Contents

Current Medicinal Chemistry - Immunology, Endocrine & Metabolic Agents, Volume 3 - Number 4

Preface [Hot topic: Protein Misfolding in the Amyloidoses and other Disorders (Guest Editor: David R. Howlett)]

, 3(4): ii - II

David R. Howlett


DOI: 10.2174/15680134103030400ii




The Many Faces of Aβ: Structures and Activity

, 3(4): 277 - 291

Dominic M. Walsh, Dean M. Hartley and Dennis J. Selkoe


DOI: 10.2174/1568013033483311




Amyloids, Aggregates and Neuronal Inclusions: Good or Bad News for Neurons?

, 3(4): 293 - 298

Hyoung-gon Lee, Xiongwei Zhu, Robert B. Petersen, George Perry and Mark A. Smith


DOI: 10.2174/1568013033483221




Direct Production of Reactive Oxygen Species from Aggregating Proteins and Peptides Implicated in the Pathogenesis of Neurodegenerative Diseases

, 3(4): 299 - 308

Brian J. Tabner, Stuart Turnbull, Omar M.A. El-Agnaf and David Allsop


DOI: 10.2174/1568013033483249




Aβ Metallobiology and the Development of Novel Metal-Protein Attenuating Compounds (MPACs) for Alzheimers Disease

, 3(4): 309 - 315

Cyril C. Curtain, Kevin J. Barnham and Ashley I. Bush


DOI: 10.2174/1568013033483276




Cerebrovascular Amyloidosis and Dementia

, 3(4): 317 - 327

Raj N. Kalaria, Alan Thomas, Arthur Oakley, Paul Ince, Akira Tamaoka, Hiroshi Mori, Rose Anne Kenny and Clive Ballard


DOI: 10.2174/1568013033483267




The Molecular Pathology of Huntingtons Disease (HD)

, 3(4): 329 - 340

David C. Rubinsztein


DOI: 10.2174/1568013033483320




Relevance of Mutations in Tau for Understanding the Tauopathies

, 3(4): 341 - 348

Michel Goedert


DOI: 10.2174/1568013033483258




Amyloid Formation by Transthyretin: From Protein Stability to Protein Aggregation

, 3(4): 349 - 360

Rui M.M. Brito, Ana Margarida Damas and Maria Joao Saraiva


DOI: 10.2174/1568013033483230




Proteoglycans and Amyloidogenic Proteins in Peripheral Amyloidosis

, 3(4): 361 - 370

Francine Gervais, Celine Morissette and Xianqi Kong


DOI: 10.2174/1568013033483294




Protein Misfolding in Disease: Cause or Response?

, 3(4): 371 - 383

David R. Howlett


DOI: 10.2174/1568013033483285




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