Last edited by Mazulmaran
Thursday, July 30, 2020 | History

6 edition of Amyloids, Prions and Other Protein Aggregates (Methods in Enzymology, Volume 309) (Methods in Enzymology) found in the catalog.

Amyloids, Prions and Other Protein Aggregates (Methods in Enzymology, Volume 309) (Methods in Enzymology)

  • 391 Want to read
  • 8 Currently reading

Published by Academic Press .
Written in English


Edition Notes

ContributionsJohn N. Abelson (Editor), Melvin I. Simon (Editor), Ronald Wetzel (Editor)
The Physical Object
Number of Pages819
ID Numbers
Open LibraryOL7326280M
ISBN 100121822109
ISBN 109780121822101

The general focus of my work is the structure of amyloids and other disease-related, misfolded proteins. In particular, I am interested in the infectious mammalian prion protein, the structure. Amyloids are protease resistant insoluble fibrils formed because of (mis)folding and aggregation of soluble proteins (Rambaran and Serpell, , Sabate et al., ).The first definition of prion was given by Prusiner (). Because the novel properties of the scrapie agent distinguish it from viruses, plasmids, and viroids, a new term "prion" is proposed to denote a small proteinaceous.

  The aggregation of proteins into structures known as amyloids is observed in many neurodegenerative diseases, including Alzheimer's disease. Amyloids are . The amyloids then act as a template to nucleate the misfolding and aggregation of normal proteins in the body, leading to the formation of many more amyloid fibrils. Amyloid fibrils of a peptide from human prion protein (left), yeast prion HET-s (center), and a peptide from transthyretin (right).

The recent data on the prionoid spread of other pathological amyloids are discussed in light of differences between prions and prion-like aggregates. On the other hand, prion-like action has also been found to support important functions such as memory, and amyloids were shown to have a variety of physiological roles from storage to scaffolding. Such aggregates can serve for the compartmentalization of certain processes, for the preservation and storage of certain proteins and mRNA, but they can also facilitate amyloid formation de novo. The journals IJMS and Life will jointly be publishing a Special Issue covering the topic "Amyloids, Prions, and Related Phenomena".


Share this book
You might also like
Converting Kearsarge or Kentucky into crane and salvage ship. Letter from the Secretary of the Navy, transmitting request for authority for use of appropriation in naval appropriation bill for 1921 for the purpose of converting either the Kearsarge or the Kentucky into a crane and salvage ship.

Converting Kearsarge or Kentucky into crane and salvage ship. Letter from the Secretary of the Navy, transmitting request for authority for use of appropriation in naval appropriation bill for 1921 for the purpose of converting either the Kearsarge or the Kentucky into a crane and salvage ship.

Weeds of the west

Weeds of the west

River navigation in England, 1600-1750

River navigation in England, 1600-1750

No Surrender

No Surrender

Narrative of a tour from the state of Indiana to the Oregon territory in the years 1841-2

Narrative of a tour from the state of Indiana to the Oregon territory in the years 1841-2

The great navigators of the eighteenth century

The great navigators of the eighteenth century

new sense of purpose: four letters to the Jews

new sense of purpose: four letters to the Jews

International Advanced Summer Institute on Microprogramming.

International Advanced Summer Institute on Microprogramming.

A century in America

A century in America

The World of Insect Life (An Inside Look)

The World of Insect Life (An Inside Look)

[Letter to Anne W. Weston]

[Letter to Anne W. Weston]

geology of the Thames Valley near Goring

geology of the Thames Valley near Goring

Jacob Lawrence in the city

Jacob Lawrence in the city

Amyloids, Prions and Other Protein Aggregates (Methods in Enzymology, Volume 309) (Methods in Enzymology) Download PDF EPUB FB2

Functional amyloids have been identified in bacteria (viz. Curlin, 36 Chaplins, 37 adhesin P1 38 and phenol soluble modulins 39), fungi (viz. HET-s, 34 hydrophobins, 40 and the yeast prions Sup35p, Rnq1p or Ure2p 41), Amyloids (viz. Spidroin, 42 eggshell chorion proteins 43 and the neuron-specific isoform of CPEB 44) and humans (viz.

the Cited by: 7. In the cell, proteins attain the native structure through a delicate and balanced network of interactions, where protein folding and aggregation exert as competing pathways.

1,2 In a protein energy landscape, amyloid-like aggregates represent an energy minimum, being usually thermodynamically more stable than the native conformation. This has lead to the hypothesis that the Cited by:   Amyloid, Prions, and Other Protein Aggregates, Part B (ISSN Book ) Kindle Edition by Ronald Wetzel (Editor), Indu Kheterpal (Editor) Format: Kindle Edition See all 3 formats and editions Hide other formats and editionsManufacturer: Academic Press.

This new volume of Methods in Enzymology along with Part B (volume ) on Amyloid, Prions and other Protein Aggregates continue in the tradition of the first volume () in containing detailed protocols and methodological insights, provided by leaders in the field, into the latest methods for investigating the structures, mechanisms of formation, and biological activities of this important class of protein.

This new volume of Methods in Enzymology along with Part B (volume ) on Amyloid, Prions and other Protein Aggregates continue in the tradition of the first volume () in containing detailed protocols and methodological insights, provided by leaders in the field, into the latest methods for investigating the structures, mechanisms of formation, and biological activities of this Manufacturer: Academic Press.

Amyloids are aggregates of proteins characterised by a fibrillar morphology of 7–13 nm in diameter, a β-sheet secondary structure (known as cross-β) and ability to be stained by particular dyes, such as Congo red.

In the human body, amyloids have been linked to the development of various diseases. Pathogenic amyloids form when previously healthy proteins lose their normal structure and.

Misfolded aggregates present in amyloid fibrils are associated with various diseases known as ‘protein misfolding’ disorders. Among them, prion diseases are unique in that the pathology can be transmitted by an infectious process involving an unprecedented agent known as a ‘prion’.

Prions are infectious proteins that can transmit biological information by propagating protein misfolding. Search in this book series. Amyloid, Prions, and Other Protein Aggregates, Part C. Indu Kheterpal and Ronald Wetzel. VolumePages () Download full volume.

Spin Labeling Analysis of Amyloids and Other Protein Aggregates. Martin Margittai, Ralf. A recent addition to this group was the finding of a large number of proteins forming non-amyloid yeast prions.

Their structural basis is still unclear. In many cases, amyloids are formed by natively unfolded proteins or protein domains. Such proteins can also form a separate liquid phase (a reversible “liquid” aggregate).

On the other and the clearance of the pre-existent prions in cell culture could be explained by the increased processing of PrP C in the presence of α-Syn amyloids.

Virtual Issue: Amyloids, prions and protein oligomers Protein aggregation into amyloid oligomers and fibrils plays a key role in a wide range of diseases as well as normal biological function.

Chapter 7: Spin Labeling Analysis of Amyloids and other Protein Aggregates. Chapter 8: Hydrogen-Deuterium Exchange Mass Spectrometry of Protein Aggregates. Chapter 9: Hydrogen-Deuterium Exchange analyzed by Matrix Assisted Laser Desorption-Ionisation Mass Spectrometry and the HET-s prion Price: $ Prions are infectious proteins that can transmit biological information by propagating protein misfolding and aggregation.

The molecular mechanism of prion conversion has a striking resemblance to the process of amyloid formation, suggesting that misfolded aggregates have an inherent ability to. This new volume of Methods in Enzymology along with Part C (volume ) on Amyloid, Prions and other Protein Aggregates continue in the tradition of the first volume () in containing detailed protocols and methodological insights, provided by leaders in the field, into the latest methods for investigating the structures, mechanisms of formation, and biological activities of this important class of.

This new volume of Methods in Enzymology along with Part C (volume ) on Amyloid, Prions and other Protein Aggregates continue in the tradition of the first volume () in containing detailed protocols and methodological insights, provided by leaders in the field, into the latest methods for investigating the structures, mechanisms of formation, and biological activities of this important class of protein.

Thus, a single protein, Sup35, can model both prion and nonprion amyloids. In yeast, these phenomena are distinguished by the frequency of polymer fragmentation. We argue that in mammals the fragmentation frequency also represents a key factor defining differing properties of prion and nonprion amyloids, including infectivity.

Misfolding and aggregation of proteins is the main feature of a group of maladies which include most of neurodegenerative diseases (such as Alzheimer’s, Parkinson’s, Huntington’s, and prion diseases), as well as several systemic amyloidosis.

Among them, prion. Amyloids and amyloid-based prions are self-perpetuating protein aggregates which can spread by converting a normal protein of the same sequence into a prion form. They are associated with diseases in humans and mammals, and control heritable traits in yeast and other fungi.

Some amyloids are implicated in biologically beneficial processes. Prions are unusual proteins that have the capacity to change shape and to selectively template that change in shape to other proteins of the same type, a property shared by prions and other amyloid-forming proteins across the evolutionary spectrum.

While amyloids can cause devastating economic hardship in an extraordinary variety of settings. Amyloids, Prions and Beta Proteins is the last volume of the three-part thematic series on Fibrous Proteins in the Advances in Protein Chemistry serial.

Fibrous proteins act as molecular scaffolds in cells providing the supporting structures of our skeletons, bones, tendons. ABSTRACT. Amyloids and amyloid-based prions are self-perpetuating protein aggregates which can spread by converting a normal protein of the same sequence into a prion form. They are associated with diseases in humans and mammals, and control heritable traits in yeast and other fungi.

Some amyloids are implicated in biologically beneficial. Amyloids are fibrillar protein aggregates associated with diseases such as Alzheimer’s disease (AD), Parkinson’s disease (PD), type II diabetes and Creutzfeldt–Jakob disease.

The process of amyloid polymerization involves three pathological protein transformations; from natively folded conformation to the cross-β conformation, from biophysically soluble to insoluble, and from. The [Het-s] infectious element of the filamentous fungus Podospora anserina is a prion.

We have recently reported that recombinant HET-s protein aggregates in vitro into amyloid fibers. In vivo, the protein aggregates specifically in the [Het-s] prion strains. Here, we show that biolistic introduction of aggregated recombinant HET-s protein into fungal cells induces emergence of the .