Evidence map›Paper›PMID 40253490›Full record

ArticleScientific reports2025

Filamentous chemokine CCL5 structure and the functional aspects.

Yi-Ting Yuan, Tzu-Ching Guo, Chu-Ya Wu, Yi-Qi Yeh, Ching-Tse Wu, Shu-Yao Hsu, Zi-Wen Weng, Meng-Ru Ho, Shang-Te Danny Hsu, Yi-Chen Chen and 4 more

Abstract read
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In one paragraph

Article in Scientific reports, 2025. 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

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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

14 authors.

Yi-Ting Yuan *Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, 30013, Taiwan.
Tzu-Ching Guo *Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, 30013, Taiwan.
Chu-Ya WuInstrumentation Center, National Tsing Hua University, Hsinchu, Taiwan.
Yi-Qi YehNational Synchrotron Radiation Research Center, Hsinchu, Taiwan.
Ching-Tse WuInstitute of Biotechnology, National Tsing Hua University, Hsinchu, Taiwan.
Shu-Yao HsuInstitute of Biotechnology, National Tsing Hua University, Hsinchu, Taiwan.
Zi-Wen WengInstitute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.
Meng-Ru HoInstitute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.
Shang-Te Danny HsuInstitute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.
Yi-Chen ChenInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, 30013, Taiwan.
Chuang-Rung ChangInstitute of Biotechnology, National Tsing Hua University, Hsinchu, Taiwan.
Kuen-Phon WuInstitute of Biological Chemistry, Academia Sinica, Taipei, Taiwan. kpwu@gate.sinica.edu.tw.
U-Ser JengDepartment of Chemical Engineering, National Tsing Hua University, Hsinchu, Taiwan. usjeng@nsrrc.org.tw.
Shih-Che SueInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, 30013, Taiwan. scsue@life.nthu.edu.tw.

Funding

Taiwan Protein Project AS-KPQ-109-TPP2The Academia Core Facility and Innovative Instrument Project AS-CFII-111-210The Ministry of Science and Technology, Taiwan 110-2113-M-007-025The Ministry of Science and Technology, Taiwan 111-2113-M-001-026-MY2
6 · The paper itself

Abstract

Human inflammation-related CC chemokine ligand 5 (hCCL5) has significant self-assembly property under physiological conditions. The mechanism and function of hCCL5 oligomerization remain unclear. Different intermolecular interactions, such as E66-K25 or E66-R44/K45, have been reported to mediate hCCL5 oligomerization. This complexity makes structural determination difficult. Based on a K25S mutation to eliminate the E66-K25 interaction, we observed hCCL5 forming a helical-sharped filament in transmission electron microscopy (TEM). The filamentous polymerization is a dominant process when the concentration reaches ~ 100 nM and the filaments further form a higher-order assembly when concentration increases. In this large filament, a combination of X-ray solution scattering and cryo-EM analysis determined the structure; NMR further confirmed the filament packing, in which the interactions of residues R44 and K45 are critically involved. The sequence

Indexed as

Chemokine CCL5Cryoelectron MicroscopyGlycosaminoglycansHumansModels, MolecularMutationProtein BindingProtein MultimerizationCCL5 protein, humanChemokine CCL5GlycosaminoglycansChemokine CCL5Chemokine secretioncryo-EMFilamentNMRSWAXS

Identifiers

PMID40253490
PMCPMC12009402

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LicenceCC BY-NC-ND
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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.