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

Mutant Neuroserpin (S49P) that causes familial encephalopathy with neuroserpin inclusion bodies is a poor proteinase inhibitor and readily forms polymers in vitro.

The Journal of biological chemistry - 10 May 2002

Belorgey Didier, Crowther Damian C, Mahadeva Ravi, Lomas David A

Abstract excerpt

Familial encephalopathy with neuroserpin inclusion bodies (FENIB) is an autosomal dominant dementia that is characterized by intraneuronal inclusions of mutant neuroserpin. We report here the expression, purification, and characterization of wild-type neuroserpin and neuroserpin containing the S49P mutation that causes FENIB. Wild-type neuroserpin formed SDS-stable complexes with tPA with an association rate...

Read the complete abstract on PubMed

Topics

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

Share to Circular Dichroism
Share to Dementia

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Electrophoresis, Polyacrylamide Gel

Share to Enzyme Inhibitors

Share to Neuropeptides

Share to Polymers

Share to Serpins

Share to Ultraviolet Rays

Source

Identifiers

PMID: 11880376
DOI: 10.1074/jbc.M200680200

Genes

SDS

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

Mutant Neuroserpin (S49P) that causes familial encephalopathy with neuroserpin inclusion bodies is a poor proteinase inhibitor and readily forms polymers in vitro.PMID 11880376Read ↗

Crystal structure of neuroserpin: a neuronal serpin involved in a conformational disease.Semantic proximity Read ↗

Neuroserpin: a serpin to think about.Semantic proximity Read ↗

Unravelling the twists and turns of the serpinopathies.Semantic proximity Read ↗

The stability and activity of human neuroserpin are modulated by a salt bridge that stabilises the reactive centre loop.Semantic proximity Read ↗

Progressive myoclonus epilepsy associated with neuroserpin inclusion bodies (neuroserpinosis)Semantic proximity Read ↗

Interactions between N-linked glycosylation and polymerisation of neuroserpin within the endoplasmic reticulum.Semantic proximity Read ↗

Familial conformational diseases and dementias.Semantic proximity Read ↗

G392E neuroserpin causing the dementia FENIB is secreted from cells but is not synaptotoxic.Semantic proximity Read ↗

Endoplasmic reticulum-associated degradation (ERAD) and autophagy cooperate to degrade polymerogenic mutant serpins.Semantic proximity Read ↗

Changes in strand 6B and helix B during neuroserpin inhibition: Implication in severity of clinical phenotype.Semantic proximity Read ↗

The intracellular accumulation of polymeric neuroserpin explains the severity of the dementia FENIBSemantic proximity Read ↗

Protein misfolding and the serpinopathies.Semantic proximity Read ↗

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