| MeSH term | MeSH ID | Detail |
|---|---|---|
| Lung Neoplasms | D008175 | 171 associated lipids |
| Body Weight | D001835 | 333 associated lipids |
18194-24-6
18194-24-6 is a lipid of Glycerophospholipids (GP) class. 18194-24-6 is associated with abnormalities such as Cerebrovascular accident, Renal tubular disorder, Atherosclerosis, Hyperlipoproteinemia Type III and Lipid Metabolism Disorders. The involved functions are known as Process, protein folding, Catalyst, Biochemical Pathway and Fold in Medical Device Material. 18194-24-6 often locates in Tissue membrane, Membrane, periplasm, vesicle membrane and outer membrane. The associated genes with 18194-24-6 are Integral Membrane Proteins, Protein Structure, RTN4 gene, RTN4R gene and Protein, Organized by Structure. The related lipids are Micelles, dimyristoylphosphatidylglycerol, 1,2-dihexadecyl-sn-glycero-3-phosphocholine, Unilamellar Vesicles and cholesteryl oleate. The related experimental models are Mouse Model, Arthritis, Adjuvant-Induced, Disease model and Xenograft Model.
Cross Reference
Introduction
To understand associated biological information of 18194-24-6, 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 18194-24-6?
18194-24-6 is suspected in Atherosclerosis, Cardiovascular Diseases, Dehydration, Abnormal shape, Renal tubular disorder, Hyperlipoproteinemia Type III and other diseases in descending order of the highest number of associated sentences.
Related references are mostly published in these journals:
| Disease | Cross reference | Weighted score | Related literature |
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Possible diseases from mapped MeSH terms on references
We collected disease MeSH terms mapped to the references associated with 18194-24-6
PubChem Associated disorders and diseases
What pathways are associated with 18194-24-6
There are no associated biomedical information in the current reference collection.
PubChem Biomolecular Interactions and Pathways
Link to PubChem Biomolecular Interactions and PathwaysWhat cellular locations are associated with 18194-24-6?
Visualization in cellular structure
Associated locations are in red color. Not associated locations are in black.
Related references are published most in these journals:
| Location | Cross reference | Weighted score | Related literatures |
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What functions are associated with 18194-24-6?
Related references are published most in these journals:
| Function | Cross reference | Weighted score | Related literatures |
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What lipids are associated with 18194-24-6?
Related references are published most in these journals:
| Lipid concept | Cross reference | Weighted score | Related literatures |
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What genes are associated with 18194-24-6?
Related references are published most in these journals:
| Gene | Cross reference | Weighted score | Related literatures |
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What common seen animal models are associated with 18194-24-6?
Mouse Model
Mouse Model are used in the study 'Association of a model class A (apolipoprotein) amphipathic alpha helical peptide with lipid: high resolution NMR studies of peptide.lipid discoidal complexes.' (Mishra VK et al., 2006).
Arthritis, Adjuvant-Induced
Arthritis, Adjuvant-Induced are used in the study 'T cell antigen receptor peptide-lipid membrane interactions using surface plasmon resonance.' (Bender V et al., 2004).
Disease model
Disease model are used in the study 'Kupffer cells do not play a role in governing the efficacy of liposomal mitoxantrone used to treat a tumor model designed to assess drug delivery to liver.' (Lim HJ et al., 2000).
Related references are published most in these journals:
| Model | Cross reference | Weighted score | Related literatures |
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NCBI Entrez Crosslinks
All references with 18194-24-6
Download all related citations| Authors | Title | Published | Journal | PubMed Link |
|---|---|---|---|---|
| Odinokov A and Ostroumov D | Structural Degradation and Swelling of Lipid Bilayer under the Action of Benzene. | 2015 | J Phys Chem B | pmid:26555804 |
| Xia Y et al. | Effects of Nanoparticle Morphology and Acyl Chain Length on Spontaneous Lipid Transfer Rates. | 2015 | Langmuir | pmid:26540211 |
| Lee TY et al. | Tuning the Photocycle Kinetics of Bacteriorhodopsin in Lipid Nanodiscs. | 2015 | Biophys. J. | pmid:26536266 |
| Madrid E and Horswell SL | Effect of Deuteration on Phase Behavior of Supported Phospholipid Bilayers: A Spectroelectrochemical Study. | 2015 | Langmuir | pmid:26536482 |
| Tanaka M et al. | Preparation and Characterization of Reconstituted Lipid-Synthetic Polymer Discoidal Particles. | 2015 | Langmuir | pmid:26531224 |
| Zhang H et al. | Structural determination of virus protein U from HIV-1 by NMR in membrane environments. | 2015 | Biochim. Biophys. Acta | pmid:26362058 |
| Björnerås J et al. | Analysing DHPC/DMPC bicelles by diffusion NMR and multivariate decomposition. | 2015 | Biochim. Biophys. Acta | pmid:26341141 |
| Akabori K and Nagle JF | Structure of the DMPC lipid bilayer ripple phase. | 2015 | Soft Matter | pmid:25503248 |
| Bodor A et al. | Membrane interactions in small fast-tumbling bicelles as studied by 31P NMR. | 2015 | Biochim. Biophys. Acta | pmid:25497765 |
| Joshi T et al. | Real-time examination of aminoglycoside activity towards bacterial mimetic membranes using Quartz Crystal Microbalance with Dissipation monitoring (QCM-D). | 2015 | Biochim. Biophys. Acta | pmid:25450807 |
| Sarpietro MG et al. | Interaction of α-Hexylcinnamaldehyde with a Biomembrane Model: A Possible MDR Reversal Mechanism. | 2015 | J. Nat. Prod. | pmid:25893313 |
| Drazenovic J et al. | Effect of lamellarity and size on calorimetric phase transitions in single component phosphatidylcholine vesicles. | 2015 | Biochim. Biophys. Acta | pmid:25445167 |
| Å egota S et al. | Ligand-Dependent Nanoparticle Clustering within Lipid Membranes Induced by Surrounding Medium. | 2015 | J Phys Chem B | pmid:25831116 |
| Ding Y et al. | Influence of the lipid membrane environment on structure and activity of the outer membrane protein Ail from Yersinia pestis. | 2015 | Biochim. Biophys. Acta | pmid:25433311 |
| Victor BL et al. | Self-assembly molecular dynamics simulations shed light into the interaction of the influenza fusion Peptide with a membrane bilayer. | 2015 | J Chem Inf Model | pmid:25826469 |
| Smrt ST et al. | The influenza hemagglutinin fusion domain is an amphipathic helical hairpin that functions by inducing membrane curvature. | 2015 | J. Biol. Chem. | pmid:25398882 |
| Losada-Pérez P et al. | Effect of cholesterol on the phase behavior of solid-supported lipid vesicle layers. | 2015 | J Phys Chem B | pmid:25812723 |
| Vad BS et al. | Phospholipid Ether Linkages Significantly Modulate the Membrane Affinity of the Antimicrobial Peptide Novicidin. | 2015 | J. Membr. Biol. | pmid:25801603 |
| Matsumoto Y et al. | Therapeutic effects of hybrid liposomes without drugs for rheumatoid arthritis. | 2015 | Drug Deliv | pmid:24344811 |
| Madej BD et al. | A Parameterization of Cholesterol for Mixed Lipid Bilayer Simulation within the Amber Lipid14 Force Field. | 2015 | J Phys Chem B | pmid:26359797 |