Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs

Forman, Mark S; Trojanowski, John Q; Lee, Virginia M-Y

doi:10.1038/nm1113

Cited by 715Alzheimer's disease research and treatmentsAmyotrophic Lateral Sclerosis ResearchPrion Diseases and Protein Misfolding

Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs

Forman, Mark S, Trojanowski, John Q, Lee, Virginia M-Y·2004·Nature Medicine

DOI 10.1038/nm1113

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Abstract

A wide variety of neurodegenerative diseases are characterized by the accumulation of intracellular or extracellular protein aggregates. More recently, the genetic identification of mutations in familial counterparts to the sporadic disorders, leading to the development of in vitro and in vivo model systems, has provided insights into disease pathogenesis. The effect of many of these mutations is the abnormal processing of misfolded proteins that overwhelms the quality-control systems of the cell, resulting in the deposition of protein aggregates in the nucleus, cytosol and/or extracellular space. Further understanding of mechanisms regulating protein processing and aggregation, as well as of the toxic effects of misfolded neurodegenerative disease proteins, will facilitate development of rationally designed therapies to treat and prevent these disorders.

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Many neurodegenerative diseases have known causes involving mutations in ubiquitously expressed proteins, yet they follow stereotyped degeneration patterns that selectively affect certain cell subsets, producing disease-specific spatial and temporal patterns.
“Many of these diseases have known causes that involve mutations in ubiquitously expressed proteins134, but they follow stereotyped patterns of degeneration that selectively affect certain cell subsets more severely, resulting in disease-specific spatial and temporal patterns of degeneration135–137 (BOX 1).”
From Systems biology and gene networks in neurodevelopmental and neurodegenerative disorders (2015) · cites this paper as [137]

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Authors: Forman, M. S., Trojanowski, J. Q., & Lee, V. M.-Y.
Affiliations: University of Pennsylvania (US)
ORCID: Trojanowski, John Q
Lee, Virginia M-Y
Venue: Nature Medicine
Publisher: Springer Science and Business Media LLC
Published: 2004-09-30
Volume: 10
Issue: 10
Pages: 1055-1063
ISSN: 1078-8956 (ISSN-L)
1546-170X
DOI: 10.1038/nm1113
OpenAlex: W2047304481
Cited by: 715
References: 105
Citations by year: 2026: 13 · 2025: 15 · 2024: 24 · 2023: 22 · 2022: 23 · 2021: 27 · 2020: 30 · 2019: 35 · 2018: 38 · 2017: 31 · 2016: 27 · 2015: 26 · 2014: 31 · 2013: 34 · 2012: 36
FWCI: 5.04
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Medicine (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute on Aging (P01AG014382, P01 AG11542, P01-AG09215, P30AG10124, P01AG011542, P01 AG-17586, P01AG014449, P01 AG14382, P30AG010124, P01AG009215, P01AG017586, P01 AG14449, K08AG020073, K08 AG20073-01)
National Institute of Neurological Disorders and Stroke (P01NS044233)
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
Keywords: neurodegenerative diseases, protein aggregation, protein misfolding, protein quality control, familial mutation, pathogenesis, treatment development
MeSH terms: Alzheimer Disease, Amyotrophic Lateral Sclerosis, Humans, Creutzfeldt-Jakob Syndrome, Models, Biological, Nerve Tissue Proteins, Peptides, Prions, Superoxide Dismutase, Amyloid beta-Peptides, Lewy Bodies, Protein Folding, Neurodegenerative Diseases, History, 20th Century, History, 21st Century, Synucleins

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Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs

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