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Destroying amyloid proteins with lasers
January 08, 2009Researchers have found that a technique used to visualize amyloid fibers in the laboratory might have the potential to destroy them in the clinic. The technique involves zapping the fluorescently-tagged fibers with a laser, which can inhibit their growth and degrade them. This study, appearing in this week's JBC, may offer a non-drug alternative to treat amyloid-based disorders like Alzheimer, Parkinson, and Huntington diseases.
Yuji Goto and colleagues had been studying amyloids, dense tangles of protein, to better understand how they form. In an effort to view amyloid formation under a microscope in real-time, they added an amyloid specific dye called thioflavin T (ThT) to the tangles and then hit it with a laser beam to induce fluorescence. Surprisingly, they found that under the right conditions, the laser could actually stop fiber growth and even degrade the amyloids.
Goto and colleagues believe the laser-excited ThT transfers some of its energy to nearby oxygen, resulting in active oxygen species that alters the surrounding protein fibers. These specific experiments focused on beta2-microglobulin, a major component of amyloids associated with dialysis-related amyloidosis (a condition that currently has no good treatment), though they believe a similar approach of light-induced decomposition should work for other types of protein amyloids.
American Society for Biochemistry and Molecular Biology
American Society for Biochemistry and Molecular Biology
Amyloid Current Events and Amyloid News RSSAn atomic-level look at an HIV accomplice
Since the discovery in 2007 that a component of human semen called SEVI boosts infectivity of the virus that causes AIDS, researchers have been trying to learn more about SEVI and how it works, in hopes of thwarting its infection-promoting activity.
Scientists find molecular trigger that helps prevent aging and disease
Researchers at Mount Sinai School of Medicine set out to address a question that has been challenging scientists for years: How do dietary restriction-and the reverse, overconsumption-produce protective effects against aging and disease?
Protein changes in heart strengthen link between Alzheimer's disease and chronic heart failure
A team of U.S., Canadian and Italian scientists led by researchers at Johns Hopkins report evidence from studies in animals and humans supporting a link between Alzheimer's disease and chronic heart failure, two of the 10 leading causes of death in the United States.
Novel mouse gene reduces major pathologies associated with Alzheimer's disease
A new study reveals that a previously undiscovered mouse gene reduces the two major pathological perturbations commonly associated with Alzheimer's disease (AD).
Mouse gene suppresses Alzheimer's plaques and tangles
Investigators at Burnham Institute for Medical Research (Burnham) and colleagues have identified a novel mouse gene (Rps23r1) that reduces the accumulation of two toxic proteins that are major players in Alzheimer's disease: amyloid beta and tau.
Amyloid beta protein gets bum rap
While too much amyloid beta protein in the brain is linked to the development of Alzheimer's disease, not enough of the protein in healthy brains can cause learning problems and forgetfulness, Saint Louis University scientists have found.
Hybrid molecules show promise for exploring, treating Alzheimer's
One of the many mysteries of Alzheimer's disease is how protein-like snippets called amyloid-beta peptides, which clump together to form plaques in the brain, may cause cell death, leading to the disease's devastating symptoms of memory loss and other mental difficulties.
Statins show dramatic drug and cell dependent effects in the brain
Besides their tremendous value in treating high cholesterol and lowering the risk of heart disease, statins have also been reported to potentially lower the risks of other diseases, such as dementia.
Manipulating Brain Inflammation May Help Clear Brain of Amyloid Plaques, Mayo Clinic Researchers Say
In a surprising reversal of long-standing scientific belief, researchers at the Mayo Clinic campus in Florida have discovered that inflammation in the brain is not the trigger that leads to buildup of amyloid deposits and development of Alzheimer's disease.
Alzheimer's lesions found in the retina
The eyes may be the windows to the soul, but new research indicates they also may mirror a brain ravaged by Alzheimer's disease.
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Amyloid, Prions, and Other Protein Aggregates, Volume 309 (Methods in Enzymology) by John N. Abelson (Editor), Melvin I. Simon (Editor), Ronald Wetzel (Editor) This volume includes a core of methodologies to attack the unique experimental problems presented by protein misassembly. Emphasis is on human biology applications, the area in which there is the most interest, in which most of the work has already been done, and in which there is the best evidence for the structural sophisitication of the protein aggregates. The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today--truly an essential... |
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The NewsHour Reports on Alzheimer's Disease Starring: Charlayne Hunter-Gault, Jim Lehrer, Susan Dentzer, Steven DeKosky, Ray Suarez Also With: MacNeil / Lehrer Productions (Producer) According to the Alzheimer's Association, as many as eight million Americans will be suffering from Alzheimer's by 2030 and 16 million by 2050. The NewsHour reports on treatments, vaccine development, research, the impact on caregivers and the growing incidence of early-onset Alzheimer's disease. This product is manufactured on demand using DVD-R recordable media. Amazon.com's standard return policy will apply. |
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Amyloid Control Slides (Pack of 10) by Azer Scientific Control slides are designed for use in monitoring stain performance in the Pathology lab. All slides feature a permanent positive charge that securely anchors all types of sections, improving the quality of preparations and readability. Size: 75x25mm. | |
![[beta]-amyloid Peptide (1-42), Human, Oncogene - Size 250 Ug - Model Pp69--25mg - Each (.25 Mg)](http://ecx.images-amazon.com/images/I/31Y1NF0J0EL._SL160_.gif) |
[beta]-amyloid Peptide (1-42), Human, Oncogene - Size 250 Ug - Model Pp69--25mg - Each (.25 Mg) by Oncogene [beta]-Amyloid Peptide (1-42), Human, Oncogene - Size 250 ug - Model PP69--25MG - Each (.25 MG) : Lyophilized.Synthetic peptide corresponding to amino acids 1-42 of the processed human amyloid peptide. Supplied in a form that is not neurotoxic prior to preincubation. The level of toxicity has recently been shown to correlate to the extent of beta sheet structure. Reconstitute with degassed HPLC grade deionized water. Purity: >95% by HPLC. FW: 4 kDa. |
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The Nature and Origin of Amyloid Fibrils (Novartis Foundation Symposia) by CIBA Foundation Symposium (Author) The term amyloid fibril refers to a protein that has self-assembled into an insoluble antiparallel β-pleated sheet quaternary structure. This process is known as amyloidogenesis, and in combination with other non-protein components these fibrils give rise to the amyloid plaques that are seen in a number of pathological processes. As recently as 25 years ago, amyloid fibrils were thought to represent a single protein entity on the basis of their unique morphological and protein-organizational characteristics. Subsequently it has been shown that a number of different amyloid proteins existso far almost 20 have been identified, each associated with a particular disorder. Among these, β-amyloid forms plaques in the brains of individuals with Alzheimers disease and Downs syndrome,... |
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Alzheimer's Disease: Cellular and Molecular Aspects of Amyloid beta (Subcellular Biochemistry) by Robin Harris (Editor), Falk Fahrenholz (Editor) Preface: To understand Alzheimer?s disease (AD) is one of the major thrusts of present-day clinical research, strongly supported by more fundamental cellular, biochemical, immunological and structural studies. It is these latter that receive attention within this book. This compilation of 20 chapters indicates the diversity of work currently in progress and summarizes the current state of knowledge. Experienced authors who are scientifically active in their fields of study have been selected as contributors to this book, in an attempt to present a reasonably complete survey of the field. Inevitably, some exciting topics for one reason or another have not been included, for which we can only apologize. Standardization of terminology is often a problem in science, not least... |
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ProteoTech receives issuance of United States patent covering treatments for human amyloid diseases.: An article from: BIOTECH Patent News by Biotech Patent News (Publisher) This digital document is an article from BIOTECH Patent News, published by Biotech Patent News on September 1, 2003. The length of the article is 5301 words. The page length shown above is based on a typical 300-word page. The article is delivered in HTML format and is available in your Amazon.com Digital Locker immediately after purchase. You can view it with any web browser. Citation Details Title: ProteoTech receives issuance of United States patent covering treatments for human amyloid diseases. Publication: BIOTECH Patent News (Newsletter) Date: September 1, 2003 Publisher: Biotech Patent News Volume: 17 Issue: 9 Distributed by Thomson... | |
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Amyloid and Amyloidosis by T. Isobe (Editor) | |
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Amyloid Proteins (Methods in Molecular Biology) by Einar M. Sigurdsson (Editor) A proven collection of readily reproducible techniques for studying amyloid proteins and their involvement in the etiology, pathogenesis, diagnosis, and therapy of amyloid diseases. The contributors provide methods for the preparation of amyloid and its precursors (oligomers and protofibrils), in vitro assays and analytical techniques for their study, and cell culture models and assays for the production of amyloid proteins. Additional chapters present readily reproducible techniques for amyloid extraction from tissue, its detection in vitro and in vivo, as well as nontransgenic methods for developing amyloid mouse models. The protocols follow the successful Methods in Molecular Biology™ series format, each offering step-by-step laboratory instructions, an introduction outlining the... |
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Cerebral Amyloid Angiopathy in Alzheimer's Disease and Related Disorders by Marcel M. Verbeek (Author), Harry V. Vinters (Author), M.M. Verbeek (Editor), R.M. de Waal (Editor), H.V. Vinters (Editor) Cerebral amyloid angiopathy (CAA) is a distinctive abnormality of small cerebral blood vessels, one that has intrigued neuroscientists for decades. The time seems right for a book which examines the phenomenon of CAA using a multifaceted approach: What does it produce clinically? How might CAA be imaged? What are the crucial biochemical/cellular events within cerebral vessel walls that lead to CAA? How can in vitro or transgenic experimental systems be used to understand the etiology of, or even potential treatments for, CAA? The editors have assembled key figures in the field of CAA research to examine these (and other) questions in a series of focused chapters that address specific issues of importance in understanding CAA and its clinical manifestations. Comprehending the... |
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