The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation
Abstract
Heat shock promoters contain one or more binding sites for a specific heat shock factor (HSF). We report the cloning and sequence of the gene encoding yeast HSF, and demonstrate that HSF is required for growth at normal temperatures (15 degrees C-30 degrees C). The activity of a promoter containing a synthetic HSF binding site varies over a 200-fold range between 15 degrees C and 39 degrees C (heat shock). This change in activity is accompanied by multiple changes in the phosphorylation state of HSF, but all forms of HSF are able to bind DNA. We propose that the expression of heat shock genes in yeast is modulated by phosphorylation of DNA-bound HSF, and that this leads to a more efficient interaction of the factor with other components of the transcriptional machinery.
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“Hsf1 is activated by hyperphosphorylation in response to specific environmental cues, which in some fungi include glucose starvation, superoxide, oxygen tension and changes in membrane lipid composition as well as heat shock10,39,45,46.”
From Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs (2012) · cites this paper as [39]
In the citing paper
“Hsf1 is essential for viability in yeasts10,38,39, and is required for the basal expression of HSP genes10,39,40.”
From Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs (2012) · cites this paper as [39]
Citations
Cites
Lindquist, S. L. (1986) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.55.070186.005443 · Cited by 4,611
A short amino acid sequence able to specify nuclear location
Kalderon, D., Roberts, B., Richardson, W. D., & Smith, A. E. (1984) · Cell · doi:10.1016/0092-8674(84)90457-4 · Cited by 2,511
Supercoil Sequencing: A Fast and Simple Method for Sequencing Plasmid DNA
Chen, E. Y., & Seeburg, P. H. (1985) · DNA · doi:10.1089/dna.1985.4.165 · Cited by 2,388
Boeke, J. D., Lacroute, F., & Fink, G. R. (1984) · Molecular and General Genetics MGG · doi:10.1007/bf00330984 · Cited by 2,354
70K heat shock related proteins stimulate protein translocation into microsomes
Chirico, W. J., Waters, M. G., & Blobel, G. (1988) · Nature · doi:10.1038/332805a0 · Cited by 1,232
Yeast RNA Polymerase II Genes: Isolation with Antibody Probes
Young, R. A., & Davis, R. W. (1983) · Science · doi:10.1126/science.6356359 · Cited by 1,077
Sequences That Regulate the Divergent GAL1-GAL10 Promoter in Saccharomyces cerevisiae
Johnston, M., & Davis, R. W. (1984) · Molecular and Cellular Biology · doi:10.1128/mcb.4.8.1440-1448.1984 · Cited by 980
Functional dissection of a eukaryotic transcriptional activator protein, GCN4 of Yeast
Hope, I. A., & Struhl, K. (1986) · Cell · doi:10.1016/0092-8674(86)90070-x · Cited by 918
Deletion analysis of GAL4 defines two transcriptional activating segments
Ma, J., & Ptashne, M. (1987) · Cell · doi:10.1016/0092-8674(87)90081-x · Cited by 887
Craig, E. A., & Schlesinger, M. J. (1985) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238509085135 · Cited by 809
Cited by
Sorted by citations
Items 201–300 of 806
Nakai, A., Kawazoe, Y., Tanabe, M., Nagata, K., & Morimoto, R. I. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.10.5268 · Cited by 112
Råbergh, C. M. I., Airaksinen, S., Soitamo, A. J., Björklund, H. V., Johansson, T., Nikinmaa, M., & Sistonen, L. (2000) · Journal of Experimental Biology · doi:10.1242/jeb.203.12.1817 · Cited by 110
Barik, S., & Banerjee, A. K. (1992) · Journal of Virology · doi:10.1128/jvi.66.2.1109-1118.1992 · Cited by 110
An inducible nuclear factor binds to a growth hormone-regulated gene.
Yoon, J., Berry, S. A., SEELIG, S. A., & Towle, H. C. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)45466-4 · Cited by 110
Characterization of the SKN7 ortholog of Aspergillus fumigatus
Lamarre, C., Ibrahim-Granet, O., Du, C., Calderone, R., & Latgé, J.-P. (2007) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2007.01.009 · Cited by 109
H�hfeld, I., Nover, L., Lyck, R., Harmening, U., Treuter, E., & Scharf, K. (1997) · Planta · doi:10.1007/s004250050110 · Cited by 109
Characterization of two genes encoding small heat-shock proteins in Arabidopsis thaliana
Takahashi, T., & Komeda, Y. (1989) · Molecular and General Genetics MGG · doi:10.1007/bf00259608 · Cited by 109
Hoeck, W. G., & Groner, B. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39373-1 · Cited by 109
Raymond, C. K., O’Hara, P. J., Eichinger, G., Rothman, J. H., & Stevens, T. H. (1990) · The Journal of Cell Biology · doi:10.1083/jcb.111.3.877 · Cited by 108
Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs
Leach, M. D., Klipp, E., Cowen, L. E., & Brown, A. J. P. (2012) · Nature Reviews Microbiology · doi:10.1038/nrmicro2875 · Cited by 107
Regulating transcription factor activity by phosphorylation
Jackson, S. P. (1992) · Trends in Cell Biology · doi:10.1016/0962-8924(92)90014-e · Cited by 107
Emerging Role of Heat Shock Proteins in Biology and Medicine
Jäättelä, M., & Wissing, D. (1992) · Annals of Medicine · doi:10.3109/07853899209149952 · Cited by 106
Nicholls, S., Leach, M. D., Priest, C. L., & Brown, A. J. P. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06883.x · Cited by 105
Effects of neurohormonal stress and aging on the activation of mammalian heat shock factor 1.
Fawcett, T. W., Sylvester, S. L., Sarge, K. D., Morimoto, R. I., & Holbrook, N. J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31631-4 · Cited by 105
Copper Differentially Regulates the Activity and Degradation of Yeast Mac1 Transcription Factor
Zhu, Z., Labbé, S., Peña, M. M. O., & Thiele, D. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.3.1277 · Cited by 105
DNA binding-induced conformational change of the yeast transcriptional activator PRTF
Tan, S., & Richmond, T. J. (1990) · Cell · doi:10.1016/0092-8674(90)90373-m · Cited by 105
A synergistic small-molecule combination directly eradicates diverse prion strain structures
Roberts, B. E., Duennwald, M. L., Wang, H., Chung, C., Lopreiato, N. P., Sweeny, E. A., Knight, M. N., & Shorter, J. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.246 · Cited by 102
Knudsen, J., Færgeman, N. J., Skøtt, H., Hummel, R., Børsting, C., Rose, T. M., Andersen, J., Højrup, P., Roepstorff, P., & Kristiansen, K. (1994) · Biochemical Journal · doi:10.1042/bj3020479 · Cited by 102
Phenotypic features of trehalase mutants in Saccharomyces cerevisiae
Nwaka, S., Mechler, B., Destruelle, M., & Holzer, H. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00105-i · Cited by 102
Cohen-Peer, R., Schuster, S., Meiri, D., Breiman, A., & Avni, A. (2010) · Plant Molecular Biology · doi:10.1007/s11103-010-9652-1 · Cited by 103
Gallo, G. J., Prentice, H. L., & Kingston, R. E. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.2.749 · Cited by 101
Glucagon gene transcription is negatively regulated by insulin in a hamster islet cell line.
Philippé, J. (1989) · Journal of Clinical Investigation · doi:10.1172/jci114214 · Cited by 101
A Tobacco DNA Binding Protein That Interacts with a Light-Responsive Box II Element
Perišić, O., & Lam, E. (1992) · The Plant Cell · doi:10.1105/tpc.4.7.831 · Cited by 101
Inhibition of the specific DNA binding activity of the dioxin receptor by phosphatase treatment.
Pongratz, I., Strömstedt, P. E., MASON, G. G. F., & Poellinger, L. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55374-6 · Cited by 101
Smith, B. J., & Yaffe, M. P. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.5.2647-2655.1991 · Cited by 101
Leach, M. D., Farrer, R. A., Tan, K., Miao, Z., Walker, L. A., Cuomo, C. A., Wheeler, R. T., Brown, A. J. P., Wong, K. H., & Cowen, L. E. (2016) · Nature Communications · doi:10.1038/ncomms11704 · Cited by 107
Mayer, F. L., Wilson, D., Jacobsen, I. D., Miramón, P., Slesiona, S., Bohovych, I., Brown, A. J. P., & Hube, B. (2012) · PLoS ONE · doi:10.1371/journal.pone.0038584 · Cited by 101
Molecular Aspects of the Stress Response: Chaperones, Membranes and Networks
Csermely, P., & VÃgh, L. (2007) · Springer eBooks · doi:10.1007/978-0-387-39975-1 · Cited by 100
RPA Assists HSF1 Access to Nucleosomal DNA by Recruiting Histone Chaperone FACT
Fujimoto, M., Takaki, E., Takii, R., Tan, K., Prakasam, R., Hayashida, N., Iemura, S., Natsume, T., & Nakai, A. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.07.026 · Cited by 99
Heat shock response and acute lung injury
Wheeler, D. S., & Wong, H. R. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.08.028 · Cited by 101
Phosphorylation of Opaque2 Changes Diurnally and Impacts Its DNA Binding Activity
Ciceri, P., Gianazza, E., Lazzari, B., Lippoli, G., Genga, A., Hoschek, G., Schmidt, R. J., & Viotti, A. (1997) · The Plant Cell · doi:10.1105/tpc.9.1.97 · Cited by 99
Raychaudhuri, P., Bagchi, S., & Nevins, J. R. (1989) · Genes & Development · doi:10.1101/gad.3.5.620 · Cited by 99
Mutka, S. C., & Walter, P. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.3.577 · Cited by 98
mRNA transport in yeast: time to reinvestigate the functions of the nucleolus.
Schneiter, R., Kadowaki, T., & Tartakoff, A. M. (1995) · Molecular Biology of the Cell · doi:10.1091/mbc.6.4.357 · Cited by 98
The gene encoding ARS-binding factor I is essential for the viability of yeast.Preprint
Rhode, P. R., Sweder, K., Oegema, K., & Campbell, J. L. (1989) · Genes & Development · doi:10.1101/gad.3.12a.1926 · Cited by 97
Choi, H.-S., Lin, Z., Li, B. S., & Liu, A. Y. ‐. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)38263-2 · Cited by 96
Regulation of the members of the mammalian heat shock factor family
Björk, J., & Sistonen, L. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07828.x · Cited by 98
Gowda, N. K. C., Kandasamy, G., Froehlich, M. S., Dohmen, R. J., & Andréasson, C. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1216778110 · Cited by 95
Heat Shock Factor 1 Drives Intergenic Association of Its Target Gene Loci upon Heat Shock
Chowdhary, S., Kainth, A. S., Pincus, D., & Gross, D. S. (2019) · Cell Reports · doi:10.1016/j.celrep.2018.12.034 · Cited by 94
Inouye, S., Katsuki, K., Izu, H., Fujimoto, M., Sugahara, K., Yamada, S., Shinkai, Y., Oka, Y., Katoh, Y., & Nakai, A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.16.5882-5895.2003 · Cited by 96
Gu, L., Jiang, T., Zhang, C., Li, X., Wang, C., Zhang, Y., Li, T., Dirk, L. M. A., Downie, A. B., & Zhao, T. (2019) · The Plant Journal · doi:10.1111/tpj.14434 · Cited by 93
Phosphotryptic Peptide Analysis of Human Progesterone Receptors
Sheridan, P. L., Evans, R. M., & Horwitz, K. B. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83379-8 · Cited by 93
Tailoring of Proteostasis Networks with Heat Shock FactorsPreprint
Joutsen, J., & Sistonen, L. (2018) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a034066 · Cited by 100
Cell cycle transition under stress conditions controlled by vertebrate heat shock factors
Nakai, A., & Ishikawa, T. (2001) · The EMBO Journal · doi:10.1093/emboj/20.11.2885 · Cited by 92
Regulated phosphorylation and dephosphorylation of GAL4, a transcriptional activator.Preprint
Mylin, L. M., Bhat, J. P., & Hopper, J. E. (1989) · Genes & Development · doi:10.1101/gad.3.8.1157 · Cited by 92
Uncoupling thermotolerance from the induction of heat shock proteins.
Smith, B. J., & Yaffe, M. P. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.24.11091 · Cited by 91
Regulation of Hsf1 and the Heat Shock Response
Pincus, D. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-40204-4_3 · Cited by 91
Transcriptional Activation in an Improved Whole-Cell Extract from Saccharomyces cerevisiae
Woontner, M., Wade, P. A., Bonner, J. J., & Jaehning, J. A. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.9.4555 · Cited by 90
Conlin, L. K., & Nelson, H. C. M. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01158-06 · Cited by 89
Structure and regulation of the SSA4 HSP70 gene of Saccharomyces cerevisiae.
Boorstein, W. R., & Craig, E. A. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30603-8 · Cited by 89
Gross, D. S., English, K. E., Collins, K. W., & Lee, S. (1990) · Journal of Molecular Biology · doi:10.1016/0022-2836(90)90387-2 · Cited by 89
Chatterjee, M. T., Khalawan, S. A., & Curran, B. P. G. (2000) · Microbiology · doi:10.1099/00221287-146-4-877 · Cited by 88
Eastmond, D. L., & Nelson, H. C. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602454200 · Cited by 90
Nuclear Dot Antigens may Specify Transcriptional Domains in the Nucleus
Xie, K., Lambie, E. J., & Snyder, M. P. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.10.6170-6179.1993 · Cited by 88
Orosz, A., Wiśniewski, J., & Wu, C. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.12.7018 · Cited by 88
Amati, B. B., & Gasser, S. M. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.10.5442 · Cited by 88
Morano, K. A., Santoro, N., Koch, K. A., & Thiele, D. J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.1.402 · Cited by 87
Naghshbandi, M. P., Tabatabaei, M., Aghbashlo, M., Gupta, V. K., Sulaiman, A., Karimi, K., Moghimi, H., & Maleki, M. (2019) · Renewable and Sustainable Energy Reviews · doi:10.1016/j.rser.2019.109353 · Cited by 86
Song, X., Liu, G., Duan, W., Liu, T., Huang, Z., Ren, J., Li, Y., & Hou, X. (2014) · Molecular Genetics and Genomics · doi:10.1007/s00438-014-0833-5 · Cited by 86
Cell Cycle-Dependent Regulation of Human DNA Polymerase α-Primase Activity by Phosphorylation
Voitenleitner, C., Rehfuess, C., Hilmes, M. A., O’Rear, L., Liao, P., Gage, D. A., Ott, R., Nasheuer, H., & Fanning, E. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.1.646 · Cited by 86
Won, K. A., & Baumann, H. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.8.3965 · Cited by 86
Fungal Cell Wall Proteins and Signaling Pathways Form a Cytoprotective Network to Combat Stresses
Ibe, C., & Munro, C. A. (2021) · Journal of Fungi · doi:10.3390/jof7090739 · Cited by 88
Gross, D. S., Adams, C. C., Lee, S., & Stentz, B. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06071.x · Cited by 85
Heat shock proteins in breast cancer progression–A suitable case for treatment?
Calderwood, S. K. (2010) · International Journal of Hyperthermia · doi:10.3109/02656736.2010.490254 · Cited by 88
Chen, Y., Barlev, N. A., Westergaard, O., & Jakobsen, B. K. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06194.x · Cited by 84
Kim, S., & Gross, D. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.449553 · Cited by 84
Olive, M. R., Peacock, W. J., & Dennis, E. S. (1991) · Nucleic Acids Research · doi:10.1093/nar/19.25.7053 · Cited by 84
Mechanisms of Signal Transduction to the Cell Nucleus
Nigg, E. A. (1990) · Advances in cancer research · doi:10.1016/s0065-230x(08)60471-6 · Cited by 85
Hsf1 on a leash – controlling the heat shock response by chaperone titration
Masser, A. E., Ciccarelli, M., & Andréasson, C. (2020) · Experimental Cell Research · doi:10.1016/j.yexcr.2020.112246 · Cited by 83
Cooperative Binding of Heat Shock Factor to the Yeast HSP82 Promoter In Vivo and In Vitro
Erkine, A. M., Magrogan, S. F., Sekinger, E. A., & Gross, D. S. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.3.1627 · Cited by 82
Halfter, H., Kavety, B., Vandekerckhove, J. S., Kiefer, F., & Gallwitz, D. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08612.x · Cited by 82
Somasundaram, T., & Bhat, S. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405813200 · Cited by 81
Damberger, F. F., Pelton, J. G., Harrison, C. J., Nelson, H. C. M., & Wemmer, D. E. (1994) · Protein Science · doi:10.1002/pro.5560031020 · Cited by 81
Berna, A., Gafny, R., Wolf, S., Lucas, W. J., Holt, C. A., & Beachy, R. N. (1991) · Virology · doi:10.1016/0042-6822(91)90609-f · Cited by 81
Lin, Y., Cheng, Y., Jin, J., Jin, X., Jiang, H., Yan, H., & Cheng, B. (2014) · PLoS ONE · doi:10.1371/journal.pone.0102825 · Cited by 80
Transcriptional regulation of the heat-shock response: a plant perspective
Gurley, W. B., & Key, J. L. (1991) · Biochemistry · doi:10.1021/bi00215a001 · Cited by 80
Self‐association of the Drosophila zeste protein is responsible for transvection effects.
Bickel, S. E., & Pirrotta, V. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07488.x · Cited by 80
Kumar, V., Roy, S., Behera, B. K., & Das, B. K. (2022) · Life · doi:10.3390/life12111777 · Cited by 79
A heat‐activated MAP kinase (HAMK) as a mediator of heat shock response in tobacco cells
Suri, S. S., & Dhindsa, R. S. (2007) · Plant Cell & Environment · doi:10.1111/j.1365-3040.2007.01754.x · Cited by 79
Cotgreave, I. A. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2004.12.004 · Cited by 79
Protein Kinase A Binds and Activates Heat Shock Factor 1
Murshid, A., Chou, S., Prince, T. L., Zhang, Y., Bharti, A. K., & Calderwood, S. K. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013830 · Cited by 79
The heat shock response in neurons and astroglia and its role in neurodegenerative diseases
Gil, R. S., Ooi, L., Yerbury, J. J., & Ecroyd, H. W. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0208-6 · Cited by 80
Complilation and characteristics of dedicated transcription factors in Saccharomyces cerevisiae
Svetlov, V. V., & Cooper, T. (1995) · Yeast · doi:10.1002/yea.320111502 · Cited by 78
Ahn, S., Liu, P. C. C., Klyachko, K. A., Morimoto, R. I., & Thiele, D. J. (2001) · Genes & Development · doi:10.1101/gad.894801 · Cited by 78
Strenkert, D., Schmollinger, S., Sommer, F., Schulz‐Raffelt, M., & Schroda, M. (2011) · The Plant Cell · doi:10.1105/tpc.111.085266 · Cited by 79
An efficient method to isolate yeast genes causing overexpression‐mediated growth arrest
Espinet, C., de la Torre-Ruiz, M. Á., Aldea, M., & Herrero, E. (1995) · Yeast · doi:10.1002/yea.320110104 · Cited by 77
Choi, H.-S., Li, B., Lin, Z., Huang, E., & Liu, A. Y. ‐. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99036-8 · Cited by 77
GAL4 Protein: Purification, Association with GAL80 Protein, and Conserved Domain Structure
Chasman, D. I., & Kornberg, R. D. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.6.2916 · Cited by 77
Lin, K., Ashizawa, K., & Cheng, S.-Y. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.16.7737 · Cited by 77
Molecular and Cellular Biology of the Heat-Shock Response
Nagao, R. T., Kimpel, J. A., & Key, J. L. (1990) · Advances in genetics · doi:10.1016/s0065-2660(08)60528-3 · Cited by 77
Huang, Y., Li, M., Wang, F., Xu, Z., Huang, W. J., Wang, G., Ma, J., & Xiong, A. (2014) · Molecular Biology Reports · doi:10.1007/s11033-014-3826-x · Cited by 76
Identification and Characterization of anSKN7Homologue inCryptococcus neoformans
Wormley, F. L., Heinrich, G., Miller, J. L., Perfect, J. R., & Cox, G. M. (2005) · Infection and Immunity · doi:10.1128/iai.73.8.5022-5030.2005 · Cited by 76
Heat- and cold-inducible regulation of HSP70 expression in zebrafish ZF4 cells
Airaksinen, S., Jokilehto, T., Råbergh, C. M. I., & Nikinmaa, M. (2003) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/s1096-4959(03)00205-7 · Cited by 76
Patriarca, E. J., & Maresca, B. (1990) · Experimental Cell Research · doi:10.1016/0014-4827(90)90143-x · Cited by 75
Bonner, J. J., Heyward, S. A., & Fackenthal, D. L. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.3.1021 · Cited by 75
A Constitutive Heat Shock Element-binding Factor Is Immunologically Identical to the Ku Autoantigen
Kim, D., Ouyang, H., Yang, S., Nussenzweig, A., Burgman, P., & Li, G. C. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.25.15277 · Cited by 75
Zhang, H., Li, G., Fu, C., Duan, S., Hu, D., & Guo, X. (2020) · Scientific Reports · doi:10.1038/s41598-020-65068-z · Cited by 74
Heat shock factor 1 is a key regulator of the stress response in Chlamydomonas
Schulz‐Raffelt, M., Lodha, M., & Schroda, M. (2007) · The Plant Journal · doi:10.1111/j.1365-313x.2007.03228.x · Cited by 72
Engelberg, D., Zandi, E., Parker, C. S., & Karin, M. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.7.4929 · Cited by 72
MAP kinase activation during heat shock in quiescent and exponentially growing mammalian cells
Dubois, M., & Bensaude, O. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)81391-c · Cited by 72
Metadata
- Authors
- Sorger, P. K., & Pelham, H. R. B.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1988-09
- Volume
- 54
- Issue
- 6
- Pages
- 855-864
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2005131012
- Cited by
- 832
- References
- 27
- Citations by year
- 2026: 8 · 2025: 6 · 2024: 12 · 2023: 6 · 2022: 21 · 2021: 10 · 2020: 16 · 2019: 11 · 2018: 15 · 2017: 10 · 2016: 22 · 2015: 9 · 2014: 15 · 2013: 25 · 2012: 17
- FWCI
- 24.28
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- heat shock transcription factor, Saccharomyces cerevisiae, heat shock promoter, protein phosphorylation, DNA binding, heat shock gene expression, transcriptional regulation, gene cloning
- MeSH terms
- Amino Acid Sequence, Base Sequence, Cell Survival, Cloning, Molecular, DNA-Binding Proteins, Gene Expression Regulation, Hot Temperature, Heat-Shock Proteins, Molecular Sequence Data, Molecular Weight, Phosphoproteins, Phosphorylation, Saccharomyces cerevisiae, Transcription Factors, Transcription, Genetic
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 ›
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