home   genetic news   bioinformatics   biotechnology   literature   journals   ethics   positions   events   sitemap
  HUM-MOLGEN -> Literature | search  

Sipe et al. 2005. Amyloid Proteins. 1st Ed.

  September, 16 2005 19:12
new and historical books in bioscience and medicine

1. Edition - October 2005
£210.00 / €315.00
799 Pages, Hardcover
ISBN 3-527-31072-X - Wiley-VCH, Weinheim

-> Wiley
-> Amazon

Short description

A first-stop reference on proteins associated with amyloidosis.

This book is the first to present a systematic overview of all known fibril-forming proteins, including their biochemical characteristics and pathophysiology. It considers the clinically recognized amyloid proteins that are known to be associated with the amyloid protein folding disorders, dealing with their common structural and thermodynamic features that lead to amyloid fibril formation and disease. Emphasis is on the thermodynamics of protein folding, the structure and physiologic effects of common oligomeric and subfibrillar intermediates and the influence of the extracellular matrix and cellular trafficking and metabolism on the genesis and catabolism of beta pleated sheet proteins.

The chapters on specific amyloid proteins all follow a common structure, allowing quick access to the desired biochemical and medical data, making this an invaluable tool for clinicians and researchers alike.

-> Preface
-> Content
-> Sample Chapter

From the contents

PART I Overview of Amyloidosis and Amyloid Proteins

Brief history of amyloidosis
Anatomic and clinical clues to in vivo mechanisms of amyloidogenesis

PART II Protein Structure and the Beta Pleated Sheet Conformation

Brief history of the beta pleated sheet conformation including glossary of terms

PART III Protein Folding, Unfolding and Refolding

Thermodynamics and protein folding
The role of post-translational chemical modifications in amyloid fibril formation
Lipid modulators of protein misfolding and aggregation
Extracellular matrix-heparan sulfate proteoglycans
Serum amyloid P component: Structural features and amyloid recognition
Apolipoprotein E

PART IV Pathways to Amyloid Fibril Formation

Partially folded intermediates in the fibrillation of natively unfolded proteins
Partially folded intermediates, random coil
Chemical interactions in amyloid fibril formation

PART V Pathophysiology of Amyloid Fibril Formation

Oligomers and cellular toxicity
Fibrils and organ dysfunction
Brain dysfunction associated with amyloid fibrils and other aggregated proteins

PART VI Amyloid Proteins

Beta amyloid protein
Prion protein
Familial dementia
Apolipoprotein, AApoAII and Amyloid A
Cystatin C
IAPP and Others

print this article mail this article
Latest News
Differentiation - free sample issue

Wanner. Höfner. 2007. Mass Spectrometry in Medicinal Chemistry.

Mirkin. Niemeyer. 2007. Nanobiotechnology II: More Concepts and Applications

Marx. Sandig. 2006. Drug Testing In Vitro: Breakthroughs and Trends in Cell Culture Technology

Hillenkamp. Peter-Katalinic. 2007. MALDI MS: A Practical Guide to Instrumentation, Methods and Applications

Call for Chapters for the Handbook of Research on Systems Biology Applications in Medicine

OpenHelix announces free trial subscriptions to its database of tutorials on genomic resources

Junghans et al. 2006. Intellectual Property Management

Cold Spring Harbor Laboratory Press to Launch CSH Protocols

Sabaté et al. 2003. Adherence to Long-Term Therapies: Evidence for Action (WHO)

Pathy. 2005. Principles and Practice of Geriatric Medicine. 4th Edition

Brigelius-Flohé. Joost. 2006. Nutritional Genomics

more news ...

Generated by News Editor 2.0 by Kai Garlipp
WWW: Kai Garlipp, Frank S. Zollmann.
7.0 © 1995-2018 HUM-MOLGEN. All rights reserved. Liability, Copyright and Imprint.