JNK Mitogen-Activated Protein Kinases
                             
                            
                            
                                
                            
                            
                                
                            
                            
                            
                                
                                    
                                            
	"JNK Mitogen-Activated Protein Kinases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, 
	MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure, 
	which enables searching at various levels of specificity.
	
	
		
			
			
				A subgroup of mitogen-activated protein kinases that activate TRANSCRIPTION FACTOR AP-1 via the phosphorylation of C-JUN PROTEINS. They are components of intracellular signaling pathways that regulate CELL PROLIFERATION; APOPTOSIS; and CELL DIFFERENTIATION.
    
			
			
				
				
					
						| Descriptor ID | D048031 | 
					
						| MeSH Number(s) | D08.811.913.696.620.682.700.567.374 D12.644.360.450.340 D12.776.476.450.340 | 
					
						| Concept/Terms | JNK Mitogen-Activated Protein KinasesJNK Mitogen-Activated Protein KinasesJNK Mitogen Activated Protein Kinasesjun-NH2-Terminal Kinasejun NH2 Terminal Kinasejun-NH2-Terminal Kinasesjun NH2 Terminal Kinasesc-jun Amino-Terminal KinaseAmino-Terminal Kinase, c-junc jun Amino Terminal Kinasec-jun N-Terminal KinaseN-Terminal Kinase, c-junc jun N Terminal Kinase
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				Below are MeSH descriptors whose meaning is more general than "JNK Mitogen-Activated Protein Kinases".
				
			 
			
			
				Below are MeSH descriptors whose meaning is more specific than "JNK Mitogen-Activated Protein Kinases".
				
			 
		 
	 
 
                                        
                                            
	
	
		
			
			
					
				This graph shows the total number of publications written about "JNK Mitogen-Activated Protein Kinases" by people in this website by year, and whether "JNK Mitogen-Activated Protein Kinases" was a major or minor topic of these publications. 
				
					 
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		            | Year | Major Topic | Minor Topic | Total | 
|---|
| 1996 | 1 | 0 | 1 | 
| 1997 | 1 | 0 | 1 | 
| 1998 | 0 | 2 | 2 | 
| 1999 | 0 | 2 | 2 | 
| 2001 | 0 | 1 | 1 | 
| 2003 | 0 | 1 | 1 | 
| 2005 | 1 | 2 | 3 | 
| 2007 | 0 | 1 | 1 | 
| 2008 | 0 | 1 | 1 | 
| 2009 | 0 | 2 | 2 | 
| 2011 | 1 | 0 | 1 | 
| 2012 | 1 | 0 | 1 | 
| 2013 | 1 | 1 | 2 | 
| 2017 | 0 | 1 | 1 | 
| 2019 | 0 | 1 | 1 | 
| 2020 | 1 | 0 | 1 | 
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				Below are the most recent publications written about "JNK Mitogen-Activated Protein Kinases" by people in Profiles.
						
					
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								JNK signaling contributes to skeletal muscle wasting and protein turnover in pancreatic cancer cachexia. Cancer Lett. 2020 10 28; 491:70-77. 
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								ZIP4 Increases Expression of Transcription Factor ZEB1 to Promote Integrin a3ß1 Signaling and Inhibit Expression of the Gemcitabine Transporter ENT1 in Pancreatic Cancer Cells. Gastroenterology. 2020 02; 158(3):679-692.e1. 
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								Serum retinol-binding protein-induced endothelial inflammation is mediated through the activation of toll-like receptor 4. Mol Vis. 2017; 23:185-197. 
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								Acceleration of biliary cholesterol secretion restores glycemic control and alleviates hypertriglyceridemia in obese db/db mice. Arterioscler Thromb Vasc Biol. 2014 Jan; 34(1):26-33. 
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								Emerging role of JNK in insulin resistance. Curr Diabetes Rev. 2013 Sep; 9(5):422-8. 
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								Ormeloxifene inhibits osteoclast differentiation in parallel to downregulating RANKL-induced ROS generation and suppressing the activation of ERK and JNK in murine RAW264.7 cells. J Mol Endocrinol. 2012 Jun; 48(3):261-70. 
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								Partial deletion of argininosuccinate synthase protects from pyrazole plus lipopolysaccharide-induced liver injury by decreasing nitrosative stress. Am J Physiol Gastrointest Liver Physiol. 2012 Feb 01; 302(3):G287-95. 
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								Phosphorylated c-Jun and Fra-1 induce matrix metalloproteinase-1 and thereby regulate invasion activity of 143B osteosarcoma cells. Biochim Biophys Acta. 2011 Aug; 1813(8):1543-53. 
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								Regulation of neurite outgrowth by interactions between the scaffolding protein, JNK-associated leucine zipper protein, and neuronal growth-associated protein superior cervical ganglia clone 10. J Biol Chem. 2010 Feb 05; 285(6):3548-3553. 
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								Fenofibrate and PBA prevent fatty acid-induced loss of adiponectin receptor and pAMPK in human hepatoma cells and in hepatitis C virus-induced steatosis. J Lipid Res. 2009 Nov; 50(11):2193-202.