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Heat shock protein

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133:. This discovery eventually led to the identification of the heat-shock proteins (HSP) or stress proteins whose expression this puffing represented. Increased synthesis of selected proteins in Drosophila cells following stresses such as heat shock was first reported in 1974. In 1974, Tissieres, Mitchell and Tracy discovered that heat-shock induces the production of a small number of proteins and inhibits the production of most others. This initial biochemical finding gave rise to a large number of studies on the induction of heat shock and its biological role. Heat shock proteins often function as 600:. Thanks to the HSP, the bound peptide is protected against degradation in dendritic cell compartments and the efficiency of cross-presentation is higher. Also internalisation of HSP-peptide complex is more efficient than internalisation of soluble antigens. Tumor cells usually express only a few neo-antigens, which can be targeted by immune system and also not all tumor cells express them. Because of that the amount of tumor antigens is restricted and high efficiency of cross-presentation is necessary for mounting strong immune response. 381:, phosphorylates a small heat shock protein, hsp20. Hsp20 phosphorylation correlates well with smooth muscle relaxation and is one significant phosphoprotein involved in the process. Hsp20 appears significant in development of the smooth muscle phenotype during development. Hsp20 also serves a significant role in preventing platelet aggregation, cardiac myocyte function and prevention of apoptosis after ischemic injury, and skeletal muscle function and muscle insulin response. 1260: 891:, tumour cells are also in a permanent stress. When HSPs from a tumour are isolated, the peptide repertoire bound by HSPs is somewhat a fingerprint of these particular tumour cells. Application of such HSPs back into patient then stimulate immune system (promotes efficient antigen presentation and act as DAMP) specifically against the tumor and leads to tumor regression. This 907:
Intracellular heat shock proteins are highly expressed in cancerous cells and are essential to the survival of these cell types due to presence of mutated and over-expressed oncogenes. Many HSPs can also promote invasiveness and metastasis formation in tumours, block apoptosis, or promote resistance
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According to Marvin et al. sHSPs independently express not only in heat shock response but also have developmental roles in embryonic or juvenile stages of mammals, teleost fish and some lower vertebral genomes. hspb1 (HSP27) is expressed during stress and during the development of embryo, somites,
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scavenger receptor has been previously proposed as the common HSP receptor. But now its relevance is controversial because the majority of DC types does not express CD91 in relevant amounts and the binding capacity for many HSPs has not been proved. Stimulation of some scavenger receptors can even
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Heat-shock proteins can be secreted from immune cells or tumour cells by non-canonical secretion pathway, or leaderless pathway, because they do not have the leader peptide, which navigate proteins into endoplasmic reticulum. The non-canonical secretion can be similar to the one, which occurs for
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Krief et al. referred hspb7 (cvHSP - cardiovascular Heat shock protein) as cardiac heat shock protein. Gata4 is an essential gene responsible for cardiac morphogenesis. It also regulates the gene expression of hspb7 and hspb12. Gata4 depletion can result in reduced transcript levels of hspb7 and
872:. Furthermore, some researchers speculate that HSPs may be involved in binding protein fragments from dead malignant cells and presenting them to the immune system. In a recent study published by Sedlacek et al., HSP was shown to effect different signaling pathways involved in 217:
The mechanism by which heat-shock (or other environmental stressors) activates the heat shock factor has been determined in bacteria. During heat stress, outer membrane proteins (OMPs) do not fold and cannot insert correctly into the outer membrane. They accumulate in the
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hspb7 also acts in the downregulation of Kupffer vesicles which is responsible for regulation of left-right asymmetry of heart in zebrafish. Along with hspb7, hspb12 is involved in cardiac laterality determination. A kinase of the nitric oxide cell signalling pathway,
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for the treatment of several types of cancer, but for various reasons unrelated to efficacy did not go on to Phase 3. HSPgp96 also shows promise as an anticancer treatment and is currently in clinical trials against non-small cell lung cancer.
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identification. Recent discoveries have shown that high concentrations of eHSP can indicate the presence of contentious tumors. Additionally, HSPs have been shown to benefit oncologist in oral cancer diagnosis. Using techniques such as dot
812:. However, there have been many recent articles alluding to a correlation between hsp70, in some cases hsp60, and DM. Another recent article discovered the ratio of ehsp70 and ihsp70 could have an effect on DM, leading to a sufficient 3609:
Staroverov, Sergey A.; Kozlov, Sergey V.; Brovko, Fedor A.; Fursova, Ksenia K.; Shardin, Vitaly V.; Fomin, Alexander S.; Gabalov, Konstantin P.; Soldatov, Dmitry A.; Zhnichkova, Elena G.; Dykman, Lev A.; Guliy, Olga I. (2022-09-01).
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during recovery from prolonged exposure to cold in the absence of heat shock. A mild heat shock pretreatment of the same kind that protects against death from subsequent heat shock also prevents death from exposure to cold.
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It is known that rapid heat hardening can be elicited by a brief exposure of cells to sub-lethal high temperature, which in turn provides protection from subsequent and more severe temperature. In 1962, Italian geneticist
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This handing over with peptides is important, because HSPs can shield hydrophobic residues in peptides which would be otherwise problematic in aquatic cytosol. Also simple diffusion of peptides would be too ineffective.
104:, which marks proteins for degradation, also has features of a heat shock protein. A conserved protein binding domain of approximately 80 amino-acid alpha crystallins are known as small heat shock proteins (sHSP). 3281:"The chaperone balance hypothesis: the importance of the extracellular to intracellular HSP70 ratio to inflammation-driven type 2 diabetes, the effect of exercise, and the implications for clinical management" 306:
Heat-shock proteins also occur under non-stressful conditions, simply "monitoring" the cell's proteins. Some examples of their role as "monitors" are that they carry old proteins to the cell's "recycling bin"
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molecules and pro-inflammatory and Th1 cytokines. HSP70 was shown to react to DAMP release, causing an influx of HSP70-positive T-EVs (tumor cells) that initiate anti-tumor immune signaling cascades.
753:(HSF 1) is a transcription factor that is involved in the general maintenance and upregulation of Hsp70 protein expression. Recently it was discovered that HSF1 is a powerful multifaceted modifier of 1413:
Cao Y, Ohwatari N, Matsumoto T, Kosaka M, Ohtsuru A, Yamashita S (August 1999). "TGF-beta1 mediates 70-kDa heat shock protein induction due to ultraviolet irradiation in human skin fibroblasts".
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cancer diagnosis markers. HSPs have also been shown to interact with cancer adaptations such as drug resistance, tumor cell production and lifespan, and the up-regulation and down-regulation of
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Also isolated HSPs from tumor cells are able to act as a specific anti-tumor vaccine by themselves. Tumour cells express a lot of HSPs because they need to chaperone mutated and over-expressed
525:. Also when HSPs are extracellular, they can guide their associated peptides into MHCII pathway, although it is not known how they are distinguished from the cross-presented ones (see below). 533:
HSPs are involved in classical macroautophagy, when protein aggregates are enclosed by double membrane and degraded afterwards. They are also involved in a special type of autophagy called
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Function of heat-shock proteins in immunity is based on their ability to bind not only whole proteins, but also peptides. The affinity and specificity of this interaction is typically low.
226:, that passes the signal through the membrane to the sigmaE transcription factor. However, some studies suggest that an increase in damaged or abnormal proteins brings HSPs into action. 4299: 2331: 1308: 238: 3965:
Didelot C, Lanneau D, Brunet M, Joly AL, De Thonel A, Chiosis G, Garrido C (2007). "Anti-cancer therapeutic approaches based on intracellular and extracellular heat shock proteins".
53:, but are now known to also be expressed during other stresses including exposure to cold, UV light and during wound healing or tissue remodeling. Many members of this group perform 415:, although its peptide-binding site has been found. But gp96 immune function could be peptide-independent, because it is involved in proper folding of many immune receptors, like 4552: 1378:
Matz JM, Blake MJ, Tatelman HM, Lavoi KP, Holbrook NJ (July 1995). "Characterization and regulation of cold-induced heat shock protein expression in mouse brown adipose tissue".
291:(shape) and prevention of unwanted protein aggregation. By helping to stabilize partially unfolded proteins, HSPs aid in transporting proteins across membranes within the cell. 690:
The role of extracellular HSPs can be miscellaneous. It depends a lot on context of tissue whether HSPs will stimulate the immune system or suppress immunity. They can promote
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Researchers are also investigating the role of HSPs in conferring stress tolerance to hybridized plants, hoping to address drought and poor soil conditions for farming.
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functions by stabilizing new proteins to ensure correct folding or by helping to refold proteins that were damaged by the cell stress. This increase in expression is
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Albakova, Zarema; Siam, Mohammad Kawsar Sharif; Sacitharan, Pradeep Kumar; Ziganshin, Rustam H.; Ryazantsev, Dmitriy Y.; Sapozhnikov, Alexander M. (2021-02-01).
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Hsp90 inhibitors are another possible treatment for autoimmunity, because hsp90 is necessary for proper folding of many pro-inflammatory proteins (components of
737:) or hspb4 is involved in the development of lens in Zebrafish as it is expressed in response to heat shock in the Zebrafish embryo in its developmental stages. 3755:"Human heat shock protein 70 enhances tumor antigen presentation through complex formation and intracellular antigen delivery without innate immune signaling" 2465:
McLemore EC, Tessier DJ, Thresher J, Komalavilas P, Brophy CM (July 2005). "Role of the small heat shock proteins in regulating vascular smooth muscle tone".
964:. Current therapeutic research areas in the treatment for DM include: long-term physical exercise, hot tub therapy (HTT), and alfalfa-derived HSP70 (aHSP70). 4292: 603:
Hsp70 and hsp90 are also involved intracellulary in cytosolic pathway of cross-presentation where they help antigens to get from endosome into the cytosol.
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Recently, there are several studies that suggest a correlation between HSPs and dual frequency ultrasound as demonstrated by the use of LDM-MED machine.
1191:. Also prevents protein folding during post-translational import into the mitochondria/chloroplast. Hsp110 provides tolerance of extreme temperature. 426:
Apart from that, HSPs can stimulate immune receptors and are important in proper folding of proteins involved in pro-inflammatory signaling pathways.
2367:"Exercise Training under Exposure to Low Levels of Fine Particulate Matter: Effects on Heart Oxidative Stress and Extra-to-Intracellular HSP70 Ratio" 287:
for other proteins. They play an important role in protein–protein interactions such as folding and assisting in the establishment of proper protein
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Tissières A, Mitchell HK, Tracy UM (April 1974). "Protein synthesis in salivary glands of Drosophila melanogaster: relation to chromosome puffs".
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There is a debate about how long can HSP keep its peptide in extracellular space, at least for hsp70 the complex with peptide is quite stable.
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Hsp27 is a major phosphoprotein during women's contractions. Hsp27 functions in small muscle migrations and appears to serve an integral role.
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and treat autoimmune diseases. The underlying mechanism is not known. HSPs (especially hsp60 and hsp70) are used in clinical studies to treat
3678: 1953:"OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain" 3718:
Nishikawa M, Takemoto S, Takakura Y (April 2008). "Heat shock protein derivatives for delivery of antigens to antigen presenting cells".
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deprivation), nitrogen deficiency (in plants) or water deprivation. As a consequence, the heat shock proteins are also referred to as
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The subset of hsp70, extracellular hsp70 (ehsp70) and intracellular hsp70 (ihsp70), has been shown to have a pivotal role in managing
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Vinocur B, Altman A (April 2005). "Recent advances in engineering plant tolerance to abiotic stress: achievements and limitations".
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Yildiz, Mehmet Taha; Tutar, Lütfi; Giritlioğlu, Nazlı Irmak; Bayram, Banu; Tutar, Yusuf (2022), Allmer, Jens; Yousef, Malik (eds.),
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Raboy B, Sharon G, Parag HA, Shochat Y, Kulka RG (1991). "Effect of stress on protein degradation: role of the ubiquitin system".
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for "Immune Response and Safety of HS110 Vaccine in Combination With Erlotinib in Patients With Non-Small Cell Lung Cancer" at
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These activities are part of a cell's own repair system, called the "cellular stress response" or the "heat-shock response".
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in the refolding of proteins damaged by heat stress. Heat shock proteins have been found in all species examined, from
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Although the most important members of each family are tabulated here, some species may express additional chaperones,
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Production of high levels of heat shock proteins can also be triggered by exposure to different kinds of environmental
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Alam, Uazman; Asghar, Omar; Azmi, Shazli; Malik, Rayaz A. (2014-01-01), Zochodne, Douglas W.; Malik, Rayaz A. (eds.),
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LOX-1 and SRECI when stimulated guide HSPs with their associated peptides into cross-presentation. LOX-1 binds mainly
2043:"Recovery of protein synthesis after heat shock: prior heat treatment affects the ability of cells to translate mRNA" 411:, and their peptide-binding sites were identified. In the case of gp96 it is not clear whether it can bind peptides 3562:"Prognosis and predictive value of heat-shock proteins expression in oral cancer: A PRISMA-compliant meta-analysis" 4044: 1739: 1187:
Protein folding and unfolding. Provides thermotolerance to cell on exposure to heat stress and protects against
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Sedlacek, Abigail L.; Kinner-Bibeau, Lauren B.; Wang, Yifei; Mizes, Alicia P.; Binder, Robert J. (2021-08-09).
1273: 961: 58: 3824:"Tunable heat shock protein-mediated NK cell responses are orchestrated by STAT1 in Antigen Presenting Cells" 549:(DC) and promote cross-presentation of their carried peptides. The most important receptors in this case are 4931: 3800: 707: 620: 267: 250: 5103: 4086:"Chaperone-Based Therapeutic Target Innovation: Heat Shock Protein 70 (HSP70) for Type 2 Diabetes Mellitus" 3446:
Nakhjavani M, Morteza A, Khajeali L, Esteghamati A, Khalilzadeh O, Asgarani F, Outeiro TF (November 2010).
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Krause M, Heck TG, Bittencourt A, Scomazzon SP, Newsholme P, Curi R, Homem de Bittencourt PI (2015-02-26).
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In the simplified view of this pathway HSPs are usually not mentioned: antigenic peptides are generated in
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Seibert P, Anklam CF, Costa-Beber LC, Sulzbacher LM, Sulzbacher MM, Sangiovo AM, et al. (June 2022).
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Mai AS, Dos Santos AB, Beber LC, Basso RD, Sulzbacher LM, Goettems-Fiorin PB, et al. (2017-12-13).
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hspb12 and this could result in cardiac myopathies in zebrafish embryos as observed by Gabriel et al.
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Heat shock proteins appear to be more susceptible to self-degradation than other proteins due to slow
96:(the most widely studied HSPs) refer to families of heat shock proteins on the order of 60, 70 and 90 3835: 3343: 3179: 2243: 2054: 957: 945: 899:
manner in clinical studies for gp96 and hsp70, but in vitro this works for all immune-relevant HSPs.
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Involved in protein folding after its post-translational import to the mitochondrion/chloroplast; a
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test researchers have been able to determine that HSP-specific phage antibodies could be beneficial
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Bendz H, Ruhland SC, Pandya MJ, Hainzl O, Riegelsberger S, Braüchle C, et al. (October 2007).
1278: 1245: 1216: 912: 881: 284: 258:(and greatly enhances survival after a subsequent higher temperature heat shock) primarily affects 134: 54: 1248:(Hsp90α and Hsp90β, for instance) or conflicts of nomenclature (Hsp72 is sometimes called Hsp70). 998:
The principal heat-shock proteins that have chaperone activity belong to five conserved classes:
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Walter S, Buchner J (April 2002). "Molecular chaperones--cellular machines for protein folding".
1982: 1898: 1617: 1605: 1438: 1360: 941: 718: 659: 638:, which can either associate with TLRs, or activate pro-inflammatory intracellular pathways like 439: 416: 345: 4084:
Mulyani WR, Sanjiwani MI, Prabawa IP, Lestari AA, Wihandani DM, Suastika K, et al. (2020).
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Jansen MA, Spiering R, Broere F, van Laar JM, Isaacs JD, van Eden W, Hilkens CM (January 2018).
2002:"Translational control of bacterial heat shock and virulence genes by temperature-sensing mRNAs" 4267: 4226:"Requirement of the Escherichia coli dnaK gene for thermotolerance and protection against H2O2" 3887:
Binder RJ (April 2008). "Heat-shock protein-based vaccines for cancer and infectious disease".
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Kampinga HH, Hageman J, Vos MJ, Kubota H, Tanguay RM, Bruford EA, et al. (January 2009).
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Ritossa F (1962). "A new puffing pattern induced by temperature shock and DNP in drosophila".
1298: 1293: 1188: 816:. Serum levels of hsp70 have also been shown to increase over time in patients with diabetes. 673: 597: 471: 359: 234: 219: 195: 118: 114: 70: 3665:, Methods in Molecular Biology, vol. 2257, New York, NY: Springer US, pp. 293–310, 3070:"An RNA aptamer perturbs heat shock transcription factor activity in Drosophila melanogaster" 2753:"Anti-Hsp90 therapy in autoimmune and inflammatory diseases: a review of preclinical studies" 1244:, and heat shock proteins not listed. In addition, many of these proteins may have multiple 4892: 4851: 4846: 4821: 4811: 4806: 4796: 4596: 4237: 4196: 4188: 4144: 4107: 4097: 4009: 3974: 3939: 3896: 3859: 3843: 3766: 3727: 3666: 3623: 3581: 3573: 3524: 3508: 3467: 3459: 3410: 3402: 3361: 3351: 3302: 3292: 3238: 3197: 3187: 3138: 3130: 3089: 3081: 3040: 3032: 2991: 2983: 2939: 2921: 2880: 2872: 2814: 2772: 2764: 2718: 2708: 2638: 2630: 2562: 2554: 2513: 2474: 2437: 2429: 2388: 2378: 2302: 2261: 2251: 2204: 2161: 2124: 2116: 2072: 2062: 2013: 1964: 1925: 1880: 1838: 1801: 1743: 1735: 1694: 1686: 1579: 1548: 1511: 1469: 1422: 1387: 1344: 1034: 972: 953: 952:. Nevertheless, it was found, that application of some HSPs into patients is able to induce 691: 378: 366: 230: 163: 151: 97: 46: 4867: 4801: 1673:
Lahvic JL, Ji Y, Marin P, Zuflacht JP, Springel MW, Wosen JE, et al. (December 2013).
1087: 1083: 333: 5098: 4321: 2861:"A central role for HSC70 in regulating antigen trafficking and MHC class II presentation" 2418:"Small heat shock proteins Hspb7 and Hspb12 regulate early steps of cardiac morphogenesis" 2291:"Stress (heat shock) proteins: molecular chaperones in cardiovascular biology and disease" 1629: 1019: 355: 255: 150:
mid-hindbrain, heart and lens in zebrafish. Expression of the hspb4 gene, which codes for
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Wu J, Liu T, Rios Z, Mei Q, Lin X, Cao S (March 2017). "Heat Shock Proteins and Cancer".
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Santoro MG (January 2000). "Heat shock factors and the control of the stress response".
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Laplante AF, Moulin V, Auger FA, Landry J, Li H, Morrow G, et al. (November 1998).
573:. SRECI is now considered to by the common heat-shock protein receptor because it binds 4645: 4640: 4201: 4176: 4112: 4085: 3864: 3823: 3586: 3529: 3496: 3472: 3447: 3415: 3390: 3330:
Birk OS, Douek DC, Elias D, Takacs K, Dewchand H, Gur SL, et al. (February 1996).
3307: 3280: 3242: 3202: 3167: 3143: 3118: 3094: 3069: 3045: 3020: 2996: 2971: 2944: 2909: 2885: 2860: 2777: 2752: 2723: 2696: 2643: 2619:"Functions of heat shock proteins in pathways of the innate and adaptive immune system" 2618: 2567: 2542: 2518: 2501: 2442: 2417: 2393: 2366: 1699: 1674: 1265: 1029: 924: 909: 873: 754: 624: 546: 42: 2478: 2266: 2231: 2129: 2104: 2077: 2042: 1969: 1952: 1929: 1867:
Marvin M, O'Rourke D, Kurihara T, Juliano CE, Harrison KL, Hutson LD (February 2008).
1806: 1789: 1748: 1723: 5134: 3696: 3643: 3612:"Phage antibodies against heat shock proteins as tools for in vitro cancer diagnosis" 3546: 3432: 3366: 3331: 2558: 2330:
Antonova G, Lichtenbeld H, Xia T, Chatterjee A, Dimitropoulou C, Catravas JD (2007).
1842: 1516: 1499: 884:. Therefore, HSPs may be useful for increasing the effectiveness of cancer vaccines. 805: 758: 263: 3916: 3795: 1986: 1902: 1609: 1442: 1364: 5001: 4983: 2181: 1391: 1288: 1241: 892: 861: 681: 502: 408: 171: 141:
to humans, suggesting that they evolved very early and have an important function.
4067: 3731: 2910:"The Role of Extracellular HSP70 in the Function of Tumor-Associated Immune Cells" 2332:"Functional significance of hsp90 complexes with NOS and sGC in endothelial cells" 761:
show significantly decreased incidence of skin tumor after topical application of
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Co-factor of DnaK/Hsp70, only for bacterial or mitochondrial/chloroplastic forms
5077: 4945: 3627: 3577: 3168:"Inhibiting heat shock factor 1 in human cancer cells with a potent RNA aptamer" 2433: 1690: 830: 482: 467: 321: 187: 183: 84:
Heat shock proteins are named according to their molecular weight. For example,
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Proceedings of the National Academy of Sciences of the United States of America
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Proceedings of the National Academy of Sciences of the United States of America
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Proceedings of the National Academy of Sciences of the United States of America
1474: 1457: 1259: 4907: 4335: 4192: 3463: 2768: 1869:"Developmental expression patterns of the zebrafish small heat shock proteins" 1283: 1255: 1183:
Hsp110 genes are derived from this superfamily and are coded HSPH1 through 4.
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Heat shock proteins appear to serve a significant cardiovascular role. Hsp90,
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Fan GC, Ren X, Qian J, Yuan Q, Nicolaou P, Wang Y, et al. (April 2005).
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Some bacterial heat shock proteins are upregulated via a mechanism involving
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Borges JC, Ramos CH (April 2005). "Protein folding assisted by chaperones".
1047: 813: 790: 677: 443: 167: 101: 4210: 4156: 4121: 4021: 3986: 3951: 3908: 3873: 3780: 3771: 3754: 3739: 3688: 3595: 3538: 3481: 3448:"Increased serum HSP70 levels are associated with the duration of diabetes" 3424: 3356: 3316: 3260: 3211: 3152: 3119:"Heat shock factor 1 is a powerful multifaceted modifier of carcinogenesis" 3103: 3054: 3005: 2953: 2894: 2836: 2786: 2732: 2652: 2576: 2527: 2486: 2451: 2402: 2383: 2347: 2216: 2173: 2067: 2027: 1978: 1937: 1894: 1708: 1601: 1539:
Wu C (1995). "Heat shock transcription factors: structure and regulation".
1434: 4251: 3375: 3297: 3036: 2813:. Advances in Cancer Research. Vol. 129. Elsevier. pp. 191–224. 2316: 2275: 2138: 2086: 2018: 2001: 1850: 1815: 1757: 1656: 1560: 1525: 1483: 1426: 1399: 395:
It was shown, that at least some of the HSPs possess this ability, mainly
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Some members of the HSP family are expressed at low to moderate levels in
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10.1002/1521-3773(20020402)41:7<1098::AID-ANIE1098>3.0.CO;2-9
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The relevance for this type of cross-presentation is high especially in
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Solit DB, Rosen N (2006). "Hsp90: a novel target for cancer therapy".
2987: 2105:"Heat shock protection against cold stress of Drosophila melanogaster" 1458:"Expression of heat shock proteins in mouse skin during wound healing" 684:), HSPs can also appear on the extracellular side of plasma membrane. 4902: 4877: 4872: 4862: 4826: 4816: 4791: 4776: 4771: 4766: 4761: 4756: 4751: 4746: 4741: 4706: 4691: 4538: 4503: 4488: 4483: 4478: 4439: 4434: 4429: 4424: 4419: 4414: 4409: 4404: 4394: 4389: 4384: 4379: 4374: 1177: 1169: 1015: 825: 714: 590: 199: 545:
When HSPs are extracellular, they can bind to specific receptors on
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and take over generated peptides. Afterwards, it can associate with
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But HSPs play an important part in transfer of unfolded proteins to
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Unfolding of insoluble protein aggregates; co-factor of DnaK/Hsp70
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Extracellular heat-shock proteins can be sensed by the immunity as
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organisms because of their essential role in protein maintenance.
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all have been reported as having roles in the cardiovasculature.
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As a result, the clinical use of heat-shock proteins is both in
703: 639: 558: 154:, increases considerably in the lens in response to heat shock. 4281: 3021:"A transcription cofactor required for the heat-shock response" 2697:"The role of heat shock proteins in antigen cross presentation" 919:
show promise as anticancer agents. The potent Hsp90 inhibitor
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attenuates mitogenic (MAPK) signaling and induces cancer cell
699: 73:(HSF). HSPs are found in virtually all living organisms, from 4090:
Diabetes, Metabolic Syndrome and Obesity: Targets and Therapy
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Lu, Wei; Wang, Yongwu; Gan, Min; Duan, Qingyun (2021-01-22).
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Salamanca HH, Antonyak MA, Cerione RA, Shi H, Lis JT (2014).
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Dai C, Whitesell L, Rogers AB, Lindquist S (September 2007).
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Rosenfeld GE, Mercer EJ, Mason CE, Evans T (September 2013).
1022:). A standard nomenclature for human HSP genes is available. 895:
is not functional against a different tumour. It was used in
537:, when they enable cytosolic proteins to get into lysosomes. 3659:"MicroRNAs and Heat Shock Proteins in Breast Cancer Biology" 1951:
Walsh NP, Alba BM, Bose B, Gross CA, Sauer RT (April 2003).
2908:
Linder, Manuel; Pogge von Strandmann, Elke (January 2021).
2809:
Graner MW (2016). "HSP90 and Immune Modulation in Cancer".
2103:
Burton V, Mitchell HK, Young P, Petersen NS (August 1988).
1740:
10.1379/1466-1268(1996)001<0097:dothsr>2.3.co;2
1211:
Maintenance of steroid receptors and transcription factors
880:
activation, gp96-activated macrophages, and activation of
804:(DM) is a immune-disease characterized by the presence of 311:) and they help newly synthesised proteins fold properly. 717:
treatment (boosting an immune response) and treatment of
4037:"Bristol-Myers Squibb Halts Development of Tanespimycin" 254:
a mild heat shock pretreatment which induces heat shock
562:
result in immunosuppression, this is the case for SRA.
283:
Several heat shock proteins function as intra-cellular
174:, exercise, exposure of the cell to harmful materials ( 3663:
miRNomics: MicroRNA Biology and Computational Analysis
1105:
Human HSPB genes. Eleven members in mammals including
222:. These OMPs are detected by DegS, an inner membrane 100:
in size, respectively. The small 8-kilodalton protein
362:, which in turn are involved in vascular relaxation. 210:
is sometimes described more generally as part of the
49:
conditions. They were first described in relation to
5051: 4982: 4971: 4654: 4631: 4589: 4329: 4315: 3227:"Chapter 15 - General aspects of diabetes mellitus" 3068:Salamanca HH, Fuda N, Shi H, Lis JT (August 2011). 668:Another possibility is release of HSPs during cell 2541:Salinthone S, Tyagi M, Gerthoffer WT (July 2008). 2230:Mitchell HK, Petersen NS, Buzin CH (August 1985). 1500:"Heat shock proteins: facts, thoughts, and dreams" 3713: 3711: 4170: 4168: 4166: 2690: 2688: 2686: 2684: 2682: 808:. Typically these symptoms are brought about by 65:of the heat shock proteins is a key part of the 2680: 2678: 2676: 2674: 2672: 2670: 2668: 2666: 2664: 2662: 2612: 2610: 2608: 2606: 1541:Annual Review of Cell and Developmental Biology 1462:The Journal of Histochemistry and Cytochemistry 117:reported that heat and the metabolic uncoupler 2965: 2963: 2854: 2852: 2850: 2848: 2846: 2804: 2802: 2800: 2798: 2796: 2604: 2602: 2600: 2598: 2596: 2594: 2592: 2590: 2588: 2586: 1862: 1860: 1578:. Vol. Appendix 1. pp. Appendix 1T. 1330: 1328: 270:. Heat shock proteins are also synthesized in 4293: 3796:"Cancer Drug Fails, So Maker Tries New Pitch" 2746: 2744: 2742: 2098: 2096: 1770:: CS1 maint: DOI inactive as of April 2024 ( 1668: 1666: 785:. Moreover, HSF1 inhibition by a potent RNA 8: 3019:Xu D, Zalmas LP, La Thangue NB (July 2008). 2543:"Small heat shock proteins in smooth muscle" 634:Heat-shock proteins can signal also through 521:In MHCII presentation, HSPs are involved in 497:, which can take the peptide further to the 2467:Journal of the American College of Surgeons 1129:Hsp40 (DNAJ*; three subfamilies in humans) 4979: 4326: 4300: 4286: 4278: 2811:Hsp90 in Cancer: Beyond the Usual Suspects 2336:Clinical Hemorheology and Microcirculation 665:, and it is induced by stress conditions. 4270:at the U.S. National Library of Medicine 4241: 4200: 4111: 4101: 4035:The Myeloma Beacon Staff (22 July 2010). 3863: 3770: 3585: 3528: 3471: 3414: 3365: 3355: 3306: 3296: 3201: 3191: 3142: 3093: 3044: 2995: 2943: 2925: 2884: 2776: 2722: 2712: 2695:Murshid A, Gong J, Calderwood SK (2012). 2642: 2566: 2517: 2441: 2392: 2382: 2371:Oxidative Medicine and Cellular Longevity 2306: 2265: 2255: 2232:"Self-degradation of heat shock proteins" 2128: 2076: 2066: 2017: 1968: 1884: 1805: 1747: 1698: 1515: 1473: 1204:Human HSPC genes. Includes Hsp90, Grp94 ( 1024: 615:(DAMPs). They are able to interact with 2041:Petersen NS, Mitchell HK (March 1981). 1324: 824:HSP expression plays a pivotal role in 509:form peptide loading complex for MHCI. 438:pathways - the classical ones and also 3720:International Journal of Pharmaceutics 2289:Benjamin IJ, McMillan DR (July 1998). 1783: 1781: 1763: 1724:"Discovery of the heat shock response" 1625: 1615: 868:(DAMPS) in boosting the response to a 4002:Current Topics in Medicinal Chemistry 1018:, and the small heat-shock proteins ( 434:HSPs are indispensable components of 121:induced a characteristic pattern of " 7: 2859:Deffit SN, Blum JS (December 2015). 1574:Li Z, Srivastava P (February 2004). 613:damage-associated molecular patterns 607:Damage-associated molecular patterns 248:Petersen and Mitchell found that in 3759:The Journal of Biological Chemistry 3233:, Diabetes and the Nervous System, 1794:The Journal of Biological Chemistry 1553:10.1146/annurev.cb.11.110195.002301 940:, HSPs can extracellularly promote 5116:Prokaryotic ubiquitin-like protein 3932:Trends in Pharmacological Sciences 3243:10.1016/B978-0-444-53480-4.00015-1 2519:10.1161/01.CIR.0000160851.41872.C6 1380:The American Journal of Physiology 1164:Human HSPA genes. Includes Hsp71 ( 653:Transport into extracellular space 25: 2751:Tukaj S, Węgrzyn G (March 2016). 2479:10.1016/j.jamcollsurg.2005.03.017 505:binds peptides and together with 369:and other physiological factors. 356:endothelial nitric oxide synthase 4137:Current Opinion in Biotechnology 3616:Biosensors and Bioelectronics: X 2559:10.1016/j.pharmthera.2008.04.005 1517:10.1097/00024382-199901000-00001 1258: 4230:Journal of General Microbiology 2547:Pharmacology & Therapeutics 619:like TLR2 or TLR4 and activate 4646:Mitochondrial targeting signal 4309:Posttranslational modification 3794:Anand, Geeta (2 August 2007). 3231:Handbook of Clinical Neurology 2109:Molecular and Cellular Biology 1392:10.1152/ajpregu.1995.269.1.R38 523:clathrin-dependent endocytosis 1: 3732:10.1016/j.ijpharm.2007.09.030 1970:10.1016/S0092-8674(03)00203-4 1930:10.1016/S0006-2952(99)00299-3 1807:10.1016/S0021-9258(19)38314-0 908:to anti-cancer drugs. Hence 680:(for example induced by some 617:pattern recognition receptors 4722:Ubiquitin-conjugating enzyme 4243:10.1099/00221287-136-10-2113 4181:Cell Stress & Chaperones 4149:10.1016/j.copbio.2005.02.001 3671:10.1007/978-1-0716-1170-8_15 3513:10.1016/j.tranon.2020.100995 3452:Cell Stress & Chaperones 3395:Cell Stress & Chaperones 3193:10.1371/journal.pone.0096330 2877:10.1016/j.molimm.2015.04.007 2757:Cell Stress & Chaperones 1843:10.1016/0022-2836(74)90447-1 1831:Journal of Molecular Biology 1788:Schlesinger MJ (July 1990). 1728:Cell Stress & Chaperones 1584:10.1002/0471142735.ima01ts58 1304:Hsp90 cis-regulatory element 950:systemic lupus erythematosus 535:chaperone-mediated autophagy 462:through protein transporter 243:Hsp90 cis-regulatory element 69:and is induced primarily by 5010:E2 SUMO-conjugating enzyme 4667:Ubiquitin-activating enzyme 4224:Delaney JM (October 1990). 3967:Current Medicinal Chemistry 3628:10.1016/j.biosx.2022.100211 3578:10.1097/MD.0000000000024274 2617:Binder RJ (December 2014). 2434:10.1016/j.ydbio.2013.06.025 2197:Protein and Peptide Letters 1691:10.1016/j.ydbio.2013.10.009 45:in response to exposure to 5157: 4993:E1 SUMO-activating enzyme 4014:10.2174/156802606777812068 3979:10.2174/092986707782360079 3944:10.1016/j.tips.2016.11.009 3848:10.1038/s41598-021-95578-3 3407:10.1007/s12192-022-01288-8 3135:10.1016/j.cell.2007.07.020 2819:10.1016/bs.acr.2015.10.001 1498:De Maio A (January 1999). 1475:10.1177/002215549804601109 676:. During special types of 672:, or secretion of HSPs in 481:and generated peptides to 470:, which then goes through 4193:10.1007/s12192-008-0068-7 3889:Expert Review of Vaccines 3464:10.1007/s12192-010-0204-z 3285:Mediators of Inflammation 2769:10.1007/s12192-016-0670-z 1180:) found only in primates. 598:tumour-immunosurveillance 4607:Survival of motor neuron 4272:Medical Subject Headings 3901:10.1586/14760584.7.3.383 2714:10.3389/fimmu.2012.00063 2635:10.4049/jimmunol.1401417 2209:10.2174/0929866053587165 1918:Biochemical Pharmacology 1645:Acta Biologica Hungarica 1274:Cellular stress response 721:(suppress of immunity). 708:antigen-presenting cells 625:co-stimulation molecules 621:antigen presenting cells 61:regulated. The dramatic 4973:Ubiquitin-like proteins 4932:Deubiquitinating enzyme 3801:The Wall Street Journal 2927:10.3390/cancers13184721 2701:Frontiers in Immunology 2308:10.1161/01.res.83.2.117 2257:10.1073/pnas.82.15.4969 1742:(inactive 2024-04-26). 1722:Ritossa F (June 1996). 944:leading to diseases as 903:Anticancer therapeutics 706:responses depending on 4065:Clinical trial number 3772:10.1074/jbc.M704129200 3501:Translational Oncology 3357:10.1073/pnas.93.3.1032 3074:Nucleic Acids Research 2068:10.1073/pnas.78.3.1708 1873:Developmental Dynamics 932:Autoimmunity treatment 186:, among many others), 158:Upregulation in stress 3237:, Elsevier: 211–222, 3037:10.1038/embor.2008.70 2623:Journal of Immunology 2422:Developmental Biology 2019:10.4161/rna.7.1.10501 2000:Narberhaus F (2010). 1790:"Heat shock proteins" 1679:Developmental Biology 1427:10.1007/s004240050905 1142:GroEL, 60kDa antigen 866:immunologic adjuvants 864:, HSPs are useful as 741:Clinical significance 4103:10.2147/DMSO.S232133 2865:Molecular Immunology 2384:10.1155/2017/9067875 2295:Circulation Research 2121:10.1128/mcb.8.8.3550 958:rheumatoid arthritis 946:rheumatoid arthritis 942:autoimmune reactions 860:Given their role in 678:apoptotic cell death 627:(CD80, CD86, CD40), 474:on plasma membrane. 436:antigen presentation 430:Antigen presentation 268:transcription of RNA 166:conditions, such as 5141:Heat shock proteins 4331:Heat shock proteins 4268:Heat-Shock+Proteins 3840:2021NatSR..1116106S 3765:(43): 31688–31702. 3348:1996PNAS...93.1032B 3298:10.1155/2015/249205 3184:2014PLoSO...996330S 2248:1985PNAS...82.4969M 2059:1981PNAS...78.1708P 1800:(21): 12111–12114. 1576:Heat-shock proteins 1386:(1 Pt 2): R38–R47. 1132:Co-factor of Hsp70 1069:Co-factor of Hsp60 751:Heat shock factor 1 719:autoimmune diseases 636:scavenger receptors 623:by upregulation of 553:, mainly SRECI and 551:scavenger receptors 489:can associate with 458:, transported into 67:heat shock response 31:Heat shock proteins 4073:ClinicalTrials.gov 4041:The Myeloma Beacon 3828:Scientific Reports 3086:10.1093/nar/gkr206 1886:10.1002/dvdy.21414 1349:10.1007/BF02172188 913:inhibitors of HSPs 876:responses such as 810:insulin deficiency 541:Cross-presentation 517:MHCII presentation 440:cross-presentation 346:alpha B crystallin 322:proteolytic action 37:) are a family of 27:Family of proteins 18:Heat-shock protein 5128: 5127: 5124: 5123: 4633:Protein targeting 4627: 4626: 4047:on 9 January 2018 4008:(11): 1205–1214. 3973:(27): 2839–2847. 3680:978-1-0716-1170-8 3080:(15): 6729–6740. 2988:10.1111/imm.12811 2871:(2 Pt A): 85–88. 2629:(12): 5765–5771. 2512:(14): 1792–1799. 2154:Angewandte Chemie 1468:(11): 1291–1301. 1299:FourU thermometer 1294:Cold-shock domain 1238: 1237: 1176:, HSPA5); Hsx70 ( 802:Diabetes mellitus 797:Diabetes mellitus 682:chemotherapeutics 472:secretory pathway 450:MHCI presentation 360:guanylate cyclase 279:Role as chaperone 235:FourU thermometer 220:periplasmic space 119:2,4-dinitrophenol 115:Ferruccio Ritossa 71:heat shock factor 59:transcriptionally 16:(Redirected from 5148: 4980: 4893:Ubiquitin ligase 4659:(ubiquitylation) 4597:Alpha crystallin 4327: 4302: 4295: 4288: 4279: 4256: 4255: 4245: 4221: 4215: 4214: 4204: 4172: 4161: 4160: 4132: 4126: 4125: 4115: 4105: 4081: 4075: 4063: 4057: 4056: 4054: 4052: 4043:. Archived from 4032: 4026: 4025: 3997: 3991: 3990: 3962: 3956: 3955: 3927: 3921: 3920: 3884: 3878: 3877: 3867: 3819: 3813: 3812: 3810: 3808: 3791: 3785: 3784: 3774: 3750: 3744: 3743: 3715: 3706: 3705: 3704: 3703: 3654: 3648: 3647: 3606: 3600: 3599: 3589: 3557: 3551: 3550: 3532: 3492: 3486: 3485: 3475: 3443: 3437: 3436: 3418: 3386: 3380: 3379: 3369: 3359: 3342:(3): 1032–1037. 3327: 3321: 3320: 3310: 3300: 3276: 3270: 3269: 3268: 3267: 3222: 3216: 3215: 3205: 3195: 3163: 3157: 3156: 3146: 3129:(6): 1005–1018. 3114: 3108: 3107: 3097: 3065: 3059: 3058: 3048: 3016: 3010: 3009: 2999: 2967: 2958: 2957: 2947: 2929: 2905: 2899: 2898: 2888: 2856: 2841: 2840: 2806: 2791: 2790: 2780: 2748: 2737: 2736: 2726: 2716: 2692: 2657: 2656: 2646: 2614: 2581: 2580: 2570: 2538: 2532: 2531: 2521: 2497: 2491: 2490: 2462: 2456: 2455: 2445: 2413: 2407: 2406: 2396: 2386: 2362: 2356: 2355: 2350:. Archived from 2327: 2321: 2320: 2310: 2286: 2280: 2279: 2269: 2259: 2227: 2221: 2220: 2192: 2186: 2185: 2160:(7): 1098–1113. 2149: 2143: 2142: 2132: 2115:(8): 3550–3552. 2100: 2091: 2090: 2080: 2070: 2053:(3): 1708–1711. 2038: 2032: 2031: 2021: 1997: 1991: 1990: 1972: 1948: 1942: 1941: 1913: 1907: 1906: 1888: 1864: 1855: 1854: 1826: 1820: 1819: 1809: 1785: 1776: 1775: 1769: 1761: 1751: 1719: 1713: 1712: 1702: 1670: 1661: 1660: 1640: 1634: 1633: 1627: 1623: 1621: 1613: 1571: 1565: 1564: 1536: 1530: 1529: 1519: 1495: 1489: 1487: 1477: 1453: 1447: 1446: 1410: 1404: 1403: 1375: 1369: 1368: 1332: 1268: 1263: 1262: 1030:molecular weight 1025: 962:type I. diabetes 954:immune tolerance 466:and loaded onto 379:protein kinase G 367:oxidative stress 231:RNA thermometers 152:alpha crystallin 21: 5156: 5155: 5151: 5150: 5149: 5147: 5146: 5145: 5131: 5130: 5129: 5120: 5047: 5022:E3 SUMO ligase 4986: 4975: 4967: 4658: 4650: 4623: 4585: 4564: 4556: 4334: 4322:protein folding 4320: 4311: 4306: 4264: 4259: 4223: 4222: 4218: 4174: 4173: 4164: 4134: 4133: 4129: 4083: 4082: 4078: 4064: 4060: 4050: 4048: 4034: 4033: 4029: 3999: 3998: 3994: 3964: 3963: 3959: 3929: 3928: 3924: 3886: 3885: 3881: 3821: 3820: 3816: 3806: 3804: 3793: 3792: 3788: 3752: 3751: 3747: 3717: 3716: 3709: 3701: 3699: 3681: 3656: 3655: 3651: 3608: 3607: 3603: 3559: 3558: 3554: 3494: 3493: 3489: 3445: 3444: 3440: 3388: 3387: 3383: 3329: 3328: 3324: 3278: 3277: 3273: 3265: 3263: 3253: 3224: 3223: 3219: 3165: 3164: 3160: 3116: 3115: 3111: 3067: 3066: 3062: 3018: 3017: 3013: 2969: 2968: 2961: 2907: 2906: 2902: 2858: 2857: 2844: 2829: 2808: 2807: 2794: 2750: 2749: 2740: 2694: 2693: 2660: 2616: 2615: 2584: 2540: 2539: 2535: 2499: 2498: 2494: 2464: 2463: 2459: 2415: 2414: 2410: 2364: 2363: 2359: 2329: 2328: 2324: 2288: 2287: 2283: 2242:(15): 4969–73. 2229: 2228: 2224: 2194: 2193: 2189: 2151: 2150: 2146: 2102: 2101: 2094: 2040: 2039: 2035: 1999: 1998: 1994: 1950: 1949: 1945: 1915: 1914: 1910: 1866: 1865: 1858: 1828: 1827: 1823: 1787: 1786: 1779: 1762: 1721: 1720: 1716: 1672: 1671: 1664: 1642: 1641: 1637: 1624: 1614: 1594: 1573: 1572: 1568: 1538: 1537: 1533: 1497: 1496: 1492: 1455: 1454: 1450: 1415:Pflügers Archiv 1412: 1411: 1407: 1377: 1376: 1372: 1343:(12): 571–573. 1334: 1333: 1326: 1322: 1264: 1257: 1254: 1246:splice variants 1181: 996: 988: 980: 934: 925:clinical trials 905: 858: 856:Cancer vaccines 853: 822: 799: 748: 743: 727: 663: 655: 647: 609: 547:dendritic cells 543: 531: 519: 452: 432: 390: 330: 324:on themselves. 304: 281: 272:D. melanogaster 256:gene expression 251:D. melanogaster 212:stress response 204:stress proteins 160: 147: 110: 28: 23: 22: 15: 12: 11: 5: 5154: 5152: 5144: 5143: 5133: 5132: 5126: 5125: 5122: 5121: 5119: 5118: 5112: 5111: 5106: 5101: 5096: 5091: 5086: 5081: 5071: 5066: 5061: 5055: 5053: 5049: 5048: 5046: 5045: 5044: 5043: 5038: 5033: 5028: 5019: 5018: 5017: 5016: 5007: 5006: 5005: 5004: 4999: 4990: 4988: 4977: 4969: 4968: 4966: 4965: 4960: 4955: 4949: 4948: 4943: 4938: 4928: 4927: 4926: 4925: 4920: 4915: 4910: 4905: 4900: 4888: 4887: 4886: 4885: 4880: 4875: 4870: 4865: 4860: 4854: 4849: 4844: 4839: 4834: 4829: 4824: 4819: 4814: 4809: 4804: 4799: 4794: 4789: 4784: 4779: 4774: 4769: 4764: 4759: 4754: 4749: 4744: 4739: 4734: 4729: 4717: 4716: 4715: 4714: 4709: 4704: 4699: 4694: 4689: 4684: 4679: 4674: 4662: 4660: 4652: 4651: 4649: 4648: 4643: 4641:Signal peptide 4637: 4635: 4629: 4628: 4625: 4624: 4622: 4621: 4620: 4619: 4614: 4604: 4599: 4593: 4591: 4587: 4586: 4584: 4583: 4582: 4581: 4576: 4571: 4566: 4562: 4558: 4554: 4544: 4543: 4542: 4541: 4536: 4531: 4526: 4521: 4516: 4511: 4506: 4501: 4496: 4491: 4486: 4481: 4470: 4469: 4468: 4467: 4462: 4457: 4452: 4447: 4442: 4437: 4432: 4427: 4422: 4417: 4412: 4407: 4402: 4397: 4392: 4387: 4382: 4377: 4366: 4365: 4356: 4351: 4346: 4340: 4338: 4324: 4313: 4312: 4307: 4305: 4304: 4297: 4290: 4282: 4276: 4275: 4263: 4262:External links 4260: 4258: 4257: 4236:(10): 2113–8. 4216: 4187:(1): 105–111. 4162: 4143:(2): 123–132. 4127: 4076: 4058: 4027: 3992: 3957: 3938:(3): 226–256. 3922: 3895:(3): 383–393. 3879: 3814: 3786: 3745: 3726:(1–2): 23–27. 3707: 3679: 3649: 3601: 3552: 3487: 3458:(6): 959–964. 3438: 3401:(5): 523–534. 3381: 3322: 3271: 3251: 3217: 3158: 3109: 3060: 3031:(7): 662–669. 3011: 2959: 2900: 2842: 2827: 2792: 2763:(2): 213–218. 2738: 2658: 2582: 2533: 2492: 2457: 2428:(2): 389–400. 2408: 2357: 2354:on 2013-01-28. 2342:(1–2): 19–35. 2322: 2301:(2): 117–132. 2281: 2222: 2203:(3): 257–261. 2187: 2144: 2092: 2033: 1992: 1943: 1908: 1879:(2): 454–463. 1856: 1837:(3): 389–398. 1821: 1777: 1714: 1685:(2): 166–180. 1662: 1635: 1626:|journal= 1593:978-0471142737 1592: 1566: 1531: 1490: 1448: 1421:(3): 239–244. 1405: 1370: 1323: 1321: 1318: 1317: 1316: 1311: 1306: 1301: 1296: 1291: 1286: 1281: 1276: 1270: 1269: 1266:Biology portal 1253: 1250: 1236: 1235: 1232: 1225: 1219: 1213: 1212: 1209: 1202: 1199: 1193: 1192: 1185: 1162: 1159: 1153: 1152: 1146: 1143: 1140: 1134: 1133: 1130: 1127: 1124: 1118: 1117: 1114: 1103: 1100: 1094: 1093: 1090: 1080: 1075: 1071: 1070: 1067: 1064: 1061: 1055: 1054: 1051: 1045: 1039: 995: 994:Classification 992: 987: 984: 978: 933: 930: 910:small molecule 904: 901: 874:carcinogenesis 857: 854: 852: 849: 821: 818: 798: 795: 781:nthracene), a 755:carcinogenesis 747: 744: 742: 739: 735:α4- crystallin 726: 723: 661: 654: 651: 645: 608: 605: 542: 539: 530: 527: 518: 515: 451: 448: 431: 428: 389: 386: 329: 328:Cardiovascular 326: 303: 300: 280: 277: 159: 156: 146: 143: 109: 106: 26: 24: 14: 13: 10: 9: 6: 4: 3: 2: 5153: 5142: 5139: 5138: 5136: 5117: 5114: 5113: 5110: 5107: 5105: 5102: 5100: 5097: 5095: 5092: 5090: 5087: 5085: 5082: 5079: 5075: 5072: 5070: 5067: 5065: 5062: 5060: 5057: 5056: 5054: 5050: 5042: 5039: 5037: 5034: 5032: 5029: 5027: 5024: 5023: 5021: 5020: 5015: 5012: 5011: 5009: 5008: 5003: 5000: 4998: 4995: 4994: 4992: 4991: 4989: 4987:(SUMOylation) 4985: 4981: 4978: 4974: 4970: 4964: 4961: 4959: 4956: 4954: 4951: 4950: 4947: 4944: 4942: 4939: 4937: 4933: 4930: 4929: 4924: 4921: 4919: 4916: 4914: 4911: 4909: 4906: 4904: 4901: 4899: 4896: 4895: 4894: 4890: 4889: 4884: 4881: 4879: 4876: 4874: 4871: 4869: 4866: 4864: 4861: 4858: 4855: 4853: 4850: 4848: 4845: 4843: 4840: 4838: 4835: 4833: 4830: 4828: 4825: 4823: 4820: 4818: 4815: 4813: 4810: 4808: 4805: 4803: 4800: 4798: 4795: 4793: 4790: 4788: 4785: 4783: 4780: 4778: 4775: 4773: 4770: 4768: 4765: 4763: 4760: 4758: 4755: 4753: 4750: 4748: 4745: 4743: 4740: 4738: 4735: 4733: 4730: 4728: 4725: 4724: 4723: 4719: 4718: 4713: 4710: 4708: 4705: 4703: 4700: 4698: 4695: 4693: 4690: 4688: 4685: 4683: 4680: 4678: 4675: 4673: 4670: 4669: 4668: 4664: 4663: 4661: 4657: 4653: 4647: 4644: 4642: 4639: 4638: 4636: 4634: 4630: 4618: 4615: 4613: 4610: 4609: 4608: 4605: 4603: 4600: 4598: 4595: 4594: 4592: 4588: 4580: 4577: 4575: 4572: 4570: 4567: 4565: 4559: 4557: 4551: 4550: 4549: 4546: 4545: 4540: 4537: 4535: 4532: 4530: 4527: 4525: 4522: 4520: 4517: 4515: 4512: 4510: 4507: 4505: 4502: 4500: 4497: 4495: 4492: 4490: 4487: 4485: 4482: 4480: 4477: 4476: 4475: 4472: 4471: 4466: 4463: 4461: 4458: 4456: 4453: 4451: 4448: 4446: 4443: 4441: 4438: 4436: 4433: 4431: 4428: 4426: 4423: 4421: 4418: 4416: 4413: 4411: 4408: 4406: 4403: 4401: 4398: 4396: 4393: 4391: 4388: 4386: 4383: 4381: 4378: 4376: 4373: 4372: 4371: 4368: 4367: 4364: 4360: 4357: 4355: 4352: 4350: 4347: 4345: 4342: 4341: 4339: 4337: 4332: 4328: 4325: 4323: 4318: 4314: 4310: 4303: 4298: 4296: 4291: 4289: 4284: 4283: 4280: 4273: 4269: 4266: 4265: 4261: 4253: 4249: 4244: 4239: 4235: 4231: 4227: 4220: 4217: 4212: 4208: 4203: 4198: 4194: 4190: 4186: 4182: 4178: 4171: 4169: 4167: 4163: 4158: 4154: 4150: 4146: 4142: 4138: 4131: 4128: 4123: 4119: 4114: 4109: 4104: 4099: 4095: 4091: 4087: 4080: 4077: 4074: 4070: 4069: 4062: 4059: 4046: 4042: 4038: 4031: 4028: 4023: 4019: 4015: 4011: 4007: 4003: 3996: 3993: 3988: 3984: 3980: 3976: 3972: 3968: 3961: 3958: 3953: 3949: 3945: 3941: 3937: 3933: 3926: 3923: 3918: 3914: 3910: 3906: 3902: 3898: 3894: 3890: 3883: 3880: 3875: 3871: 3866: 3861: 3857: 3853: 3849: 3845: 3841: 3837: 3833: 3829: 3825: 3818: 3815: 3803: 3802: 3797: 3790: 3787: 3782: 3778: 3773: 3768: 3764: 3760: 3756: 3749: 3746: 3741: 3737: 3733: 3729: 3725: 3721: 3714: 3712: 3708: 3698: 3694: 3690: 3686: 3682: 3676: 3672: 3668: 3664: 3660: 3653: 3650: 3645: 3641: 3637: 3633: 3629: 3625: 3621: 3617: 3613: 3605: 3602: 3597: 3593: 3588: 3583: 3579: 3575: 3572:(3): e24274. 3571: 3567: 3563: 3556: 3553: 3548: 3544: 3540: 3536: 3531: 3526: 3522: 3518: 3514: 3510: 3507:(2): 100995. 3506: 3502: 3498: 3491: 3488: 3483: 3479: 3474: 3469: 3465: 3461: 3457: 3453: 3449: 3442: 3439: 3434: 3430: 3426: 3422: 3417: 3412: 3408: 3404: 3400: 3396: 3392: 3385: 3382: 3377: 3373: 3368: 3363: 3358: 3353: 3349: 3345: 3341: 3337: 3333: 3326: 3323: 3318: 3314: 3309: 3304: 3299: 3294: 3290: 3286: 3282: 3275: 3272: 3262: 3258: 3254: 3252:9780444534804 3248: 3244: 3240: 3236: 3232: 3228: 3221: 3218: 3213: 3209: 3204: 3199: 3194: 3189: 3185: 3181: 3178:(5): e96330. 3177: 3173: 3169: 3162: 3159: 3154: 3150: 3145: 3140: 3136: 3132: 3128: 3124: 3120: 3113: 3110: 3105: 3101: 3096: 3091: 3087: 3083: 3079: 3075: 3071: 3064: 3061: 3056: 3052: 3047: 3042: 3038: 3034: 3030: 3026: 3022: 3015: 3012: 3007: 3003: 2998: 2993: 2989: 2985: 2981: 2977: 2973: 2966: 2964: 2960: 2955: 2951: 2946: 2941: 2937: 2933: 2928: 2923: 2919: 2915: 2911: 2904: 2901: 2896: 2892: 2887: 2882: 2878: 2874: 2870: 2866: 2862: 2855: 2853: 2851: 2849: 2847: 2843: 2838: 2834: 2830: 2828:9780128022900 2824: 2820: 2816: 2812: 2805: 2803: 2801: 2799: 2797: 2793: 2788: 2784: 2779: 2774: 2770: 2766: 2762: 2758: 2754: 2747: 2745: 2743: 2739: 2734: 2730: 2725: 2720: 2715: 2710: 2706: 2702: 2698: 2691: 2689: 2687: 2685: 2683: 2681: 2679: 2677: 2675: 2673: 2671: 2669: 2667: 2665: 2663: 2659: 2654: 2650: 2645: 2640: 2636: 2632: 2628: 2624: 2620: 2613: 2611: 2609: 2607: 2605: 2603: 2601: 2599: 2597: 2595: 2593: 2591: 2589: 2587: 2583: 2578: 2574: 2569: 2564: 2560: 2556: 2552: 2548: 2544: 2537: 2534: 2529: 2525: 2520: 2515: 2511: 2507: 2503: 2496: 2493: 2488: 2484: 2480: 2476: 2472: 2468: 2461: 2458: 2453: 2449: 2444: 2439: 2435: 2431: 2427: 2423: 2419: 2412: 2409: 2404: 2400: 2395: 2390: 2385: 2380: 2376: 2372: 2368: 2361: 2358: 2353: 2349: 2345: 2341: 2337: 2333: 2326: 2323: 2318: 2314: 2309: 2304: 2300: 2296: 2292: 2285: 2282: 2277: 2273: 2268: 2263: 2258: 2253: 2249: 2245: 2241: 2237: 2233: 2226: 2223: 2218: 2214: 2210: 2206: 2202: 2198: 2191: 2188: 2183: 2179: 2175: 2171: 2167: 2163: 2159: 2155: 2148: 2145: 2140: 2136: 2131: 2126: 2122: 2118: 2114: 2110: 2106: 2099: 2097: 2093: 2088: 2084: 2079: 2074: 2069: 2064: 2060: 2056: 2052: 2048: 2044: 2037: 2034: 2029: 2025: 2020: 2015: 2011: 2007: 2003: 1996: 1993: 1988: 1984: 1980: 1976: 1971: 1966: 1962: 1958: 1954: 1947: 1944: 1939: 1935: 1931: 1927: 1923: 1919: 1912: 1909: 1904: 1900: 1896: 1892: 1887: 1882: 1878: 1874: 1870: 1863: 1861: 1857: 1852: 1848: 1844: 1840: 1836: 1832: 1825: 1822: 1817: 1813: 1808: 1803: 1799: 1795: 1791: 1784: 1782: 1778: 1773: 1767: 1759: 1755: 1750: 1745: 1741: 1737: 1733: 1729: 1725: 1718: 1715: 1710: 1706: 1701: 1696: 1692: 1688: 1684: 1680: 1676: 1669: 1667: 1663: 1658: 1654: 1651:(1–3): 3–20. 1650: 1646: 1639: 1636: 1631: 1619: 1611: 1607: 1603: 1599: 1595: 1589: 1585: 1581: 1577: 1570: 1567: 1562: 1558: 1554: 1550: 1546: 1542: 1535: 1532: 1527: 1523: 1518: 1513: 1509: 1505: 1501: 1494: 1491: 1485: 1481: 1476: 1471: 1467: 1463: 1459: 1452: 1449: 1444: 1440: 1436: 1432: 1428: 1424: 1420: 1416: 1409: 1406: 1401: 1397: 1393: 1389: 1385: 1381: 1374: 1371: 1366: 1362: 1358: 1354: 1350: 1346: 1342: 1338: 1331: 1329: 1325: 1319: 1315: 1312: 1310: 1307: 1305: 1302: 1300: 1297: 1295: 1292: 1290: 1287: 1285: 1282: 1280: 1277: 1275: 1272: 1271: 1267: 1261: 1256: 1251: 1249: 1247: 1243: 1242:co-chaperones 1233: 1230: 1226: 1224: 1220: 1218: 1215: 1214: 1210: 1207: 1203: 1200: 1198: 1195: 1194: 1190: 1186: 1184: 1179: 1175: 1171: 1167: 1163: 1160: 1158: 1155: 1154: 1151: 1147: 1145:Hsp60 (HSPE) 1144: 1141: 1139: 1136: 1135: 1131: 1128: 1125: 1123: 1120: 1119: 1115: 1112: 1108: 1104: 1101: 1099: 1096: 1095: 1091: 1089: 1085: 1081: 1079: 1076: 1073: 1072: 1068: 1066:Hsp10 (HSPD) 1065: 1062: 1060: 1057: 1056: 1052: 1049: 1046: 1043: 1040: 1038: 1036: 1031: 1027: 1026: 1023: 1021: 1017: 1013: 1009: 1005: 1001: 993: 991: 985: 983: 981: 974: 970: 965: 963: 959: 955: 951: 947: 943: 939: 931: 929: 926: 922: 918: 915:, especially 914: 911: 902: 900: 898: 894: 890: 885: 883: 879: 875: 871: 867: 863: 855: 850: 848: 846: 842: 841: 836: 832: 827: 819: 817: 815: 811: 807: 806:hyperglycemia 803: 796: 794: 792: 788: 784: 780: 776: 772: 768: 764: 760: 759:knockout mice 756: 752: 745: 740: 738: 736: 732: 724: 722: 720: 716: 711: 709: 705: 701: 697: 693: 688: 685: 683: 679: 675: 671: 666: 664: 652: 650: 648: 641: 637: 632: 630: 626: 622: 618: 614: 606: 604: 601: 599: 594: 592: 588: 584: 580: 576: 572: 568: 563: 560: 556: 552: 548: 540: 538: 536: 528: 526: 524: 516: 514: 510: 508: 504: 500: 496: 492: 488: 484: 480: 475: 473: 469: 465: 461: 457: 449: 447: 445: 441: 437: 429: 427: 424: 422: 418: 414: 410: 406: 402: 398: 393: 387: 385: 382: 380: 374: 370: 368: 363: 361: 357: 353: 349: 347: 343: 339: 335: 327: 325: 323: 318: 315: 312: 310: 301: 299: 297: 292: 290: 286: 278: 276: 273: 269: 265: 264:messenger RNA 261: 257: 253: 252: 246: 244: 240: 236: 232: 227: 225: 221: 215: 213: 209: 205: 201: 197: 193: 189: 185: 181: 177: 173: 169: 165: 157: 155: 153: 144: 142: 140: 136: 132: 128: 124: 120: 116: 107: 105: 103: 99: 95: 91: 87: 82: 80: 76: 72: 68: 64: 60: 56: 52: 48: 44: 40: 36: 32: 19: 4984:SUMO protein 4330: 4233: 4229: 4219: 4184: 4180: 4140: 4136: 4130: 4093: 4089: 4079: 4066: 4061: 4049:. Retrieved 4045:the original 4040: 4030: 4005: 4001: 3995: 3970: 3966: 3960: 3935: 3931: 3925: 3892: 3888: 3882: 3834:(1): 16106. 3831: 3827: 3817: 3805:. Retrieved 3799: 3789: 3762: 3758: 3748: 3723: 3719: 3700:, retrieved 3662: 3652: 3619: 3615: 3604: 3569: 3565: 3555: 3504: 3500: 3490: 3455: 3451: 3441: 3398: 3394: 3384: 3339: 3335: 3325: 3288: 3284: 3274: 3264:, retrieved 3234: 3230: 3220: 3175: 3171: 3161: 3126: 3122: 3112: 3077: 3073: 3063: 3028: 3025:EMBO Reports 3024: 3014: 2982:(1): 51–59. 2979: 2975: 2920:(18): 4721. 2917: 2913: 2903: 2868: 2864: 2810: 2760: 2756: 2704: 2700: 2626: 2622: 2553:(1): 44–54. 2550: 2546: 2536: 2509: 2505: 2495: 2473:(1): 30–36. 2470: 2466: 2460: 2425: 2421: 2411: 2374: 2370: 2360: 2352:the original 2339: 2335: 2325: 2298: 2294: 2284: 2239: 2235: 2225: 2200: 2196: 2190: 2157: 2153: 2147: 2112: 2108: 2050: 2046: 2036: 2012:(1): 84–89. 2009: 2005: 1995: 1963:(1): 61–71. 1960: 1956: 1946: 1924:(1): 55–63. 1921: 1917: 1911: 1876: 1872: 1834: 1830: 1824: 1797: 1793: 1766:cite journal 1734:(2): 97–98. 1731: 1727: 1717: 1682: 1678: 1648: 1644: 1638: 1575: 1569: 1544: 1540: 1534: 1507: 1503: 1493: 1465: 1461: 1451: 1418: 1414: 1408: 1383: 1379: 1373: 1340: 1337:Experimental 1336: 1309:ROSE element 1289:Co-chaperone 1239: 1221:ClpB, ClpA, 1201:HtpG, C62.5 1182: 1032: 1028:Approximate 997: 989: 986:Agricultural 966: 935: 906: 893:immunisation 886: 862:presentation 859: 851:Applications 838: 823: 800: 778: 774: 770: 766: 749: 728: 712: 689: 686: 667: 656: 633: 610: 602: 595: 564: 544: 532: 520: 511: 503:calreticulin 476: 453: 433: 425: 412: 409:calreticulin 394: 391: 383: 375: 371: 364: 358:and soluble 350: 331: 319: 316: 313: 305: 295: 293: 289:conformation 282: 271: 266:rather than 249: 247: 239:ROSE element 233:such as the 228: 216: 211: 208:upregulation 203: 184:trace metals 172:inflammation 161: 148: 111: 83: 63:upregulation 41:produced by 34: 30: 29: 5078:neddylation 4344:Hsp10/GroES 4336:Chaperonins 4096:: 559–568. 4068:NCT01504542 2506:Circulation 2377:: 9067875. 2006:RNA Biology 1547:: 441–469. 1510:(1): 1–12. 1116:Chaperones 1082:In humans: 1042:Prokaryotic 982:cascades). 831:immunoassay 354:binds both 260:translation 188:ultraviolet 127:chromosomes 98:kilodaltons 4370:Hsp40/DnaJ 4317:Chaperones 3702:2022-09-11 3622:: 100211. 3291:: 249205. 3266:2022-08-30 2976:Immunology 1320:References 1284:Chaperonin 1172:), Grp78 ( 1168:), Hsp72 ( 1150:chaperonin 1074:20–30 kDa 1048:Eukaryotic 936:Acting as 897:autologous 731:crystallin 585:, hsp110, 491:proteasome 479:proteasome 456:proteasome 309:proteasome 302:Management 285:chaperones 206:and their 192:starvation 135:chaperones 131:Drosophila 51:heat shock 4656:Ubiquitin 4602:Clusterin 4051:9 January 3856:2045-2322 3697:237291365 3644:251559265 3636:2590-1370 3547:229324108 3521:1936-5233 3433:250114357 2936:2072-6694 1628:ignored ( 1618:cite book 1357:0014-4754 1279:Chaperone 1113:or HspB1 1098:20-30 kDa 1053:Function 1050:proteins 1044:proteins 1010:/HSP110, 889:oncogenes 814:biomarker 791:apoptosis 529:Autophagy 444:autophagy 421:integrins 336:, hsp70, 168:infection 125:" in the 108:Discovery 102:ubiquitin 55:chaperone 47:stressful 5135:Category 4936:Ataxin 3 4211:18663603 4157:15831376 4122:32161482 4022:16842157 3987:18045130 3952:28012700 3917:42072204 3909:18393608 3874:34373574 3807:10 April 3781:17684010 3740:17980980 3689:34432285 3596:33546049 3566:Medicine 3539:33338880 3482:20496051 3425:35767179 3317:25814786 3261:25410224 3212:24800749 3172:PLOS ONE 3153:17889646 3104:21576228 3055:18451878 3006:28804903 2954:34572948 2895:25953005 2837:26916006 2787:26786410 2733:22566944 2653:25480955 2577:18579210 2528:15809372 2487:15978441 2452:23850773 2403:29387296 2348:17641392 2217:15777275 2174:12491239 2028:20009504 1987:11316659 1979:12679035 1938:10605935 1903:25079120 1895:18161059 1709:24140541 1610:11858453 1602:18432918 1443:28219505 1435:10398851 1365:32525462 1252:See also 1227:Hsp104 ( 882:NK cells 845:oncomirs 840:in-vitro 674:exosomes 670:necrosis 388:Immunity 241:and the 224:protease 145:Function 139:bacteria 75:bacteria 39:proteins 4859:(CDC34) 4252:2269877 4202:2673902 4113:7051252 3865:8352880 3836:Bibcode 3587:7837937 3530:7749402 3473:3024058 3416:9485348 3376:8577709 3344:Bibcode 3308:4357135 3203:4011729 3180:Bibcode 3144:2586609 3095:3159435 3046:2475325 2997:5721256 2945:8466959 2914:Cancers 2886:4623969 2778:4786535 2724:3342350 2644:4304677 2568:2581864 2443:3777613 2394:5745714 2317:9686751 2276:3927294 2244:Bibcode 2182:8509592 2139:3145413 2087:6785759 2055:Bibcode 1851:4219221 1816:2197269 1758:9222594 1700:3924900 1657:1668897 1561:8689565 1526:9921710 1484:9774628 1400:7631901 1217:100 kDa 923:was in 870:vaccine 787:aptamer 783:mutagen 757:. HSF1 413:in vivo 196:hypoxia 190:light, 180:arsenic 176:ethanol 123:puffing 4903:Cullin 4274:(MeSH) 4250:  4209:  4199:  4155:  4120:  4110:  4020:  3985:  3950:  3915:  3907:  3872:  3862:  3854:  3779:  3738:  3695:  3687:  3677:  3642:  3634:  3594:  3584:  3545:  3537:  3527:  3519:  3480:  3470:  3431:  3423:  3413:  3374:  3364:  3315:  3305:  3259:  3249:  3210:  3200:  3151:  3141:  3102:  3092:  3053:  3043:  3004:  2994:  2952:  2942:  2934:  2893:  2883:  2835:  2825:  2785:  2775:  2731:  2721:  2707:: 63. 2651:  2641:  2575:  2565:  2526:  2485:  2450:  2440:  2401:  2391:  2346:  2315:  2274:  2267:390479 2264:  2215:  2180:  2172:  2137:  2130:363594 2127:  2085:  2078:319202 2075:  2026:  1985:  1977:  1936:  1901:  1893:  1849:  1814:  1756:  1749:248460 1746:  1707:  1697:  1655:  1608:  1600:  1590:  1559:  1524:  1482:  1441:  1433:  1398:  1363:  1355:  1197:90 kDa 1178:HSPA1B 1170:HSPA1A 1157:70 kDa 1138:60 kDa 1122:40 kDa 1102:Hsp20 1063:GroES 1059:10 kDa 1016:HSP100 921:17-AAG 826:cancer 820:Cancer 765:(7,12- 729:Alpha 715:cancer 591:GRP170 344:, and 200:oxygen 182:, and 164:stress 79:humans 5094:ATG12 5084:FAT10 5074:NEDD8 5059:ISG15 5052:Other 5041:PIAS4 5036:PIAS3 5031:PIAS2 5026:PIAS1 4976:(UBL) 4958:BIRC6 4918:FANCL 4590:Other 4579:TRAP1 4548:Hsp90 4474:Hsp70 4363:GroEL 4359:HSP60 4354:Hsp47 4349:Hsp27 3913:S2CID 3693:S2CID 3640:S2CID 3543:S2CID 3429:S2CID 3367:40025 2178:S2CID 1983:S2CID 1899:S2CID 1606:S2CID 1504:Shock 1439:S2CID 1361:S2CID 1206:HSPC4 1166:HSPA8 1161:DnaK 1126:DnaJ 1111:HSPB6 1107:Hsp27 1088:GRPE2 1084:GRPE1 1020:sHSPs 1012:HSP90 1008:HSP70 1004:HSP60 1000:HSP33 938:DAMPs 917:Hsp90 878:STAT1 835:ELISA 773:ethyl 746:HSF 1 583:hsp90 579:hsp70 575:hsp60 571:hsp70 567:hsp60 555:LOX-1 495:hsp70 487:Hsp90 401:hsp90 397:hsp70 352:Hsp90 342:hsp20 338:hsp27 334:hsp84 94:Hsp90 90:Hsp70 86:Hsp60 43:cells 5109:UBL5 5099:FUB1 5089:ATG8 5069:UFM1 5064:URM1 5014:UBC9 5002:SAE2 4997:SAE1 4963:UFC1 4953:ATG3 4946:CYLD 4941:USP6 4923:UBR1 4913:MDM2 4712:SAE1 4707:NAE1 4702:ATG7 4697:UBA7 4692:UBA6 4687:UBA5 4682:UBA3 4677:UBA2 4672:UBA1 4617:SMN2 4612:SMN1 4248:PMID 4207:PMID 4153:PMID 4118:PMID 4053:2018 4018:PMID 3983:PMID 3948:PMID 3905:PMID 3870:PMID 3852:ISSN 3809:2018 3777:PMID 3736:PMID 3685:PMID 3675:ISBN 3632:ISSN 3592:PMID 3535:PMID 3517:ISSN 3478:PMID 3421:PMID 3372:PMID 3313:PMID 3289:2015 3257:PMID 3247:ISBN 3208:PMID 3149:PMID 3123:Cell 3100:PMID 3051:PMID 3002:PMID 2950:PMID 2932:ISSN 2891:PMID 2833:PMID 2823:ISBN 2783:PMID 2729:PMID 2649:PMID 2573:PMID 2524:PMID 2483:PMID 2448:PMID 2399:PMID 2375:2017 2344:PMID 2313:PMID 2272:PMID 2213:PMID 2170:PMID 2135:PMID 2083:PMID 2024:PMID 1975:PMID 1957:Cell 1934:PMID 1891:PMID 1847:PMID 1812:PMID 1772:link 1754:PMID 1705:PMID 1653:PMID 1630:help 1598:PMID 1588:ISBN 1557:PMID 1522:PMID 1480:PMID 1431:PMID 1396:PMID 1353:ISSN 1314:HSF1 1229:CLPB 1223:ClpX 1189:H2O2 1078:GrpE 975:and 973:MAPK 969:PI3K 960:and 833:and 763:DMBA 725:Lens 704:Treg 692:Th17 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Index

Heat-shock protein
proteins
cells
stressful
heat shock
chaperone
transcriptionally
upregulation
heat shock response
heat shock factor
bacteria
humans
Hsp60
Hsp70
Hsp90
kilodaltons
ubiquitin
Ferruccio Ritossa
2,4-dinitrophenol
puffing
chromosomes
Drosophila
chaperones
bacteria
alpha crystallin
stress
infection
inflammation
ethanol
arsenic

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