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Libros sobre el tema "Ubiquitin protease"

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Publicado: 4 de mayo de 2024

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1

P, Zwickl y Baumeister W. 1946-, eds. The Proteasome-ubiquitin protein degradation pathway. Berlin: Springer, 2002.

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2

Patterson, Cam y Douglas M. Cyr. Ubiquitin-Proteasome Protocols. New Jersey: Humana Press, 2005. http://dx.doi.org/10.1385/1592598951.

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3

Cam, Patterson y Cyr Douglas M, eds. Ubiquitin-proteasome protocols. Totowa, N.J: Humana Press, 2005.

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4

Mayor, Thibault y Gary Kleiger, eds. The Ubiquitin Proteasome System. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8706-1.

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5

Zwickl, Peter y Wolfgang Baumeister, eds. The Proteasome — Ubiquitin Protein Degradation Pathway. Berlin, Heidelberg: Springer Berlin Heidelberg, 2002. http://dx.doi.org/10.1007/978-3-642-59414-4.

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6

Dohmen, R. Jürgen y Martin Scheffner, eds. Ubiquitin Family Modifiers and the Proteasome. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-474-2.

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7

J, Ciechanover Aaron y Masucci Maria G, eds. The ubiquitin-proteasome proteolytic system: From classical biochemistry to human diseases. Singapore: World Scientific, 2002.

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8

name, No. The ubiquitin-proteasome proteolytic system: From classical biochemistry to human diseases. Singapore: World Scientific, 2002.

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9

Di, Napoli Mario y Wójcik Cezary 1968-, eds. The ubiquitin proteasome system in the central nervous system: From physiology to pathology : 2008 update. Hauppauge, NY: Nova Science, 2009.

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10

(Editor), Peter Zwickl y Wolfgang Baumeister (Editor), eds. The Proteasome-Ubiquitin Protein Degradation Pathway. Springer, 2002.

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11

Zhan, Xianquan, ed. Ubiquitin - Proteasome Pathway. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.87547.

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12

Patterson, Cam y Douglas M. Cyr. Ubiquitin-Proteasome Protocols. Humana Press, 2010.

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13

Ubiquitin-proteasome protocols. Totowa, NJ: Humana Press, 2004.

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14

Rechsteiner, Martin, Aaron J. Ciechanover y R. John Mayer. Ubiquitin-Proteasome System. Wiley & Sons, Incorporated, John, 2008.

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15

Rechsteiner, Martin, Aaron J. Ciechanover y R. John Mayer. Ubiquitin-Proteasome System. Wiley & Sons, Limited, John, 2008.

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16

Ciechanover, Aaron J. y Maria G. Masucci. The Ubiquitin-Proteasome Proteolytic System. WORLD SCIENTIFIC, 2002. http://dx.doi.org/10.1142/5051.

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17

Rechsteiner, Martin, Aaron J. Ciechanover y R. John Mayer. Ubiquitin-Proteasome System and Disease. Wiley & Sons, Incorporated, John, 2008.

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18

Baumeister, Wolfgang y Peter Zwickl. Proteasome -- Ubiquitin Protein Degradation Pathway. Springer London, Limited, 2012.

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19

Mayor, Thibault y Gary Kleiger. Ubiquitin Proteasome System: Methods and Protocols. Springer New York, 2019.

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20

Zwickl, Peter. The Proteasome - Ubiquitin Protein Degradation Pathway. Brand: Springer, 2011.

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21

Stefanis, Leonidas y J. N. Keller. Proteasome in Neurodegeneration. Springer London, Limited, 2007.

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22

Mayer, J. y R. Layfield. The Ubiquitin-proteasome System (Essays in Biochemistry). Portland Pr, 2005.

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23

(Editor), Cam Patterson y Douglas M. Cyr (Editor), eds. Ubiquitin-Proteasome Protocols (Methods in Molecular Biology). Humana Press, 2005.

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24

Rechsteiner, Martin, Aaron J. Ciechanover y R. John Mayer. Cell Biology of the Ubiquitin-Proteasome System. Wiley & Sons, Incorporated, John, 2008.

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25

The Ubiquitin Proteasome System: Methods and Protocols. Humana, 2018.

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26

(Editor), Leonidas Stefanis y J. N. Keller (Editor), eds. The Proteasome in Neurodegeneration. Springer, 2006.

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27

(Editor), R. John Mayer, Aaron J. Ciechanover (Editor) y Martin Rechsteiner (Editor), eds. Protein Degradation: The Ubiquitin-Proteasome System (Protein Degradation). Wiley-VCH, 2006.

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28

Cheng, Jinke y Tasneem Bawa-Khalfe. Methods for Reversing Protein Modification: Ubiquitin and SUMO-Specific Proteases. Taylor & Francis Group, 2021.

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29

Scheffner, Martin y R. Jürgen Dohmen. Ubiquitin Family Modifiers and the Proteasome: Reviews and Protocols. Humana Press, 2016.

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30

Ubiquitin Family Modifiers And The Proteasome Reviews And Protocols. Humana Press, 2012.

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31

Gomes, Aldrin V. Ubiquitin Proteasome System: A Review and Directions for Research. Nova Science Publishers, Incorporated, 2018.

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32

Rechsteiner, Martin, Aaron J. Ciechanover y R. John Mayer. Cell Biology of the Ubiquitin-Proteasome System Vol. 3. Wiley & Sons, Limited, John, 2007.

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33

Noncatalytic effect of the ubiquitin ligase Hul5 on proteasome function. 2009.

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34

(Editor), R. John Mayer, Aaron J. Ciechanover (Editor) y Martin Rechsteiner (Editor), eds. Protein Degradation: Cell Biology of the Ubiquitin-Proteasome System (Protein Degradation). Wiley-VCH, 2006.

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35

Ang, Xiaolu Lulu Lim. Substrates of the SCF-beta-TRCP E3 ubiquitin ligase complex: Mechanisms of recognition and delivery to the proteasome. 2009.

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36

(Editor), Aaron J. Ciechanover y Maria G. Masucci (Editor), eds. The Ubiquitin-Proteasome Proteolytic System: From Classical Biochemistry to Human Diseases. World Scientific Publishing, 2003.

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37

Summers, Matthew, ed. Ubiquitin Proteasome System - Current Insights into Mechanism Cellular Regulation and Disease. IntechOpen, 2019. http://dx.doi.org/10.5772/intechopen.78430.

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38

(Editor), R. John Mayer, Aaron J. Ciechanover (Editor) y Martin Rechsteiner (Editor), eds. Protein Degradation: Vol. 4: The Ubiquitin-Proteasome System and Disease (Protein Degradation). Wiley-VCH, 2007.

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39

(Editor), Mario Di Napoli y Cezary Wojcik (Editor), eds. The Ubiquitin Proteasome System in the Central Nervous System: From Physiology to Pathology. Nova Science Pub Inc, 2008.

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40

Sharifnia, Tanaz. The ubiquitin-proteasome system: Roles in tumor suppressor destabilization and prospects for targeted therapies. 2005.

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41

Koerner, Tobias. Einfluss einer Hyperglykämie auf die Expression von Proteinen des Ubiquitin-Proteasom-Systems im Skelett- und Herzmuskel. 2011.

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42

Wilson, Van G. Sumoylation: Molecular Biology and Biochemistry (Horizonbioscience). Taylor & Francis, 2004.

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43

Renton, Alan E. y Alison M. Goate. Genetics of Dementia. Editado por Dennis S. Charney, Eric J. Nestler, Pamela Sklar y Joseph D. Buxbaum. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780190681425.003.0051.

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Resumen
The genetic architecture of dementia is polygenic and complex, with risk alleles spanning frequency–effect size space. Despite significant progress, most genes influencing these disorders await discovery. Known risk loci implicate perturbed pathways that coalesce around recurring mechanistic themes, notably the autophagosome-lysosome system, the cytoskeleton, endocytosis, innate immunity, lipid metabolism, mitochondria, and the ubiquitin-proteasome system. Phenotypic and pathophysiological pleiotropy suggests some conditions form continuous clinicopathogenetic disease spectra blurring classical diagnoses. Future large-scale genome sequencing of global populations will significantly elucidate etiopathogenesis and is likely to reframe nosology. Furthermore integrative prospective cohort studies have the potential to revolutionize our understanding of dementia.
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44

Nakamura, Tomohiro y 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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45

(Editor), R. J. Mayer, I. R. Brown (Editor) y Peter Jenner (Series Editor), eds. Heat Shock Proteins in the Nervous System (Neuroscience Perspectives). Academic Press, 1994.

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46

(Editor), R. J. Mayer, I. R. Brown (Editor) y Peter Jenner (Series Editor), eds. Heat Shock Proteins in the Nervous System (Neuroscience Perspectives). Academic Press, 1994.

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