| D008077 |
Lipoproteins, LDL |
A class of lipoproteins of small size (18-25 nm) and light (1.019-1.063 g/ml) particles with a core composed mainly of CHOLESTEROL ESTERS and smaller amounts of TRIGLYCERIDES. The surface monolayer consists mostly of PHOSPHOLIPIDS, a single copy of APOLIPOPROTEIN B-100, and free cholesterol molecules. The main LDL function is to transport cholesterol and cholesterol esters to extrahepatic tissues. |
Low-Density Lipoprotein,Low-Density Lipoproteins,beta-Lipoprotein,beta-Lipoproteins,LDL(1),LDL(2),LDL-1,LDL-2,LDL1,LDL2,Low-Density Lipoprotein 1,Low-Density Lipoprotein 2,LDL Lipoproteins,Lipoprotein, Low-Density,Lipoproteins, Low-Density,Low Density Lipoprotein,Low Density Lipoprotein 1,Low Density Lipoprotein 2,Low Density Lipoproteins,beta Lipoprotein,beta Lipoproteins |
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| D011485 |
Protein Binding |
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. |
Plasma Protein Binding Capacity,Binding, Protein |
|
| D002460 |
Cell Line |
Established cell cultures that have the potential to propagate indefinitely. |
Cell Lines,Line, Cell,Lines, Cell |
|
| D002478 |
Cells, Cultured |
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others. |
Cultured Cells,Cell, Cultured,Cultured Cell |
|
| D006360 |
Heat-Shock Proteins |
Proteins which are synthesized in eukaryotic organisms and bacteria in response to hyperthermia and other environmental stresses. They increase thermal tolerance and perform functions essential to cell survival under these conditions. |
Stress Protein,Stress Proteins,Heat-Shock Protein,Heat Shock Protein,Heat Shock Proteins,Protein, Stress |
|
| D006801 |
Humans |
Members of the species Homo sapiens. |
Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man |
|
| D000091342 |
Endoplasmic Reticulum Chaperone BiP |
An ENDOPLASMIC RETICULUM specific chaperone of the HSP70 family. They are involved in folding and oligomerization of secreted and membrane proteins and ENDOPLASMIC RETICULUM STRESS related UNFOLDED PROTEIN RESPONSE. |
Binding-immunoglobulin Protein Molecular Chaperone,Glucose Regulated Protein 78 kDa,Grp78,HSPA5 Protein,Heat-Shock Protein 5,Molecular Chaperone BiP,Molecular Chaperone GRP78,BiP, Molecular Chaperone,Binding immunoglobulin Protein Molecular Chaperone,GRP78, Molecular Chaperone,Heat Shock Protein 5,Protein, HSPA5 |
|
| D000818 |
Animals |
Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. |
Animal,Metazoa,Animalia |
|
| D000873 |
Anthracenes |
A group of compounds with three aromatic rings joined in linear arrangement. |
|
|
| D001692 |
Biological Transport |
The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments. |
Transport, Biological,Biologic Transport,Transport, Biologic |
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