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

Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation.

Protein science : a publication of the Protein Society - 1 Apr 2001

Chiti F, Taddei N, Stefani M, Dobson C M, Ramponi G

Abstract excerpt

It is known that human muscle acylphosphatase (AcP) is able, under appropriate conditions in vitro, to aggregate and form amyloid fibrils of the type associated with human diseases. A number of compounds were tested for their ability to bind specifically to the native conformation of AcP under co...

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
Share to Circular Dichroism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli

Share to In Vitro Techniques

Share to Kinetics

Share to Protein Conformation

Share to Protein Denaturation

Source

Open in PubMed Open full text

Identifiers

PMID: 11274479
DOI: 10.1110/ps.42401
PMCID: PMC2373972

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-11274479-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation.PMID 11274479Read ↗

Stabilization of a native protein mediated by ligand binding inhibits amyloid formation independently of the aggregation pathway.Semantic proximity Read ↗

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

Molecular mechanisms of fibrillogenesis and the protective role of amyloid P component: two possible avenues for therapy.Semantic proximity Read ↗

Mutational analysis of the aggregation-prone and disaggregation-prone regions of 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 ↗

Targeting Amyloid Aggregation: An Overview of Strategies and MechanismsSemantic proximity Read ↗

A Spider Silk-derived Solubility Domain Inhibits Nuclear and Cytosolic Protein Aggregation in Human CellsSemantic proximity Read ↗

A Rational Design Strategy for the Selective Activity Enhancement of a Molecular Chaperone toward a Target Substrate.Semantic proximity Read ↗

Amyloid-Driven Allostery.Semantic proximity Read ↗

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

Apolipoprotein A-I: the dual face of a protein.Semantic proximity Read ↗

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

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