Evidence map›Paper›PMID 36545626›Full record

ArticleRSC advances2022

Dual activity inhibition of threonine aspartase 1 by a single bisphosphate ligand.

Alexander Höing, Robin Struth, Christine Beuck, Neda Rafieiolhosseini, Daniel Hoffmann, Roland H Stauber, Peter Bayer, Jochen Niemeyer, Shirley K Knauer

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in RSC advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 62% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. 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

9 authors at 2 institutions in 1 country.

Alexander HöingMolecular Biology II, Center of Medical Biotechnology (ZMB)/Center for Nanointegration Duisburg-Essen (CENIDE), University of Duisburg-Essen, Universitätsstrasse 5 45141 Essen Germany shirley.knauer@uni-due.de.ORCID https://orcid.org/0000-0002-3762-4832
Robin StruthOrganic Chemistry, Center for Nanointegration Duisburg-Essen (CENIDE), University of Duisburg-Essen, Universitätsstrasse 7 45141 Essen Germany jochen.niemeyer@uni-due.de.ORCID https://orcid.org/0000-0002-5130-4990
Christine BeuckStructural and Medicinal Biochemistry, Center for Medical Biotechnology (ZMB), University of Duisburg-Essen, Universitätsstrasse 5 45141 Essen Germany.ORCID https://orcid.org/0000-0001-7513-7384
Neda RafieiolhosseiniBioinformatics and Computational Biophysics, Center for Medical Biotechnology (ZMB), University of Duisburg-Essen, Universitätsstrasse 5 45141 Essen Germany.ORCID https://orcid.org/0000-0002-2347-7747
Daniel HoffmannBioinformatics and Computational Biophysics, Center for Medical Biotechnology (ZMB), University of Duisburg-Essen, Universitätsstrasse 5 45141 Essen Germany.ORCID https://orcid.org/0000-0003-2973-7869
Roland H StauberMolecular and Cellular Oncology/ENT, University Medical Center Mainz (UMM) Langenbeckstrasse 1 55101 Mainz Germany.ORCID https://orcid.org/0000-0002-1341-4523
Peter BayerStructural and Medicinal Biochemistry, Center for Medical Biotechnology (ZMB), University of Duisburg-Essen, Universitätsstrasse 5 45141 Essen Germany.ORCID https://orcid.org/0000-0003-0435-7202
Jochen NiemeyerOrganic Chemistry, Center for Nanointegration Duisburg-Essen (CENIDE), University of Duisburg-Essen, Universitätsstrasse 7 45141 Essen Germany jochen.niemeyer@uni-due.de.ORCID https://orcid.org/0000-0002-9295-4260
Shirley K KnauerMolecular Biology II, Center of Medical Biotechnology (ZMB)/Center for Nanointegration Duisburg-Essen (CENIDE), University of Duisburg-Essen, Universitätsstrasse 5 45141 Essen Germany shirley.knauer@uni-due.de.ORCID https://orcid.org/0000-0003-4321-0924
University of Duisburg-Essen · DEJohannes Gutenberg University Mainz · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Therapy resistance remains a challenge for the clinics. Here, dual-active chemicals that simultaneously inhibit independent functions in disease-relevant proteins are desired though highly challenging. As a model, we here addressed the unique protease threonine aspartase 1, involved in various cancers. We hypothesized that targeting basic residues in its bipartite nuclear localization signal (NLS) by precise bisphosphate ligands inhibits additional steps required for protease activity. We report the bisphosphate anionic bivalent inhibitor 11d, selectively binding to the basic NLS cluster (

Identifiers

PMID36545626
PMCPMC9709806
OpenAlexW4312113466

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.