProteinsCysteine SynthaseIsoenzymesMultienzyme ComplexesSerine O-Acetyltransferasecysteine biosynthesiscysteine synthase complexO-acetylserine sulfhydrylaseprotein paintingSAXSserine acetyltransferase

Identifiers

PMID31640223
PMCPMC6829319
OpenAlexW2980345132

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.