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Articles 1 - 3 of 3
Full-Text Articles in Social and Behavioral Sciences
Monotremes Provide A Key To Understanding The Evolutionary Significance Of Epididymal Sperm Maturation, Brett Nixon, Russell Jones, Jean-Louis Dacheux, Heath Ecroyd
Monotremes Provide A Key To Understanding The Evolutionary Significance Of Epididymal Sperm Maturation, Brett Nixon, Russell Jones, Jean-Louis Dacheux, Heath Ecroyd
Heath Ecroyd
"It has been widely accepted that mammalian spermatozoa are infertile when they leave the testes and require a period of maturation in both the epididymis and the female reproductive tract before acquiring the ability to fertilize an oocyte. However, the necessity for such a complex process of posttesticular sperm maturation appears to be unique to mammals because it is well established that these processes do not directly influence the fertilizing ability of the spermatozoa of birds, reptiles, and other lower vertebrates. Because of their key evolutionary position and form of reproduction, we contend that monotremes (platypus and echidna) provide a …
Nmr Spectroscopy Of 14-3-3zeta Reveals A Flexible C-Terminal Extension: Differentiation Of The Chaperone And Phosphoserine-Binding Activities Of 14-3-3zeta, H Fu, Danielle Williams, Heath Ecroyd, John Carver, Lixin Zhang, Huanqin Dai, Joanna Woodcock, K Goodwin
Nmr Spectroscopy Of 14-3-3zeta Reveals A Flexible C-Terminal Extension: Differentiation Of The Chaperone And Phosphoserine-Binding Activities Of 14-3-3zeta, H Fu, Danielle Williams, Heath Ecroyd, John Carver, Lixin Zhang, Huanqin Dai, Joanna Woodcock, K Goodwin
Heath Ecroyd
Intracellular 14-3-3 proteins bind to many proteins, via a specific phosphoserine motif, regulating diverse cellular tasks including cell signalling and disease progression. The 14-3-3 isoform is a molecular chaperone, preventing the stressinduced aggregation of target proteins in a manner comparable with that of the unrelated sHsps (small heat-shock proteins). 1H-NMR spectroscopy revealed the presence of a flexible and unstructured C-terminal extension, 12 amino acids in length, which protrudes from the domain core of 14-3-3 and is similar in structure and length to the C-terminal extension of mammalian sHsps. The extension stabilizes 14-3-3, but has no direct role in chaperone action. …
Enhanced Molecular Chaperone Activity Of The Small Heat-Shock Protein Alphab-Cystallin Following Covalent Immobilization Onto A Solid-Phase Support, V Bellotti, Heath Ecroyd, J Carver, H J Griesser, B Thierry, J G Shapter, S S Griesser, S Giorgetti, M R Nussio, J A Gerrard, J Garvey
Enhanced Molecular Chaperone Activity Of The Small Heat-Shock Protein Alphab-Cystallin Following Covalent Immobilization Onto A Solid-Phase Support, V Bellotti, Heath Ecroyd, J Carver, H J Griesser, B Thierry, J G Shapter, S S Griesser, S Giorgetti, M R Nussio, J A Gerrard, J Garvey
Heath Ecroyd
The well-characterized small heat-shock protein, alphaB-crystallin, acts as a molecular chaperone by interacting with unfolding proteins to prevent their aggregation and precipitation. Structural perturbation (e.g., partial unfolding) enhances the in vitro chaperone activity of alphaB-crystallin. Proteins often undergo structural perturbations at the surface of a synthetic material, which may alter their biological activity. This study investigated the activity of alphaB-crystallin when covalently bound to a support surface; alphaB-crystallin was immobilized onto a range of solid material surfaces, and its characteristics and chaperone activity were assessed. Immobilization was achieved via a plasma-deposited thin polymeric interlayer containing aldehyde surface groups and reductive …