Protein misfolding and degradation in genetic diseases.

doi:10.1002/(SICI)1098-1004(1999)14:3<186::AID-HUMU2>3.0.CO;2-J

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

Back to search

Article

Protein misfolding and degradation in genetic diseases.

Human mutation - 1 Jan 1999

Bross P, Corydon T J, Andresen B S, Jørgensen M M, Bolund L, Gregersen N

Abstract excerpt

Investigations of genetic diseases such as cystic fibrosis, alpha-1-antitrypsin deficiency, phenylketonuria, mitochondrial acyl-CoA dehydrogenase deficiencies, and many others have shown that enhanced proteolytic degradation of mutant proteins is a common molecular pathological mechanism. Detailed studies of the fate of mutant proteins in some of these diseases have revealed that impaired or aberrant folding of...

Topics

Cell Compartmentation
Endoplasmic Reticulum
Genetic Diseases, Inborn
Humans
Intracellular Fluid
Lysosomes
Mitochondria
Molecular Chaperones
Mutation
Peptide Hydrolases
Protein Binding
Protein Conformation
Protein Folding
Proteins

Source

Open in PubMed

Identifiers

PMID: 10477427
DOI: 10.1002/(SICI)1098-1004(1999)14:3<186::AID-HUMU2>3.0.CO;2-J

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics