Jesus Avila

Jose J. Lucas

Felix Hernandez

Ana Martinez

This book provides up-to-date information on the use of transgenic mouse models in the study of neurodegenerative disorders. The editors have extensive knowledge and experience in this field and the book is aimed at undergraduates, postgraduates and academics.

Animal Models for Neurodegenerative Disease

R. Brandt

K. S. Kosik

Brain Microtubule Associated Proteins lays a firm foundation for understanding the brain microtubule associated proteins and how they contribute to the neurodegeneration of Alzheimer's disease. Few other reference works contain within a single source such a complete treatment of this topic. The authors cast a broad net over the field by devoting the first four chapters to each of the major brain microtubule associated proteins, MAP1A, MAP1B, MAP2 and tau. Completing this background material are chapters on the cellular role of these proteins in developing neurons and the sorting of tau to axons. The remaining chapters focus on tau - its kinases, its phosphatases, and other post-translational modifications such as ubiquitination and glycation. The second part of the book takes a more practical approach and includes chapters on the purification of microtubule associated proteins, functional assays using gene-transfer experiments, immunofluorescence and video microscopic analysis. This book is intended not only to be a reference source for expert laboratories but also to provide information which will allow a novice in the field to choose the best method for a particular purpose.

Brain Microtuble Associated Proteins

This work focuses on the structural and functional description of the microtubule proteins. The objective of the authors is to establish a relationship between the structure of microtubule proteins and the functions in which these polymers are involved. This book covers topics which have been treated only in a preliminary manner in previous works, such as microtubule dynamics and microtubule poisons. Microtubules display a variety of cellular roles and are vital for the separation and correct distribution of chromosomes during cell division. They also play an important role in morphogenesis, intracellular transport, secretion, and motility. Microtubule Proteins is a concise, easy-to-read text which is particularly of interest to cell biologists, chemists, neurochemists, and graduate students interested in cell biology.

Microtubule Proteins

C. Laura Sayas

Monica Mendes Sousa

Shaping the Brain by Neuronal Cytoskeleton: from Development to Disease and Regeneration

Naruhiko Sahara

Neurofibrillary tangles (NFTs) composed of intracellular aggregates of tau protein are a key neuropathological feature of Alzheimer’s Disease (AD) and other neurodegenerative diseases, collectively termed tauopathies. The abundance of NFTs has been reported to correlate positively with the severity of cognitive impairment in AD. However, accumulating evidences derived from studies of experimental models have identified that NFTs themselves may not be neurotoxic. Now, many of tau researchers are seeking a “toxic” form of tau protein. Moreover, it was suggested that a “toxic” tau was capable to seed aggregation of native tau protein and to propagate in a prion-like manner. However, the exact neurotoxic tau species remain unclear. Because mature tangles seem to be non-toxic component, “tau oligomers” as the candidate of “toxic” tau have been investigated for more than one decade. In this topic, we will discuss our consensus of “tau oligomers” because the term of “tau oligomers” [e.g. dimer (disulfide bond-dependent or independent), multimer (more than dimer), granular (definition by EM or AFM) and maybe small filamentous aggregates] has been used by each researchers definition. From a biochemical point of view, tau protein has several unique characteristics such as natively unfolded conformation, thermo-stability, acid-stability, and capability of post-translational modifications. Although tau protein research has been continued for a long time, we are still missing the mechanisms of NFT formation. It is unclear how the conversion is occurred from natively unfolded protein to abnormally mis-folded protein. It remains unknown how tau protein can be formed filaments [e.g. paired helical filament (PHF), straight filament and twisted filament] in cells albeit in vitro studies confirmed tau self-assembly by several inducing factors. Researchers are still debating whether tau oligomerization is primary event rather than tau phosphorylation in the tau pathogenesis. Inhibition of either tau phosphorylation or aggregation has been investigated for the prevention of tauopathies, however, it will make an irrelevant result if we don’t know an exact target of neurotoxicity. It is a time to have a consensus of definition, terminology and methodology for the identification of “tau oligomers”.

Tau oligomers

Miguel Medina

Untangling the Role of Tau in Physiology and Pathology

Jesus Avila

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