Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Cryo electron microscopy of ex-vivo murine SAA amyloid fibrils

ABSTRACT:

SUBMITTER: Matthias Schmidt

PROVIDER: EMPIAR-10825 | biostudies-other |

REPOSITORIES: biostudies-other

ACCESS DATA

Json Xml

Publications

Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids.

Liberta Falk F Loerch Sarah S Rennegarbe Matthies M Schierhorn Angelika A Westermark Per P Westermark Gunilla T GT Hazenberg Bouke P C BPC Grigorieff Nikolaus N Fändrich Marcus M Schmidt Matthias M

Nature communications 20190307 1

Systemic AA amyloidosis is a worldwide occurring protein misfolding disease of humans and animals. It arises from the formation of amyloid fibrils from the acute phase protein serum amyloid A. Here, we report the purification and electron cryo-microscopy analysis of amyloid fibrils from a mouse and a human patient with systemic AA amyloidosis. The obtained resolutions are 3.0 Å and 2.7 Å for the murine and human fibril, respectively. The two fibrils differ in fundamental properties, such as pres ...[more]

PMID: 30846696

Similar Datasets

Cryo electron microscopy of ex-vivo human SAA amyloid fibrils

Project description: Not available

| EMPIAR-10734 | biostudies-other

Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy.

Project description:High resolution structural information on amyloid fibrils is crucial for the understanding of their formation mechanisms and for the rational design of amyloid inhibitors in the context of protein misfolding diseases. The Src-homology 3 domain of phosphatidyl-inositol-3-kinase (PI3K-SH3) is a model amyloid system that plays a pivotal role in our basic understanding of protein misfolding and aggregation. Here, we present the atomic model of the PI3K-SH3 amyloid fibril with a resolution determined to 3.4?Å by cryo-electron microscopy (cryo-EM). The fibril is composed of two intertwined protofilaments that create an interface spanning 13 residues from each monomer. The model comprises residues 1-77 out of 86 amino acids in total, with the missing residues located in the highly flexible C-terminus. The fibril structure allows us to rationalise the effects of chemically conservative point mutations as well as of the previously reported sequence perturbations on PI3K-SH3 fibril formation and growth.

| S-EPMC6704188 | biostudies-literature

Nanoscale flexibility parameters of Alzheimer amyloid fibrils determined by electron cryo-microscopy.

Project description: Not available

| S-EPMC2913414 | biostudies-literature

Structural polymorphism of amyloid fibrils in ATTR amyloidosis revealed by cryo-electron microscopy.

Project description:ATTR amyloidosis is caused by the deposition of transthyretin in the form of amyloid fibrils in virtually every organ of the body, including the heart. This systemic deposition leads to a phenotypic variability that has not been molecularly explained yet. In brain amyloid conditions, previous studies suggest an association between clinical phenotype and the molecular structures of their amyloid fibrils. Here we investigate whether there is such an association in ATTRv amyloidosis patients carrying the mutation I84S. Using cryo-electron microscopy, we determined the structures of cardiac fibrils extracted from three ATTR amyloidosis patients carrying the ATTRv-I84S mutation, associated with a consistent clinical phenotype. We found that in each ATTRv-I84S patient, the cardiac fibrils exhibited different local conformations, and these variations can co-exist within the same fibril. Our finding suggests that one amyloid disease may associate with multiple fibril structures in systemic amyloidoses, calling for further studies.

| S-EPMC10794703 | biostudies-literature

Cryo electron microscopy of in vitro recombinant SAA1.1 amyloid fibrils

Project description: Not available

| EMPIAR-11027 | biostudies-other

Structural polymorphism of amyloid fibrils in ATTR amyloidosis revealed by cryo-electron microscopy

Project description:Identification of tryptic and non tryptic fragments in ATTRv-I84S and wild type control sample (Supplementary table 2). Sample ID 1120233: wild type Sample ID 1123799: I84S, Patient 2 Sample ID 1123800: I84S, Patient 3 Sample ID1123801: I84S, Patient 1

2023-10-06 | MSV000093062 | MassIVE

Structural polymorphism of amyloid fibrils in ATTR amyloidosis revealed by cryo-electron microscopy

Project description:Identification of ATTR C-terminal fragment by LC/MS QTOF in ATTRv-I84S samples (Supplementary Fig.3 and supplementary table 1) 1126546: Patient 2 1126547: Patient 3 1126548 :Patient 1

2023-10-06 | MSV000093061 | MassIVE

2.7 A cryo-EM structure of ex vivo RML prion fibrils.

Project description:Mammalian prions propagate as distinct strains and are composed of multichain assemblies of misfolded host-encoded prion protein (PrP). Here, we present a near-atomic resolution cryo-EM structure of PrP fibrils present in highly infectious prion rod preparations isolated from the brains of RML prion-infected mice. We found that prion rods comprise single-protofilament helical amyloid fibrils that coexist with twisted pairs of the same protofilaments. Each rung of the protofilament is formed by a single PrP monomer with the ordered core comprising PrP residues 94-225, which folds to create two asymmetric lobes with the N-linked glycans and the glycosylphosphatidylinositol anchor projecting from the C-terminal lobe. The overall architecture is comparable to that of recently reported PrP fibrils isolated from the brain of hamsters infected with the 263K prion strain. However, there are marked conformational variations that could result from differences in PrP sequence and/or represent distinguishing features of the distinct prion strains.

| S-EPMC9279362 | biostudies-literature

Ex vivo murine AApoAII amyloid fibril

Project description: Not available

| EMPIAR-11525 | biostudies-other

Cryo electron microscopy of hIAPP fibrils seeded by patient-extracted fibrils

Project description: Not available

| EMPIAR-10868 | biostudies-other