References
- Richter K, Haslbeck M, Buchner J. The heat shock response: life on the verge of death. Mol Cell 2010;40:253-66
- Tissieres A, Mitchell HK, Tracy UM. Protein synthesis in salivary glands of Drosophila melanogaster: relation to chromosome puffs. J Mol Biol 1974;84:389-98
- Kriehuber T, Rattei T, Weinmaier T, et al. Independent evolution of the core domain and its flanking sequences in small heat shock proteins. FASEB J 2010;24:3633-42
- van den IJssel PR, Norman DG, Quinlan RA. Molecular chaperones: small heat shock proteins in the limelight. Curr Biol 1999;9:R103-R5
- Mymrikov EV, Seit-Nebi AS, Gusev NB. Large potentials of small heat shock proteins. Physiol Rev 2011;91:1123-59
- Boelens WC, Croes Y, De Jong WW. Interaction between alpha B-crystallin and the human 20S proteasomal subunit C8/alpha 7. Bioch Biophys Acta 2001;1544:311-19
- Singh BN, Rao KS, Rao Ch M. Ubiquitin-proteasome-mediated degradation and synthesis of MyoD is modulated by alphaB-crystallin, a small heat shock protein, during muscle differentiation. Biochim Biophys Acta 2010;1803:288-99
- Mao YW, Liu JP, Xiang H, Li DW. Human alphaA- and alphaB-crystallins bind to Bax and Bcl-X(S) to sequester their translocation during staurosporine-induced apoptosis. Cell Death Differ 2004;11:512-26
- Liu S, Li J, Tao Y, Xiao X. Small heat shock protein alphaB-crystallin binds to p53 to sequester its translocation to mitochondria during hydrogen peroxide-induced apoptosis. Biochem Biophys Res Commun 2007;354:109-14
- Kase S, He S, Sonoda S, et al. alphaB-crystallin regulation of angiogenesis by modulation of VEGF. Blood 2010;115:3398-406
- Horwitz J. Alpha-crystallin. Exp Eye Res 2003;76:145-53
- Slingsby C, Wistow GJ, Clark AR. Evolution of crystallins for a role in the vertebrate eye lens. Protein Sci 2013;22:367-80
- Arrigo AP. Human small heat shock proteins: protein interactomes of homo- and hetero-oligomeric complexes: an update. FEBS Lett 2013;587:1959-69
- Kannan R, Sreekumar PG, Hinton DR. Novel roles for alpha-crystallins in retinal function and disease. Prog Retin Eye Res 2012;31:576-604
- Carra S, Rusmini P, Crippa V, et al. Different anti-aggregation and pro-degradative functions of the members of the mammalian sHSP family in neurological disorders. Philos Trans R Soc Lond B Biol Sci 2013;368:20110409
- Kampinga HH, Hageman J, Vos MJ, et al. Guidelines for the nomenclature of the human heat shock proteins. Cell Stress Chaperones 2009;14:105-11
- Sun Y, MacRae TH. The small heat shock proteins and their role in human disease. FEBS J 2005;272:2613-27
- Bakthisaran R, Tangirala R, Rao CM. Small heat shock proteins: Role in cellular functions and pathology. Biochim Biophys Acta 2014;1854:291-319
- Kampinga HH, Garrido C. HSPBs: small proteins with big implications in human disease. Int J Biochem Cell Biol 2012;44:1706-10
- Kappe G, Franck E, Verschuure P, et al. The human genome encodes 10 alpha-crystallin-related small heat shock proteins: HspB1-10. Cell Stress Chaperones 2003;8:53-61
- Perng MD, Muchowski PJ, Clarke JI, et al. Divergence in the effects upon intermediate filaments of the cataract inducing mutation R120G within the sHSP family. Invest Opht Vis Sci 2001;42:S874-S
- Irobi J, Van Impe K, Seeman P, et al. Hot-spot residue in small heat-shock protein 22 causes distal motor neuropathy. Nat Genet 2004;36:597-601
- Braun N, Zacharias M, Peschek J, et al. Multiple molecular architectures of the eye lens chaperone alphaB-crystallin elucidated by a triple hybrid approach. Proc Natl Acad Sci USA 2011;108:20491-6
- Peschek J, Braun N, Rohrberg J, et al. Regulated structural transitions unleash the chaperone activity of alphaB-crystallin. Proc Natl Acad Sci USA 2013;110:E3780-9
- Laganowsky A, Benesch JL, Landau M, et al. Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function. Protein Sci 2010;19:1031-43
- Hochberg GK, Ecroyd H, Liu C, et al. The structured core domain of alphaB-crystallin can prevent amyloid fibrillation and associated toxicity. Proc Natl Acad Sci USA 2014;111:E1562-70
- Jehle S, Rajagopal P, Bardiaux B, et al. Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers. Nat Struct Mol Biol 2010;17:1037-42
- Delbecq SP, Klevit RE. One size does not fit all: the oligomeric states of alphaB crystallin. FEBS Lett 2013;587:1073-80
- Baranova EV, Weeks SD, Beelen S, et al. Three-Dimensional Structure of alpha-Crystallin Domain Dimers of Human Small Heat Shock Proteins HSPB1 and HSPB6. J Mol Biol 2011;411:110-22
- Garrido C, Paul C, Seigneuric R, Kampinga HH. The small heat shock proteins family: the long forgotten chaperones. Int J Biochem Cell Biol 2012;44:1588-92
- De Jong WW, Caspers GJ, Leunissen JA. Genealogy of the alpha-crystallin–small heat-shock protein superfamily. Int J Biol Macromol 1998;22:151-62
- Haslbeck M, Vierling E. A First Line of Stress Defense: Small Heat Shock Proteins and their function in protein homeostasis. J Mol Biol 2015;427(7):1537-48
- Caspers GJ, Leunissen JA, De Jong WW. The expanding small heat-shock protein family, and structure predictions of the conserved "alpha-crystallin domain". J Mol Evol 1995;40:238-48
- Bagneris C, Bateman OA, Naylor CE, et al. Crystal structures of alpha-crystallin domain dimers of alphaB-crystallin and Hsp20. J Mol Biol 2009;392:1242-52
- Clark AR, Naylor CE, Bagneris C, et al. Crystal structure of R120G disease mutant of human alphaB-crystallin domain dimer shows closure of a groove. J Mol Biol 2011;408:118-34
- Jehle S, Vollmar BS, Bardiaux B, et al. N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity. Proc Natl Acad Sci USA 2011;108:6409-14
- Hilton GR, Benesch JL. Two decades of studying non-covalent biomolecular assemblies by means of electrospray ionization mass spectrometry. J R So Interface 2012;9:801-16
- Basha E, O’Neill H, Vierling E. Small heat shock proteins and alpha-crystallins: dynamic proteins with flexible functions. Trends Biochem Sci 2012;37:106-17
- McHaourab HS, Lin YL, Spiller BW. Crystal structure of an activated variant of small heat shock protein Hsp16.5. Biochemistry 2012;51:5105-12
- Haslbeck M, Weinkauf S, Buchner J. Regulation of the chaperone function of small Hsps. In: Tanguay RM, Hightower LE, editors. The Small HSP World. Cham: Springer International Publishing, Switzerland 2015; ISBN: 978-3-319-16076-4; in press
- Jakob U, Gaestel M, Engel K, Buchner J. Small heat shock proteins are molecular chaperones. J Biol Chem 1993;268:1517-20
- Horwitz J. Alpha-crystallin can function as a molecular chaperone. Proc Natl Acad Sci USA 1992;89:10449-53
- De Jong WW, Leunissen JA, Voorter CE. Evolution of the alpha-crystallin/small heat-shock protein family. Mol Biol Evol 1993;10:103-26
- Haslbeck M, Miess A, Stromer T, et al. Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104. J Biol Chem 2005;280:23861-8
- Stromer T, Ehrnsperger M, Gaestel M, Buchner J. Analysis of the interaction of small heat shock proteins with unfolding proteins. J Biol Chem 2003;278:18015-21
- Stengel F, Baldwin AJ, Painter AJ, et al. Quaternary dynamics and plasticity underlie small heat shock protein chaperone function. Proc Natl Acad Sci USA 2010;107:2007-12
- Ehrnsperger M, Graber S, Gaestel M, Buchner J. Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J 1997;16:221-9
- Kampinga HH, Brunsting JF, Stege GJ, et al. Cells overexpressing Hsp27 show accelerated recovery from heat-induced nuclear protein aggregation. Biochem Biophys Res Commun 1994;204:1170-7
- Mogk A, Deuerling E, Vorderwulbecke S, et al. Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation. Mol Microbiol 2003;50:585-95
- Lee GJ, Roseman AM, Saibil HR, Vierling E. A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J 1997;16:659-71
- Veinger L, Diamant S, Buchner J, Goloubinoff P. The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network. J Biol Chem 1998;273:11032-7
- Basha E, Lee GJ, Breci LA, et al. The identity of proteins associated with a small heat shock protein during heat stress in vivo indicates that these chaperones protect a wide range of cellular functions. J Biol Chem 2004;279:7566-75
- Haslbeck M, Braun N, Stromer T, et al. Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae. EMBO J 2004;23:638-49
- Bepperling A, Alte F, Kriehuber T, et al. Alternative bacterial two-component small heat shock protein systems. Proc Natl Acad Sci USA 2012;109:20407-12
- Fu X, Shi X, Yan L, et al. In vivo substrate diversity and preference of small heat shock protein IbpB as revealed by using a genetically incorporated photo-cross-linker. J Biol Chem 2013;288:31646-54
- Fan Q, Huang LZ, Zhu XJ, et al. Identification of proteins that interact with alpha A-crystallin using a human proteome microarray. Mol Vis 2014;20:117-24
- Cheng C, Xia CH, Huang Q, et al. Altered chaperone-like activity of alpha-crystallins promotes cataractogensis. J Biol Chem 2010;285:41187-93
- Andley UP, Malone JP, Townsend RR. In vivo substrates of the lens molecular chaperone alphaA-crystallin and alphaB-crystallin. PLoS One 2014;9:e95507
- Arrigo AP, Gibert P. HspB1, HspB5 and HspB4 in human cancers: potent oncogenic role of some of their client proteins. Cancers 2014;6:333-65
- Voss OH, Batra S, Kolattukudy SJ, et al. Binding of caspase-3 prodomain to heat shock protein 27 regulates monocyte apoptosis by inhibiting caspase-3 proteolytic activation. J Biol Chem 2007;282:25088-99
- Pandey P, Farber R, Nakazawa A, et al. Hsp27 functions as a negative regulator of cytochrome c-dependent activation of procaspase-3. Oncogene 2000;19:1975-81
- Hu WF, Gong L, Cao Z, et al. alphaA- and alphaB-crystallins interact with caspase-3 and Bax to guard mouse lens development. Curr Mol Med 2012;12:177-87
- Gonzalez-Mejia ME, Voss OH, Murnan EJ, Doseff AI. Apigenin-induced apoptosis of leukemia cells is mediated by a bimodal and differentially regulated residue-specific phosphorylation of heat-shock protein-27. Cell Death Dis 2010;1:e64
- Acunzo J, Katsogiannou M, Rocchi P. Small heat shock proteins HSP27 (HspB1), alphaB-crystallin (HspB5) and HSP22 (HspB8) as regulators of cell death. Int J Biochem Cell Biol 2012;44:1622-31
- Andrieu C, Taieb D, Baylot V, et al. Heat shock protein 27 confers resistance to androgen ablation and chemotherapy in prostate cancer cells through eIF4E. Oncogene 2010;29:1883-96
- Kostenko S, Moens U. Heat shock protein 27 phosphorylation: kinases, phosphatases, functions and pathology. Cell Mol Life Sci 2009;66:3289-307
- de Wit NJ, Verschuure P, Kappe G, et al. Testis-specific human small heat shock protein HSPB9 is a cancer/testis antigen, and potentially interacts with the dynein subunit TCTEL1. Eur J Cell Biol 2004;83:337-45
- Arrigo AP, Gibert B. Protein interactomes of three stress inducible small heat shock proteins: HspB1, HspB5 and HspB8. Int J Hyperthermia 2013;29:409-22
- Perng MD, Cairns L, van den IJssel P, et al. Intermediate filament interactions can be altered by HSP27 and alphaB-crystallin. J Cell Sci 1999;112. Pt 13 2099-112
- Kayser J, Haslbeck M, Dempfle L, et al. The small heat shock protein Hsp27 affects assembly dynamics and structure of keratin intermediate filament networks. Biophys J 2013;105:1778-85
- Cox D, Carver JA, Ecroyd H. Preventing alpha-synuclein aggregation: the role of the small heat-shock molecular chaperone proteins. Biochim Biophys Acta 2014;1842:1830-43
- Treweek TM, Meehan S, Ecroyd H, Carver JA. Small heat-shock proteins: important players in regulating cellular proteostasis. Cell Mol Life Sci 2015;72:429-51
- Duennwald ML, Echeverria A, Shorter J. Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans. PLoS Biol 2012;10:e1001346
- Sharma KK, Kumar GS, Murphy AS, Kester K. Identification of 1,1’-bi(4-anilino)naphthalene-5,5’-disulfonic acid binding sequences in alpha-crystallin. J Biol Chem 1998;273:15474-8
- Ghosh JG, Shenoy AKJr, Clark JI. Interactions between important regulatory proteins and human alphaB crystallin. Biochemistry 2007;46:6308-17
- Ahrman E, Lambert W, Aquilina JA, et al. Chemical cross-linking of the chloroplast localized small heat-shock protein, Hsp21, and the model substrate citrate synthase. Protein Sci 2007;16:1464-78
- Jaya N, Garcia V, Vierling E. Substrate binding site flexibility of the small heat shock protein molecular chaperones. Proc Natl Acad Sci USA 2009;106:15604-9
- Cheng G, Basha E, Wysocki VH, Vierling E. Insights into small heat shock protein and substrate structure during chaperone action derived from hydrogen/deuterium exchange and mass spectrometry. J Biol Chem 2008;283:26634-42
- Ghosh JG, Estrada MR, Clark JI. Interactive domains for chaperone activity in the small heat shock protein, human alphaB crystallin. Biochemistry 2005;44:14854-69
- Bhattacharyya J, Padmanabha Udupa EG, Wang J, Sharma KK. Mini-alphaB-crystallin: a functional element of alphaB-crystallin with chaperone-like activity. Biochemistry 2006;45:3069-76
- Banerjee PR, Pande A, Shekhtman A, Pande J. Molecular Mechanism of the Chaperone Function of Mini-alpha-Crystallin, a 19-Residue Peptide of Human alpha-Crystallin. Biochemistry 2015;54:505-15
- Treweek TM, Rekas A, Walker MJ, Carver JA. A quantitative NMR spectroscopic examination of the flexibility of the C-terminal extensions of the molecular chaperones, alphaA- and alphaB-crystallin. Exp Eye Res 2010;91:691-9
- Horwitz J. The function of alpha-crystallin in vision. Semin Cell Dev Biol 2000;11:53-
- Gamerdinger M, Carra S, Behl C. Emerging roles of molecular chaperones and co-chaperones in selective autophagy: focus on BAG proteins. J Mol Med 2011;89:1175-82
- Minoia M, Boncoraglio A, Vinet J, et al. BAG3 induces the sequestration of proteasomal clients into cytoplasmic puncta: implications for a proteasome-to-autophagy switch. Autophagy 2014;10:1603-21
- Rayner K, Chen YX, McNulty M, et al. Extracellular release of the atheroprotective heat shock protein 27 is mediated by estrogen and competitively inhibits acLDL binding to scavenger receptor-A. Circ Res 2008;103:133-41
- Clayton A, Turkes A, Navabi H, et al. Induction of heat shock proteins in B-cell exosomes. J Cell Sci 2005;118:3631-8
- van Noort JM, Bsibsi M, Nacken P, et al. The link between small heat shock proteins and the immune system. Int J Biochem Cell Biol 2012;44:1670-9
- Henderson B, Pockley AG. Molecular chaperones and protein-folding catalysts as intercellular signaling regulators in immunity and inflammation. J Leukoc Biol 2010;88:445-62
- Pockley AG, Henderson B, Multhoff G. Extracellular cell stress proteins as biomarkers of human disease. Biochemi Soc Trans 2014;42:1744-51
- Sreekumar PG, Kannan R, Kitamura M, et al. alphaB crystallin is apically secreted within exosomes by polarized human retinal pigment epithelium and provides neuroprotection to adjacent cells. PLoS One 2010;5:e12578
- Gangalum RK, Atanasov IC, Zhou ZH, Bhat SP. AlphaB-crystallin is found in detergent-resistant membrane microdomains and is secreted via exosomes from human retinal pigment epithelial cells. J Biol Chem 2011;286:3261-9
- Bsibsi M, Holtman IR, Gerritsen WH, et al. Alpha-B-crystallin induces an immune-regulatory and antiviral microglial response in preactive multiple sclerosis lesions. J Neuropathol Exp Neurol 2013;72:970-9
- Bruinsma IB, de Jager M, Carrano A, et al. Small heat shock proteins induce a cerebral inflammatory reaction. J Neurosci 2011;31:11992-2000
- Ecroyd H, Carver JA. Crystallin proteins and amyloid fibrils. Cell Mol Life Sci 2009;66:62-81
- Seidel K, Vinet J, Dunnen WF, et al. The HSPB8-BAG3 chaperone complex is upregulated in astrocytes in the human brain affected by protein aggregation diseases. Neuropathol Appl Neurobiol 2012;38:39-53
- Shammas SL, Waudby CA, Wang S, et al. Binding of the molecular chaperone alphaB-crystallin to Abeta amyloid fibrils inhibits fibril elongation. Biophys J 2011;101:1681-9
- Humphreys DT, Carver JA, Easterbrook-Smith SB, Wilson MR. Clusterin has chaperone-like activity similar to that of small heat shock proteins. J Biol Chem 1999;274:6875-81
- Janig E, Haslbeck M, Aigelsreiter A, et al. Clusterin associates with altered elastic fibers in human photoaged skin and prevents elastin from ultraviolet-induced aggregation in vitro. Am J Pathol 2007;171:1474-82
- Walter S, Buchner J. Molecular chaperones-cellular machines for protein folding. Angew Chem Int Ed Engl 2002;41:1098-113
- McHaourab HS, Godar JA, Stewart PL. Structure and mechanism of protein stability sensors: chaperone activity of small heat shock proteins. Biochemistry 2009;48:3828-37
- Basha E, Jones C, Wysocki V, Vierling E. Mechanistic differences between two conserved classes of small heat shock proteins found in the plant cytosol. J Biol Chem 2010;285:11489-97
- Aquilina JA, Benesch JL, Ding LL, et al. Subunit exchange of polydisperse proteins: mass spectrometry reveals consequences of alphaA-crystallin truncation. J Biol Chem 2005;280:14485-91
- Shi J, Koteiche HA, McDonald ET, et al. Cryoelectron microscopy analysis of small heat shock protein 16.5 (Hsp16.5) complexes with T4 lysozyme reveals the structural basis of multimode binding. J Biol Chem 2013;288:4819-30
- Kantorow M, Piatigorsky J. Phosphorylations of alpha A- and alpha B-crystallin. Int J Biol Macromol 1998;22:307-14
- Gaestel M. sHsp-phosphorylation: enzymes, signaling pathways and functional implications. Prog Mol Subcell Biol 2002;28:151-69
- Derham BK, Harding JJ. α-crystallin as a molecular chaperone. Prog Retin Eye Res 1999;18:463-509
- Uniport. Available from: www.uniprot.org
- Moroni M, Garland D. In vitro dephosphorylation of α-crystallin is dependent on the state of oligomerization. Biochim Biophys Acta 2001;1546:282-90
- Hayes D, Napoli V, Mazurkie A, et al. Phosphorylation dependence of hsp27 multimeric size and molecular chaperone function. J Biol Chem 2009;284:18801-7
- Rogalla T, Ehrnsperger M, Preville X, et al. Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor α by phosphorylation. J Biol Chem 1999;274:18947-56
- Gupta R, Srivastava OP. Deamidation affects structural and functional properties of human alphaA-crystallin and its oligomerization with alphaB-crystallin. J Biol Chem 2004;279:44258-69
- Satish Kumar M, Mrudula T, Mitra N, Bhanuprakash Reddy G. Enhanced degradation and decreased stability of eye lens alpha-crystallin upon methylglyoxal modification. Exp Eye Res 2004;79:577-83
- Chen SJ, Sun TX, Akhtar NJ, Liang JJ. Oxidation of human lens recombinant alphaA-crystallin and cysteine-deficient mutants. J Mol Biol 2001;305:969-76
- Chalova AS, Sudnitsyna MV, Semenyuk PI, et al. Effect of disulfide crosslinking on thermal transitions and chaperone-like activity of human small heat shock protein HspB1. Cell Stress Chaperones 2014;19:963-72
- Eaton P, Fuller W, Shattock MJ. S-thiolation of HSP27 regulates its multimeric aggregate size independently of phosphorylation. J Biol Chem 2002;277:21189-96
- Oya-Ito T, Liu BF, Nagaraj RH. Effect of methylglyoxal modification and phosphorylation on the chaperone and anti-apoptotic properties of heat shock protein 27. J Cell Biochem 2006;99:279-91
- Ahmad MF, Singh D, Taiyab A, et al. Selective Cu2+ binding, redox silencing, and cytoprotective effects of the small heat shock proteins alphaA- and alphaB-crystallin. J Mol Biol 2008;382:812-24
- Mainz A, Bardiaux B, Kuppler F, et al. Structural and mechanistic implications of metal binding in the small heat-shock protein alphaB-crystallin. J Biol Chem 2012;287:1128-38
- Zavialov A, Benndorf R, Ehrnsperger M, et al. The effect of the intersubunit disulfide bond on the structural and functional properties of the small heat shock protein Hsp25. Int J Biol Macromol 1998;22:163-73
- Arrigo AP. The cellular “networking” of mammalian Hsp27 and its functions in the control of protein folding, redox state and apoptosis. Adv Exp Med Biol 2007;594:14-26
- Pasupuleti N, Matsuyama S, Voss O, et al. The anti-apoptotic function of human alphaA-crystallin is directly related to its chaperone activity. Cell Death Dis 2010;1:e31
- Christians ES, Ishiwata T, Benjamin IJ. Small heat shock proteins in redox metabolism: implications for cardiovascular diseases. Int J Biochem Cell Biol 2012;44:1632-45
- Horwitz J, Bova MP, Ding LL, et al. Lens alpha-crystallin: function and structure. Eye 1999;13(Pt 3b):403-8
- Sugiyama Y, Suzuki A, Kishikawa M, et al. Muscle develops a specific form of small heat shock protein complex composed of MKBP/HSPB2 and HSPB3 during myogenic differentiation. J Biol Chem 2000;275:1095-104
- Fontaine JM, Sun X, Benndorf R, Welsh MJ. Interactions of HSP22 (HSPB8) with HSP20, alphaB-crystallin, and HSPB3. Biochem Biophys Res Commun 2005;337:1006-11
- Sun XK, Fontaine JM, Rest JS, et al. Interaction of human HSP22 (HSPB8) with other small heat shock proteins. J Biol Chem 2004;279:2394-402
- Rohl A, Rohrberg J, Buchner J. The chaperone Hsp90: changing partners for demanding clients. Trends Biochem Sci 2013;38:253-62
- Chafekar SM, Wisen S, Thompson AD, et al. Pharmacological tuning of heat shock protein 70 modulates polyglutamine toxicity and aggregation. ACS Chem Biol 2012;7:1556-64
- Walter GM, Raveh A, Mok SA, et al. High-throughput screen of natural product extracts in a yeast model of polyglutamine proteotoxicity. Chem Biol Drug Des 2014;83:440-9
- Gibert B, Hadchity E, Czekalla A, et al. Inhibition of heat shock protein 27 (HspB1) tumorigenic functions by peptide aptamers. Oncogene 2011;30:3672-81
- Li X, Colvin T, Rauch JN, et al. Validation of the Hsp70-Bag3 protein-protein interaction as a potential therapeutic target in cancer. Mol Cancer Ther 2015. [Epub ahead of print]
- de Thonel A, Le Mouel A, Mezger V. Transcriptional regulation of small HSP-HSF1 and beyond. Int J Biochem Cell Biol 2012;44:1593-612
- Westerheide SD, Morimoto RI. Heat shock response modulators as therapeutic tools for diseases of protein conformation. J Biol Chem 2005;280:33097-100
- Hosokawa N, Hirayoshi K, Kudo H, et al. Inhibition of the activation of heat shock factor in vivo and in vitro by flavonoids. Mol Cell Biol 1992;12:3490-8
- Hirakawa T, Rokutan K, Nikawa T, Kishi K. Geranylgeranylacetone induces heat shock proteins in cultured guinea pig gastric mucosal cells and rat gastric mucosa. Gastroenterology 1996;111:345-57
- Haldimann P, Muriset M, Vigh L, Goloubinoff P. The novel hydroxylamine derivative NG-094 suppresses polyglutamine protein toxicity in Caenorhabditis elegans. J Biol Chem 2011;286:18784-94
- Kakkar V, Meister-Broekema M, Minoia M, et al. Barcoding heat shock proteins to human diseases: looking beyond the heat shock response. Dis Model Mech 2014;7:421-34
- Azad AA, Zoubeidi A, Gleave ME, Chi KN. Targeting heat shock proteins in metastatic castration-resistant prostate cancer. Nature Rev Urol 2015;12:26-36
- Zoubeidi A, Gleave M. Small heat shock proteins in cancer therapy and prognosis. Int J Biochem Cell Biol 2012;44:1646-56
- Stetler RA, Gao Y, Signore AP, et al. HSP27: mechanisms of cellular protection against neuronal injury. Curr Mol Med 2009;9:863-72
- Ousman SS, Tomooka BH, van Noort JM, et al. Protective and therapeutic role for alphaB-crystallin in autoimmune demyelination. Nature 2007;448:474-9