palmitic acid

palmitic acid is a lipid of Fatty Acyls (FA) class. The involved functions are known as Apoptosis, Synthesis, inhibitors, Oxidation and targeting. Palmitic acid often locates in Extracellular, Muscle, Protoplasm, Body tissue and Blood. The related lipids are Palmitates, Sodium Palmitate and saturated fat.

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Introduction

To understand associated biological information of palmitic acid, we collected biological information of abnormalities, associated pathways, cellular/molecular locations, biological functions, related genes/proteins, lipids and common seen animal/experimental models with organized paragraphs from literatures.

What diseases are associated with palmitic acid?

There are no associated biomedical information in the current reference collection.

No disease MeSH terms mapped to the current reference collection.

PubChem Associated disorders and diseases

What pathways are associated with palmitic acid

There are no associated biomedical information in the current reference collection.

PubChem Biomolecular Interactions and Pathways

Link to PubChem Biomolecular Interactions and Pathways

What cellular locations are associated with palmitic acid?

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What functions are associated with palmitic acid?


Related references are published most in these journals:

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What lipids are associated with palmitic acid?

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What genes are associated with palmitic acid?

There are no associated biomedical information in the current reference collection.

What common seen animal models are associated with palmitic acid?

There are no associated biomedical information in the current reference collection.

NCBI Entrez Crosslinks

All references with palmitic acid

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Authors Title Published Journal PubMed Link
Whitt MA and Rose JK Fatty acid acylation is not required for membrane fusion activity or glycoprotein assembly into VSV virions. 1991 Virology pmid:1660205
Brassard DL et al. Influenza B virus NB glycoprotein is a component of the virion. 1996 Virology pmid:8661386
Baird NL et al. Myristylation and palmitylation of HSV-1 UL11 are not essential for its function. 2010 Virology pmid:19944438
MacDonald RC et al. Inhibition of sendai virus-induced hemolysis by long chain fatty acids. 1984 Virology pmid:6324464
Peränen J et al. The alphavirus replicase protein nsP1 is membrane-associated and has affinity to endocytic organelles. 1995 Virology pmid:7747433
Grosenbach DW et al. Identification and analysis of vaccinia virus palmitylproteins. 2000 Virology pmid:11017799
Hansen SG et al. Analysis of the site occupancy constraints of primary amino acid sequences in the motif directing palmitylation of the vaccinia virus 37-kDa envelope protein. 1999 Virology pmid:9927580
Petit CM et al. Palmitoylation of the cysteine-rich endodomain of the SARS-coronavirus spike glycoprotein is important for spike-mediated cell fusion. 2007 Virology pmid:17134730
Ponimaskin E and Schmidt MF Domain-structure of cytoplasmic border region is main determinant for palmitoylation of influenza virus hemagglutinin (H7). 1998 Virology pmid:9791024
Baird NL et al. Sequences in the UL11 tegument protein of herpes simplex virus that control association with detergent-resistant membranes. 2008 Virology pmid:18261757