Evidence map›Paper›PMID 31333815›Full record

ArticleComputational and structural biotechnology journal2019

Oxidation State Dependent Conformational Changes of HMGB1 Regulate the Formation of the CXCL12/HMGB1 Heterocomplex.

Enrico M A Fassi, Jacopo Sgrignani, Gianluca D'Agostino, Valentina Cecchinato, Maura Garofalo, Giovanni Grazioso, Mariagrazia Uguccioni, Andrea Cavalli

Open access · goldAbstract read
In one paragraph

Article in Computational and structural biotechnology journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.7field-weighted citation impact, top 19% 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

16 citing papers in PubMed, 27 citations in OpenAlex.

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  8. The Therapeutic Potential of Pyroptosis in Melanoma.International journal of molecular sciences · 2023
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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

8 authors at 4 institutions in 2 countries.

Enrico M A FassiInstitute for Research in Biomedicine, Università della Svizzera Italiana, CH-6500 Bellinzona, Switzerland.
Jacopo SgrignaniInstitute for Research in Biomedicine, Università della Svizzera Italiana, CH-6500 Bellinzona, Switzerland.
Gianluca D'AgostinoInstitute for Research in Biomedicine, Università della Svizzera Italiana, CH-6500 Bellinzona, Switzerland.
Valentina CecchinatoInstitute for Research in Biomedicine, Università della Svizzera Italiana, CH-6500 Bellinzona, Switzerland.
Maura GarofaloInstitute for Research in Biomedicine, Università della Svizzera Italiana, CH-6500 Bellinzona, Switzerland.
Giovanni GraziosoDipartimento di Scienze Farmaceutiche, Università degli Studi di Milano, Milan, Italy.
Mariagrazia UguccioniInstitute for Research in Biomedicine, Università della Svizzera Italiana, CH-6500 Bellinzona, Switzerland.
Andrea CavalliInstitute for Research in Biomedicine, Università della Svizzera Italiana, CH-6500 Bellinzona, Switzerland.
Università della Svizzera italiana · CHHumanitas University · ITSIB Swiss Institute of Bioinformatics · CHUniversity of Milan · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

High-mobility Group Box 1 (HMGB1) is an abundant protein present in all mammalian cells and involved in several processes. During inflammation or tissue damage, HMGB1 is released in the extracellular space and, depending on its redox state, can form a heterocomplex with CXCL12. The heterocomplex acts exclusively via the chemokine receptor CXCR4 enhancing leukocyte recruitment. Here, we used multi-microsecond molecular dynamics (MD) simulations to elucidate the effect of the disulfide bond on the structure and dynamics of HMGB1. The results of the MD simulations show that the presence or lack of the disulfide bond between Cys23 and Cys45 modulates the conformational space explored by HMGB1, making the reduced protein more suitable to form a complex with CXCL12.

Indexed as

Conformational ensembleCXCL12CXCL12, C-X-C motif chemokine 12CXCR4, C-X-C chemokine receptor type 4ds-HMGB1, Disulfide High-mobility Group Box 1fr-HMGB1, Full reduced High-mobility Group Box 1HMGB1HMGB1, High-mobility Group Box 1MD, Molecular dynamicsMolecular dynamicsProtein-protein dockingRMSD, Root mean square deviationRoG, Radius of gyrationSASA, Solvent accessible surface areaTLR2 or TLR4, Toll-like Receptor 2 or 4

Identifiers

PMID31333815
PMCPMC6617219
OpenAlexW2951923332

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.