khellin

Khellin is a lipid of Polyketides (PK) class. The involved functions are known as Diastasis and Selection, Genetic.

Cross Reference

Introduction

To understand associated biological information of khellin, 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 khellin?

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

Possible diseases from mapped MeSH terms on references

We collected disease MeSH terms mapped to the references associated with khellin

MeSH term MeSH ID Detail
Mycobacterium Infections D009164 7 associated lipids
Total 1

PubChem Associated disorders and diseases

What pathways are associated with khellin

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 khellin?

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

What functions are associated with khellin?


Related references are published most in these journals:

Function Cross reference Weighted score Related literatures

What lipids are associated with khellin?

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

What genes are associated with khellin?

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

What common seen animal models are associated with khellin?

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

NCBI Entrez Crosslinks

All references with khellin

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Authors Title Published Journal PubMed Link
Janssen S et al. Exploring prospects of novel drugs for tuberculosis. 2012 Drug Des Devel Ther pmid:22973091
Normoyle KP and Brieher WM Cyclase-associated protein (CAP) acts directly on F-actin to accelerate cofilin-mediated actin severing across the range of physiological pH. 2012 J. Biol. Chem. pmid:22904322
Koo MS et al. Strain specific transcriptional response in Mycobacterium tuberculosis infected macrophages. 2012 Cell Commun. Signal pmid:22280836
Günther J et al. Lipopolysaccharide priming enhances expression of effectors of immune defence while decreasing expression of pro-inflammatory cytokines in mammary epithelia cells from cows. 2012 BMC Genomics pmid:22235868
Morley SC The actin-bundling protein L-plastin: a critical regulator of immune cell function. 2012 Int J Cell Biol pmid:22194750
Lapalikar GV et al. F420H2-dependent degradation of aflatoxin and other furanocoumarins is widespread throughout the actinomycetales. 2012 PLoS ONE pmid:22383957
Kilicaslan I and Coskun S Spontaneous stone passage: is it Ammi visnaga effect? 2012 Urol. Res. pmid:22990409
Haug KG et al. Pharmacokinetic evaluation of visnagin and Ammi visnaga aqueous extract after oral administration in rats. 2012 Planta Med. pmid:23096256
Hölttä-Vuori M et al. Endosomal actin remodeling by coronin-1A controls lipoprotein uptake and degradation in macrophages. 2012 Circ. Res. pmid:22223354
Seto S et al. Coronin-1a inhibits autophagosome formation around Mycobacterium tuberculosis-containing phagosomes and assists mycobacterial survival in macrophages. 2012 Cell. Microbiol. pmid:22256790