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

Mutational analysis of the aggregation-prone and disaggregation-prone regions of acylphosphatase.

Journal of molecular biology - 10 Apr 2009

Calamai Martino, Tartaglia Gian Gaetano, Vendruscolo Michele, Chiti Fabrizio, Dobson Christopher M

Abstract excerpt

We have performed an extensive mutational analysis of aggregation and disaggregation of amyloid-like protofibrils of human muscle acylphosphatase. Our findings indicate that the regions that promote aggregation in 25% (v/v) 2,2,2 trifluoroethanol (TFE) are different from those that promote disaggregation under milder conditions (5% TFE). Significant changes in the rate of disaggregation of protofibrils in 5% TFE...

Read the complete abstract on PubMed

Topics

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

Share to Acid Anhydride Hydrolases
Share to Amyloid

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Enzyme Stability

Share to In Vitro Techniques

Share to Muscles

Share to Protein Folding

Share to Protein Structure, Quaternary

Share to Spectrometry, Fluorescence

Source

Identifiers

PMID: 18809411
DOI: 10.1016/j.jmb.2008.09.003

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutational analysis of the aggregation-prone and disaggregation-prone regions of acylphosphatase.PMID 18809411Read ↗

Folding and aggregation are selectively influenced by the conformational preferences of the alpha-helices of muscle acylphosphatase.Semantic proximity Read ↗

Stabilisation of alpha-helices by site-directed mutagenesis reveals the importance of secondary structure in the transition state for acylphosphatase folding.Semantic proximity Read ↗

Structural and thermodynamic investigations on the aggregation and folding of acylphosphatase by molecular dynamics simulations and solvation free energy analysis.Semantic proximity Read ↗

Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation.Semantic proximity Read ↗

Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases.Semantic proximity Read ↗

Perfecting prediction of mutational impact on the aggregation propensity of the ALS-associated hnRNPA2 prion-like protein.Semantic proximity Read ↗

Structural characterization of the transition state for folding of muscle acylphosphatase.Semantic proximity Read ↗

Alterations in local stability and dynamics of A4V SOD1 in the presence of trifluoroethanol.Semantic proximity Read ↗

Impact of pathogenic mutations on the refolding ability and stability of human mitochondrial Phenylalanyl-tRNA synthetase.Semantic proximity Read ↗

Single-residue physicochemical characteristics kinetically partition membrane protein self-assembly and aggregation.Semantic proximity Read ↗

Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding.Semantic proximity Read ↗

Rapid oligomer formation of human muscle acylphosphatase induced by heparan sulfate.Semantic proximity Read ↗

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