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

A nanobody binding to non-amyloidogenic regions of the protein human lysozyme enhances partial unfolding but inhibits amyloid fibril formation.

The journal of physical chemistry. B - 24 Oct 2013

De Genst Erwin, Chan Pak-Ho, Pardon Els, Hsu Shang-Te D, Kumita Janet R, Christodoulou John, Menzer Linda, Chirgadze Dimitri Y, Robinson Carol V, Muyldermans Serge, Matagne André, Wyns Lode, Dobson Christopher M, Dumoulin Mireille

Abstract excerpt

We report the effects of the interaction of two camelid antibody fragments, generally called nanobodies, namely cAb-HuL5 and a stabilized and more aggregation-resistant variant cAb-HuL5G obtained by protein engineering, on the properties of two amyloidogenic variants of human lysozyme, I56T and D...

Read the complete abstract on PubMed

Topics

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

Share to Amyloid
Share to Muramidase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Protein Denaturation

Share to Protein Folding

Share to Protein Stability

Share to Single-Domain Antibodies

Share to Solubility

Source

Open in PubMed Open full text

Identifiers

PMID: 23919586
DOI: 10.1021/jp403425z
PMCID: PMC4612432

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-23919586-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A nanobody binding to non-amyloidogenic regions of the protein human lysozyme enhances partial unfolding but inhibits amyloid fibril formation.PMID 23919586Read ↗

Engineering a Camelid Antibody Fragment That Binds to the Active Site of Human Lysozyme and Inhibits Its Conversion into Amyloid FibrilsSemantic proximity Read ↗

A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme.Semantic proximity Read ↗

Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations.Semantic proximity Read ↗

Local cooperativity in an amyloidogenic state of human lysozyme observed at atomic resolution.Semantic proximity Read ↗

Effect of Humanizing Mutations on the Stability of the Llama Single-Domain Variable Region.Semantic proximity Read ↗

Characterisation of the structural, dynamic and aggregation properties of the W64R amyloidogenic variant of human lysozyme.Semantic proximity Read ↗

Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme.Semantic proximity Read ↗

Rationalising lysozyme amyloidosis: insights from the structure and solution dynamics of T70N lysozyme.Semantic proximity Read ↗

Structural and folding dynamic properties of the T70N variant of human lysozyme.Semantic proximity Read ↗

Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic beta2-microglobulin variant.Semantic proximity Read ↗

Inherent Biophysical Properties Modulate the Toxicity of Soluble Amyloidogenic Light Chains.Semantic proximity Read ↗

Concurrent structural and biophysical traits link with immunoglobulin light chains amyloid propensitySemantic proximity Read ↗

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