Results 51 to 60 of about 43,221 (257)
Crystalline bacterial catalase [PDF]
Biochemical Journal, 1947 It is now fifty-four years since Gottstein1 discovered that some bacteria are able to decompose hydrogen peroxide with evolution of gaseous oxygen, an activity he attributed to their possessing an intracellular enzyme which later came to be called ‘catalase’.
D, Herbert, J, Pinsent
openaire +3 more sources
Changes in function but not oligomeric size are associated with αB-crystallin lysine substitution
Biochemistry and Biophysics Reports, 2018 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.
Steven Droho +2 more
doaj +1 more source
Changes in zebrafish (Danio rerio) lens crystallin content during development. [PDF]
, 2013 PurposeThe roles that crystallin proteins play during lens development are not well understood. Similarities in the adult crystallin composition of mammalian and zebrafish lenses have made the latter a valuable model for examining lens function.
Corbin, Rebecca W +4 more
core +1 more source
Small heat-shock proteins: important players in regulating cellular proteostasis [PDF]
, 2015 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.
Carver, John A. +3 more
core +1 more source
Mass Spectrometry Reviews, EarlyView.ABSTRACT One of the great triumphs of mass spectrometry‐based peptide and protein characterization is the characterization of their modifications as most modifications have a characteristic mass shift. What happens when the modification does not change the mass of the peptide?
Samuel Okyem, Jonathan V. Sweedler
wiley +1 more source
Tau-crystallin/alpha-enolase: one gene encodes both an enzyme and a lens structural protein. [PDF]
, 1988 tau-Crystallin has been a major component of the cellular lenses of species throughout vertebrate evolution, from lamprey to birds. Immunofluorescence analysis of the embryonic turtle lens, using antiserum to lamprey tau-crystallin showed that the ...
de Jong, WW +6 more
core
Proteomic Profiling of Myofiber Repair Annexins and Their Role in Duchenne Muscular Dystrophy
PROTEOMICS, EarlyView.ABSTRACT Myofiber regeneration and membrane repair play crucial roles in maintaining the continuous physiological functioning of the neuromuscular system. A swift and efficient repair mechanism enables the rapid restoration of sarcolemmal integrity following cellular impairment in damaged skeletal muscles.
Paul Dowling +6 more
wiley +1 more source
PLoS ONE, 2012 β/γ-Crystallins, the major structural proteins in human lens, are highly conserved in their tertiary structures but distinct in the quaternary structures. The N- and C-terminal extensions have been proposed to play a crucial role in mediating the size of
Jia Xu +5 more
doaj +1 more source
Thermal stress induced aggregation of aquaporin 0 (AQP0) and protection by α-crystallin via its chaperone function. [PDF]
PLoS ONE, 2013 Aquaporin 0 (AQP0) formerly known as membrane intrinsic protein (MIP), is expressed exclusively in the lens during terminal differentiation of fiber cells.
Satyanarayana Swamy-Mruthinti +3 more
doaj +1 more source
Wrapping the alpha-crystallin domain fold in a chaperone assembly [PDF]
, 2005 Small heat shock proteins (sHsps) are oligomers that perform a protective function by binding denatured proteins. Although ubiquitous, they are of variable sequence except for a C-terminal similar to 90-residue "alpha-crystallin domain".
Basha +57 more
core +1 more source