Evidence map›Paper›PMID 40563206›Full record

ArticleProtein science : a publication of the Protein Society2025

Guanidinylation of the cold shock protein YB-1: Molecular basis, structural changes and Notch-3 receptor binding.

Anna Leitz, Batuhan Kav, Xiyang Liu, Hebah Fatafta, Vera Jankowski, Bastian Aggeler, Yingying Gao, Ina Verena Martin, Kristian Vogt, Rafael Kramann and 4 more

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2025. 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
–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

1 citing paper in PubMed.

  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

14 authors.

Anna LeitzDepartment of Nephrology and Clinical Immunology, RWTH Aachen University, Aachen, Germany.
Batuhan KavInstitute of Biological Information Processing: Structural Biochemistry, Forschungszentrum Jülich, Jülich, Germany.
Xiyang LiuDepartment of Nephrology and Clinical Immunology, RWTH Aachen University, Aachen, Germany.
Hebah FataftaInstitute of Biological Information Processing: Structural Biochemistry, Forschungszentrum Jülich, Jülich, Germany.
Vera JankowskiInstitute for Molecular Cardiovascular Research (IMCAR), RWTH Aachen University, Aachen, Germany.
Bastian AggelerInstitute of Biological Information Processing: Structural Biochemistry, Forschungszentrum Jülich, Jülich, Germany.
Yingying GaoDepartment of Nephrology and Clinical Immunology, RWTH Aachen University, Aachen, Germany.
Ina Verena MartinDepartment of Nephrology and Clinical Immunology, RWTH Aachen University, Aachen, Germany.
Kristian VogtDepartment of Nephrology and Clinical Immunology, RWTH Aachen University, Aachen, Germany.
Rafael KramannDepartment of Nephrology and Clinical Immunology, RWTH Aachen University, Aachen, Germany.
Tammo OstendorfDepartment of Nephrology and Clinical Immunology, RWTH Aachen University, Aachen, Germany.
Thomas RauenDepartment of Nephrology and Clinical Immunology, RWTH Aachen University, Aachen, Germany.
Birgit StrodelInstitute of Biological Information Processing: Structural Biochemistry, Forschungszentrum Jülich, Jülich, Germany.ORCID 0000-0002-8734-7765
Ute RaffetsederDepartment of Nephrology and Clinical Immunology, RWTH Aachen University, Aachen, Germany.ORCID 0000-0002-7236-9793

Funding

Deutsche Forschungsgemeinschaft INST 948/4S-1 FU6.6Deutsche Forschungsgemeinschaft KFO 5011Deutsche Forschungsgemeinschaft OS 196/2-1Deutsche Forschungsgemeinschaft OS 196/4-1Deutsche Forschungsgemeinschaft RA 1927/5-3Deutsche Forschungsgemeinschaft RA 740/11-1Deutsche Forschungsgemeinschaft RA 740/8-1Deutsche Forschungsgemeinschaft RA 740/9-1Deutsche Forschungsgemeinschaft SFB/TRR57 P17Deutsche Forschungsgemeinschaft TRR 219 Project-ID 322900939 subproject S-03Faculty of Medicine of the RWTH 692414; 120/23National Natural Science Foundation of China 201806380070National Natural Science Foundation of China 202008310175
6 · The paper itself

Abstract

Posttranslational modifications of Y-box binding protein (YB)-1 are the prerequisite for its very different protein functions. Here, we investigate the underlying molecular mechanisms of YB-1 guanidinylation and link increased serum urea levels as well as the activity of glycine amidinotransferase (GATM) with guanidinylation. Computer simulations show changes in stability and conformation of the YB-1 protein induced by these modifications. In particular, the secondary structure of the doubly guanidinylated YB-1 (YB-1-2G) shows a reduced tendency to form β-sheets, and the modified cold shock domain is more exposed to the solvent. Protein-protein docking techniques in conjunction with molecular dynamics simulations confirm the binding between YB-1 and its receptor Notch-3 at EGF domains 17-24 but show no significant differences in the binding behavior of YB-1 and YB-1-2G. This is confirmed in two different types of receptor-ligand binding assays. In addition, we demonstrate for the first time a high-affinity binding of YB-1 to another ligand binding site on the Notch-3 receptor, thereby achieving effective displacement of the canonical ligand Jagged. In conclusion, we identified molecular processes that lead to the guanidinylation of YB-1 and revealed their effects on the structure and binding to receptor Notch-3.

Indexed as

Receptor, Notch3Y-Box-Binding Protein 1AnimalsBinding SitesHumansMolecular Docking SimulationMolecular Dynamics SimulationProtein BindingProtein Processing, Post-TranslationalReceptor, Notch3Y-Box-Binding Protein 1YBX1 protein, humanguanidinylationJagged‐1Notch‐3receptor‐ligand interactionYB‐1YB‐1‐2G

Identifiers

PMID40563206
PMCPMC12198050

What Socratic 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 Socratic graph.