Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Induction of protein conformational change in mouse senile amyloidosis.

The Journal of biological chemistry - 6 Sept 2002

Xing Yanming, Nakamura Akihiro, Korenaga Tatsumi, Guo Zhanjun, Yao Junjie, Fu Xiaoying, Matsushita Takatoshi, Kogishi Kumiko, Hosokawa Masanori, Kametani Fuyuki, Mori Masayuki, Higuchi Keiichi

Abstract excerpt

Aggregated amyloid fibrils can induce further polymerization of precursor proteins in vitro, thus providing a possible basis for propagation or transmission in the pathogenesis of amyloidoses. Previously, we postulated that the transmission of amyloid fibrils induces conformational changes of endogenous amyloid protein in mouse senile amyloidosis (Xing, Y., Nakamura, A., Chiba, T., Kogishi, K., Matsushita, T.,...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Time Factors
Share to Amyloid

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Amyloid Neuropathies

Share to Apolipoprotein A-II

Share to Microscopy, Electron

Share to Protein Conformation

Share to Protein Folding

Share to Tissue Distribution

Source

Identifiers

PMID: 12077115
DOI: 10.1074/jbc.M111570200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Induction of protein conformational change in mouse senile amyloidosis.PMID 12077115Read ↗

Tissue distribution, biochemical properties, and transmission of mouse type A AApoAII amyloid fibrils.Semantic proximity Read ↗

Transmission of amyloidosis in offspring of mice with AApoAII amyloidosis.Semantic proximity Read ↗

A mouse model of cardiac immunoglobulin light chain amyloidosis reveals insights into tissue accumulation and toxicity of amyloid fibrilsSemantic proximity Read ↗

Insights into the Structural Basis of Amyloid Resistance Provided by Cryo-EM Structures of AApoAII Amyloid Fibrils.Semantic proximity Read ↗

Accelerated senile amyloidosis induced by amyloidogenic Apoa-II gene shortens the life span of mice but does not accelerate the rate of senescence.Semantic proximity Read ↗

Understanding AL amyloidosis with a little help from in vivo modelsSemantic proximity Read ↗

Accelerated APOA-II senile amyloidosis in a <i>PAI-1</i> (plasminogen activator inhibitor 1) knock-out modelSemantic proximity Read ↗

Assessment of the biochemical basis underlying the resistance against systemic amyloidosis.Semantic proximity Read ↗

Polymorphism of Amyloid Fibrils In VivoSemantic proximity Read ↗

Amyloidosis modifier genes in the less amyloidogenic a/j mouse strain.Semantic proximity Read ↗

Wild type ApoA-II gene does not rescue senescence-accelerated mouse (SAMP1) from short life span and accelerated mortality.Semantic proximity Read ↗

AA amyloidosis-resistant CE/J mice have Saa1 and Saa2 genes that encode an identical SAA isoform.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.