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

Investigating the effects of mutations on protein aggregation in the cell.

The Journal of biological chemistry - 18 Mar 2005

Calloni Giulia, Zoffoli Sara, Stefani Massimo, Dobson Christopher M, Chiti Fabrizio

Abstract excerpt

The conversion of peptides and proteins into highly ordered and intractable aggregates is associated with a range of debilitating human diseases and represents a widespread problem in biotechnology. Protein engineering studies carried out in vitro have shown that mutations promote aggregation when they either destabilize the native state of a globular protein or accelerate the conversion of unfolded or partially...

Read the complete abstract on PubMed

Topics

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

Share to Benzothiazoles
Share to Biotechnology
Share to Macromolecular Substances

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Muramidase

Share to Protein Denaturation

Share to Solubility

Share to Thiazoles

Source

Identifiers

PMID: 15611128
DOI: 10.1074/jbc.M412951200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Investigating the effects of mutations on protein aggregation in the cell.PMID 15611128Read ↗

Mutations and off-pathway aggregation of proteins.Semantic proximity Read ↗

Toxicity of protein oligomers is rationalized by a function combining size and surface hydrophobicity.Semantic proximity Read ↗

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

Position-dependent electrostatic protection against protein aggregation.Semantic proximity Read ↗

Sequence determinants of protein aggregation: tools to increase protein solubilitySemantic proximity Read ↗

An in vivo platform to select and evolve aggregation-resistant proteins.Semantic proximity Read ↗

Solubis: optimize your protein.Semantic proximity Read ↗

Soluble oligomerization provides a beneficial fitness effect on destabilizing mutations.Semantic proximity Read ↗

Concentration-dependent mutational scanning probes the cellular folding landscape of α-synuclein in yeast.Semantic proximity Read ↗

Mutations enhance the aggregation propensity of the Alzheimer's A beta peptide.Semantic proximity Read ↗

Influence of the valine zipper region on the structure and aggregation of the basic leucine zipper (bZIP) domain of activating transcription factor 5 (ATF5).Semantic proximity Read ↗

Mutational Scanning of α-Synuclein using a Clickable Protein Tag Reveals Determinants of Membrane-Induced AggregationSemantic proximity Read ↗

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