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HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine

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Novel Signal Transduction Pathway Utilized by Extracellular HSP70

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A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors

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Hsp27 negatively regulates cell death by interacting with cytochrome c

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CD91 Is a Common Receptor for Heat Shock Proteins gp96, hsp90, hsp70, and Calreticulin

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Endocytosed HSP60s Use Toll-like Receptor 2 (TLR2) and TLR4 to Activate the Toll/Interleukin-1 Receptor Signaling Pathway in Innate Immune Cells

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Regulation of actin filament dynamics by p38 map kinase-mediated phosphorylation of heat shock protein 27

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Human hsp27, Drosophila hsp27 and human alphaB-crystallin expression-mediated increase in glutathione is essential for the protective activity of these proteins against TNFalpha-induced cell death.

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Exosome-dependent Trafficking of HSP70

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Heat Shock Protein 70 Promotes Cell Survival by Inhibiting Lysosomal Membrane Permeabilization

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Targeted gene disruption of Hsp70-2 results in failed meiosis, germ cell apoptosis, and male infertility.

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Heat Shock Proteins Come of Age: Primitive Functions Acquire New Roles in an Adaptive World

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Involvement of LOX-1 in Dendritic Cell-Mediated Antigen Cross-Presentation

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Global Profiling of the Cell Surface Proteome of Cancer Cells Uncovers an Abundance of Proteins with Chaperone Function

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HSP27 inhibits cytochrome c‐dependent activation of procaspase‐9

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The Endoplasmic Reticulum-resident Heat Shock Protein Gp96 Activates Dendritic Cells via the Toll-like Receptor 2/4 Pathway

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Induction of Chinese hamster HSP27 gene expression in mouse cells confers resistance to heat shock. HSP27 stabilization of the microfilament organization.

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Hsp27 as a Negative Regulator of Cytochrome c Release

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A stress‐inducible 72‐kDa heat‐shock protein (HSP72) is expressed on the surface of human tumor cells, but not on normal cells

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Hsp70 Inhibits Heat-induced Apoptosis Upstream of Mitochondria by Preventing Bax Translocation

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Mutational Analysis of Hsp90 Function: Interactions with a Steroid Receptor and a Protein Kinase

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Inhibition of Daxx-Mediated Apoptosis by Heat Shock Protein 27

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Caspase Activation Is Required for Terminal Erythroid Differentiation

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Heat shock protein 90

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TNF-Induced Recruitment and Activation of the IKK Complex Require Cdc37 and Hsp90

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Cutting Edge: Receptor-Mediated Endocytosis of Heat Shock Proteins by Professional Antigen-Presenting Cells

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Endotoxin Contamination in Recombinant Human Heat Shock Protein 70 (Hsp70) Preparation Is Responsible for the Induction of Tumor Necrosis Factor α Release by Murine Macrophages

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Selective depletion of heat shock protein 70 (Hsp70) activates a tumor-specific death program that is independent of caspases and bypasses Bcl-2

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Heat Shock Protein 27 Controls Apoptosis by Regulating Akt Activation

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CD40, an extracellular receptor for binding and uptake of Hsp70–peptide complexes

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The transport of proteins into the nucleus requires the 70-kilodalton heat shock protein or its cytosolic cognate.

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Disruption of Hsp90 Function Results in Degradation of the Death Domain Kinase, Receptor-interacting Protein (RIP), and Blockage of Tumor Necrosis Factor-induced Nuclear Factor-κB Activation

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HSP27 Is a Ubiquitin-Binding Protein Involved in I-κBα Proteasomal Degradation

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Hsp72 functions as a natural inhibitory protein of c-Jun N-terminal kinase

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Heat Shock Protein 27 Increases after Androgen Ablation and Plays a Cytoprotective Role in Hormone-Refractory Prostate Cancer

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Expression of the Molecular Chaperone Hsp70 in Detergent-resistant Microdomains Correlates with Its Membrane Delivery and Release

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Heat shock protein expression and drug resistance in breast cancer patients treated with induction chemotherapy

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Bag1–Hsp70 mediates a physiological stress signalling pathway that regulates Raf-1/ERK and cell growth

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Heat Shock Protein 72 Modulates Pathways of Stress-induced Apoptosis

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Photodynamic Therapy–Induced Cell Surface Expression and Release of Heat Shock Proteins: Relevance for Tumor Response

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A Signal Peptide Derived from hsp60 Binds HLA-E and Interferes with CD94/NKG2A Recognition

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Heat shock protein 70 binding inhibits the nuclear import of apoptosis-inducing factor

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Stimulation of Th1-Polarizing Cytokines, C-C Chemokines, Maturation of Dendritic Cells, and Adjuvant Function by the Peptide Binding Fragment of Heat Shock Protein 70

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The native structure of the activated Raf protein kinase is a membrane-bound multi-subunit complex.

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Heat Shock Proteins gp96 and hsp70 Activate the Release of Nitric Oxide by APCs

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Treatment of Colon and Lung Cancer Patients withex VivoHeat Shock Protein 70-Peptide-Activated, Autologous Natural Killer Cells

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Immunization of cancer patients with autologous cancer-derived heat shock protein gp96 preparations: A pilot study

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Geldanamycin and its analogue 17-allylamino-17-demethoxygeldanamycin lowers Bcr-Abl levels and induces apoptosis and differentiation of Bcr-Abl-positive human leukemic blasts.

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HSP27 as a mediator of confluence-dependent resistance to cell death induced by anticancer drugs.

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Vaccination with autologous tumor-derived heat-shock protein gp96 after liver resection for metastatic colorectal cancer.

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The heat‐shock protein receptors: some answers and more questions

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Blockade of Hsp27 overcomes Bortezomib/proteasome inhibitor PS-341 resistance in lymphoma cells.

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Heat shock protein 70 (Hsp70) stimulates proliferation and cytolytic activity of natural killer cells

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Recombinant Human Heat Shock Protein 60 Does Not Induce the Release of Tumor Necrosis Factor α from Murine Macrophages

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Essential role of CD91 in re-presentation of gp96-chaperoned peptides

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Heat Shock Protein-chaperoned Peptides but Not Free Peptides Introduced into the Cytosol Are Presented Efficiently by Major Histocompatibility Complex I Molecules

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The role of heat shock protein (hsp70) in dendritic cell maturation: Hsp70 induces the maturation of immature dendritic cells but reduces DC differentiation from monocyte precursors

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The Receptor for Heat Shock Protein 60 on Macrophages Is Saturable, Specific, and Distinct from Receptors for Other Heat Shock Proteins

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Heat Shock Protein 70 Inhibits Caspase-Dependent and -Independent Apoptosis in Jurkat T Cells

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Altered states: selectively drugging the Hsp90 cancer chaperone

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Interaction of Heat Shock Protein 70 Peptide with NK Cells Involves the NK Receptor CD94

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Cell Surface-bound Heat Shock Protein 70 (Hsp70) Mediates Perforin-independent Apoptosis by Specific Binding and Uptake of Granzyme B

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