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

Structural Analysis of Multi-component Amyloid Systems by Chemometric SAXS Data Decomposition.

Structure (London, England : 1993) - 3 Jan 2017

Herranz-Trillo Fátima, Groenning Minna, van Maarschalkerweerd Andreas, Tauler Romà, Vestergaard Bente, Bernadó Pau

Abstract excerpt

Formation of amyloids is the hallmark of several neurodegenerative pathologies. Structural investigation of these complex transformation processes poses significant experimental challenges due to the co-existence of multiple species. The additive nature of small-angle X-ray scattering (SAXS) data allows for probing the evolution of these mixtures of oligomeric states, but the decomposition of SAXS data into...

Read the complete abstract on PubMed

Topics

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

Share to Algorithms
Share to alpha-Synuclein

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Insulin

Share to Least-Squares Analysis

Share to Multiprotein Complexes

Share to Protein Multimerization

Share to Scattering, Small Angle

Share to X-Ray Diffraction

Source

Identifiers

PMID: 27889205
DOI: 10.1016/j.str.2016.10.013

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 8 closest

Structural Analysis of Multi-component Amyloid Systems by Chemometric SAXS Data Decomposition.PMID 27889205Read ↗

Specter: linear deconvolution for targeted analysis of data-independent acquisition mass spectrometry proteomics.Semantic proximity Read ↗

Exploring ensemble structures of Alzheimer’s amyloid β (1-42) monomer using linear regression for the MD simulation and NMR chemical shiftSemantic proximity Read ↗

Comprehensive Structural and Thermodynamic Analysis of Prefibrillar WT α-Synuclein and Its G51D, E46K, and A53T Mutants by a Combination of Small-Angle X-ray Scattering and Variational Bayesian Weighting.Semantic proximity Read ↗

Optimization of human plasma 1H NMR spectroscopic data processing for high-throughput metabolic phenotyping studies and detection of insulin resistance related to type 2 diabetes.Semantic proximity Read ↗

Data-driven biomarker analysis using computational omics approaches to assess neurodegenerative disease progressionSemantic proximity Read ↗

A framework for automated multimodal HDX-MS analysisSemantic proximity Read ↗

Integrated Clinomics and Molecular Dynamics Simulation Approaches Reveal the SAA1.1 Allele as a Biomarker in Alkaptonuria Disease Severity.Semantic proximity Read ↗

The contribution of biophysical and structural studies of protein self-assembly to the design of therapeutic strategies for amyloid diseasesSemantic proximity Read ↗

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