Cargando…
Changes in function but not oligomeric size are associated with αB-crystallin lysine substitution()
αB-Crystallin, ubiquitously expressed in many tissues including the ocular lens, is a small heat shock protein that can prevent protein aggregation. A number of post-translation modifications are reported to modify αB-crystallin function. Recent studies have identified αB-crystallin lysine residues...
Autores principales: | Droho, Steven, Keener, Mitchell E., Mueller, Niklaus H. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5986625/ https://www.ncbi.nlm.nih.gov/pubmed/29872727 http://dx.doi.org/10.1016/j.bbrep.2018.03.001 |
Ejemplares similares
-
Role of αBI5 and αBT162 residues in subunit interaction during oligomerization of αB-crystallin
por: Murugesan, Raju, et al.
Publicado: (2008) -
Impact of Subunit Composition on the Uptake of α-Crystallin by Lens and Retina
por: Mueller, Niklaus H., et al.
Publicado: (2015) -
Changes in relative histone abundance and heterochromatin in αA-crystallin and αB-crystallin knock-in mutant mouse lenses
por: Andley, Usha P., et al.
Publicado: (2020) -
Structure/function studies of dogfish α-crystallin, comparison with bovine α-crystallin
por: Ghahghaei, A., et al.
Publicado: (2009) -
In Vivo Substrates of the Lens Molecular Chaperones αA-Crystallin and αB-Crystallin
por: Andley, Usha P., et al.
Publicado: (2014)