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How and why certain proteins misfold and how this misfolding is
linked to many disease processes has become a well-documented topic
of study. Protein Misfolding and Cellular Stress in Disease and
Aging: Concepts and Protocols moves beyond the basics to emphasize
the molecular effects of protein misfolding at a cellular level, to
delineate the impacts and cellular reactions that play a role in
pathogenetic mechanisms, and to pinpoint possible manipulations and
treatment strategies that can counteract, modify, or delay the
consequences of misfolding. The volume begins with several concepts
and approaches developed in the recent past including a connection
to the research field of aging, where protein misfolding diseases
have been equated to premature aging processes, and the book's
coverage continues with detailed descriptions of protocols for
relevant experimental approaches. Written in the highly successful
Methods in Molecular Biology (TM) series format, protocols chapters
include introductions to their respective topics, lists of the
necessary materials and reagents, step-by-step, readily
reproducible laboratory protocols, and tips on troubleshooting and
avoiding known pitfalls. Authoritative and cutting-edge, Protein
Misfolding and Cellular Stress in Disease and Aging: Concepts and
Protocols aims to aid researchers in the field, as well as medical
professionals and molecular biologists, in shaping and performing
research related to this intriguing and vital subject.
For decades it has been known that structured conformations are
important for the proper functioning of most cellular proteins.
However, appreciation that protein folding to the functional
conformations as well as the structural maintenance of protein
molecules are very complex processes has only emerged during the
last ten years. The intimate interplay uncovered by this scientific
development led us to realize that perturbations of the protein
folding process and disturbances of conformational maintenance are
major disease mechanisms. This development has given rise to the
concept of conformational diseases and the broader signature of
protein folding diseases, comprising diseases in which mutations or
environmental stresses may result in a partial misfolding that
leads then to alternative conformations capable of disturbing
cellular processes. This may happen by self-association
(aggregation), as in prion and Alzheimer's diseases, or by
incorporation of alternatively folded subunits into structural
entities, as in collagen diseases. Another possibility is that
folding to the native structure is impaired or abolished, resulting
in decreased stea- state levels of the correctly folded protein, as
is observed in cystic fibrosis and 1-antitrypsin deficiency, as
well as in many enzyme deficiencies. In addition, deficiencies of
proteins that are engaged in assisting and supervising protein
folding (protein quality control) may impair the folding of many
other proteins, resulting in pathological phenotypes. Examples of
this are the spastic paraplegia attributable to mutations in
mitochondrial protease/chaperone complexes.
For decades it has been known that structured conformations are
important for the proper functioning of most cellular proteins.
However, appreciation that protein folding to the functional
conformations as well as the structural maintenance of protein
molecules are very complex processes has only emerged during the
last ten years. The intimate interplay uncovered by this scientific
development led us to realize that perturbations of the protein
folding process and disturbances of conformational maintenance are
major disease mechanisms. This development has given rise to the
concept of conformational diseases and the broader signature of
protein folding diseases, comprising diseases in which mutations or
environmental stresses may result in a partial misfolding that
leads then to alternative conformations capable of disturbing
cellular processes. This may happen by self-association
(aggregation), as in prion and Alzheimer s diseases, or by
incorporation of alternatively folded subunits into structural
entities, as in collagen diseases. Another possibility is that
folding to the native structure is impaired or abolished, resulting
in decreased stea- state levels of the correctly folded protein, as
is observed in cystic fibrosis and 1-antitrypsin deficiency, as
well as in many enzyme deficiencies. In addition, deficiencies of
proteins that are engaged in assisting and supervising protein
folding (protein quality control) may impair the folding of many
other proteins, resulting in pathological phenotypes. Examples of
this are the spastic paraplegia attributable to mutations in
mitochondrial protease/chaperone complexes."
How and why certain proteins misfold and how this misfolding is
linked to many disease processes has become a well-documented topic
of study. Protein Misfolding and Cellular Stress in Disease and
Aging: Concepts and Protocols moves beyond the basics to emphasize
the molecular effects of protein misfolding at a cellular level, to
delineate the impacts and cellular reactions that play a role in
pathogenetic mechanisms, and to pinpoint possible manipulations and
treatment strategies that can counteract, modify, or delay the
consequences of misfolding. The volume begins with several concepts
and approaches developed in the recent past including a connection
to the research field of aging, where protein misfolding diseases
have been equated to premature aging processes, and the book's
coverage continues with detailed descriptions of protocols for
relevant experimental approaches. Written in the highly successful
Methods in Molecular Biology (TM) series format, protocols chapters
include introductions to their respective topics, lists of the
necessary materials and reagents, step-by-step, readily
reproducible laboratory protocols, and tips on troubleshooting and
avoiding known pitfalls. Authoritative and cutting-edge, Protein
Misfolding and Cellular Stress in Disease and Aging: Concepts and
Protocols aims to aid researchers in the field, as well as medical
professionals and molecular biologists, in shaping and performing
research related to this intriguing and vital subject.
In this unique overview of the Hsp60 chaperonin, Peter Bross
addresses molecular biologists, medical research scientists and
individuals interested in molecular or general biology. First,
Bross discusses the basics of the Hsp60 chaperonin in terms of its
structure and the molecular mechanisms determining its function.
Second, the author highlights the multiple roles of Hsp60 for
cellular systems and regulatory pathways, especially in connection
with neurodegenerative diseases caused by Hsp60 deficiency.
Finally, the author highlights controversial observations
suggesting additional, non-standard functions of Hsp60 in and
outside mitochondria as well as possible gaps in our understanding
of the chaperonin. This volume serves as a snapshot suitable for
experienced researcher working in fields related to molecular
chaperones yet still accessible to researchers entering the field.
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