Cited by 119Heat shock proteins researchCell death mechanisms and regulationClusterin in disease pathology

The DOI matches its Crossref record; 201 of the 202 references it cites were found in a registry or an index.

Hsp70: Anti-apoptotic and Tumorigenic Protein

Rérole, Anne-Laure, Jego, Gaëtan, Garrido, Carmen·2011·Methods in Molecular Biology

Open this paper in CoChat — free account

Abstract

Heat shock protein 70 (Hsp70) is a powerful chaperone whose expression is induced in response to a wide variety of physiological and environmental insults, including anticancer chemotherapy, thus allowing the cell to survive to lethal conditions. Hsp70 cytoprotective properties may be explained by its anti-apoptotic function. Indeed, this protein can inhibit key effectors of the apoptotic machinery at the pre- and postmitochondrial level. In cancer cells, the expression of Hsp70 is abnormally high, and Hsp70 may participate in oncogenesis and in resistance to chemotherapy. In rodent models, Hsp70 overexpression increases tumor growth and metastatic potential. Depletion or inhibition of Hsp70 frequently reduces the size of the tumors and even can cause their complete involution. But Hsp70 can also be found in the extracellular medium. Its role is then immunogenic and the term chaperokine to define the extracellular chaperones has been advanced. Hsp70 tumorigenic functions as well as the strategies that are being developed in cancer therapy in order to inhibit Hsp70 are commented in this chapter.

Integrity signals

Registry

Crossref · 10.1007/978-1-61779-295-3_16

Cites

201 of 201 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Apoptosis: A Basic Biological Phenomenon with Wideranging Implications in Tissue Kinetics
Kerr, J. F. R., Wyllie, A. H., & Currie, A. R. (1972) · British Journal of Cancer · doi:10.1038/bjc.1972.33 · Cited by 15,673
Cytochrome c and dATP-Dependent Formation of Apaf-1/Caspase-9 Complex Initiates an Apoptotic Protease Cascade
Li, P., Nijhawan, D., Budihardjo, I., Srinivasula, S. M., Ahmad, M., Alnemri, E. S., & Wang, X. (1997) · Cell · doi:10.1016/s0092-8674(00)80434-1 · Cited by 7,289
Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
Datta, S. R., Dudek, H., Tao, X., Masters, S., Fu, H., Gotoh, Y., & Greenberg, M. E. (1997) · Cell · doi:10.1016/s0092-8674(00)80405-5 · Cited by 5,689
Cleavage of BID by Caspase 8 Mediates the Mitochondrial Damage in the Fas Pathway of Apoptosis
Li, H., Zhu, H., Xu, C.-J., & Yuan, J. (1998) · Cell · doi:10.1016/s0092-8674(00)81590-1 · Cited by 4,445
The Danger Model: A Renewed Sense of Self
Matzinger, P. (2002) · Science · doi:10.1126/science.1071059 · Cited by 4,205
Protein folding in the cell
Gething, M.-J. H., & Sambrook, J. (1992) · Nature · doi:10.1038/355033a0 · Cited by 4,158
Proapoptotic BAX and BAK: A Requisite Gateway to Mitochondrial Dysfunction and Death
Wei, M. C., Zong, W.-X., Cheng, E. H.-Y., Lindsten, T., Panoutsakopoulou, V., Ross, A. J., Roth, K. A., MacGregor, G. R., Thompson, C. B., & Korsmeyer, S. J. (2001) · Science · doi:10.1126/science.1059108 · Cited by 3,988
Bid, a Bcl2 Interacting Protein, Mediates Cytochrome c Release from Mitochondria in Response to Activation of Cell Surface Death Receptors
Luo, X., Budihardjo, I., Zou, H., Slaughter, C., & Wang, X. (1998) · Cell · doi:10.1016/s0092-8674(00)81589-5 · Cited by 3,626
Smac, a Mitochondrial Protein that Promotes Cytochrome c–Dependent Caspase Activation by Eliminating IAP Inhibition
Du, C., Fang, M., Li, Y., Li, L., & Wang, X. (2000) · Cell · doi:10.1016/s0092-8674(00)00008-8 · Cited by 3,513
Mammalian Caspases: Structure, Activation, Substrates, and Functions During Apoptosis
Earnshaw, W. C., Martins, L. M., & Kaufmann, S. H. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.383 · Cited by 2,758
Regulation of Cell Death Protease Caspase-9 by Phosphorylation
Cardone, M. H., Roy, N., Stennicke, H. R., Salvesen, G. S., Franke, T. F., Stanbridge, E., Frisch, S., & Reed, J. C. (1998) · Science · doi:10.1126/science.282.5392.1318 · Cited by 2,481
Caspases: killer proteases
Nicholson, D. W., & Thornberry, N. A. (1997) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(97)01085-2 · Cited by 2,418
A new puffing pattern induced by temperature shock and DNP in drosophila
Ritossa, F. (1962) · Cellular and Molecular Life Sciences · doi:10.1007/bf02172188 · Cited by 2,146
NF-κB activation by tumour necrosis factor requires the Akt serine–threonine kinase
Nidai Ozes, O., Mayo, L. D., Gustin, J. A., Pfeffer, S. R., Pfeffer, L. M., & Donner, D. B. (1999) · Nature · doi:10.1038/43466 · Cited by 1,832
BCL-2, BCL-XL Sequester BH3 Domain-Only Molecules Preventing BAX- and BAK-Mediated Mitochondrial Apoptosis
Cheng, E. H. Y., Wei, M. C., Weiler, S., Flavell, R. A., Mak, T. W., Lindsten, T., & Korsmeyer, S. J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00320-3 · Cited by 1,735
HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine
Asea, A. A. A., Kraeft, S., Kurt‐Jones, E. A., Stevenson, M. A., Chen, L. B., Finberg, R. W., Koo, G. C., & Calderwood, S. K. (2000) · Nature Medicine · doi:10.1038/74697 · Cited by 1,642
Molecular Chaperones and Protein Quality Control
Bukau, B., Weissman, J. S., & Horwich, A. L. (2006) · Cell · doi:10.1016/j.cell.2006.04.014 · Cited by 1,580
Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome
Beere, H. M., Wolf, B. B., Cain, K., Mosser, D. D., Mahboubi, A., Kuwana, T., Tailor, P., Morimoto, R. I., Cohen, G. M., & Green, D. R. (2000) · Nature Cell Biology · doi:10.1038/35019501 · Cited by 1,513
Novel Signal Transduction Pathway Utilized by Extracellular HSP70
Asea, A., Rehli, M., Kabingu, E., Boch, J. A., Baré, O., Auron, P. E., Stevenson, M. A., & Calderwood, S. K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200497200 · Cited by 1,510
Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications
Ciocca, D. R., & Calderwood, S. K. (2005) · Cell Stress and Chaperones · doi:10.1379/csc-99r.1 · Cited by 1,420
Interaction of Hsp 70 with Newly Synthesized Proteins: Implications for Protein Folding and Assembly
Beckmann, R. P., Mizzen, L., & Welch, W. J. (1990) · Science · doi:10.1126/science.2188360 · Cited by 1,291
Protein synthesis in salivary glands of Drosophila melanogaster: Relation to chromosome puffs
Tissieres, A., Mitchell, H. K., & Tracy, U. M. (1974) · Journal of Molecular Biology · doi:10.1016/0022-2836(74)90447-1 · Cited by 1,227
The heat shock protein 70 family: Highly homologous proteins with overlapping and distinct functions
Daugaard, M., Rohde, M., & Jäättelä, M. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.05.039 · Cited by 1,177
Protein kinase B/Akt-mediated phosphorylation promotes nuclear exclusion of the winged helix transcription factor FKHR1
Biggs, W., Meisenhelder, J., Hunter, T. R., Cavenee, W. K., & Arden, K. C. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.13.7421 · Cited by 1,128
Pathways of chaperone-mediated protein folding in the cytosol
Young, J. C., Agashe, V. R., Siegers, K., & Hartl, F. U. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1492 · Cited by 1,121
Roles of heat-shock proteins in innate and adaptive immunity.
Srivastava, P. (2002) · Nature reviews. Immunology · doi:10.1038/nri749 · Cited by 1,069
Membrane-associated Hsp72 from tumor-derived exosomes mediates STAT3-dependent immunosuppressive function of mouse and human myeloid-derived suppressor cells
Chalmin, F., Ladoire, S., Mignot, G., Vincent, J., Bruchard, M., Rémy-Martin, J.-P., Boireau, W., Rouleau, A., Simon, B., Lanneau, D., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci40483 · Cited by 1,029
Self-citation
Apoptosis signaling by death receptors
Schulze‐Osthoff, K., Ferrari, D., Łoś, M., Wesselborg, S., & Peter, M. E. (1998) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1998.2540439.x · Cited by 981
CD91 Is a Common Receptor for Heat Shock Proteins gp96, hsp90, hsp70, and Calreticulin
Basu, S., Binder, R. J., Ramalingam, T., & Srivastava, P. K. (2001) · Immunity · doi:10.1016/s1074-7613(01)00111-x · Cited by 900
Heat-shock protein 70 antagonizes apoptosis-inducing factor
Ravagnan, L., Gurbuxani, S. K., Susín, S. A., Maisse, C., Daugas, É., Zamzami, N., Mak, T. W., Jäättelä, M., Penninger, J. M., Garrido, C., et al. (2001) · Nature Cell Biology · doi:10.1038/ncb0901-839 · Cited by 859
Self-citation
A Mechanism for the Specific Immunogenicity of Heat Shock Protein-Chaperoned Peptides
Suto, R., & Srivastava, P. K. (1995) · Science · doi:10.1126/science.7545313 · Cited by 826
BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and BakPreprint
Zong, W., Lindsten, T., Ross, A. J., MacGregor, G. R., & Thompson, C. B. (2001) · Genes & Development · doi:10.1101/gad.897601 · Cited by 809
Endocytosed HSP60s Use Toll-like Receptor 2 (TLR2) and TLR4 to Activate the Toll/Interleukin-1 Receptor Signaling Pathway in Innate Immune Cells
Vabulas, R. M., Ahmad-Nejad, P., da Costa, C., Miethke, T., Kirschning, C. J., Häcker, H., & Wagner, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103217200 · Cited by 805
Heat Shock Proteins: Endogenous Modulators of Apoptotic Cell Death
Garrido, C., Gurbuxani, S. K., Ravagnan, L., & Kroemer, G. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5427 · Cited by 790
Self-citation
The Chaperone Function of hsp70 Is Required for Protection against Stress-Induced Apoptosis
Mosser, D., Caron, A., Bourget, L., Meriin, A. B., Sherman, M., Morimoto, R., & Massie, B. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.19.7146-7159.2000 · Cited by 768
Correlation between synthesis of heat shock proteins and development of thermotolerance in Chinese hamster fibroblasts.
Li, G. C., & Werb, Z. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.10.3218 · Cited by 735
Cathepsin B contributes to TNF-α–mediated hepatocyte apoptosis by promoting mitochondrial release of cytochrome c
Guicciardi, M. E., Deussing, J. M., Miyoshi, H., Bronk, S. F., Svingen, P. A., Peters, C., Kaufmann, S. H., & Gores, G. J. (2000) · Journal of Clinical Investigation · doi:10.1172/jci9914 · Cited by 710
Heat Shock Protein 70 Surface-Positive Tumor Exosomes Stimulate Migratory and Cytolytic Activity of Natural Killer Cells
Gastpar, R., Gehrmann, M., Bausero, M. A., Asea, A. A. A., Groß, C. C., Schroeder, J. A., & Multhoff, G. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-3804 · Cited by 696
Hsp70 exerts its anti‐apoptotic function downstream of caspase‐3‐like proteases
Jäättelä, M., Wissing, D., Kokholm, K., Kallunki, T., & Egeblad, M. (1998) · The EMBO Journal · doi:10.1093/emboj/17.21.6124 · Cited by 679
Heat Shock Proteins 27 and 70: Anti-Apoptotic Proteins with Tumorigenic Properties
Garrido, C., Brunet, M., Mirjolet, C., Zermati, Y., Schmitt, E., & Kroemer, G. (2006) · Cell Cycle · doi:10.4161/cc.5.22.3448 · Cited by 676
Self-citation
CD91: a receptor for heat shock protein gp96
Binder, R. J., Han, D. K. M., & Srivastava, P. K. (2000) · Nature Immunology · doi:10.1038/77835 · Cited by 674
Cathepsin B Acts as a Dominant Execution Protease in Tumor Cell Apoptosis Induced by Tumor Necrosis Factor
Foghsgaard, L., Wissing, D., Mauch, D., Lademann, U. A., Bastholm, L., Boes, M. L., Elling, F., Leist, M., & Jäättelä, M. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.5.999 · Cited by 629
Heat shock protein 70-associated peptides elicit specific cancer immunity.
Udono, H., & Srivastava, P. K. (1993) · The Journal of Experimental Medicine · doi:10.1084/jem.178.4.1391 · Cited by 621
Escaping Cell Death: Survival Proteins in Cancer
Jäättelä, M. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4455 · Cited by 608
Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function
Cheetham, M. E., & Caplan, A. J. (1998) · Cell Stress and Chaperones · doi:10.1379/1466-1268(1998)003 · Cited by 604
Intracellular and extracellular functions of heat shock proteins: repercussions in cancer therapy
Schmitt, E., Gehrmann, M., Brunet, M., Multhoff, G., & Garrido, C. (2006) · Journal of Leukocyte Biology · doi:10.1189/jlb.0306167 · Cited by 589
Self-citation
HtrA2 Promotes Cell Death through Its Serine Protease Activity and Its Ability to Antagonize Inhibitor of Apoptosis Proteins
Verhagen, A. M., Silke, J., Ekert, P. G., Pakusch, M., Kaufmann, H., Connolly, L. M., Day, C. L., Tikoo, A., Burke, R., Wrobel, C. N., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109891200 · Cited by 558
Negative regulation of cytochrome c‐mediated oligomerization of Apaf‐1 and activation of procaspase‐9 by heat shock protein 90
Pandey, P., Saleh, A., Nakazawa, A., Kumar, S., Srinivasula, S. M., Kumar, V., Weichselbaum, R. R., Nalin, C. M., Alnemri, E. S., Kufe, D. W., et al. (2000) · The EMBO Journal · doi:10.1093/emboj/19.16.4310 · Cited by 556
Heat Shock Protein 70 Promotes Cell Survival by Inhibiting Lysosomal Membrane Permeabilization
Nylandsted, J., Gyrd-Hansen, M., Danielewicz, A., Fehrenbacher, N., Lademann, U., Høyer-Hansen, M., Weber, E., Multhoff, G., Rohde, M., & Jäättelä, M. (2004) · The Journal of Experimental Medicine · doi:10.1084/jem.20040531 · Cited by 545
Heat Shock Proteins Come of Age: Primitive Functions Acquire New Roles in an Adaptive World
Srivastava, P. K., Ménoret, A., Basu, S., Binder, R. J., & McQuade, K. L. (1998) · Immunity · doi:10.1016/s1074-7613(00)80570-1 · Cited by 540
Targeted gene disruption of Hsp70-2 results in failed meiosis, germ cell apoptosis, and male infertility.
Dix, D. J., Allen, J. W., Collins, B. W., Mori, C., Nakamura, N., Poorman‐Allen, P., Goulding, E. H., & Eddy, E. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.8.3264 · Cited by 540
Global Profiling of the Cell Surface Proteome of Cancer Cells Uncovers an Abundance of Proteins with Chaperone Function
Shin, B. K., Wang, H., Yim, A. M., Naour, F. L., Brichory, F., Jang, J. H., Zhao, R., Puravs, E., Tra, J., Michael, C. W., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210455200 · Cited by 520
Molecular chaperones and the stress of oncogenesis
Mosser, D. D., & Morimoto, R. I. (2004) · Oncogene · doi:10.1038/sj.onc.1207529 · Cited by 512
Heat shock proteins as cellular lifeguards
Jäättelä, M. (1999) · Annals of Medicine · doi:10.3109/07853899908995889 · Cited by 482
Hsp70 Translocates into the Plasma Membrane after Stress and Is Released into the Extracellular Environment in a Membrane-Associated Form that Activates Macrophages
Vega, V. L., Rodríguez-Silva, M., Frey, T., Gehrmann, M., Díaz, J. C., Steinem, C., Multhoff, G., Arispe, N. J., & Maio, A. D. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.6.4299 · Cited by 461
A Small Molecule Inhibitor of Inducible Heat Shock Protein 70
Leu, J. I.-J., Pimkina, J. S., Frank, A. K., Murphy, M. E., & George, D. L. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.023 · Cited by 451
Hsp70 Inhibits Heat-induced Apoptosis Upstream of Mitochondria by Preventing Bax Translocation
Stankiewicz, A. R., Lachapelle, G., Foo, C. P. Z., Radicioni, S. M., & Mosser, D. D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509497200 · Cited by 443
Cathepsin D Triggers Bax Activation, Resulting in Selective Apoptosis-inducing Factor (AIF) Relocation in T Lymphocytes Entering the Early Commitment Phase to Apoptosis
Bidère, N., Lorenzo, H. K., Carmona, S., Laforge, M., Harper, F., Dumont, C., & Senik, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301911200 · Cited by 435
How death shapes life during development
Baehrecke, E. H. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm931 · Cited by 420
Cleavage of poly(ADP-ribose) polymerase: a sensitive parameter to study cell death
Duriez, P. J., & Shah, G. M. (1997) · Biochemistry and Cell Biology · doi:10.1139/o97-043 · Cited by 420
Receptor-Mediated Uptake of Antigen/Heat Shock Protein Complexes Results in Major Histocompatibility Complex Class I Antigen Presentation via Two Distinct Processing Pathways
Castellino, F., Boucher, P. E., Eichelberg, K., Mayhew, M., Rothman, J. E., Houghton, A. N., & Germain, R. N. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.191.11.1957 · Cited by 404
Mitochondria are selective targets for the protective effects of heat shock against oxidative injury.
Polla, B. S., Kantengwa, S., François, D., Salvioli, S., Franceschi, C., Marsac, C., & Cossarizza, A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.13.6458 · Cited by 402
Caspase Activation Is Required for Terminal Erythroid Differentiation
Zermati, Y., Garrido, C., Amsellem, S., Fishelson, S., Bouscary, D., Valensi, F., Varet, B. R., Solary, É., & Hermine, O. (2001) · The Journal of Experimental Medicine · doi:10.1084/jem.193.2.247 · Cited by 400
Self-citation
Cutting Edge: Receptor-Mediated Endocytosis of Heat Shock Proteins by Professional Antigen-Presenting Cells
Arnold-Schild, D., Hanau, D., Spehner, D., Schmid, C., Rammensee, H., de la Salle, H., & Schild, H. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.7.3757 · Cited by 398
Heat Shock Proteins 70 and 90 Inhibit Early Stages of Amyloid β-(1–42) Aggregation in Vitro
Evans, C. G., Wisén, S., & Gestwicki, J. E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606192200 · Cited by 396
Selective depletion of heat shock protein 70 (Hsp70) activates a tumor-specific death program that is independent of caspases and bypasses Bcl-2
Nylandsted, J., Rohde, M., Brand, K., Bastholm, L., Elling, F., & Jäättelä, M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.14.7871 · Cited by 393
Heat shock protein 72 on tumor cells: a recognition structure for natural killer cells
Multhoff, G., Botzler, C., Jennen, L., Schmidt, J., Ellwart, J. W., & Issels, R. D. (1997) · The Journal of Immunology · doi:10.4049/jimmunol.158.9.4341 · Cited by 387
Mitochondrial membrane permeabilization is a critical step of lysosome-initiated apoptosis induced by hydroxychloroquine
Boya, P., Gonzalez-Polo, R.-A., Poncet, D., Andreau, K., Vieira, H. L., Roumier, T., Perfettini, J.-L., & Kroemer, G. (2003) · Oncogene · doi:10.1038/sj.onc.1206622 · Cited by 385
70-kD heat shock-related protein is one of at least two distinct cytosolic factors stimulating protein import into mitochondria.
Murakami, H., Pain, D., & Blobel, G. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.107.6.2051 · Cited by 379
Caspase-independent cell death in T lymphocytes
Jäättelä, M., & Tschopp, J. (2003) · Nature Immunology · doi:10.1038/ni0503-416 · Cited by 373
CHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70
Qian, S., McDonough, H., Boellmann, F., Cyr, D., & Patterson, C. (2006) · Nature · doi:10.1038/nature04600 · Cited by 369
Heat shock proteins, cellular chaperones that modulate mitochondrial cell death pathways
Parcellier, A., Gurbuxani, S. K., Schmitt, E., Solary, É., & Garrido, C. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00623-5 · Cited by 359
Self-citation
Injected cytochrome c induces apoptosis
Zhivotovsky, B., Orrenius, S., Brustugun, O. T., & Døskeland, S. O. (1998) · Nature · doi:10.1038/35060 · Cited by 351
Cross-Presentation of Glycoprotein 96–Associated Antigens on Major Histocompatibility Complex Class I Molecules Requires Receptor-Mediated Endocytosis
Singh‐Jasuja, H., Toes, R. E. M., Spee, P., Münz, C., Hilf, N., Schoenberger, S. P., Ricciardi‐Castagnoli, P., Neefjes, J., Rammensee, H., Arnold-Schild, D., et al. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.191.11.1965 · Cited by 348
Stress-Inducible Cellular Responses
Feige, U., Yahara, I., Morimoto, R. I., & Polla, B. S. (1995) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-9088-5 · Cited by 338
The transport of proteins into the nucleus requires the 70-kilodalton heat shock protein or its cytosolic cognate.
Shi, Y., & Thomas, J. O. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.5.2186 · Cited by 335
Heat Shock Protein 70 Is Secreted from Tumor Cells by a Nonclassical Pathway Involving Lysosomal Endosomes
Mambula, S. S., & Calderwood, S. K. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.11.7849 · Cited by 334
Hsp70 regulates erythropoiesis by preventing caspase-3-mediated cleavage of GATA-1
Ribeil, J., Zermati, Y., Vandekerckhove, J., Cathelin, S., Kersual, J., Dussiot, M., Coulon, S., Moura, I. C., Zeuner, A., Kirkegaard‐Sørensen, T., et al. (2006) · Nature · doi:10.1038/nature05378 · Cited by 331
Self-citation
The Hsp110 and Grp170 stress proteins: newly recognized relatives of the Hsp70s
Easton, D. P., Kaneko, Y., & Subjeck, J. R. (2000) · Cell Stress and Chaperones · doi:10.1379/1466-1268(2000)005 · Cited by 328
A novel, small molecule inhibitor of Hsc70/Hsp70 potentiates Hsp90 inhibitor induced apoptosis in HCT116 colon carcinoma cells
Massey, A. J., Williamson, D. S., Browne, H. L., Murray, J. B., Dokurno, P., Shaw, T., Macias, A. T., Daniels, Z., Geoffroy, S., Dopson, M., et al. (2009) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-009-1194-3 · Cited by 322
Hsp72 functions as a natural inhibitory protein of c‐Jun N‐terminal kinase
Park, H.-S., Lee, J., Huh, S., Seo, J., & Choi, E. (2001) · The EMBO Journal · doi:10.1093/emboj/20.3.446 · Cited by 317
Dual Targeting of HSC70 and HSP72 Inhibits HSP90 Function and Induces Tumor-Specific Apoptosis
Powers, M. V., Clarke, P. A., & Workman, P. (2008) · Cancer Cell · doi:10.1016/j.ccr.2008.08.002 · Cited by 307
Atractyloside‐induced release of cathepsin B, a protease with caspase‐processing activity
Vancompernolle, K., Herreweghe, F. V., PYNAERT, G. N., de Craen, M. V., Vos, K. J. D., Totty, N., Sterling, A., Fiers, W., Vandenabeele, P., & Grooten, J. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01275-7 · Cited by 304
Triptolide Induces Pancreatic Cancer Cell Death via Inhibition of Heat Shock Protein 70
Phillips, P. A., Dudeja, V., McCarroll, J. A., Borja–Cacho, D., Dawra, R. K., Grizzle, W. E., Vickers, S. M., & Saluja, A. K. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-1077 · Cited by 304
Heat shock protein expression and drug resistance in breast cancer patients treated with induction chemotherapy
Vargas-Roig, L. M., Gago, F. E., Tello, O. M., Aznar, J. C., & Ciocca, D. R. (1998) · International Journal of Cancer · doi:10.1002/(sici)1097-0215(19981023)79:5 · Cited by 302
Not all J domains are created equal: Implications for the specificity of Hsp40–Hsp70 interactions
Hennessy, F., Nicoll, W. S., Zimmermann, R., Cheetham, M. E., & Blatch, G. L. (2005) · Protein Science · doi:10.1110/ps.051406805 · Cited by 294
Photo-Oxidative Disruption of Lysosomal Membranes Causes Apoptosis of Cultured Human Fibroblasts
Brunk, U. T., Dalen, H., Roberg, K. B., & Hellquist, H. B. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00007-5 · Cited by 283
Heat shock protein 70 binding inhibits the nuclear import of apoptosis-inducing factor
Gurbuxani, S. K., Schmitt, E., Candé, C., Parcellier, A., Hammann, A., Daugas, É., Kouranti, I., Spahr, C. S., Pance, A., Kroemer, G., et al. (2003) · Oncogene · doi:10.1038/sj.onc.1206794 · Cited by 266
Self-citation
Regulation of mitochondrial membrane permeabilization by BCL-2 family proteins and caspases
Breckenridge, D. G., & Xue, D. (2004) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2004.09.009 · Cited by 265
Anti-Inflammatory Effect of Heat Shock Protein Induction Is Related to Stabilization of IκBα Through Preventing IκB Kinase Activation in Respiratory Epithelial Cells
Yoo, C., Lee, S., Lee, C.-T., Kim, Y. W., Han, S., & Shim, Y.-S. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.164.10.5416 · Cited by 263
The journal of clinical investigation
(1993) · Journal of the American Dietetic Association · doi:10.1016/0002-8223(93)92071-5 · Cited by 253
Hsp70 promotes TNF-mediated apoptosis by binding IKKγ and impairing NF-κB survival signalingPreprint
Ran, R., Lu, A., Zhang, L., Tang, Y., Zhu, H., Xu, H., Feng, Y., Han, C., Zhou, G., Rigby, A. C., et al. (2004) · Genes & Development · doi:10.1101/gad.1188204 · Cited by 251
Treatment of Colon and Lung Cancer Patients withex VivoHeat Shock Protein 70-Peptide-Activated, Autologous Natural Killer Cells
Krause, S. W., Gastpar, R., Andreesen, R., Groß, C. C., Ullrich, H., Thonigs, G., Pfister, K., & Multhoff, G. (2004) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-03-0683 · Cited by 246
Modulating Poly (ADP-Ribose) Polymerase Activity: Potential for the Prevention and Therapy of Pathogenic Situations Involving DNA Damage and Oxidative Stress
Decker, P., & Muller, S. (2002) · Current Pharmaceutical Biotechnology · doi:10.2174/1389201023378265 · Cited by 245
Protein-Damaging Stresses Activate c-Jun N-Terminal Kinase via Inhibition of Its Dephosphorylation: a Novel Pathway Controlled by HSP72
Meriin, A. B., Yaglom, J. A., Gabai, V. L., Mosser, D. D., Zon, L. I., & Sherman, M. Y. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.4.2547 · Cited by 237
The heat‐shock protein receptors: some answers and more questions
Binder, R. J., Vatner, R. E., & Srivastava, P. K. (2004) · Tissue Antigens · doi:10.1111/j.1399-0039.2004.00299.x · Cited by 235
Heat shock protein 70 overexpression affects the response to ultraviolet light in murine fibroblasts. Evidence for increased cell viability and suppression of cytokine release.
Simon, M. M., Reikerstorfer, A., Schwarz, A., Krone, C. L., Luger, T. A., Jäättelä, M., & Schwarz, T. (1995) · Journal of Clinical Investigation · doi:10.1172/jci117800 · Cited by 235
Chemical Manipulation of Hsp70 ATPase Activity Regulates Tau Stability
Jinwal, U. K., Miyata, Y., Koren, J., Jones, J. R., Trotter, J. H., Chang, L., O’Leary, J. C., Morgan, D., Lee, D. C., Shults, C. L., et al. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.3345-09.2009 · Cited by 233
Apoptosis-inducing factor (AIF): caspase-independent after all
Candé, C., Vahsen, N., Garrido, C., & Kroemer, G. (2004) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401400 · Cited by 232
Self-citation
Heat Shock Protein 70 Increases Tumorigenicity and Inhibits Apoptosis in Pancreatic Adenocarcinoma
Aghdassi, A. A., Phillips, P. A., Dudeja, V., Dhaulakhandi, D. B., Sharif, R., Dawra, R. K., Lerch, M. M., & Saluja, A. K. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-1567 · Cited by 230
Lysosomal destabilization in p53-induced apoptosis
Yuan, X., Li, W., Dalen, H., Lotem, J., Kama, R., Sachs, L., & Brunk, U. T. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092135599 · Cited by 230
Novel Adenosine-Derived Inhibitors of 70 kDa Heat Shock Protein, Discovered Through Structure-Based Design
Williamson, D. S., Borgognoni, J., Clay, A., Daniels, Z., Dokurno, P., Drysdale, M. J., Foloppe, N., Francis, G. L., Graham, C. J., Howes, R., et al. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm801627a · Cited by 228
Triptolide, an Inhibitor of the Human Heat Shock Response That Enhances Stress-induced Cell Death
Westerheide, S. D., Kawahara, T. L. A., Orton, K., & Morimoto, R. I. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512044200 · Cited by 226
In Vivo Chaperone Activity of Heat Shock Protein 70 and Thermotolerance
Nollen, E. A. A., Brunsting, J. F., Roelofsen, H., Weber, L. A., & Kampinga, H. H. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.3.2069 · Cited by 225
Heat shock protein 70 (Hsp70) stimulates proliferation and cytolytic activity of natural killer cells
Multhoff, G., Mizzen, L., Winchester, C., Milner, C. M., Wenk, S., Eissner, G., Kampinga, H. H., Laumbacher, B., & Johnson, J. P. (1999) · Experimental Hematology · doi:10.1016/s0301-472x(99)00104-6 · Cited by 223
Recombinant Human Heat Shock Protein 60 Does Not Induce the Release of Tumor Necrosis Factor α from Murine Macrophages
Gao, B., & Tsan, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303161200 · Cited by 221
Heat Shock Protein-chaperoned Peptides but Not Free Peptides Introduced into the Cytosol Are Presented Efficiently by Major Histocompatibility Complex I Molecules
Binder, R. J., Blachère, N. E., & Srivastava, P. K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011547200 · Cited by 216
Cathepsin B Mediates Caspase-Independent Cell Death Induced by Microtubule Stabilizing Agents in Non-Small Cell Lung Cancer Cells
Bröker, L. E., Huisman, C., Span, S. W., Rodríguez, J. A., Kruyt, F. A. E., & Giaccone, G. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-3060 · Cited by 206
The Receptor for Heat Shock Protein 60 on Macrophages Is Saturable, Specific, and Distinct from Receptors for Other Heat Shock Proteins
Habich, C., Baumgart, K., Kolb, H., & Burkart, V. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.168.2.569 · Cited by 201
Heat Shock Protein 70 Inhibits Caspase-Dependent and -Independent Apoptosis in Jurkat T Cells
Creagh, E. M., Carmody, R. J., & Cotter, T. G. (2000) · Experimental Cell Research · doi:10.1006/excr.2000.4856 · Cited by 197
Hsp70 Overexpression Sequesters AIF and Reduces Neonatal Hypoxic/Ischemic Brain Injury
Matsumori, Y., Hong, S. M., Aoyama, K., Fan, Y., Kayama, T., Sheldon, R. A., Vexler, Z. S., Ferriero, D. M., Weinstein, P. R., & Liu, J. (2005) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/sj.jcbfm.9600080 · Cited by 195
Microinjection of Cathepsin D Induces Caspase-Dependent Apoptosis in Fibroblasts
Roberg, K. B., Kågedal, K., & Öllinger, K. M. (2002) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64160-0 · Cited by 194
Interaction of Heat Shock Protein 70 Peptide with NK Cells Involves the NK Receptor CD94
Groß, C. C., Hansch, D., Gastpar, R., & Multhoff, G. (2003) · Biological Chemistry · doi:10.1515/bc.2003.030 · Cited by 194
Hsp70 interactions with the p53 tumour suppressor protein
Żylicz, M., King, F. W., & Wawrzynów, A. (2001) · The EMBO Journal · doi:10.1093/emboj/20.17.4634 · Cited by 192
Oxidative stress, growth factor starvation and Fas activation may all cause apoptosis through lysosomal leak
Brunk, U. T., & Svensson, I. (1999) · Redox Report · doi:10.1179/135100099101534675 · Cited by 184
Alternative Mechanism by which IFN-γ Enhances Tumor Recognition: Active Release of Heat Shock Protein 72
Bausero, M. A., Gastpar, R., Multhoff, G., & Asea, A. A. A. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.5.2900 · Cited by 183
Allosteric Regulation of Hsp70 Chaperones by a Proline Switch
Vogel, M., Bukau, B., & Mayer, M. P. (2006) · Molecular Cell · doi:10.1016/j.molcel.2005.12.017 · Cited by 177
Cell death regulation by the mammalian IAP antagonist Diablo/Smac
Verhagen, A. M. W., & Vaux, D. L. (2002) · APOPTOSIS · doi:10.1023/a:1014318615955 · Cited by 175
Mechanistic role of heat shock protein 70 in Bcr-Abl–mediated resistance to apoptosis in human acute leukemia cells
Guo, F., Sigua, C. A., Bali, P., George, P., Fiskus, W. C., Scuto, A., Annavarapu, S., Mouttaki, A., Sondarva, G. V., Wei, S., et al. (2004) · Blood · doi:10.1182/blood-2004-05-2041 · Cited by 175
Hsp72 and Stress Kinase c-jun N-Terminal Kinase Regulate the Bid-Dependent Pathway in Tumor Necrosis Factor-Induced Apoptosis
Gabai, V. L., Mabuchi, K., Mosser, D. D., & Sherman, M. Y. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.10.3415-3424.2002 · Cited by 172
Heat Shock Protein Hsp72 Is a Negative Regulator of Apoptosis Signal-Regulating Kinase 1
Park, H.-S., Cho, S., Kim, C. K., Hwang, H. S., Noh, K. T., Kim, M.-S., Huh, S.-H., Kim, M., Ryoo, K., Kim, E. K., et al. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.22.7721-7730.2002 · Cited by 171
Over‐expression of hsp70 confers tumorigenicity to mouse fibrosarcoma cells
Jäättelä, M. (1995) · International Journal of Cancer · doi:10.1002/ijc.2910600520 · Cited by 170
Hsc70 and Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability
Arispe, N. J., Doh, M., Šimáková, O., Kurganov, B. I., & Maio, A. D. (2004) · The FASEB Journal · doi:10.1096/fj.04-2088com · Cited by 163
Hsp72-Mediated Suppression of c-Jun N-Terminal Kinase Is Implicated in Development of Tolerance to Caspase-Independent Cell Death
Gabai, V. L., Yaglom, J. A., Volloch, V., Meriin, A. B., Force, T. L., Koutroumanis, M., Bernard Massie, B., Mosser, D. D., & Sherman, M. Y. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.18.6826-6836.2000 · Cited by 158
Heat Shock Protein 70 Neutralization Exerts Potent Antitumor Effects in Animal Models of Colon Cancer and Melanoma
Schmitt, E., Maingret, L., Puig, P., Rérole, A.-L., Ghiringhelli, F., Hammann, A., Solary, É., Kroemer, G., & Garrido, C. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3778 · Cited by 148
Self-citation
Heat shock proteins, tumor immunogenicity and antigen presentation: an integrated view
Wells, A. D., & Malkovský, M. (2000) · Immunology Today · doi:10.1016/s0167-5699(99)01558-3 · Cited by 147
Overexpression of the heat shock protein 70 enhances the TCR/CD3- and Fas/Apo-1/CD95-mediated apoptotic cell death in Jurkat T cells
Liossis, S. C., Ding, X. Z., Kiang, J. G., & Tsokos, G. C. (1997) · The Journal of Immunology · doi:10.4049/jimmunol.158.12.5668 · Cited by 146
Glycoprotein 96 Can Chaperone Both MHC Class I- and Class II-Restricted Epitopes for In Vivo Presentation, but Selectively Primes CD8+ T Cell Effector Function
Doody, A. D. H., Kovalchin, J., Mihalyo, M. A., Hagymasi, A. T., Drake, C. G., & Adler, A. J. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.10.6087 · Cited by 144
Positive and negative regulation of apoptotic pathways by cytotoxic agents in hematological malignancies
Solary, É., Droin, N. M., Bettaı̈eb, A., Corcos, L., Dimanche‐Boitrel, M., & Garrido, C. (2000) · Leukemia · doi:10.1038/sj.leu.2401902 · Cited by 137
Self-citation
Cardenolide-Induced Lysosomal Membrane Permeabilization Demonstrates Therapeutic Benefits in Experimental Human Non-Small Cell Lung Cancers
Mijatovic, T., Mathieu, V., Gaussin, J., Nève, N. D., Ribaucour, F., Quaquebeke, E. V., Dumont, P., Darro, F., & Robert Kiss, A. (2006) · Neoplasia · doi:10.1593/neo.05850 · Cited by 136
The Turn Motif Is a Phosphorylation Switch That Regulates the Binding of Hsp70 to Protein Kinase C
Gao, T., & Newton, A. C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204335200 · Cited by 134
FANCC interacts with Hsp70 to protect hematopoietic cells from IFN‐γ/TNF‐α‐mediated cytotoxicity
Pang, Q., Keeble, W. W., Christianson, T. A., Faulkner, G. R., & Bagby, G. C. (2001) · The EMBO Journal · doi:10.1093/emboj/20.16.4478 · Cited by 134
Human Heat Shock Protein 70 Enhances Tumor Antigen Presentation through Complex Formation and Intracellular Antigen Delivery without Innate Immune Signaling
Bendz, H., Ruhland, S. C., Pandya, M. J., Hainzl, O., Riegelsberger, S., Bräuchle, C., Mayer, M. P., Büchner, J., Issels, R. D., & Noeßner, E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704129200 · Cited by 130
Chaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/α‐synuclein complex by Hip
Roodveldt, C., Bertoncini, C. W., Andersson, A., van der Goot, A. T., Hsu, S. D., Fernández-Montesinos, R., de Jong, J., van Ham, T. J., Nollen, E. A. A., Pozo, D., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.298 · Cited by 129
Distinct hsp70 Domains Mediate Apoptosis-inducing Factor Release and Nuclear Accumulation
Ruchalski, K. L., Mao, H., Li, Z., Wang, Z., Gillers, S., Wang, Y., Mosser, D. D., Gabai, V. L., Schwartz, J. H., & Borkan, S. C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513728200 · Cited by 126
Heat shock proteins refine the danger theory
Todryk, S. M., Melcher, A. A., Dalgleish, A. G., & Vile, R. G. (2000) · Immunology · doi:10.1046/j.1365-2567.2000.00002.x · Cited by 125
Heat shock proteins: biological functions and clinical application as personalized vaccines for human cancer
Castelli, C., Rivoltini, L., Rini, F., Belli, F., Testori, A., Maio, M., Mazzaferro, V., Coppa, J. C., Srivastava, P. K., & Parmiani, G. (2004) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-003-0481-9 · Cited by 122
A Novel Class of Small Molecule Inhibitors of Hsp90
Yi, F., & Regan, L. (2008) · ACS Chemical Biology · doi:10.1021/cb800162x · Cited by 117
p23, a simple protein with complex activities
Felts, S. J., & Toft, D. O. (2003) · Cell Stress and Chaperones · doi:10.1379/1466-1268(2003)008 · Cited by 116
Hsp70 protects against UVB induced apoptosis by preventing release of cathepsins and cytochrome c in human melanocytes
Bivik, C. A., Rosdahl, I. K., & Öllinger, K. M. (2006) · Carcinogenesis · doi:10.1093/carcin/bgl152 · Cited by 115
HSP70 Deficiency Results in Activation of c-Jun N-terminal Kinase, Extracellular Signal-regulated Kinase, and Caspase-3 in Hyperosmolarity-induced Apoptosis
Lee, J., Lee, J., & Seo, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m412393200 · Cited by 112
Re-evaluating the role of heat-shock protein–peptide interactions in tumour immunity
Nicchitta, C. V. (2003) · Nature reviews. Immunology · doi:10.1038/nri1089 · Cited by 111
Plasma Levels of Heat Shock Protein 70 in Patients with Prostate Cancer: A Potential Biomarker for Prostate Cancer
Abe, M., Manola, J. B., Oh, W. K., Parslow, D., George, D. J., Austin, C. L., & Kantoff, P. W. (2004) · Clinical Prostate Cancer · doi:10.3816/cgc.2004.n.013 · Cited by 108
The Anti-apoptotic Function of Hsp70 in the Interferon-inducible Double-stranded RNA-dependent Protein Kinase-mediated Death Signaling Pathway Requires the Fanconi Anemia Protein, FANCC
Pang, Q., Christianson, T. A., Keeble, W. W., Koretsky, T., & Bagby, G. C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m209386200 · Cited by 106
GRP94/gp96 Elicits ERK Activation in Murine Macrophages
Reed, R. C., Berwin, B. L., Baker, J. P., & Nicchitta, C. V. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305480200 · Cited by 106
Hsp70 translocates to the nuclei and nucleoli, binds to XRCC1 and PARP-1, and protects HeLa cells from single-strand DNA breaks
Kotoglou, P., Kalaitzakis, A., Vezyraki, P., Tzavaras, T., Michalis, L. K., Dantzer, F., Jung, J. U., & Angelidis, C. E. (2008) · Cell Stress and Chaperones · doi:10.1007/s12192-008-0093-6 · Cited by 103
Binding of heat shock protein 70 to extracellular phosphatidylserine promotes killing of normoxic and hypoxic tumor cells
Schilling, D., Gehrmann, M., Steinem, C., Maio, A. D., Pockley, A. G., Abend, M., Molls, M., & Multhoff, G. (2009) · The FASEB Journal · doi:10.1096/fj.08-125229 · Cited by 103
Stress proteins and immunity mediated by cytotoxic T lymphocytes
Schild, H., Arnold-Schild, D., Lammert, E., & Rammensee, H. (1999) · Current Opinion in Immunology · doi:10.1016/s0952-7915(99)80019-3 · Cited by 100
Death by chaperone: HSP90, HSP70 or both?
Powers, M. V., Clarke, P. A., & Workman, P. (2009) · Cell Cycle · doi:10.4161/cc.8.4.7583 · Cited by 99
Surface Expression of Hsp25 and Hsp72 Differentially Regulates Tumor Growth and Metastasis
Bausero, M. A., Page, D. T., Osinaga, E., & Asea, A. A. A. (2004) · Tumor Biology · doi:10.1159/000081387 · Cited by 99
Overexpression of the heat-shock protein 70 is associated to imatinib resistance in chronic myeloid leukemia
Pocaly, M., Lagarde, V., Étienne, G., Ribeil, J., Claverol, S., Bonneu, M., Moreau‐Gaudry, F., Guyonnet‐Dupérat, V., Hermine, O., Melo, J. V., et al. (2006) · Leukemia · doi:10.1038/sj.leu.2404463 · Cited by 98
Mechanisms of HSP72 release
Asea, A. A. A. (2007) · Journal of Biosciences · doi:10.1007/s12038-007-0057-5 · Cited by 94
Enhanced Immunogenicity of Heat Shock Protein 70 Peptide Complexes from Dendritic Cell-Tumor Fusion Cells
Enomoto, Y., Bharti, A. K., Khaleque, A. A., Song, B., Liu, C., Apostolopoulos, V., Xing, P., Calderwood, S. K., & Gong, J. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.9.5946 · Cited by 94
Triptolide therapy for neuroblastoma decreases cell viability in vitro and inhibits tumor growth in vivo
Antonoff, M. B., Chugh, R., Borja–Cacho, D., Dudeja, V., Clawson, K. A., Skube, S. J., Sorenson, B. S., Saltzman, D. A., Vickers, S. M., & Saluja, A. K. (2009) · Surgery · doi:10.1016/j.surg.2009.04.023 · Cited by 88
Induction of hsp70-Mediated Th17 Autoimmunity Can Be Exploited as Immunotherapy for Metastatic Prostate Cancer
Kottke, T. J., Sanchez-Perez, L. A., Díaz, R. M., Thompson, J., Chong, H., Harrington, K. J., Calderwood, S. K., Pulido, J. S., Georgopoulos, N. T., Selby, P. J., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-2259 · Cited by 87
Smac/Diablo Antagonizes Ubiquitin Ligase Activity of Inhibitor of Apoptosis Proteins
Creagh, E. M., Murphy, B. M., Duriez, P. J., Duckett, C. S., & Martin, S. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313859200 · Cited by 84
Regulation of the human apoptotic DNase/RNase Endonuclease G: involvement of Hsp70 and ATP
Kalinowska, M., Garncarz, W., Pietrowska, M., Garrard, W. T., & Widłak, P. (2005) · APOPTOSIS · doi:10.1007/s10495-005-0410-9 · Cited by 81
Characterization of a Receptor for Heat Shock Protein 70 on Macrophages and Monocytes
Sondermann, H., Becker, T., Mayhew, M., Wieland, F., & Hartl, F. U. (2000) · Biological Chemistry · doi:10.1515/bc.2000.144 · Cited by 81
Selective depletion of inducible HSP70 enhances immunogenicity of rat colon cancer cells
Gurbuxani, S. K., Bruey, J.-M., Fromentin, A., Larmonier, N., Parcellier, A., Jäättelä, M., Martin, F., Solary, É., & Garrido, C. (2001) · Oncogene · doi:10.1038/sj.onc.1204948 · Cited by 81
Self-citation
Mortalin sensitizes human cancer cells to MKT-077-induced senescence
Deocaris, C. C., Widodo, N., Shrestha, B. G., Kaur, K., Ohtaka, M., Yamasaki, K., Kaul, S. C., & Wadhwa, R. (2007) · Cancer Letters · doi:10.1016/j.canlet.2006.12.038 · Cited by 80
Activation of Fas inhibits heat‐induced activation of HSF1 and up‐regulation of hsp70
Schett, G. A., Steiner, C.-W., Gröger, M., Winkler, S., Graninger, W. B., Smolen, J. S., Xu, Q., & Steiner, G. E. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.8.833 · Cited by 79
Modulation of Akt and ERK1/2 Pathways by Resveratrol in Chronic Myelogenous Leukemia (CML) Cells Results in the Downregulation of Hsp70
Mustafi, S. B., Chakraborty, P. K., & Raha, S. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008719 · Cited by 73
Proteomic analysis of autoantibodies in patients with hepatocellular carcinoma
高島, 元., Kuramitsu, Y., Yokoyama, Y., Iizuka, N., HARADA, T., Fujimoto, M., Sakaida, I., Okita, K., Oka, M., & Nakamura, K. (2006) · PROTEOMICS · doi:10.1002/pmic.200500346 · Cited by 73
Co-translational Folding of Caspase-activated DNase with Hsp70, Hsp40, and Inhibitor of Caspase-activated DNase
Sakahira, H., & Nagata, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110071200 · Cited by 71
Heat shock protein 70 inhibits the nuclear import of apoptosis‐inducing factor to avoid DNA fragmentation in TF‐1 cells during erythropoiesis
Lui, J. C. K., & Kong, S. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.11.082 · Cited by 70
Chemosensitization by a non-apoptogenic heat shock protein 70-binding apoptosis-inducing factor mutant.
Schmitt, E., Parcellier, A., Gurbuxani, S. K., Candé, C., Hammann, A., Morales, M. C., Hunt, C. R., Dix, D. J., Kroemer, R. T., Giordanetto, F., et al. (2003) · PubMed · Cited by 69
Self-citation
Quercetin Enhances Susceptibility to NK Cell-mediated Lysis of Tumor Cells Through Induction of NKG2D Ligands and Suppression of HSP70
Bae, J.-H., Kim, J.-Y., Kim, M., Chang, S.-H., Park, Y.-S., Son, C., Park, S.-J., Chung, J. S., Lee, E., Kim, S.-H., et al. (2010) · Journal of Immunotherapy · doi:10.1097/cji.0b013e3181d32f22 · Cited by 68
A novel endothelial-specific heat shock protein HspA12B is required in both zebrafish development and endothelial functions in vitro
Hu, G., Tang, J. X., Zhang, B., Lin, Y., Hanai, J., Galloway, J. L., Bedell, V. M., Bahary, N., Han, Z., Ramchandran, R., et al. (2006) · Journal of Cell Science · doi:10.1242/jcs.03179 · Cited by 68
High-Affinity Interactions between Peptides and Heat Shock Protein 70 Augment CD8+ T Lymphocyte Immune Responses
Flechtner, J. B., Cohane, K. P., Mehta, S., Slusarewicz, P., Leonard, A. K., Barber, B. H., Levey, D. L., & Andjelić, S. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.2.1017 · Cited by 65
Radioresistance is associated to increased Hsp70 content in human glioblastoma cell lines
da Rocha, A. B., Regner, A., Grivicich, I., Schunemann, D. P., Diel, C. L., Kovaleski, G., de Farias, C. B., Mondadori, E., Almeida, L., Filho, A. B., et al. (2004) · International Journal of Oncology · doi:10.3892/ijo.25.3.777 · Cited by 65
A Role for Hsc70 in Regulating Nucleocytoplasmic Transport of a Temperature-sensitive p53 (p53Val-135)
Akakura, S., Yoshida, M., Yoneda, Y., & Horinouchi, S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100200200 · Cited by 63
HSP70 Induction by ING Proteins Sensitizes Cells to Tumor Necrosis Factor Alpha Receptor-Mediated Apoptosis
Feng, X., Bonni, S., & Riabowol, K. T. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01538-06 · Cited by 63
HEAT SHOCK INHIBITS PHOSPHORYLATION OF I-κBα
Shanley, T. P., Ryan, M. A., Eaves-Pyles, T. D., & Wong, H. R. (2000) · Shock · doi:10.1097/00024382-200014040-00005 · Cited by 60
Genomic Mechanisms of p210BCR-ABL Signaling
Ray, S., Lu, Y. C., Kaufmann, S. H., Gustafson, W. C., Karp, J. E., Boldogh, I. R., Fields, A. P., & Brasier, A. R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401851200 · Cited by 55
Control of Metastasized Pancreatic Carcinomas in SCID/Beige Mice with Human IL-2/TKD-Activated NK Cells
Stangl, S., Wortmann, A., Gürtler, U., & Multhoff, G. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.10.6270 · Cited by 53
A pilot study with a therapeutic vaccine based on hydroxyapatite ceramic particles and self-antigens in cancer patients
Ciocca, D. R., Frayssinet, P., & Cuello-Carrión, F. D. (2007) · Cell Stress and Chaperones · doi:10.1379/csc-218r.1 · Cited by 53
A novel therapeutic fusion protein vaccine by two different families of heat shock proteins linked with HPV16 E7 generates potent antitumor immunity and antiangiogenesis
Liu, B., Ye, D., Song, X., Zhao, X., Yi, L., Song, J., Zhang, Z., & Zhao, Q. (2008) · Vaccine · doi:10.1016/j.vaccine.2007.12.034 · Cited by 51
AEG3482 Is an Antiapoptotic Compound that Inhibits Jun Kinase Activity and Cell Death through Induced Expression of Heat Shock Protein 70
Salehi, A. H., Morris, S. J., Ho, W.-C., Dickson, K. M., Doucet, G., Milutinovic, S., Durkin, J. P., Gillard, J. W., & Barker, P. A. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2005.11.012 · Cited by 51
2-phenylacetylenesulfonamide (PAS) induces p53-independent apoptotic killing of B-chronic lymphocytic leukemia (CLL) cells
Steele, A. J., Prentice, A. G., Hoffbrand, A. V., Yogashangary, B. C., Hart, S., Lowdell, M. W., Samuel, E. R., North, J. M., Nacheva, E. P., Chanalaris, A., et al. (2009) · Blood · doi:10.1182/blood-2008-11-190587 · Cited by 47
A New Connection
Voos, W. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00002-9 · Cited by 46
Killing of Normal Melanocytes, Combined with Heat Shock Protein 70 and CD40L Expression, Cures Large Established Melanomas
Sanchez-Perez, L. A., Kottke, T. J., Daniels, G. A., Díaz, R. M., Thompson, J., Pulido, J. S., Melcher, A. A., & Vile, R. G. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.6.4168 · Cited by 44
Inhibition of Simian Virus 40 replication by targeting the molecular chaperone function and ATPase activity of T antigen
Wright, C. M., Seguin, S. P., Fewell, S. W., Zhang, H., Ishwad, C., Vats, A. N., Lingwood, C. A., Wipf, P., Fanning, E., Pipas, J. M., et al. (2009) · Virus Research · doi:10.1016/j.virusres.2008.12.018 · Cited by 42
Heat shock protein 70 binds caspase-activated DNase and enhances its activity in TCR-stimulated T cells
Liu, Q., Kishi, H., Ohtsuka, K., & Muraguchi, A. (2003) · Blood · doi:10.1182/blood-2002-11-3499 · Cited by 41
Natural killer cells play a key role in the antitumor immunity generated by chaperone‐rich cell lysate vaccination
Zeng, Y., Chen, X., Larmonier, N., Larmonier, C. B., Li, G., Sepassi, M., Marron, M., Andreansky, S. S., & Katsanis, E. (2006) · International Journal of Cancer · doi:10.1002/ijc.22150 · Cited by 38
Involvement of calcium in the differential induction of heat shock protein 70 by heat shock protein 90 inhibitors, geldanamycin and radicicol, in human non-small cell lung cancer H460 cells
Chang, Y., Lee, L.-C., Sun, F., Chao, C., Fu, H., & Lai, Y. (2005) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20623 · Cited by 38
Synergistic promotion of breast cancer cells death by targeting molecular chaperone GRP78 and heat shock protein 70
Li, M., Wang, J., Jing, J., Hua, H. M., Luo, T. L., Xu, L., Wang, R., Liu, D., & Jiang, Y. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00575.x · Cited by 38
Both CD4 + and CD8 + T cell epitopes fused to heat shock cognate protein 70 (hsc70) can function to eradicate tumors
Mizukami, S., Kajiwara, C., Ishikawa, H., Katayama, I., Yui, K., & Udono, H. (2008) · Cancer Science · doi:10.1111/j.1349-7006.2008.00788.x · Cited by 37
Geldanamycin inhibits TGF-β signaling through induction of Hsp70
Yun, C.-H., Yoon, S.-Y., Nguyen, T. T., Cho, H.-Y., Kim, T. H., Kim, S.-T., Kim, B.-C., Hong, Y., Kim, S., & Lee, H.-J. (2009) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2009.12.003 · Cited by 37
Cytotoxic T lymphocytes carrying a pattern recognition protein Tag7 can detect evasive, HLA-negative but Hsp70-exposing tumor cells, thereby ensuring FasL/Fas-mediated contact killing
Sashchenko, L. P., Dukhanina, E. A., Shatalov, Y. V., Yashin, D. V., Lukyanova, T. I., Kabanova, O. D., Romanova, E. A., Khaidukov, S. V., Galkin, A. V., Gnuchev, N. V., et al. (2007) · Blood · doi:10.1182/blood-2006-12-064444 · Cited by 33
70‐kDa heat shock proteins: Specific interactions with HLA‐DR molecules and their peptide fragments
Haug, M., Schepp, C. P., Kalbacher, H., Dannecker, G. E., & Holzer, U. (2007) · European Journal of Immunology · doi:10.1002/eji.200636811 · Cited by 33
Therapeutic vaccination with dendritic cells pulsed with tumor-derived Hsp70 and a COX-2 inhibitor induces protective immunity against B16 melanoma
Toomey, D., Conroy, H., Jarnicki, A., Higgins, S. C., Sutton, C. E., & Mills, K. H. G. (2008) · Vaccine · doi:10.1016/j.vaccine.2008.04.005 · Cited by 31
Heat Shock Proteins (HSP70 and HSP27) as Markers of Epithelial Dysplasia in Oral Leukoplakia
Lestón, J. M. S., Varela‐Centelles, P. I., Ramirez, J. R., Cameselle‐Teijeiro, J., Romero, M. A., & Aguirre, J. M. (2006) · American Journal of Dermatopathology · doi:10.1097/01.dad.0000211509.44865.bb · Cited by 29
Fusion proteins of Hsp70 with tumor-associated antigen acting as a potent tumor vaccine and the C‐terminal peptide-binding domain of Hsp70 being essential in inducing antigen-independent anti-tumor response in vivo
Zhang, H., & Huang, W. (2006) · Cell Stress and Chaperones · doi:10.1379/csc-191r.1 · Cited by 29
Helicobacter pylori inhibits expression of heat shock protein 70 (HSP70) in human epithelial cell line. Importance of Cag A protein.
Targosz, A., Pierzchalski, P., Krawiec, A., Szczyrk, U., Brzozowski, T., Konturek, S. J., & Ww, P. (2006) · PubMed · Cited by 21
CD28 costimulation is required not only to induce IL-12 receptor but also to render Janus kinases / STAT4 responsive to IL-12 stimulation in TCR-triggered T cells
Park, W.-R., Park, C.-S., Tomura, M., Ahn, H.-J., Nakahira, Y., 岩崎, 正., Gao, P. H., Abe, R., Hamaoka, T., & Fujiwara, H. (2001) · European Journal of Immunology · doi:10.1002/1521-4141(200105)31:5 · Cited by 20
Benzo(a)pyrene inhibits expression of inducible heat shock protein 70 in vascular endothelial cells
Gong, Z., Yang, J., Yang, M., Wang, F., Wei, Q., Tanguay, R. M., & Wu, T. (2006) · Toxicology Letters · doi:10.1016/j.toxlet.2006.07.307 · Cited by 16
Induction of leukemia‐specific antibodies by immunotherapy with leukemia‐cell‐derived heat shock protein 70
Jimbo, J., Sato, K., Hosoki, T., Shindo, M., Ikuta, K., Torimoto, Y., & Kohgo, Y. (2008) · Cancer Science · doi:10.1111/j.1349-7006.2008.00829.x · Cited by 14
The Intrinsic Pathway of Apoptosis
Kaufmann, S. H. (2007) · Humana Press eBooks · doi:10.1007/978-1-59745-221-2_1 · Cited by 10
Abstract A212: A novel, small molecule inhibitor of Hsc70/Hsp70 potentiates Hsp90 inhibitor-induced apoptosis in HCT116 colon carcinoma cells
Massey, A. J., Borgognoni, J., Browne, H. L., Daniels, Z., Dokurno, P., Drysdale, M. J., Francis, G. L., Graham, C. J., Macias, A. T., Matassova, N., et al. (2009) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.targ-09-a212 · Cited by 2
Untitled work
(1996) · doi:10.1379/1466-1268(1996)001

Sorted by citations

The effects of oxidative stress on female reproduction: a review
Agarwal, A. K., Aponte, A., Premkumar, B. J., Shaman, A. A., & Gupta, S. (2012) · Reproductive Biology and Endocrinology · doi:10.1186/1477-7827-10-49 · Cited by 1,721
Heat Shock Proteins and Cancer
Wu, J., Liu, T., Rios, Z., Mei, Q., Lin, X., & Cao, S. (2016) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2016.11.009 · Cited by 726
The HSP70 family and cancer
Murphy, M. E. (2013) · Carcinogenesis · doi:10.1093/carcin/bgt111 · Cited by 529
Targeting Heat Shock Proteins in Cancer: A Promising Therapeutic Approach
Chatterjee, S., & Burns, T. F. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18091978 · Cited by 498
Programmed cell death in aging
Tower, J. (2015) · Ageing Research Reviews · doi:10.1016/j.arr.2015.04.002 · Cited by 426

See all 119

Authors: Rérole, A.-L., Jego, G., & Garrido, C.
Affiliations: Inserm (FR)
Corresponding author: Garrido, Carmen
ORCID: Garrido, Carmen
Venue: Methods in Molecular Biology
Publisher: Humana Press
Published: 2011
Volume: 787
Pages: 205-230
ISSN: 1064-3745 (ISSN-L)
1940-6029
DOI: 10.1007/978-1-61779-295-3_16
OpenAlex: W7663529
Cited by: 118
References: 202
Citations by year: 2025: 5 · 2024: 6 · 2023: 9 · 2022: 5 · 2021: 8 · 2020: 9 · 2019: 9 · 2018: 6 · 2017: 6 · 2016: 15 · 2015: 9 · 2014: 12 · 2013: 11 · 2012: 7
FWCI: 12.87
Type: book chapter
Language: en
Open access: closed
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: Methods in molecular biology (publishedVersion)
PubMed (publishedVersion)
Funders: Ligue Contre le Cancer
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Health Sciences › Medicine › Oncology › Clusterin in disease pathology
Keywords: HSP70, heat shock proteins, anti-apoptotic effects, carcinogenesis, chemoresistance, metastasis, extracellular Hsp70, apoptosis, cancer therapy, Hsp70 inhibitors
MeSH terms: Antineoplastic Agents, Cell Differentiation, Humans, Neoplasm Metastasis, Neoplasms, Stress, Physiological, Gene Expression, Apoptosis, HSP70 Heat-Shock Proteins, Cell Proliferation, Apoptosis Regulatory Proteins, Receptors, Death Domain, Immunomodulation

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Hsp70: Anti-apoptotic and Tumorigenic Protein

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks