Books on the topic 'Stress activated protein kinase'

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1

Posas, Francesc, and Angel R. Nebreda, eds. Stress-Activated Protein Kinases. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/978-3-540-75569-2.

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2

Francesc, Posas, and Nebreda Angel R, eds. Stress-activated protein kinases. New York: Springer, 2008.

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3

Dai, Tianang. Characterization of a novel stress-activated protein kinase pathway. Ottawa: National Library of Canada, 1996.

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4

Chang, Malcolm Elliott. Role of the stress activated protein kinases (sapk's) in mediating resistance to the antineoplastic agent adriamycin (ADR). Ottawa: National Library of Canada, 1998.

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5

Cordero, Mario D., and Benoit Viollet, eds. AMP-activated Protein Kinase. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-43589-3.

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6

Randall, Susan. Interactions among the mitogen-activated protein kinase cascades and the identification of a novel cdc2-related protein kinase. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1999.

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7

Ho, Jenny Mei-Yen. The activation of mitogen-activated protein kinase pathways by the TEL-JAK2 oncoprotein. Ottawa: National Library of Canada, 2000.

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8

Glogowski, Emily Anne Cherry. Effect of high glucose on endothelin-1 and platelet-derived growth factor stimulation of mesangial cell protein kinase C and mitogen-activated protein kinase. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1999.

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9

MAP kinase signaling protocols. 2nd ed. New York, N.Y: Humana Press, 2010.

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10

Asefaw, Senai. Stimulation of myocardial AMP-activated protein kinase by AICAR increases cardiac glucose uptake and causes GLUT4 and GLUT1 translocation in vivo. [New Haven, Conn: s.n.], 1999.

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11

Francesc Posas,Angel R. Nebreda. Stress-Activated Protein Kinases. Springer, 2008.

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12

Posas, Francesc, and Angel R. Nebreda. Stress-Activated Protein Kinases. Springer London, Limited, 2008.

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13

Posas, Francesc, and Angel R. Nebreda. Stress-Activated Protein Kinases. Springer, 2010.

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14

Cordero, Mario D., and Benoit Viollet. AMP-activated Protein Kinase. Springer, 2016.

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15

Cordero, Mario D., and Benoit Viollet. AMP-Activated Protein Kinase. Springer, 2016.

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16

Cordero, Mario D., and Benoit Viollet. AMP-activated Protein Kinase. Springer, 2018.

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17

AMP-Activated Protein Kinase Signalling. MDPI, 2019. http://dx.doi.org/10.3390/books978-3-03897-663-9.

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18

Chong, Karen Lynn. Characterization of the human, interferon inducible, dsRNA-activated protein kinase (p68 kinase). 1993.

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19

Ing, Y. Lynn. MLK-3: Identification and characterization of a protein kinase involved in mitogen-activated protein kinase signal transduction pathways. 1998.

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20

MAP Kinase Signaling Protocols. Humana Press, 2004.

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21

Böhm, Christina. Mitogen-activated protein kinases function in arthritis: ˜Dieœ Funktion von Mitogen-aktivierten Proteinkinasen in der Arthritis. 2011.

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22

Targonsky, Elisha. Pharmacological and hormonal regulation of AMP-activated protein kinase in the pancreatic [beta]-cell. 2005.

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23

Arthur, J. Simon C. MSKs. Taylor & Francis Group, 2013.

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24

Seger, Rony. MAP Kinase Signaling Protocols. Humana Press, 2016.

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25

NKIAMRE: A novel conserved cdc2-related kinase with features of both mitogen-activated protein kinases and cyclin-dependent kinases. Ottawa: National Library of Canada, 2002.

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26

Holappa, Lynn D. Identification and expression of a wheat protein kinase gene regulated by abscisic acid and by environmental stress. 1994.

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27

Schmidt, Ulrike. Secondary Messenger Systems in PTSD. Edited by Israel Liberzon and Kerry J. Ressler. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190215422.003.0014.

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Abstract:
Second messengers such as cyclic adenosine monophosphate (cAMP), cyclic guanosine monophosphate (cGMP), inositoltriphosphate, and diacylglycerol (DAG) are a prerequisite for the signal transduction of extracellular receptors. The latter are central for cellular function and thus are implicated in the pathobiology of a variety of disorders, such as schizophrenia, bipolar disorder, major depression, and post-traumatic stress disorder (PTSD). This chapter focuses on the involvement of second messenger molecules and their regulators as direct targets in human and animal PTSD and aims to stimulate the underdeveloped research in this field. The synthesis of literature reveals that second messengers clearly play a central role in PTSD-associated brain regions and processes. In particular, pituitary adenylate cyclase-activating polypeptide (PACAP), an important regulator of intracellular cAMP levels, as well as protein kinase c, the major target of DAG, belong to the hitherto most promising PTSD candidate molecules directly involved in second messenger signaling.
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28

Zilliox, Lindsay, and James W. Russell. Diabetic and Prediabetic Neuropathy. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780199937837.003.0115.

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Impaired glucose regulation (IGR) constitutes a spectrum of impaired glucose and metabolic regulation that can result in neuropathy. Several different pathways of injury in the diabetic peripheral nervous system that include metabolic dysregulation induced by metabolic syndrome induce oxidative stress, failure of nitric oxide regulation, and dysfunction of certain key signaling pathways. Oxidative stress can directly injure both dorsal route ganglion neurons and axons. Modulation of the nitric oxide system may have detrimental effects on endothelial function and neuronal survival. Reactive oxidative species can alter mitochondrial function, protein and DNA structure, interfere with signaling pathways, and deplete antioxidant defenses. Advanced glycelation end (AGE) products and formation of ROS are activated by and in turn regulate key signal transduction pathways.
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