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Long-lived proteins in human aging a...

Truscott, Roger J. W.

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Long-lived proteins in human aging and disease

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Long-lived proteins in human aging and disease/ edited by Roger J.W. Truscott.
其他作者:	Truscott, Roger J. W.
出版者:	Weinheim :Wiley-VCH, : c2021.,
面頁冊數:	1 online resource.
內容註:	Introduction to the Book -- Long-Lived Cells and Long-Lived Proteins in the Human Body / Roger JW Truscott -- Imaging Mass Spectrometry of Long-Lived Proteins / Kevin L Schey -- Eye Lens Crystallins: Remarkable Long-Lived Proteins / Aidan B Grosas, John A Carver -- Spontaneous Breakdown of Long-Lived Proteins in Aging and Their Implications in Disease / Michael G Friedrich -- Modifications of Long-Lived Proteins that Affect Protein Solubility / Larry L David -- Degradation of Long-Lived Proteins as a Cause of Autoimmune Diseases / Roger JW Truscott -- How Isomerization and Epimerization in Long-Lived Proteins Affect Lysosomal Degradation and Proteostasis / Ryan R Julian -- The Maillard Reaction: Protein Modification by Ascorbic Acid / Vincent M Monnier, David R Sell, Grant Hom, Shiyuan Dong, Benlian Wang, Xingjun Fan.
標題:	Aging - Molecular aspects. -
電子資源:	https://onlinelibrary.wiley.com/doi/book/10.1002/9783527826759
ISBN:	9783527826759

Long-lived proteins in human aging and disease
Long-lived proteins in human aging and disease[electronic resource] /edited by Roger J.W. Truscott. - Weinheim :Wiley-VCH,c2021. - 1 online resource.

Includes bibliographical references and index.

Introduction to the Book -- Long-Lived Cells and Long-Lived Proteins in the Human Body / Roger JW Truscott -- Imaging Mass Spectrometry of Long-Lived Proteins / Kevin L Schey -- Eye Lens Crystallins: Remarkable Long-Lived Proteins / Aidan B Grosas, John A Carver -- Spontaneous Breakdown of Long-Lived Proteins in Aging and Their Implications in Disease / Michael G Friedrich -- Modifications of Long-Lived Proteins that Affect Protein Solubility / Larry L David -- Degradation of Long-Lived Proteins as a Cause of Autoimmune Diseases / Roger JW Truscott -- How Isomerization and Epimerization in Long-Lived Proteins Affect Lysosomal Degradation and Proteostasis / Ryan R Julian -- The Maillard Reaction: Protein Modification by Ascorbic Acid / Vincent M Monnier, David R Sell, Grant Hom, Shiyuan Dong, Benlian Wang, Xingjun Fan.

"While most proteins in the human body are short-lived and are constantly being regenerated, this is not true for all. A significant fraction of proteins in long-lived cells such as nerve cells are likewise long-lived and will age over time by accumulating damage and other modifications. Scientists are only beginning to understand how this aging of long-lived proteins contributes to age-dependent diseases such as dementia and cancer Divided into six major sections, this comprehensive overview on an emerging topic in the molecular life sciences covers all aspects of the aging of (long-lived) proteins. Analytical methods to study protein half-life and the accumulation of modifications are presented, followed by several examples of long-lived proteins found in humans and other organisms. Next, the molecular mechanisms of aging on the protein level are described, in particular the most common side chain modifications, followed by a discussion of the consequences of protein aging on cellular and organ function. Finally, the impact of protein aging on several age-related disases in humans is dissected, and their role in limiting human lifespan is discussed"--

ISBN: 9783527826759Subjects--Topical Terms:

541762
Aging
--Molecular aspects.

LC Class. No.: QP551

Dewey Class. No.: 612.6/7

Long-lived proteins in human aging and disease
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245 0 0 $a Long-lived proteins in human aging and disease $h [electronic resource] / $c edited by Roger J.W. Truscott.
260 $a Weinheim : $b Wiley-VCH, $c c2021.
300 $a 1 online resource.
504 $a Includes bibliographical references and index.
505 0 $a Introduction to the Book -- Long-Lived Cells and Long-Lived Proteins in the Human Body / Roger JW Truscott -- Imaging Mass Spectrometry of Long-Lived Proteins / Kevin L Schey -- Eye Lens Crystallins: Remarkable Long-Lived Proteins / Aidan B Grosas, John A Carver -- Spontaneous Breakdown of Long-Lived Proteins in Aging and Their Implications in Disease / Michael G Friedrich -- Modifications of Long-Lived Proteins that Affect Protein Solubility / Larry L David -- Degradation of Long-Lived Proteins as a Cause of Autoimmune Diseases / Roger JW Truscott -- How Isomerization and Epimerization in Long-Lived Proteins Affect Lysosomal Degradation and Proteostasis / Ryan R Julian -- The Maillard Reaction: Protein Modification by Ascorbic Acid / Vincent M Monnier, David R Sell, Grant Hom, Shiyuan Dong, Benlian Wang, Xingjun Fan.
520 $a "While most proteins in the human body are short-lived and are constantly being regenerated, this is not true for all. A significant fraction of proteins in long-lived cells such as nerve cells are likewise long-lived and will age over time by accumulating damage and other modifications. Scientists are only beginning to understand how this aging of long-lived proteins contributes to age-dependent diseases such as dementia and cancer Divided into six major sections, this comprehensive overview on an emerging topic in the molecular life sciences covers all aspects of the aging of (long-lived) proteins. Analytical methods to study protein half-life and the accumulation of modifications are presented, followed by several examples of long-lived proteins found in humans and other organisms. Next, the molecular mechanisms of aging on the protein level are described, in particular the most common side chain modifications, followed by a discussion of the consequences of protein aging on cellular and organ function. Finally, the impact of protein aging on several age-related disases in humans is dissected, and their role in limiting human lifespan is discussed"-- $c Provided by publisher.
588 $a Description based on print version record.
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650 0 $a Proteins. $3 558769
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700 1 $a Truscott, Roger J. W. $3 3621088
856 4 0 $u https://onlinelibrary.wiley.com/doi/book/10.1002/9783527826759