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

Overexpression of caveolin-1 is sufficient to phenocopy the behavior of a disease-associated mutant.

Traffic (Copenhagen, Denmark) - 1 Jun 2013

Hanson Caroline A, Drake Kimberly R, Baird Michelle A, Han Bing, Kraft Lewis J, Davidson Michael W, Kenworthy Anne K

Abstract excerpt

Mutations and alterations in caveolin-1 expression levels have been linked to a number of human diseases. How misregulation of caveolin-1 contributes to disease is not fully understood, but has been proposed to involve the intracellular accumulation of mutant forms of the protein. To better understand the molecular basis for trafficking defects that trap caveolin-1 intracellularly, we compared the properties of a...

Read the complete abstract on PubMed

Topics

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

Share to Caveolin 1
Share to Chlorocebus aethiops

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to COS Cells

Share to HeLa Cells

Share to Mutation, Missense

Share to Phosphorylation

Share to Protein Conformation

Share to Protein Transport

Source

Open in PubMed Open full text

Identifiers

PMID: 23469926
DOI: 10.1111/tra.12066
PMCID: PMC3674505

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

Overexpression of caveolin-1 is sufficient to phenocopy the behavior of a disease-associated mutant.PMID 23469926Read ↗

Structural characterization of a breast cancer-associated mutation in caveolin-1Semantic proximity Read ↗

Using Caveolin-1 epithelial immunostaining patterns to stratify human breast cancer patients and predict the Caveolin-1 (P132L) mutation.Semantic proximity Read ↗

Structural analysis of the P132L disease mutation in caveolin-1 reveals its role in the assembly of oligomeric complexes.Semantic proximity Read ↗

Absence of the caveolin-1 P132L mutation in cancers of the breast and other organs.Semantic proximity Read ↗

Caveolin-1 mutations in human breast cancer: functional association with estrogen receptor alpha-positive status.Semantic proximity Read ↗

Caveolin in breast cancerSemantic proximity Read ↗

Caveolin-1 (P132L), a common breast cancer mutation, confers mammary cell invasiveness and defines a novel stem cell/metastasis-associated gene signature.Semantic proximity Read ↗

Caveolin-1 P132L mutation in human cancers: 1 CAVeat to be voiced.Semantic proximity Read ↗

Proteostatic regulation of caveolins avoids premature oligomerisation and preserves ER homeostasisSemantic proximity Read ↗

Conformational defects slow Golgi exit, block oligomerization, and reduce raft affinity of caveolin-1 mutant proteins.Semantic proximity Read ↗

Biochemical and pathological changes result from mutated Caveolin-3 in muscle.Semantic proximity Read ↗

Caveolin-1 Deficiency (−/−) Conveys Premalignant Alterations in Mammary Epithelia, with Abnormal Lumen Formation, Growth Factor Independence, and Cell InvasivenessSemantic proximity Read ↗

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