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Articles 1 - 9 of 9
Full-Text Articles in Physical Sciences and Mathematics
Cyclicity In The Nearshore Marine To Coastal, Lower Permian, Pebbley Beach Formation, Southern Sydney Basin, Australia: A Record Of Relative Sea-Level Fluctuations At The Close Of The Late Palaeozoic Gondwanan Ice Age, Brian G. Jones, Stuart C. Tye, James A. Maceachern, Kerrie L. Bann, Christopher R. Fielding
Cyclicity In The Nearshore Marine To Coastal, Lower Permian, Pebbley Beach Formation, Southern Sydney Basin, Australia: A Record Of Relative Sea-Level Fluctuations At The Close Of The Late Palaeozoic Gondwanan Ice Age, Brian G. Jones, Stuart C. Tye, James A. Maceachern, Kerrie L. Bann, Christopher R. Fielding
B. G. Jones
The Lower Permian (Artinskian to Sakmarian) Pebbley Beach Formation of the southernmost Sydney Basin in New South Wales, Australia, records sediment accumulation in shallow marine to coastal environments at the close of the Late Palaeozoic Gondwanan ice age. This paper presents a sequence stratigraphic re-evaluation of the upper half of the unit based on the integration of sedimentology and ichnology. Ten facies are recognized, separated into two facies associations. Facies Association A (7 facies) comprises variably bioturbated siltstones and sandstones with marine body fossils, interpreted to record sediment accumulation in open marine environments ranging from lower offshore to middle shoreface …
Aeolian-Fluvial Interaction: Evidence For Late Quaternary Channel Change And Wind-Rift Linear Dune Formation In The Northwestern Simpson Desert, Australia, Gerald C. Nanson, Brian G. Jones, David M. Price, Tim Pietsch, C Bristow, Cameron B. Hollands
Aeolian-Fluvial Interaction: Evidence For Late Quaternary Channel Change And Wind-Rift Linear Dune Formation In The Northwestern Simpson Desert, Australia, Gerald C. Nanson, Brian G. Jones, David M. Price, Tim Pietsch, C Bristow, Cameron B. Hollands
B. G. Jones
In central Australia the most easterly extent of the MacDonnell Ranges borders the northwestern Simpson Desert where widely spaced strike ridges intercept the regional linear dunefield. Topographic basins have disrupted regional drainage lines and isolated dune sets from the main dunefield. In the western part of Camel Flat basin large, red coloured linear dunes of fine sand, ~ 74 ka and older, are oriented almost due north. Through gaps in the ranges the Todd River traversed the eastern part of the basin until ~25 ka when it apparently avulsed ~25 km eastwards to its present position. Subsequently, linear dunes, smaller, …
Macroglobulin And Haptoglobin Suppress Amyloid Formation By Interacting With Prefibrillar Protein Species, Justin J. Yerbury, Janet R. Kumita, Sarah Meehan, Christopher M. Dobson, Mark R. Wilson
Macroglobulin And Haptoglobin Suppress Amyloid Formation By Interacting With Prefibrillar Protein Species, Justin J. Yerbury, Janet R. Kumita, Sarah Meehan, Christopher M. Dobson, Mark R. Wilson
Mark R Wilson
α2-Macroglobulin (α2M) and haptoglobin (Hp) are both abundant secreted glycoproteins that are best known for their protease trapping and hemoglobin binding activities, respectively. Like the small heat shock proteins, both these glycoproteins have in common the ability to protect a range of proteins from stress-induced amorphous aggregation and have been described as extracellular chaperones. Using an array of biophysical techniques, this study establishes that in vitro at substoichiometric levels and under physiological conditions α2M and Hp both inhibit the formation of amyloid fibrils from a range of proteins. We also provide evidence that both α2M and Hp interact with prefibrillar …
Potential Roles Of Abundant Extracellular Chaperones In The Control Of Amyloid Formation And Toxicity, Mark R. Wilson, Justin J. Yerbury, Stephen Poon
Potential Roles Of Abundant Extracellular Chaperones In The Control Of Amyloid Formation And Toxicity, Mark R. Wilson, Justin J. Yerbury, Stephen Poon
Mark R Wilson
The in vivo formation of fibrillar proteinaceous deposits called amyloid is associated with more than 40 serious human diseases, collectively referred to as protein deposition diseases. In many cases the amyloid deposits are extracellular and are found associated with newly identified abundant extracellular chaperones (ECs). Evidence is presented suggesting an important regulatory role for ECs in amyloid formation and disposal in the body. A model is presented which proposes that, under normal conditions, ECs stabilize extracellular misfolded proteins by binding to them, and then guide them to specific cell receptors for uptake and subsequent degradation. Thus ECs and their receptors …
The Two-Faced Nature Of Small Heat Shock Proteins: Amyloid Assembly And The Inhibition Of Fibril Formation. Relevance To Disease States, Heath W. Ecroyd, S Meehan, John A. Carver
The Two-Faced Nature Of Small Heat Shock Proteins: Amyloid Assembly And The Inhibition Of Fibril Formation. Relevance To Disease States, Heath W. Ecroyd, S Meehan, John A. Carver
Heath Ecroyd
The ability of small heat-shock proteins (sHsps) such as alphaB-crystallin to inhibit the amorphous (disordered) aggregation of varied target proteins in a chaperone-like manner has been well described. The mechanistic details of this action are not understood. Amyloid fibril formation is an alternative off-folding pathway that leads to highly ordered beta-sheet-containing aggregates. Amyloid fibril formation is associated with a broad range of protein conformational diseases such as Alzhiemer's, Parkinson's and Huntington's and sHsp expression is elevated in the protein deposits that are characteristic of these disease states. The ability of sHsps to prevent fibril formation has been less well characterised. …
Carbanions: Formation, Structure And Thermochemistry, Stephen J. Blanksby, John H. Bowie
Carbanions: Formation, Structure And Thermochemistry, Stephen J. Blanksby, John H. Bowie
Stephen Blanksby
This chapter deals with even-electron carbanions: their formation, structure and thermochemical properties in the gas phase. There are a number of excellent reviews already available on the chemistry of carbanions: these discuss in the main, reactivity and anion molecule chemistry.1-4 In this chapter we focus primarily on the formation, structure and thermochemistry of simple hydrocarbon anions while other chapters in this encyclopaedia cover the broader aspects of carbanion chemistry (see Volume 1, “Strained Ring and Highly Basic Carbanions” and this volume, Reactions of Organic Molecules with Organic Ions: “Reactions of Anions with Carbonyl Centres: C–C Bond Forming Reactions”, and Unimolecular …
Carboxymethylated-K-Casein: A Convenient Tool For The Identification Of Polyphenolic Inhibitors Of Amyloid Fibril Formation, John A. Carver, Peter J. Duggan, Heath Ecroyd, Yanqin Liu, Adam G. Meyer, C E. Tranberg
Carboxymethylated-K-Casein: A Convenient Tool For The Identification Of Polyphenolic Inhibitors Of Amyloid Fibril Formation, John A. Carver, Peter J. Duggan, Heath Ecroyd, Yanqin Liu, Adam G. Meyer, C E. Tranberg
Heath Ecroyd
Reduced and carboxymethylated-κ-casein (RCM-κ-CN) is a milk-derived amyloidogenic protein that readily undergoes nucleation-dependent aggregation and amyloid fibril formation via a similar pathway to disease-specific amyloidogenic peptides like amyloid beta (Aβ), which is associated with Alzheimer’s disease. In this study, a series of flavonoids, many known to be inhibitors of Aβ fibril formation, were screened for their ability to inhibit RCM-κ-CN fibrilisation, and the results were compared with literature data on Aβ inhibition. Flavonoids that had a high degree of hydroxylation and molecular planarity gave good inhibition of RCM-κ-CN fibril formation. IC50 values were between 10- and 200-fold higher with RCM-κ-CN …
The Dissociated Form Of Kappa-Casein Is The Precursor To Its Amyloid Fibril Formation, Heath Ecroyd, David Thorn, Yanqin Liu, John Carver
The Dissociated Form Of Kappa-Casein Is The Precursor To Its Amyloid Fibril Formation, Heath Ecroyd, David Thorn, Yanqin Liu, John Carver
Heath Ecroyd
Bovine milk kappa-casein forms a self-associating oligomeric micelle-like species, in equilibrium with dissociated forms. In its native form, intra- and inter-molecular disulfide bonds lead to the formation of multimeric species ranging from monomers to decamers. When incubated under conditions of physiological pH and temperature, both reduced and non-reduced kappa-casein form highly structured beta-sheet amyloid fibrils. We investigated whether the precursor to kappa-casein fibril formation is a dissociated state of the protein or its oligomeric micelle-like form. We show that reduced kappa-casein is capable of forming fibrils well below its critical micelle concentration, i.e. at concentrations where only dissociated forms of …
Alphab-Crystallin Inhibits The Cell Toxicity Associated With Amyloid Fibril Formation By Kappa-Casein And The Amyloid-Beta Peptide, Francis C. Dehle, Heath Ecroyd, Ian F. Musgrave, John A. Carver
Alphab-Crystallin Inhibits The Cell Toxicity Associated With Amyloid Fibril Formation By Kappa-Casein And The Amyloid-Beta Peptide, Francis C. Dehle, Heath Ecroyd, Ian F. Musgrave, John A. Carver
Heath Ecroyd
Amyloid fibril formation is associated with diseases such as Alzheimer’s, Parkinson’s, and prion diseases. Inhibition of amyloid fibril formation by molecular chaperone proteins, such as the small heat-shock protein αB-crystallin, may play a protective role in preventing the toxicity associated with this form of protein misfolding. Reduced and carboxymethylated κ-casein (RCMκ-CN), a protein derived from milk, readily and reproducibly forms fibrils at physiological temperature and pH. We investigated the toxicity of fibril formation by RCMκ-CN using neuronal model PC12 cells and determined whether the inhibition of fibril formation altered its cell toxicity. To resolve ambiguities in the literature, we also …