Evidence map›Paper›PMID 30514002›Full record

ArticleInternational journal of molecular sciences2018

Insight into Inhibitor Binding in the Eukaryotic Proteasome: Computations of the 20S CP.

Milan Hodošček, Nadia Elghobashi-Meinhardt

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

2 authors.

Milan HodoščekNational Institute of Chemistry, Hajdrihova 19, 1001 Ljubljana, Slovenia. milan@cmm.ki.si.
Nadia Elghobashi-MeinhardtDepartment of Chemistry and Biochemistry, Freie Universität Berlin, 14195 Berlin, Germany. nadia.elghobashi-meinhardt@fu-berlin.de.ORCID 0000-0002-1023-6856

Funding

Javna Agencija za Raziskovalno Dejavnost RS P1-0002Volkswagen Foundation 86539
6 · The paper itself

Abstract

A combination of molecular dynamics (MD) simulations and computational analyses uncovers structural features that may influence substrate passage and exposure to the active sites within the proteolytic chamber of the 20S proteasome core particle (CP). MD simulations of the CP reveal relaxation dynamics in which the CP slowly contracts over the 54 ns sampling period. MD simulations of the SyringolinA (SylA) inhibitor within the proteolytic B 1 ring chamber of the CP indicate that favorable van der Waals and electrostatic interactions account for the predominant association of the inhibitor with the walls of the proteolytic chamber. The time scale required for the inhibitor to travel from the center of the proteolytic chamber to the chamber wall is on the order of 4 ns, accompanied by an average energetic stabilization of approximately -20 kcal/mol.

Indexed as

EukaryotaModels, MolecularMolecular Dynamics SimulationPeptides, CyclicProteasome Endopeptidase ComplexProteasome InhibitorsThermodynamicsPeptides, CyclicProteasome Endopeptidase ComplexProteasome Inhibitorssyringolin Aproteasome, CP

Identifiers

PMID30514002
PMCPMC6321098

What OpenQuestion holds

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Registered trials

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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.