In one paragraphArticle in International journal of molecular sciences, 2026. 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
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 registryThe 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 literatureWho cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
4 · The recordCorrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
5 · Who and what moneyAuthors and funding
16 authors.
Maria A TimchenkoInstitute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino 142290, Russia.ORCID 0000-0003-2547-8804 Oxana V GalzitskayaInstitute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino 142290, Russia.ORCID 0000-0002-3962-1520 Alexander V ChulkovDepartment of Fundamental Medicine, Mari State University, Pl. Lenina 1, Yoshkar-Ola 424001, Russia.ORCID 0009-0004-2813-442X Ilya V LikhachevInstitute of Protein Research, Russian Academy of Sciences, Pushchino 142290, Russia.ORCID 0000-0002-4926-5654 Anna V GlyakinaInstitute of Protein Research, Russian Academy of Sciences, Pushchino 142290, Russia.
Maxim V MolchanovInstitute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino 142290, Russia.
Nikolay V MolochkovInstitute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino 142290, Russia.
Nikita V PenkovInstitute of Cell Biophysics, FRC PSCBR, Russian Academy of Sciences, Pushchino 142290, Russia.ORCID 0000-0003-2212-5640 Liya G BobylevaInstitute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino 142290, Russia.
Vitalii A BalobanovInstitute of Protein Research, Russian Academy of Sciences, Pushchino 142290, Russia.
Alexander Ye YegorovInstitute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino 142290, Russia.ORCID 0000-0003-0629-4014 Sergey G GuryanovInstitute of Protein Research, Russian Academy of Sciences, Pushchino 142290, Russia.ORCID 0000-0003-3058-5460 Alexey D NikulinInstitute of Protein Research, Russian Academy of Sciences, Pushchino 142290, Russia.
Dmitry N LyabinInstitute of Protein Research, Russian Academy of Sciences, Pushchino 142290, Russia.
Ivan M VikhlyantsevInstitute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino 142290, Russia.ORCID 0000-0001-6063-6789 Alexander G BobylevScientific Center of Genetics and Life Sciences, Sirius University of Science and Technology, Sirius Federal Territory 354340, Russia.
Funding
State Program of the Sirius Federal Territory "Scientific and technological development of the Sirius Federal Territory" Agreement No. 18-03, dated 10 September 2024
6 · The paper itselfAbstract
The central role of YB-1 in messenger ribonucleoprotein particle (mRNP) metabolism and stress-granule biology highlights the importance of defining the determinants of its self-assembly. YB-1 fibrillogenesis has been attributed primarily to the cold shock domain (CSD). Here, we show that the YB-1 fragment spanning residues 1-129 (AP-CSD) form amyloid fibrils under near-physiological ionic strength (0.12-0.15 M KCl). Fibrillization proceeds without a pronounced exponential growth phase and increases approximately linearly over 45-50 h. Far-UV circular dichroism (CD) and attenuated total reflection Fourier-transform infrared spectroscopy (ATR-FTIR) indicate no substantial change in overall secondary-structure content during aggregation. In parallel,
Indexed as
AmyloidY-Box-Binding Protein 1Circular DichroismHumansProtein AggregatesProtein DomainsProtein Structure, SecondarySpectroscopy, Fourier Transform InfraredX-Ray DiffractionAmyloidProtein AggregatesY-Box-Binding Protein 1YBX1 protein, humanamyloid fibrilsATR-FTIRcircular dichroismcold shock domaincross-β structureprotein aggregationsolution NMRX-ray fiber diffractionYB-1
Identifiers
PMID42074193
PMCPMC13116819
What OpenQuestion holds
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LicenceCC BY
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