Idioma:

Small heat-shock proteins: important players in regulating cellular proteostasis

Treweek, Teresa M ; Meehan, Sarah ; Ecroyd, Heath ; Carver, John A

Cellular and molecular life sciences : CMLS, 2015-02, Vol.72 (3), p.429-451 [Periódico revisado por pares]

Basel: Springer-Verlag

Texto completo disponível

Citações Citado por

Enviar para

Título:
Small heat-shock proteins: important players in regulating cellular proteostasis
Autor: Treweek, Teresa M ; Meehan, Sarah ; Ecroyd, Heath ; Carver, John A
Assuntos: alpha-Crystallins - metabolism ; Biochemistry ; Biomedical and Life Sciences ; Biomedicine ; Cataracts ; Cell Biology ; Heat shock proteins ; Heat-Shock Proteins - chemistry ; Heat-Shock Proteins - genetics ; Heat-Shock Proteins - physiology ; Homeostasis ; Homeostasis - genetics ; Homeostasis - physiology ; Humans ; Life Sciences ; mammals ; Models, Biological ; Models, Molecular ; Molecular Chaperones - genetics ; Molecular Chaperones - physiology ; Multiple Sclerosis - genetics ; Multiple Sclerosis - metabolism ; Neoplasms - genetics ; Neoplasms - metabolism ; Neurodegeneration ; Neurodegenerative Diseases - genetics ; Neurodegenerative Diseases - metabolism ; oxidation ; Phosphorylation ; Polymerization ; post-translational modification ; Protein Aggregation, Pathological - metabolism ; protein depletion ; Protein Processing, Post-Translational - genetics ; Protein Processing, Post-Translational - physiology ; Proteins ; Review ; temperature
É parte de: Cellular and molecular life sciences : CMLS, 2015-02, Vol.72 (3), p.429-451
Notas: http://dx.doi.org/10.1007/s00018-014-1754-5
ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
content type line 23
ObjectType-Review-1
Descrição: Small heat-shock proteins (sHsps) are a diverse family of intra-cellular molecular chaperone proteins that play a critical role in mitigating and preventing protein aggregation under stress conditions such as elevated temperature, oxidation and infection. In doing so, they assist in the maintenance of protein homeostasis (proteostasis) thereby avoiding the deleterious effects that result from loss of protein function and/or protein aggregation. The chaperone properties of sHsps are therefore employed extensively in many tissues to prevent the development of diseases associated with protein aggregation. Significant progress has been made of late in understanding the structure and chaperone mechanism of sHsps. In this review, we discuss some of these advances, with a focus on mammalian sHsp hetero-oligomerisation, the mechanism by which sHsps act as molecular chaperones to prevent both amorphous and fibrillar protein aggregation, and the role of post-translational modifications in sHsp chaperone function, particularly in the context of disease.
Editor: Basel: Springer-Verlag
Idioma: Inglês

Links

View this record in MEDLINE/PubMed

Voltar para lista de resultados

Realização: Logos de Redes Sociais:

Small heat-shock proteins: important players in regulating cellular proteostasis

Treweek, Teresa M ; Meehan, Sarah ; Ecroyd, Heath ; Carver, John A

Basel: Springer-Verlag

Buscando em bases de dados remotas. Favor aguardar.