Books on the topic 'Cysteine protease'

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1

Cystatins: Protease inhibitors, biomarkers, and immunomodulators. New York: Nova Science, 2011.

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2

Massimi, Isabella. SspB cysteine protease of Staphylococcus aureus promotes detachment of human keratinocytes and degrades fibronectin and vitronectin. Ottawa: National Library of Canada, 2001.

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3

Kirschke, Heidrun. Lysosomal cysteine proteases. 2nd ed. Oxford: Oxford University Press, 1997.

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4

Quigley, Kim. The use of deuterium kinetic solvent isotope effects and the proton inventory method in the elucidation of the catalyticmechanism of the cysteine protease papain. Birmingham: University of Birmingham, 1987.

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5

Robinson, Mark W., and John P. Dalton, eds. Cysteine Proteases of Pathogenic Organisms. Boston, MA: Springer US, 2011. http://dx.doi.org/10.1007/978-1-4419-8414-2.

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6

Cysteine proteases of pathogenic organisms. New York: Springer Science+Business Media, 2011.

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7

Philippe, Taupin, ed. The cystatin superfamily of proteinase inhibitors. New York: Nova Science Publishers, 2007.

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8

Turk, Boris. Papain-like cysteine proteinases: Regulation by proteinase inhibitors and pH. Uppsala: SverigesLantbruksuniversitet, 1996.

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9

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

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10

Estrada, Sergio. Cystatin A, a mammalian cysteine proteinase inhibitor: Mechanism of inhibition of target proteinases by recombinant cystatin A variants. Uppsala: Sveriges Lantbruksuniversitet, 1998.

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11

F, Shaughnessy Michael, Veenman Marcel, and Kennedy Cynthia Kleyn, eds. Meta-cognition: A recent review of research, theory, and perspectives. New York: Nova Science Publishers, Inc., 2008.

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12

F, Shaughnessy Michael, Veenman Marcel, and Kennedy Cynthia Kleyn, eds. Meta-cognition: A recent review of research, theory, and perspectives. New York: Nova Science Publishers, Inc., 2008.

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13

F, Shaughnessy Michael, Veenman Marcel, and Kennedy Cynthia Kleyn, eds. Meta-cognition: A recent review of research, theory, and perspectives. New York: Nova Science Publishers, Inc., 2007.

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14

Tonge, Peter James. A study of the structure and mechanism of the cysteine proteinase papain using vibrational spectroscopy. Birmingham: University of Birmingham, 1986.

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15

Caspases, paracaspases, and metacaspases: Methods and protocols. New York: Humana, 2014.

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16

Vito, Turk, and International Symposium on Cysteine Proteinases and Their Inhibitors (1st : 1985 : Portorož, Slovenia), eds. Cysteine proteinases and their inhibitors: Proceedings of the international symposium, Portorož, Yugoslavia, September 15-18, 1985. Berlin: De Gruyter, 1986.

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17

Turk, Vito. Cysteine Proteinases and their Inhibitors: Proceedings of the International Symposium Portoroz, Yugoslavia, September 15-18 1985. De Gruyter, Inc., 2019.

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18

Immunization with Porphyromonas Gingivalis Cysteine Protease: Effects on Experimental Gingivitis and Ligature-Induced Periodontitis in Macaca Fascicularis. Storming Media, 1997.

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19

Zerovnik, Eva. Human Stefins And Cystatins. Nova Biomedical Books, 2006.

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20

Dalton, John P., and Mark W. Robinson. Cysteine Proteases of Pathogenic Organisms. Springer, 2011.

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21

Dalton, John P., and Mark W. Robinson. Cysteine Proteases of Pathogenic Organisms. Springer, 2016.

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22

Rawlings, Neil D., Heidrun Kirschke, and A. J. Barrett. Lysosomal Cysteine Proteases. Protein Profile Series. Oxford University Press, 1998.

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23

Barrett, Alan J., Neil D. Rawlings, and Heidrun Kirschke. Lysosomal Cysteine Proteinases. Oxford University Press, USA, 1998.

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24

Akpinar, Ozlem. Characterization of recombinant proteinase inhibitors in surimi application. 1998.

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25

Merrick, Joav. Cysteine: Biosynthesis, Chemical Structure and Toxicity. Nova Science Publishers, Incorporated, 2012.

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26

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

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27

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

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28

MISRA, RAHUL, RUCHI SUNDRIYAL, and SURYA PRAKASH DWIVEDI. CYSTEINE PROTEINASE PROTEIN OF TRICHOMONAS VAGINALIS: In-silico Homology Modeling and Docking study. LAP Lambert Academic Publishing, 2010.

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29

(Editor), Michael F. Shaughnessy, Marcel V. e. Vennemann (Editor), and Cynthia Kleyn Kennedy (Editor), eds. Meta-Cognition: A Recent Review of Research, Theory, and Perspectives. Nova Science Publishers Inc, 2008.

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30

Barrett, Alan J., John N. Abelson, and Melvin I. Simon. Proteolytic Enzymes: Serine and Cysteine Peptidases. Elsevier Science & Technology Books, 1994.

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31

Turk, Vito. Cysteine Proteinases and Their Inhibitors Proceedings of the International Symposium Portoroz, Yugoslavia, September 15-18, 1985. Walter De Gruyter Inc, 1986.

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32

Proteolytic Enzymes: Serine and Cysteine Peptidases, Volume 244 (Methods in Enzymology). Academic Press, 1994.

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33

Barrett, Alan J., John N. Abelson, and Melvin I. Simon. Proteolytic Enzymes: Aspartic and Metallo Peptidases. Elsevier Science & Technology Books, 1995.

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34

(Editor), John N. Abelson, Melvin I. Simon (Editor), and Alan J. Barrett (Editor), eds. Proteolytic Enzymes: Serine and Cysteine Peptidases, Volume 244 (Methods in Enzymology). Academic Press, 1994.

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35

Linton, Steven D., and Tom O'Brien. Design of Caspase Inhibitors As Potential Clinical Agents. Taylor & Francis Group, 2008.

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36

Linton, Steven D., and Tom O'Brien. Design of Caspase Inhibitors As Potential Clinical Agents. Taylor & Francis Group, 2008.

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37

Linton, Steven D., and Tom O'Brien. Design of Caspase Inhibitors As Potential Clinical Agents. Taylor & Francis Group, 2019.

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38

Design of Caspase Inhibitors as Potential Clinical Agents (Enzyme Inhibitors). CRC, 2008.

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39

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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Abstract:
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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