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Books on the topic 'Misfolding disease'

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Author: Grafiati

Published: 9 March 2023

Last updated: 10 March 2023

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1

Bross, Peter, and Niels Gregersen. Protein Misfolding and Disease. New Jersey: Humana Press, 2003. http://dx.doi.org/10.1385/1592593941.

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2

Hill, Andrew F., Kevin J. Barnham, Stephen P. Bottomley, and Roberto Cappai, eds. Protein Folding, Misfolding, and Disease. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-60327-223-0.

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3

name, No. Protein misfolding and disease: Principles and protocols. Totowa, NJ: Humana Press, Inc., 2003.

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4

Peter, Bross, and Gregersen Niels, eds. Protein misfolding and disease: Principles and protocols. Totowa, N.J: Humana Press, 2003.

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5

Protein folding, misfolding, and disease: Methods and protocols. New York: Humana, 2011.

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6

Bross, Peter, and Niels Gregersen, eds. Protein Misfolding and Cellular Stress in Disease and Aging. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-756-3.

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7

Protein misfolding and cellular stress in disease and aging: Concepts and protocols. New York: Humana Press, 2010.

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8

Ramirez-Alvarado, Marina, Jeffery W. Kelly, and Christopher M. Dobson, eds. Protein Misfolding Diseases. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470572702.

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9

Gomes, Cláudio M., ed. Protein Misfolding Diseases. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-8820-4.

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10

Ferenc, Orosz, Ovádi Judit 1941-, and SpringerLink (Online service), eds. Protein Folding and Misfolding: Neurodegenerative Diseases. Dordrecht: Springer Netherlands, 2009.

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11

Uversky, Vladimir N., and Anthony L. Fink, eds. Protein Misfolding, Aggregation, and Conformational Diseases. Boston, MA: Springer US, 2006. http://dx.doi.org/10.1007/b136464.

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12

Uversky, Vladimir N., and Anthony L. Fink, eds. Protein Misfolding, Aggregation, and Conformational Diseases. Boston, MA: Springer US, 2007. http://dx.doi.org/10.1007/978-0-387-36534-3.

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13

Ovádi, Judit, and Ferenc Orosz, eds. Protein Folding and Misfolding: Neurodegenerative Diseases. Dordrecht: Springer Netherlands, 2009. http://dx.doi.org/10.1007/978-1-4020-9434-7.

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14

N, Uversky Vladimir, and Fink Anthony L. 1943-, eds. Protein misfolding, aggregation, and conformational diseases. New York, N.Y: Springer Science+Business Media, 2006.

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15

N, Uversky Vladimir, and Fink Anthony L. 1943-, eds. Protein misfolding, aggregation and conformational diseases. New York: Springer, 2007.

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16

N, Uversky Vladimir, and Fink Anthony L. 1943-, eds. Protein misfolding, aggregation and conformational diseases. New York: Springer, 2006.

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17

Marina, Ramirez-Alvarado, Kelly Jeffery W, and Dobson C. M, eds. Protein misfolding diseases: Current and emerging principles and therapies. Hoboken, N.J: Wiley, 2010.

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18

1930-, Smith H. J., Simons Claire, and Sewell Robert D. E, eds. Protein misfolding in neurodegenerative diseases: Mechanisms and therapeutic strategies. Boca Raton: Taylor & Francis, 2008.

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19

Gregersen, Niels, and Peter Bross. Protein Misfolding and Disease. Humana Press, 2010.

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20

Protein Misfolding and Disease (Methods in Molecular Biology). Humana Press, 2003.

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21

Molecular Targets in Protein Misfolding and Neurodegenerative Disease. Elsevier, 2015. http://dx.doi.org/10.1016/c2013-0-15458-x.

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22

Chemical Modulators of Protein Misfolding and Neurodegenerative Disease. Elsevier, 2015. http://dx.doi.org/10.1016/c2014-0-01580-8.

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23

Seneci, Pierfausto. Molecular Targets in Protein Misfolding and Neurodegenerative Disease. Elsevier Science & Technology Books, 2018.

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24

Barnham, Kevin J., Stephen P. Bottomley, Roberto Cappai, and Andrew F. Hill. Protein Folding, Misfolding, and Disease: Methods and Protocols. Humana Press, 2016.

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25

Seneci, Pierfausto. Chemical Modulators of Protein Misfolding and Neurodegenerative Disease. Elsevier Science & Technology Books, 2015.

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26

Seneci, Pierfausto. Molecular Targets in Protein Misfolding and Neurodegenerative Disease. Elsevier Science & Technology Books, 2014.

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27

Seneci, Pierfausto. Molecular Targets in Protein Misfolding and Neurodegenerative Disease. Elsevier Science & Technology Books, 2014.

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28

Seneci, Pierfausto. Chemical Modulators of Protein Misfolding and Neurodegenerative Disease. Elsevier Science & Technology Books, 2015.

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29

Williams, Danielle, and Tara L. Pukala. Protein Misfolding, Aggregation and Disease: Insights from Mass Spectrometry. Wiley & Sons, Incorporated, John, 2021.

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30

Williams, Danielle, and Tara L. Pukala. Protein Misfolding, Aggregation and Disease: Insights from Mass Spectrometry. Wiley & Sons, Limited, John, 2021.

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31

Williams, Danielle, and Tara L. Pukala. Protein Misfolding, Aggregation and Disease: Insights from Mass Spectrometry. Wiley & Sons, Incorporated, John, 2021.

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32

Nakamura, Tomohiro, and Stuart A. Lipton. Neurodegenerative Diseases as Protein Misfolding Disorders. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190233563.003.0002.

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Neurodegenerative diseases (NDDs) often represent disorders of protein folding. Rather than large aggregates, recent evidence suggests that soluble oligomers of misfolded proteins are the most neurotoxic species. Emerging evidence points to small, soluble oligomers of misfolded proteins as the cause of synaptic dysfunction and loss, the major pathological correlate to disease progression in many NDDs including Alzheimer’s disease. The protein quality control machinery of the cell, which includes molecular chaperones as found in the endoplasmic reticulum (ER), the ubiquitin-proteasome system (UPS), and various forms of autophagy, can counterbalance the accumulation of misfolded proteins to some extent. Their ability to eliminate the neurotoxic effects of misfolded proteins, however, declines with age. A plausible explanation for the age-dependent deterioration of the quality control machinery involves compromise of these systems by excessive generation of reactive oxygen species (ROS), such as superoxide anion (O2-), and reactive nitrogen species (RNS), such as nitric oxide (NO). The resulting redox stress contributes to the accumulation of misfolded proteins. Here, we focus on aberrantly increased generation of NO-related species since this process appears to accelerate the manifestation of key neuropathological features, including protein misfolding. We review the chemical mechanisms of posttranslational modification by RNS such as protein S-nitrosylation of critical cysteine thiol groups and nitration of tyrosine residues, showing how they contribute to the pathogenesis of NDDs.

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33

Gregersen, Niels, and Peter Bross. Protein Misfolding and Cellular Stress in Disease and Aging: Concepts and Protocols. Humana Press, 2016.

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34

Safar, Jiri G. Prion Paradigm of Human Neurodegenerative Diseases Caused by Protein Misfolding. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190233563.003.0005.

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Data accumulated from different laboratories argue that a growing number of proteins causing neurodegeneration share certain characteristics with prions. Prion-like particles were produced from synthetic amyloid beta (Aβ‎) peptides of Alzheimer’s disease (AD), from recombinant α‎-synuclein linked to Parkinson’s disease (PD), and from recombinant tau associated with frontotemporal dementias (FTD). Evidence from human prions reveals that variable disease phenotypes, rates of propagation, and targeting of different brain structures are determined by distinct conformers (strains) of pathogenic prion protein. Recent progress in the development of advanced biophysical tools identified the structural characteristics of Aβ‎ in the brain cortex of phenotypically diverse AD patients and thus allowed an investigation of the prion paradigm of AD. The findings of distinctly structured strains of human brain Aβ‎, forming a unique spectrum of oligomeric particles in the cortex of rapidly progressive cases, implicates these structures in variable rates of propagation in the brain.

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35

Kelly, Jeffery W., Marina Ramirez-Alvarado, and Christopher M. Dobson. Protein Misfolding Diseases. Wiley & Sons, Incorporated, John, 2010.

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36

Sewell, Robert D. E. Protein Misfolding in Neurodegenerative Diseases. Taylor & Francis Group, 2019.

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37

Gogia, Neha, Vidyadhara Devarunda Jaganath, and Sandeep Kumar Singh. Protein Misfolding in Neurodegenerative Diseases. Elsevier Science & Technology Books, 2024.

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38

E, Sewell Robert D., and Robert D. Sewell. Protein Misfolding in Neurodegenerative Diseases. Taylor & Francis Group, 2007.

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39

Cummings, Jeffrey L., and Jagan A. Pillai. Neurodegenerative Diseases. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190233563.003.0001.

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Neurodegenerative diseases (NDDs) are growing in frequency and represent a major threat to public health. Advances in scientific progress have made it clear that NDDs share many underlying processes, including shared intracellular mechanisms such as protein misfolding and aggregation, cell-to-cell prion-like spread, growth factor signaling abnormalities, RNA and DNA disturbances, glial cell changes, and neuronal loss. Transmitter deficits are shared across many types of disorders. Means of studying NDDs with human iPS cells and transgenic models are similar. The progression of NDDs through asymptomatic, prodromal, and manifest stages is shared across disorders. Clinical features of NDDs, including cognitive impairment, disease progression, age-related effects, terminal stages, neuropsychiatric manifestations, and functional disorders and disability, have many common elements. Clinical trials, biomarkers, brain imaging, and regulatory aspects of NDD can share information across NDDs. Disease-modifying and transmitter-based therapeutic interventions, clinical trials, and regulatory approaches to treatments for NDDs are also similar.

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40

Ovádi, Judit, and Ferenc Orosz. Protein folding and misfolding : neurodegenerative diseases: Neurodegenerative diseases. Judit Ovadi, 2010.

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41

Gomes, Cláudio M. Protein Misfolding Diseases: Methods and Protocols. Springer New York, 2018.

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42

Gomes, Cláudio M. Protein Misfolding Diseases: Methods and Protocols. Springer New York, 2019.

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43

Cummings, Jeffrey L., and Jagan A. Pillai, eds. Neurodegenerative Diseases. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190233563.001.0001.

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With an increasingly aging population, neurodegenerative diseases-such as Alzheimer’s disease, Lewy body dementia, frontotemporal dementia, and Parkinson’s disease-are becoming more prevalent in the world. This is an area of rapidly growing high-impact research as these neurodegenerative diseases are a huge burden for individuals, families, and societies both in quality of life and in healthcare costs. Finding novel therapeutic targets for neurodegenerative diseases is the premier medical challenge for this century. Classically each of these diseases has been viewed as a distinct entity with well-delineated clinical and pathological features. Recent research findings have revealed multiple commonalities across them; proteomic, genetic, cellular, and network mechanisms across neurodegenerative diseases. This conceptual revolution in our understanding of these neurodegenerative diseases as sharing unifying features is underpinned by underlying protein misfolding dysfunction and its consequences over time. As we search for new therapies and management of these neurodegenerative diseases, this book provides an effective source book of insights from experts that have played key roles in this conceptual revolution. Our goal is to enable better care of patients and to help build collaboration across research in multiple specializations that could help advance future insights and facilitate novel therapeutics.

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44

Cummings, Jeffrey L., and Kate Zhong. Clinical Trials and Drug Development in Neurodegenerative Diseases. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190233563.003.0018.

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This chapter describes the common therapeutic targets, approaches to clinical trial design, biomarkers, and therapeutic interventions across neurodegenerative disorders (NDDs). Each unique NDD-Alzheimer’s disease (AD), Parkinson’s disease (PD), amyotrophic lateral sclerosis (ALS), etc.-has a unique phenotype associated with the regional cell population most affected. Each disease, however, is associated with protein misfolding, oxidation, inflammation, apoptosis, and cell death. If vulnerable cell populations include transmitter source nuclei, transmitter deficits also emerge (e.g. cholinergic abnormalities in AD and dopaminergic deficits in PD). Biomarkers show regionally appropriate brain atrophy or process-related cerebrospinal deficits. Clinical trial designs share features for symptomatic interventions (e.g. cholinesterase inhibitors in AD and dopamine agents in PD) and disease-modifying therapies. Biomarkers play similar roles in trials for NDD, including demonstrating target engagement and supporting disease modification. No disease-modifying therapies have been approved for any NDDs; all programs face similar pharmacokinetic, pharmacodynamic, and regulatory challenges in therapeutic development.

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45

Lázaro, Diana Fernandes, Tiago F. Outeiro, Arianna Bellucci, and Patrik Brundin, eds. Protein Misfolding and Spreading Pathology in Neurodegenerative Diseases. Frontiers Media SA, 2020. http://dx.doi.org/10.3389/978-2-88963-507-8.

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46

Kelly, Jeffery W., Marina Ramirez-Alvarado, and Christopher M. Dobson. Protein Misfolding Diseases: Current and Emerging Principles and Therapies. Wiley & Sons, Incorporated, John, 2010.

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47

Kelly, Jeffery W., Marina Ramirez-Alvarado, and Christopher M. Dobson. Protein Misfolding Diseases: Current and Emerging Principles and Therapies. Wiley & Sons, Incorporated, John, 2011.

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48

Sewell, Robert D. E. Protein Misfolding in Neurodegenerative Diseases: Mechanisms and Therapeutic Strategies. Taylor & Francis Group, 2007.

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49

Sewell, Robert D. E. Protein Misfolding in Neurodegenerative Diseases: Mechanisms and Therapeutic Strategies. Taylor & Francis Group, 2007.

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50

Kelly, Jeffery W., Marina Ramirez-Alvarado, Christopher M. Dobson, and Marina Ramirez-Alvarado. Protein Misfolding Diseases: Current and Emerging Principles and Therapies. Wiley & Sons, Incorporated, John, 2010.

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