001     1043722
005     20250820202246.0
024 7 _ |a 10.1002/pro.70188
|2 doi
024 7 _ |a 0961-8368
|2 ISSN
024 7 _ |a 1469-896X
|2 ISSN
024 7 _ |a 10.34734/FZJ-2025-03008
|2 datacite_doi
024 7 _ |a 40563206
|2 pmid
024 7 _ |a WOS:001516471300001
|2 WOS
037 _ _ |a FZJ-2025-03008
082 _ _ |a 610
100 1 _ |a Leitz, Anna
|0 P:(DE-HGF)0
|b 0
245 _ _ |a Guanidinylation of the cold shock protein YB ‐1: Molecular basis, structural changes and Notch‐3 receptor binding
260 _ _ |a Hoboken, NJ
|c 2025
|b Wiley
336 7 _ |a article
|2 DRIVER
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|b journal
|m journal
|0 PUB:(DE-HGF)16
|s 1752754940_1979
|2 PUB:(DE-HGF)
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a Journal Article
|0 0
|2 EndNote
520 _ _ |a 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.
536 _ _ |a 5241 - Molecular Information Processing in Cellular Systems (POF4-524)
|0 G:(DE-HGF)POF4-5241
|c POF4-524
|f POF IV
|x 0
588 _ _ |a Dataset connected to CrossRef, Journals: juser.fz-juelich.de
700 1 _ |a Kav, Batuhan
|0 P:(DE-Juel1)178946
|b 1
700 1 _ |a Liu, Xiyang
|0 P:(DE-HGF)0
|b 2
700 1 _ |a Fatafta, Hebah
|0 P:(DE-Juel1)176262
|b 3
700 1 _ |a Jankowski, Vera
|0 P:(DE-HGF)0
|b 4
700 1 _ |a Aggeler, Bastian
|0 P:(DE-HGF)0
|b 5
700 1 _ |a Gao, Yingying
|0 P:(DE-HGF)0
|b 6
700 1 _ |a Martin, Ina Verena
|0 P:(DE-HGF)0
|b 7
700 1 _ |a Vogt, Kristian
|0 P:(DE-HGF)0
|b 8
700 1 _ |a Kramann, Rafael
|0 P:(DE-HGF)0
|b 9
700 1 _ |a Ostendorf, Tammo
|0 P:(DE-HGF)0
|b 10
700 1 _ |a Rauen, Thomas
|0 P:(DE-HGF)0
|b 11
700 1 _ |a Strodel, Birgit
|0 P:(DE-Juel1)132024
|b 12
|e Corresponding author
700 1 _ |a Raffetseder, Ute
|0 0000-0002-7236-9793
|b 13
|e Corresponding author
773 _ _ |a 10.1002/pro.70188
|g Vol. 34, no. 7, p. e70188
|0 PERI:(DE-600)2000025-X
|n 7
|p e70188
|t Protein science
|v 34
|y 2025
|x 0961-8368
856 4 _ |u https://juser.fz-juelich.de/record/1043722/files/Protein%20Science%20-%202025%20-%20Leitz%20-%20Guanidinylation%20of%20the%20cold%20shock%20protein%20YB%E2%80%901%20Molecular%20basis%20structural%20changes%20and.pdf
|y OpenAccess
909 C O |o oai:juser.fz-juelich.de:1043722
|p openaire
|p open_access
|p OpenAPC_DEAL
|p driver
|p VDB
|p openCost
|p dnbdelivery
910 1 _ |a Forschungszentrum Jülich
|0 I:(DE-588b)5008462-8
|k FZJ
|b 12
|6 P:(DE-Juel1)132024
913 1 _ |a DE-HGF
|b Key Technologies
|l Natural, Artificial and Cognitive Information Processing
|1 G:(DE-HGF)POF4-520
|0 G:(DE-HGF)POF4-524
|3 G:(DE-HGF)POF4
|2 G:(DE-HGF)POF4-500
|4 G:(DE-HGF)POF
|v Molecular and Cellular Information Processing
|9 G:(DE-HGF)POF4-5241
|x 0
914 1 _ |y 2025
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0200
|2 StatID
|b SCOPUS
|d 2025-01-01
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0160
|2 StatID
|b Essential Science Indicators
|d 2025-01-01
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)1050
|2 StatID
|b BIOSIS Previews
|d 2025-01-01
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)1190
|2 StatID
|b Biological Abstracts
|d 2025-01-01
915 _ _ |a Creative Commons Attribution CC BY 4.0
|0 LIC:(DE-HGF)CCBY4
|2 HGFVOC
915 _ _ |a JCR
|0 StatID:(DE-HGF)0100
|2 StatID
|b PROTEIN SCI : 2022
|d 2025-01-01
915 _ _ |a DEAL Wiley
|0 StatID:(DE-HGF)3001
|2 StatID
|d 2025-01-01
|w ger
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)1030
|2 StatID
|b Current Contents - Life Sciences
|d 2025-01-01
915 _ _ |a WoS
|0 StatID:(DE-HGF)0113
|2 StatID
|b Science Citation Index Expanded
|d 2025-01-01
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0150
|2 StatID
|b Web of Science Core Collection
|d 2025-01-01
915 _ _ |a OpenAccess
|0 StatID:(DE-HGF)0510
|2 StatID
915 _ _ |a IF >= 5
|0 StatID:(DE-HGF)9905
|2 StatID
|b PROTEIN SCI : 2022
|d 2025-01-01
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0300
|2 StatID
|b Medline
|d 2025-01-01
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0199
|2 StatID
|b Clarivate Analytics Master Journal List
|d 2025-01-01
915 p c |a APC keys set
|2 APC
|0 PC:(DE-HGF)0000
915 p c |a Local Funding
|2 APC
|0 PC:(DE-HGF)0001
915 p c |a DFG OA Publikationskosten
|2 APC
|0 PC:(DE-HGF)0002
915 p c |a DEAL: Wiley 2019
|2 APC
|0 PC:(DE-HGF)0120
920 _ _ |l yes
920 1 _ |0 I:(DE-Juel1)IBI-7-20200312
|k IBI-7
|l Strukturbiochemie
|x 0
980 1 _ |a FullTexts
980 _ _ |a journal
980 _ _ |a VDB
980 _ _ |a UNRESTRICTED
980 _ _ |a I:(DE-Juel1)IBI-7-20200312
980 _ _ |a APC


LibraryCollectionCLSMajorCLSMinorLanguageAuthor
Marc 21