CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin.
By Sreyashi Basu, R. Binder, T. Ramalingam, P. Srivastava. Immunity, 2001
1,188 citations recorded by the source corpus.
Subfields: Cell Biology, Molecular Biology, Physical and Theoretical Chemistry
View Paper: https://www.semanticscholar.org/paper/51ac081ff8c54ab80cc6cfdd8cc540a0ac9dcb59
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In Cell Biology
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In Physical and Theoretical Chemistry
Citations in the corpus
- C1q and Mannose Binding Lectin Engagement of Cell Surface Calreticulin and Cd91 Initiates Macropinocytosis and Uptake of Apoptotic Cells (2001, background): “A recent report has suggested that CRT may bind to the multifunctional receptor, CD91 (98); we show colocalization of CRT with CD91 on the HMDM cell surface (Fig.”
- Toll-like receptors. (2003, background): “CD91 (α-macroglobulin receptor) has been identified as a receptor for several heat shock proteins, including HSP70 (65).”
- Medical application of functionalized magnetic nanoparticles. (2005, background): “The released HSP–peptide complexes encounter APCs that express specific receptors such as CD91 (61).”
- DAMPs, PAMPs, and LAMPs in Immunity and Sterile Inflammation. (2020, neutral): “F or p er so na l u se o nl y. Table 1 Noninfectious (or sterile) immunostimulatory molecular patternsa Molecular pattern Receptor Physiological purpose Potential role in immune-mediated disease or treatment Intracellular DAMPs cDAMPs (nucleus) Double-stranded DNA TLR9 (128), AIM2 (129, 130) Damage ”
- Roles of heat-shock proteins in innate and adaptive immunity (2002, background): “Interaction of HSP–peptide complexes with CD91 leads to internalization of the complexes into a non-acidic endosomal compartment, followed by a transfer of the complex, or of the peptide alone, to the cytoso”
- The sterile inflammatory response (2010, neutral): “HMGB1 (39), SAP130 (40), IL-1α (37), IL-33 (41), DNA (42, 43), S100 proteins (44), heat shock proteins (45, 46) and others (47).”