P104L Caveolin-3 transgenic mice displays signs of endoplasmic reticulum stress

descriptionPublicationkeyboard_double_arrow_right Conference object 01 Jan 2012Embargo end date: 11 Sep 2012 English Publisher:German Medical Science GMS Publishing House

Authors: Brauers, E; Roos, A; Buchkremer, S; Sunada, Y; Weis, J;

doi: 10.3205/12dgnn008

P104L Caveolin-3 transgenic mice displays signs of endoplasmic reticulum stress

- Summary
- Subjects
- Related research
  (7)
- Metrics

tips_and_updates
Recommended

Abstract

Mutations in Caveolin-3, which is mainly expressed in muscle cells, cause autosomal dominant myopathies of different severity ranging from asymptomatic hyperCKemia to lethal LGMD-1C and cardiomyopathy. The molecular pathogenesis of caveolin-3-related muscular disorders is still largely unknown. Previously,[for full text, please go to the a.m. URL]

57th Annual Meeting of the German Society for Neuropathology and Neuroanatomy (DGNN)

Keywords

ddc: 610, 610 Medical sciences; Medicine

7 Research products, page 1 of 1

Limb-girdle Muscular Dystrophy (LGMD-1C) Mutants of Caveolin-3 Undergo Ubiquitination and Proteasomal Degradation
2000IsAmongTopNSimilarDocuments
Phenotypic Behavior of Caveolin-3 Mutations That Cause Autosomal Dominant Limb Girdle Muscular Dystrophy (LGMD-1C)
1999IsAmongTopNSimilarDocuments
The caveolin‐3 P104L mutation in LGMD‐1C patients inhibits non‐insulin‐stimulated glucose metabolism and growth but promotes myocyte proliferation
2019IsAmongTopNSimilarDocuments
Hints for a cure in a muscular dystrophy variant
2000IsAmongTopNSimilarDocuments
Phenotypic behavior of caveolin-3 mutations that cause autosomal dominant limb girdle muscular dystrophy (LGMD-1C). Retention of LGMD-1C caveolin-3 mutants within the golgi complex.
1999IsAmongTopNSimilarDocuments
The Caveolin-3 P104L mutation of LGMD-1C leads to disordered glucose metabolism in muscle cells
2017IsAmongTopNSimilarDocuments
Limb-girdle muscular dystrophy (LGMD-1C) mutants of caveolin-3 undergo ubiquitination and proteasomal degradation. Treatment with proteasomal inhibitors blocks the dominant negative effect of LGMD-1C mutanta and rescues wild-type caveolin-3.
2000IsAmongTopNSimilarDocuments

Impact byBIP!

	citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).	0
	popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.	Average
	influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).	Average
	impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.	Average

P104L Caveolin-3 transgenic mice displays signs of endoplasmic reticulum stress

P104L Caveolin-3 transgenic mice displays signs of endoplasmic reticulum stress

7 Research products, page 1 of 1

Limb-girdle Muscular Dystrophy (LGMD-1C) Mutants of Caveolin-3 Undergo Ubiquitination and Proteasomal Degradation

Phenotypic Behavior of Caveolin-3 Mutations That Cause Autosomal Dominant Limb Girdle Muscular Dystrophy (LGMD-1C)

The caveolin‐3 P104L mutation in LGMD‐1C patients inhibits non‐insulin‐stimulated glucose metabolism and growth but promotes myocyte proliferation

Hints for a cure in a muscular dystrophy variant

Phenotypic behavior of caveolin-3 mutations that cause autosomal dominant limb girdle muscular dystrophy (LGMD-1C). Retention of LGMD-1C caveolin-3 mutants within the golgi complex.

The Caveolin-3 P104L mutation of LGMD-1C leads to disordered glucose metabolism in muscle cells

Limb-girdle muscular dystrophy (LGMD-1C) mutants of caveolin-3 undergo ubiquitination and proteasomal degradation. Treatment with proteasomal inhibitors blocks the dominant negative effect of LGMD-1C mutanta and rescues wild-type caveolin-3.