Habich, Christiane <br/><br/>
The receptor for heat shock protein 60 on macrophages is saturable, specific, and distinct from receptors for other heat shock proteins.  [electronic resource] 

 -  Journal of immunology (Baltimore, Md. : 1950)  Jan 2002 
 - 569-76 p.  digital 
<br/><br/> Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0022-1767 
<br/><br/><label>Standard No.: </label>10.4049/jimmunol.168.2.569  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Animals<br/>Antigens, Neoplasm--metabolism<br/>Binding Sites--immunology<br/>Cell Line<br/>Chaperonin 60--analysis<br/>Drosophila Proteins<br/>HSP70 Heat-Shock Proteins--metabolism<br/>HSP90 Heat-Shock Proteins--metabolism<br/>Heat-Shock Proteins--metabolism<br/>Humans<br/>Ligands<br/>Macrophages--chemistry<br/>Membrane Glycoproteins--analysis<br/>Mice<br/>Mice, Inbred C57BL<br/>Microscopy, Confocal<br/>Nitric Oxide--biosynthesis<br/>Protein Binding--immunology<br/>Receptors, Cell Surface--analysis<br/>Receptors, Immunologic--analysis<br/>Toll-Like Receptor 2<br/>Toll-Like Receptor 4<br/>Toll-Like Receptors<br/>Tumor Necrosis Factor-alpha--biosynthesis