Hsc70 and Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability.
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Heat shock proteins as danger signals for cancer detectionExtracellular Release and Signaling by Heat Shock Protein 27: Role in Modifying Vascular InflammationPhosphatidylserine and phosphatidylethanolamine in mammalian cells: two metabolically related aminophospholipidsHeat shock proteins and heat shock factor 1 in carcinogenesis and tumor development: an updateHSPA8/HSC70 chaperone protein: structure, function, and chemical targeting.Tumor-specific Hsp70 plasma membrane localization is enabled by the glycosphingolipid Gb3.Calreticulin: non-endoplasmic reticulum functions in physiology and disease.Monitoring charge flux to quantify unusual ligand-induced ion channel activity for use in biological nanopore-based sensorsMonoclonal antibody to novel cell surface epitope on Hsc70 promotes morphogenesis of bile ducts in newborn rat liverHeat shock protein 70 binds its own messenger ribonucleic acid as part of a gene expression self-limiting mechanism.Heat shock protein 70 is acute phase reactant: response elicited by tumor treatment with photodynamic therapyStress down south: meeting report of the fifth International Workshop on the Molecular Biology of Stress Responses.Extracellular heat shock proteins: a new location, a new function.Rescuing of deficient killing and phagocytic activities of macrophages derived from non-obese diabetic mice by treatment with geldanamycin or heat shock: potential clinical implications.Functional diversification and specialization of cytosolic 70-kDa heat shock proteins.Interaction of heat shock protein 70 with membranes depends on the lipid environment.A unique role for heat shock protein 70 and its binding partner tissue transglutaminase in cancer cell migration.Therapeutic aspects of chaperones/heat-shock proteins in neuro-oncology.Regulation of apoptotic and inflammatory cell signaling in cerebral ischemia: the complex roles of heat shock protein 70Evidence of a role for both anti-Hsp70 antibody and endothelial surface membrane Hsp70 in atherosclerosis.Bacterial Hsp70 (DnaK) and mammalian Hsp70 interact differently with lipid membranes.Membranes: a meeting point for lipids, proteins and therapiesDetergent resistant membrane-associated IDE in brain tissue and cultured cells: Relevance to Abeta and insulin degradation.Hsp70 and cardiac surgery: molecular chaperone and inflammatory regulator with compartmentalized effects.Binding of heat shock protein 70 to extracellular phosphatidylserine promotes killing of normoxic and hypoxic tumor cells.In vivo imaging of CT26 mouse tumours by using cmHsp70.1 monoclonal antibody.Molecular chaperones and protein-folding catalysts as intercellular signaling regulators in immunity and inflammation.Extracellular heat shock proteins, cellular export vesicles, and the Stress Observation System: a form of communication during injury, infection, and cell damage. It is never known how far a controversial finding will go! Dedicated to Ferruccio RitoThe heat shock proteins as targets for radiosensitization and chemosensitization in cancerHunting the chameleon: structural conformations of the intrinsically disordered protein alpha-synuclein.The complex function of hsp70 in metastatic cancer.Melanoma cell surface-expressed phosphatidylserine as a therapeutic target for cationic anticancer peptide, temporin-1CEa.Exogenously delivered heat shock protein 70 displaces its endogenous analogue and sensitizes cancer cells to lymphocytes-mediated cytotoxicity.Immunogenic cell death: can it be exploited in PhotoDynamic Therapy for cancer?Identification of genes responsive to paeoniflorin, a heat shock protein-inducing compound, in human leukemia U937 cells.Enzymatic measurement of phosphatidylserine in cultured cells.Sulfatide-Hsp70 interaction promotes Hsp70 clustering and stabilizes binding to unfolded protein.A new feature of the stress response: increase in endocytosis mediated by Hsp70.Biochemical characterization of the interaction between HspA1A and phospholipids.Fluorescent analysis of the cell-selective Alzheimer's disease aβ Peptide surface membrane binding: influence of membrane components.
P2860
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P2860
Hsc70 and Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability.
description
2004 nî lūn-bûn
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2004年の論文
@ja
2004年学术文章
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@zh-hans
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@zh-my
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name
Hsc70 and Hsp70 interact with ...... ng in a decrease of viability.
@en
Hsc70 and Hsp70 interact with ...... ng in a decrease of viability.
@nl
type
label
Hsc70 and Hsp70 interact with ...... ng in a decrease of viability.
@en
Hsc70 and Hsp70 interact with ...... ng in a decrease of viability.
@nl
prefLabel
Hsc70 and Hsp70 interact with ...... ng in a decrease of viability.
@en
Hsc70 and Hsp70 interact with ...... ng in a decrease of viability.
@nl
P2093
P356
P1433
P1476
Hsc70 and Hsp70 interact with ...... ng in a decrease of viability.
@en
P2093
Antonio De Maio
Michael Doh
Nelson Arispe
Olga Simakova
P304
P356
10.1096/FJ.04-2088COM
P407
P577
2004-11-01T00:00:00Z