N-Formylmethionine Leucyl-Phenylalanine
                             
                            
                            
                                
                            
                            
                                
                            
                            
                            
                                
                                    
                                            
	"N-Formylmethionine Leucyl-Phenylalanine" 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 formylated tripeptide originally isolated from bacterial filtrates that is positively chemotactic to polymorphonuclear leucocytes, and causes them to release lysosomal enzymes and become metabolically activated.
    
			
			
				
				
					
						| Descriptor ID | D009240 | 
					
						| MeSH Number(s) | D02.886.030.676.450.440 D12.125.072.050.685.445 D12.125.142.666.500 D12.125.166.676.450.440 D12.644.456.400 D23.125.685 | 
					
						| Concept/Terms | N-Formylmethionine Leucyl-PhenylalanineN-Formylmethionine Leucyl-PhenylalanineLeucyl-Phenylalanine, N-FormylmethionineN Formylmethionine Leucyl PhenylalanineFormylmethionyl-Leucyl-PhenylalanineFormylmethionyl Leucyl PhenylalanineN-Formyl-Methionyl-Leucyl-PhenylalanineN Formyl Methionyl Leucyl PhenylalanineFormylmet-Leu-PheFormylmet Leu PheFormylmethionylleucylphenylalanine
 Formylmethionyl PeptideFormylmethionyl PeptidePeptide, FormylmethionylN-Formylated PeptideN Formylated PeptidePeptide, N-Formylated
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				Below are MeSH descriptors whose meaning is more general than "N-Formylmethionine Leucyl-Phenylalanine".
				
			 
			
			
				Below are MeSH descriptors whose meaning is more specific than "N-Formylmethionine Leucyl-Phenylalanine".
				
			 
		 
	 
 
                                        
                                            
	
	
		
			
			
					
				This graph shows the total number of publications written about "N-Formylmethionine Leucyl-Phenylalanine" by people in this website by year, and whether "N-Formylmethionine Leucyl-Phenylalanine" was a major or minor topic of these publications. 
				
					 
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		            | Year | Major Topic | Minor Topic | Total | 
|---|
| 1999 | 0 | 1 | 1 | 
| 2000 | 0 | 2 | 2 | 
| 2001 | 1 | 1 | 2 | 
| 2007 | 0 | 2 | 2 | 
| 2009 | 0 | 1 | 1 | 
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				Below are the most recent publications written about "N-Formylmethionine Leucyl-Phenylalanine" by people in Profiles.
						
					
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								Counterregulation of clathrin-mediated endocytosis by the actin and microtubular cytoskeleton in human neutrophils. Am J Physiol Cell Physiol. 2009 Apr; 296(4):C857-67. 
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								Heat shock protein 27 regulates neutrophil chemotaxis and exocytosis through two independent mechanisms. J Immunol. 2007 Feb 15; 178(4):2421-8. 
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								The actin cytoskeleton regulates exocytosis of all neutrophil granule subsets. Am J Physiol Cell Physiol. 2007 May; 292(5):C1690-700. 
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								Hypertonic saline activation of p38 MAPK primes the PMN respiratory burst. Shock. 2001 Oct; 16(4):285-9. 
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								Blood transfusion and the two-insult model of post-injury multiple organ failure. Shock. 2001 Apr; 15(4):302-6. 
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								The lipid fraction of post-hemorrhagic shock mesenteric lymph (PHSML) inhibits neutrophil apoptosis and enhances cytotoxic potential. Shock. 2000 Sep; 14(3):404-8. 
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								Hypertonic saline inhibits neutrophil (PMN) priming via attenuation of p38 MAPK signaling. Shock. 2000 Sep; 14(3):265-9; discussion 269-70. 
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								Posthemorrhagic shock mesenteric lymph primes circulating neutrophils and provokes lung injury. J Surg Res. 1999 May 15; 83(2):83-8. 
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								Determination of the rate of superoxide generation from biological systems by spin trapping: use of rapid oxygen depletion to measure the decay rate of spin adducts. Free Radic Biol Med. 1994 Sep; 17(3):215-23. 
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								Dynamic state of beta 2 integrin phosphorylation: regulation of neutrophil aggregation involves a phosphatase-dependent pathway. Clin Immunol Immunopathol. 1994 May; 71(2):216-22.