[English] 日本語
Yorodumi Papers
- Database of articles cited by EMDB/PDB/SASBDB data -

+
Search query

Keywords
Structure methods
Author
Journal
IF

-
Structure paper

TitleSeeding biosensor cell line that reproduces the Alzheimer tau fold.
Journal, issue, pagesJ Biol Chem, Vol. 301, Issue 12, Page 110952, Year 2025
Publish dateNov 17, 2025
AuthorsTaxiarchis Katsinelos / Sofia Lövestam / Chao Qi / Benjamin Ryskeldi-Falcon / Jennifer A Macdonald / Gabriel Stephenson / Bernardino Ghetti / Ann McKee / Sjors H W Scheres / Michel Goedert /
PubMed AbstractThe assembly of tau protein into amyloid filaments through templated seeding is believed to underlie the propagation of pathology in neurodegenerative diseases, such as Alzheimer's disease (AD) and ...The assembly of tau protein into amyloid filaments through templated seeding is believed to underlie the propagation of pathology in neurodegenerative diseases, such as Alzheimer's disease (AD) and other tauopathies. A commonly used model system for studying this process is through the induction of tau filament formation in cultured cells following the addition of tau seeds isolated from the human brain. However, little is known about the structures of seeded filaments; some biosensor cell lines are unable to reproduce the tau filament structures from AD, because they overexpress tau fragments that do not cover the whole of the ordered filament core. Here, we describe a novel tau seeding biosensor model in human embryonic kidney 293T cells that overexpress residues K297-E391 of human 4R tau. The construct contains an N-terminal hemagglutinin tag, which allows the specific detection of the amplified template. The biosensor cells detected filaments seeded by material from sporadic three-repeat (3R) + four-repeat (4R) tauopathies, with little activity by seeds from 3R-only or 4R-only tauopathies. The sensitivity of seed detection from 3R + 4R tauopathies in our system was similar to or higher than for previously reported biosensors. We also structurally characterized the AD-seeded tau filaments by cryo-EM. Most of the cell-derived filaments consisted of two protofilaments with the Alzheimer's fold but with a "head-to-head" interprotofilament packing. Our results establish a sensitive biosensor cell line with specificity toward seeds from 3R + 4R tauopathies.
External linksJ Biol Chem / PubMed:41260337 / PubMed Central
MethodsEM (helical sym.)
Resolution3.4 Å
Structure data

54909

9shs

EMDB-54909, PDB-9shs:
Head to Head tau filament with the Alzheimer's fold
Method: EM (helical sym.) / Resolution: 3.4 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / TAU / HELICAL / FILAMENT / FIBRIL / AMYLOID / ALZHEIMER'S DISEASE / PAIRED HELICAL FILAMENT

+
About Yorodumi Papers

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi Papers

Database of articles cited by EMDB/PDB/SASBDB data

  • Database of articles cited by EMDB, PDB, and SASBDB entries
  • Using PubMed data

Related info.:EMDB / PDB / SASBDB / Yorodumi / EMN Papers / Changes in new EM Navigator and Yorodumi

Read more