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Tuesday, July 28, 2020 | History

3 edition of Protein phosphorylation in aging and age-related disease found in the catalog.

Protein phosphorylation in aging and age-related disease

Protein phosphorylation in aging and age-related disease

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  • 2 Currently reading

Published by Elsevier in Amsterdam, Boston .
Written in English

    Subjects:
  • Phosphoproteins.,
  • Apoptosis.,
  • Cellular signal transduction.,
  • Aging -- Molecular aspects.,
  • Transcription factors.,
  • Phosphorylation.,
  • Cell Aging -- physiology.,
  • Aging -- metabolism.,
  • Phosphoproteins -- metabolism.,
  • Phosphorylation.,
  • Signal Transduction -- physiology.,
  • Tauopathies -- physiopathology.

  • Edition Notes

    Includes bibliographical references.

    Statementvolume editor, Mark P. Mattson.
    SeriesAdvances in cell aging and gerontology -- v. 16.
    ContributionsMattson, Mark Paul.
    Classifications
    LC ClassificationsQP552.P5 P767 2004
    The Physical Object
    Paginationvii, 178 p. :
    Number of Pages178
    ID Numbers
    Open LibraryOL18212350M
    ISBN 100444515836
    LC Control Number2003064334

    Jacques Fantini, Nouara Yahi, in Brain Lipids in Synaptic Function and Neurological Disease, Abstract. Parkinson’s disease is the second most common age-related neurodegenerative etiological basis is still unknown, but it is closely associated with the behavior of α-synuclein, a “chameleon” protein exhibiting exceptional conformational plasticity. T.K. Sawyer, in Comprehensive Medicinal Chemistry II, Protein phosphorylation has become a central focus of drug discovery as the result of the identification and validation of promising therapeutic targets such as protein kinases, protein phosphatases, and phosphoprotein binding domains. 1–24 With respect to such protein phosphorylation therapeutic targets, significant progress has.

    Protein Phosphorylation. Protein phosphorylation is a central signaling event in eukaryotes and is orchestrated by protein kinases that catalyze the transfer of the γ-phosphoryl group of a nucleoside triposphate (usually adenosine triphosphate, ATP) to an amino acid hydroxyl group (commonly serine, threonine, or tyrosine) of a protein substrate. Age-related muscle loss, called sarcopenia, is a natural part of aging. After you begin to lose as much as 3% to 5% per decade. Most men will lose about 30% of their muscle mass during their lifetimes. Less muscle means greater weakness and less mobility, both of .

    Age-related protein aggregation and lipofuscin accumulation result in an accumulation of cellular debris impervious to lysosomal and proteasomal degradation. The mitochondrial role in the chronic inflammation of aging is explored. The authors then turn to the role of exercise in correcting the cellular decline of aging.   Tinkering with roundworm proteins offers hope for anti-aging drugs. by tagging with green fluorescence protein (GFP) in C. elegans. of mitochondria are associated with age-related diseases.


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Protein phosphorylation in aging and age-related disease Download PDF EPUB FB2

The authors in addition to considering the roles of protein phosphorylation in aging describe the evidence that abnormalities in protein phosphorylation contribute to the pathogenesis of major age-related diseases including diabetes, atherosclerosis and neurodegenerative disorders such as Alzheimer's and Parkinson's Edition: 1.

ISBN: OCLC Number: Description: vii, pages: illustrations ; 24 cm. Contents: Ch. Organismal Aging and Phosphorylation of Transcription Factors / Peter W. Atadja and Paul O. Kwon --Ch. orylation of Cell Cycle Proteins at Senescence / Charanjit Sandhu --Ch.

n Phosphorylation in T-cell Signaling: Effect of Age / Bulbul Chakravarti and. Search in this book series. Protien Phosphorylation in Aging and Age-related Disease. M.P. Mattson.

Vol Pages () Download full volume. Previous volume. Next volume. Protein phosphorylation in T-cell signaling: effect of age.

Bulbul Chakravarti, Deb N. Chakravarti. Protein phosphorylation is a PTM that is of common occurrence in cells and is necessary for the activation or inactivation of protein molecules, in particular, as seen in enzymes that affect metabolic pathways or processes.

From: Epigenetics in Human Disease (Second Edition), Interleukin-6 in Aging and Chronic Disease: A Magnificent Pathway. and the role of IL-6 in aging and age-related conditions is now clearly established. However, some of Ershler’s questions are still in search of an answer.

induce the phosphorylation, ubiquitinization, and subsequent degradation of the IKB protein by the proteasome. It is involved in virtually all cellular processes by regulating protein function, localization and stability and by mediating protein-protein interactions.

Furthermore, aberrant protein phosphorylation is implicated in the onset and the progression of human diseases such as cancer and neurodegenerative disorders. Protein Oxidation and Aging. Aging is associated with the accumulation of inactive or less active, more heat-labile forms of numerous enzymes (25, 26).

The possibility that these age-related changes are due, at least in part, to oxidative modification is indicated by the facts. Protein Phosphorylation in Aging and Age-Related Disease. Product View Product Details.

Recent Advances in Psychology and Aging. Product Type: Book. Edition: 1. Volume: First Published Hardcover: eBook: View Product Details. Membrane Lipid Signaling in Aging and Age-Related Disease. Product Type. Interestingly, proteins are considered to be standing at the crossroads of cancer, aging, and age-related neurodegenerative diseases.

There are great possibilities to improve the above-mentioned diseases and conditions through intervention in the activity of the protein family. The bulk of the book focuses on specific sleep disorders associated with aging and age-related neurodegenerative disorders.

A comprehensive consideration of this topic is woven through a number of chapters that address both basic research and clinical aspects of sleep abnormalities during aging and in disease. The strength of the mechanisms involved in the control of health and lifespan determines the rate of aging in any organism.

Aging is fueled by the accumulation of damage in a multitude of tissues, causing many age-related diseases including cardio-vascular diseases, neuro-degenerating diseases, metabolic syndrome and cancer[].We know that a healthy life-style, good habits, exercise.

Protein phosphorylation is a reversible post-translational modification of proteins in which an amino acid residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group.

Phosphorylation alters the structural conformation of a protein, causing it to become activated, deactivated, or modifying its imately human proteins have sites that. Protein phosphorylation in aging and age-related disease. Amsterdam ; Boston: Elsevier, (DLC) (OCoLC) Material Type: Document, Internet resource: Document Type: Internet Resource, Computer File: All Authors / Contributors: Mark Paul Mattson.

INTRODUCTION. Alzheimer’s disease (AD) is defined in part by the appearance of neurofibrillary lesions in the neocortex and other brain regions (reviewed in []).The lesions accumulate aggregated forms of tau, a microtubule-associated protein that normally functions in human brain as an ensemble of six monomeric isoforms to stabilize microtubules and promote their assembly (reviewed in []).

Purchase Protein Phosphorylation in Health and Disease, Volume - 1st Edition. Print Book & E-Book. ISBN  Age-related α-synuclein phosphorylation. Phosphorylation at Ser has been reported to be the predominant modification of α-synuclein in Lewy bodies.

17 An antibody that specifically recognizes phospho-Ser α-synuclein 4 was used to determine whether neuronal cell bodies in the primate substantia nigra contain this modified form of the protein and whether α-synuclein phosphorylation. Phosphorylation does not prompt, nor prevent, the formation of alpha-synuclein toxic species in a rat model of Parkinson's disease.

Hum. Mol. Genet. 18, – /hmg/ddn ; Bahr B. A., Wisniewski M. L., Butler D. Positive lysosomal modulation as a unique strategy to treat age-related protein accumulation diseases.

Figure 1. Gene expression changes and master switch driving age related cognitive decline Brain aging accompanies alteration in expression (red circles represent downregulation; blue circles represent upregulation) of genes belonging to multiple pathways. Epigenetic modifications particularly decrease in DNMT1 and increase in HDAC2 level might be the master regulators and accordingly.

The focus of this book is on the role of protein metabolism and homeostasis in aging. An overview is provided of the current knowledge in the area, including protein synthesis, accuracy and repair, post-translational modifications, degradation and turnover, and how they define and influence aging.

Furthermore, nobiletin reduced tau phosphorylation in the hippocampus of SAMP8 mice. Together, the markedly beneficial effects of nobiletin represent a potentially useful treatment for ameliorating the learning and memory deficits, oxidative stress, and hyperphosphorylation of tau in aging as well as age-related neurodegenerative diseases such.

Substantial phosphorylation of IRS1 at specific Ser sites occurs in type 2 diabetes- or age-related memory deficits independently of amyloid-β (Aβ). Furthermore, we present the first evidence that, in APPKI NL-G-F mice showing Aβ42 elevation, the increased phosphorylation of IRS1 at multiple Ser sites occurs without memory impairment.We show that phosphorylation of the L-type channel Cav by cAMP-dependent protein kinase is increased >2-fold in the hippocampus of aged rats.

The hippocampus is critical for learning and is one of the first brain regions to be affected in Alzheimer's disease.The protein phosphorylation is strongly dependent on the Ca 2+-induced mitochondrial permeability transition pore (mPTP) opening.

2′,3′-Cyclic nucleotide-3′-phosphodiesterase (CNPase) was phosphorylated by protein kinases A and C. CNPase and melatonin (MEL) might interact with calmodulin.

The effects of the calmodulin antagonist.