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

Two stable unfolding intermediates of the disease-causing L68Q variant of human cystatin C.

Biochemistry - 8 Dec 1998

Gerhartz B, Ekiel I, Abrahamson M

Abstract excerpt

In hereditary cystatin C amyloid angiopathy (HCCAA), presence of the Leu68 --> Gln substitution in cystatin C is coupled to a decreased concentration of this major cysteine proteinase inhibitor in cerebrospinal fluid and leads to its amyloid deposition in the brain. We established a high-yield expression system for L68Q cystatin C in Escherichia coli resulting in inclusion body accumulation at a level of 40% of...

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 Dimerization
Share to Genetic Variation

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Glutamine

Share to Hydrogen-Ion Concentration

Share to Leucine

Share to Magnetic Resonance Spectroscopy

Share to Protein Folding

Source

Identifiers

PMID: 9860845
DOI: 10.1021/bi980873u

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Two stable unfolding intermediates of the disease-causing L68Q variant of human cystatin C.PMID 9860845Read ↗

Increased body temperature accelerates aggregation of the Leu-68-->Gln mutant cystatin C, the amyloid-forming protein in hereditary cystatin C amyloid angiopathy.Semantic proximity Read ↗

Folding-related dimerization of human cystatin C.Semantic proximity Read ↗

Purification of human wild-type or variant cystatin C from conditioned media of transfected cells.Semantic proximity Read ↗

Crystallization and preliminary X-ray diffraction analysis of Val57 mutants of the amyloidogenic protein human cystatin C.Semantic proximity Read ↗

The cerebral hemorrhage-producing cystatin C variant (L68Q) in extracellular fluids.Semantic proximity Read ↗

Synthesis and physicochemical studies of amyloidogenic hexapeptides derived from human cystatin C.Semantic proximity Read ↗

Cellular processing of the amyloidogenic cystatin C variant of hereditary cerebral hemorrhage with amyloidosis, Icelandic type.Semantic proximity Read ↗

NMR structural studies of human cystatin C dimers and monomers.Semantic proximity Read ↗

The Molecular Pathology of Hereditary Cystatin C Amyloid Angiopathy Causing Brain HemorrhageSemantic proximity Read ↗

Hereditary cystatin C amyloid angiopathy: monitoring the presence of the Leu-68-->Gln cystatin C variant in cerebrospinal fluids and monocyte cultures by MS.Semantic proximity Read ↗

The role of the Val57 amino-acid residue in the hinge loop of the human cystatin C. Conformational studies of the beta2-L1-beta3 segments of wild-type human cystatin C and its mutants.Semantic proximity Read ↗

Endogenous aggregates of amyloidogenic cystatin C variant are removed by THP-1 cells in vitro and induce differentiation and a proinflammatory response.Semantic proximity Read ↗

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