hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures.
Open accessAbstract
hsp82 is one of the most highly conserved and abundantly synthesized heat shock proteins of eucaryotic cells. The yeast Saccharomyces cerevisiae contains two closely related genes in the HSP82 gene family. HSC82 was expressed constitutively at a very high level and was moderately induced by high temperatures. HSP82 was expressed constitutively at a much lower level and was more strongly induced by heat. Site-directed disruption mutations were produced in both genes. Cells homozygous for both mutations did not grow at any temperature. Cells carrying other combinations of the HSP82 and HSC82 mutations grew well at 25 degrees C, but their ability to grow at higher temperatures varied with gene copy number. Thus, HSP82 and HSC82 constitute an essential gene family in yeast cells. Although the two proteins had different patterns of expression, they appeared to have equivalent functions; growth at higher temperatures required higher concentrations of either protein. Biochemical analysis of hsp82 from vertebrate cells suggests that the protein binds to a variety of other cellular proteins, keeping them inactive until they have reached their proper intracellular location or have received the proper activation signal. We speculate that the reason cells require higher concentrations of hsp82 or hsc82 for growth at higher temperatures is to maintain proper levels of complex formation with these other proteins.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The text we found for this paper looks like another document, so the self-check wasn’t run.
Cites
Molecular Cloning: A Laboratory Manual
Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589 · see citing works
Molecular Cloning. A Laboratory Manual
Wood, E. (1983) · Biochemical Education · doi:10.1016/0307-4412(83)90068-7 · Cited by 29,534 · see citing works
A comprehensive set of sequence analysis programs for the VAX
Devereux, J., Haeberli, P. E., & Smithies, O. (1984) · Nucleic Acids Research · doi:10.1093/nar/12.1part1.387 · Cited by 14,222 · see citing works
Transformation of intact yeast cells treated with alkali cations
Ito, H., Fukuda, Y., Murata, K., & Kimura, A. (1983) · Journal of Bacteriology · doi:10.1128/jb.153.1.163-168.1983 · Cited by 7,518 · see citing works
Lindquist, S., & Craig, E. A. (1988) · Annual Review of Genetics · doi:10.1146/annurev.ge.22.120188.003215 · Cited by 5,304 · see citing works
Self-citation[12] One-step gene disruption in yeast
Rothstein, R. J. (1983) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(83)01015-0 · Cited by 3,282 · see citing works
High-frequency transformation of yeast: autonomous replication of hybrid DNA molecules.
Struhl, K., Stinchcomb, D. T., Scherer, S., & Davis, R. W. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.3.1035 · Cited by 1,456 · see citing works
Transformation in yeast: Development of a hybrid cloning vector and isolation of the can1 gene
Broach, J. R., Strathern, J. N., & Hicks, J. B. (1979) · Gene · doi:10.1016/0378-1119(79)90012-x · Cited by 1,073 · see citing works
A regulatory upstream promoter element in the Drosophila Hsp 70 heat-shock gene
Pelham, H. R. B. (1982) · Cell · doi:10.1016/0092-8674(82)90249-5 · Cited by 1,046 · see citing works
Principles of protein–protein recognition
Chothia, C., & Janin, J. (1975) · Nature · doi:10.1038/256705a0 · Cited by 1,014 · see citing works
Finley, D., Özkaynak, E., & Varshavsky, A. J. (1987) · Cell · doi:10.1016/0092-8674(87)90711-2 · Cited by 860 · see citing works
The htpR gene product of E. coli is a sigma factor for heat-shock promoters
Grossman, A. D., Erickson, J. W., & Gross, C. A. (1984) · Cell · doi:10.1016/0092-8674(84)90493-8 · Cited by 592 · see citing works
Key features of heat shock regulatory elements.
Αmin, J., Ananthan, J., & Voellmy, R. W. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.9.3761 · Cited by 572 · see citing works
[49] Rapid DNA isolations for enzymatic and hybridization analysis
Davis, R. W., Thomas, M., Cameron, J., John, T. P. S., Scherer, S., & Padgett, R. A. (1980) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(80)65051-4 · Cited by 555 · see citing works
Germline Transformation Used to Define Key Features of Heat-Shock Response Elements
Xiao, H., & Lis, J. T. (1988) · Science · doi:10.1126/science.3125608 · Cited by 455 · see citing works
The structure of transposable yeast mating type loci
Nasmyth, K., & Tatchell, K. (1980) · Cell · doi:10.1016/s0092-8674(80)80051-1 · Cited by 437 · see citing works
Joab, I., Radanyi, C., Renoir, M., Buchou, T., CATELLI, M. G., Binart, N., Mešter, J., & Baulieu, É.-É. (1984) · Nature · doi:10.1038/308850a0 · Cited by 434 · see citing works
Brugge, J. S., ERIKSON, E., & Erikson, R. L. (1981) · Cell · doi:10.1016/0092-8674(81)90055-6 · Cited by 362 · see citing works
Two mammalian heat shock proteins, HSP90 and HSP100, are actin-binding proteins.
Koyasu, S., Nishida, E., Kadowaki, T., Matsuzaki, F., Iida, K., Harada, F., Kasuga, M., Sakai, H., & Yahara, I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.21.8054 · Cited by 329 · see citing works
Mazzarella, R. A., & Green, M. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47496-0 · Cited by 289 · see citing works
Mutations of the heat inducible 70 kilodalton genes of yeast confer temperature sensitive growth
Craig, E. A., & Jacobsen, K. (1984) · Cell · doi:10.1016/0092-8674(84)90279-4 · Cited by 286 · see citing works
Activation of heat-shock genes in eukaryotes
Pelham, H. R. B. (1985) · Trends in Genetics · doi:10.1016/0168-9525(85)90012-5 · Cited by 265 · see citing works
Sánchez, E. R., Meshinchi, S., Tienrungroj, W., Schlesinger, M. J., Toft, D. O., & Pratt, W. B. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48191-4 · Cited by 263 · see citing works
Petko, L., & Lindquist, S. L. (1986) · Cell · doi:10.1016/0092-8674(86)90563-5 · Cited by 231 · see citing works
Self-citationBlackman, R. K., & Meselson, M. S. (1986) · Journal of Molecular Biology · doi:10.1016/s0022-2836(86)80001-8 · Cited by 223 · see citing works
Eukaryotic Mr 83,000 heat shock protein has a homologue in Escherichia coli.
Bardwell, J. C. A., & Craig, E. A. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.15.5177 · Cited by 212 · see citing works
Craig, E. A., Kramer, J., & Kosic-Smithers, J. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.12.4156 · Cited by 202 · see citing works
Key Features of Heat Shock Regulatory Elements
Αmin, J., Ananthan, J., & Voellmy, R. W. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.9.3761-3769.1988 · Cited by 197 · see citing works
Complete sequence of the heat shock-inducible HSP90 gene of Saccharomyces cerevisiae.
Farrelly, F. W., & FINKELSTEIN, D. B. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)91077-x · Cited by 188 · see citing works
Self-citationPolypeptide components of two 8 S forms of chicken oviduct progesterone receptor.
Dougherty, J. J., Puri, R. K., & Toft, D. O. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42893-6 · Cited by 186 · see citing works
Ancient heat shock gene is dispensable
Bardwell, J. C. A., & Craig, E. A. (1988) · Journal of Bacteriology · doi:10.1128/jb.170.7.2977-2983.1988 · Cited by 181 · see citing works
Induction of the heat shock regulon does not produce thermotolerance in Escherichia coli.Preprint
VanBogelen, R. A., Acton, M., & Neidhardt, F. C. (1987) · Genes & Development · doi:10.1101/gad.1.6.525 · Cited by 177 · see citing works
Buss, J. E., Kamps, M. P., & Sefton, B. M. (1984) · Molecular and Cellular Biology · doi:10.1128/mcb.4.12.2697 · Cited by 172 · see citing works
Nucleotide sequence of a cDNA for a member of the human 90-kDa heat-shock protein family
Rebbe, N. F., Ware, J. L., Bertina, R. M., Modrich, P. L., & Stafford, D. W. (1987) · Gene · doi:10.1016/0378-1119(87)90012-6 · Cited by 166 · see citing works
Transit of pp60v-src to the plasma membrane.
Courtneidge, S. A., & Bishop, J. M. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.23.7117 · Cited by 165 · see citing works
Brugge, J. S., Yonemoto, W. M., & Darrow, D. (1983) · Molecular and Cellular Biology · doi:10.1128/mcb.3.1.9-19.1983 · Cited by 159 · see citing works
Calmodulin-regulated binding of the 90-kDa heat shock protein to actin filaments.
Nishida, E., Koyasu, S., Sakai, H., & Yahara, I. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)66671-2 · Cited by 158 · see citing works
Dragon, E. A., Sias, S. R., KATO, E. A., & Gabe, J. D. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.3.1271-1275.1987 · Cited by 132 · see citing works
Transcriptional regulation of an hsp70 heat shock gene in the yeast Saccharomyces cerevisiae.
Slater, M. R., & Craig, E. A. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.5.1906 · Cited by 128 · see citing works
Neidhardt, F. C., VanBogelen, R. A., & Lau, E. T. (1983) · Journal of Bacteriology · doi:10.1128/jb.153.2.597-603.1983 · Cited by 127 · see citing works
Rose, D. W., Wettenhall, R. E. H., Kudlicki, W. A., Kramer, G., & Hardesty, B. (1987) · Biochemistry · doi:10.1021/bi00395a003 · Cited by 126 · see citing works
Lipsich, L. A., Cutt, J. R., & Brugge, J. S. (1982) · Molecular and Cellular Biology · doi:10.1128/mcb.2.7.875 · Cited by 117 · see citing works
Changing patterns of gene expression during sporulation in yeast.
Kurtz, S. E., & Lindquist, S. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.23.7323 · Cited by 117 · see citing works
Self-citationSánchez, E. R., Redmond, T., Scherrer, L. C., Bresnick, E. H., Welsh, M. J., & Pratt, W. B. (1988) · Molecular Endocrinology · doi:10.1210/mend-2-8-756 · Cited by 113 · see citing works
Redeuilh, G., Moncharmont, B., Secco, C., & Baulieu, E. E. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48188-4 · Cited by 111 · see citing works
Widelitz, R. B., Magun, B. E., & Gerner, E. W. (1986) · Molecular and Cellular Biology · doi:10.1128/mcb.6.4.1088 · Cited by 101 · see citing works
Thermotolerance in Mammalian Cells: A Possible Role for Heat Shock Proteins
Li, G. C., & Laszlo, A. (1985) · Elsevier eBooks · doi:10.1016/b978-0-12-066290-6.50017-6 · Cited by 98 · see citing works
Brugge, J. S., Yonemoto, W. M., & Darrow, D. (1983) · Molecular and Cellular Biology · doi:10.1128/mcb.3.1.9 · Cited by 89 · see citing works
Watson, K., Dunlop, G., & Cavicchioli, R. (1984) · FEBS Letters · doi:10.1016/0014-5793(84)81145-x · Cited by 71 · see citing works
Renoir, J. M., Buchou, T., & Baulieu, E. E. (1986) · Biochemistry · doi:10.1021/bi00369a010 · Cited by 63 · see citing works
Lee, Y. J., & Dewey, W. C. (1988) · Journal of Cellular Physiology · doi:10.1002/jcp.1041350306 · Cited by 59 · see citing works
Kennedy, I. M., Burdon, R. H., & Leader, D. P. (1984) · FEBS Letters · doi:10.1016/0014-5793(84)80331-2 · Cited by 54 · see citing works
Transcriptional Regulation of an hsp70 Heat Shock Gene in the Yeast Saccharomyces Cerevisiae
Slater, M. R., & Craig, E. A. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.5.1906-1916.1987 · Cited by 54 · see citing works
Sánchez, E. R., Housley, P. R., & Pratt, W. B. (1986) · Journal of Steroid Biochemistry · doi:10.1016/0022-4731(86)90025-7 · Cited by 52 · see citing works
Purification and characterization of arginase from Neurospora crassa.
Borkovich, K. A., & Weiss, R. L. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48206-3 · Cited by 50 · see citing works
Self-citationAdkins, B., Hunter, T. R., & Sefton, B. M. (1982) · Journal of Virology · doi:10.1128/jvi.43.2.448-455.1982 · Cited by 49 · see citing works
Lipsich, L. A., Cutt, J. R., & Brugge, J. S. (1982) · Molecular and Cellular Biology · doi:10.1128/mcb.2.7.875-880.1982 · Cited by 37 · see citing works
Widelitz, R. B., Magun, B. E., & Gerner, E. W. (1986) · Molecular and Cellular Biology · doi:10.1128/mcb.6.4.1088-1094.1986 · Cited by 19 · see citing works
Ziemiecki, A. (1986) · Virology · doi:10.1016/0042-6822(86)90048-6 · Cited by 18 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Parsell, D. A., & Lindquist, S. (1993) · Annual Review of Genetics · doi:10.1146/annurev.ge.27.120193.002253 · Cited by 2,275 · see citing works
Self-citationHSP90 at the hub of protein homeostasis: emerging mechanistic insights
Taipale, M., Jarosz, D. F., & Lindquist, S. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2918 · Cited by 1,818 · see citing works
Self-citationSchopf, F. H., Biebl, M. M., & Buchner, J. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.20 · Cited by 1,540 · see citing works
Remodeling of Yeast Genome Expression in Response to Environmental Changes
Causton, H. C., Ren, B., Koh, S. S., Harbison, C. T., Kanin, E. I., Jennings, E. G., Lee, T. I., True, H. L., Lander, E. S., & Young, R. A. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.2.323 · Cited by 1,364 · see citing works
Stebbins, C. E., Russo, A. A., Schneider, C. B., Rosen, N. X., Hartl, F. U., & Pavletich, N. P. (1997) · Cell · doi:10.1016/s0092-8674(00)80203-2 · Cited by 1,370 · see citing works
Prodromou, C., Roe, S. M., O’Brien, R., Ladbury, J. E., Piper, P. W., & Pearl, L. H. (1997) · Cell · doi:10.1016/s0092-8674(00)80314-1 · Cited by 1,258 · see citing works
Structure and mechanism of the Hsp90 molecular chaperone machinery
Pearl, L. H., & Prodromou, C. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142738 · Cited by 1,103 · see citing works
Pathways of chaperone-mediated protein folding in the cytosol
Young, J. C., Agashe, V. R., Siegers, K., & Hartl, F. U. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1492 · Cited by 1,101 · see citing works
Modulation of Akt kinase activity by binding to Hsp90
Sato, S., Fujita, N., & Tsuruo, T. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.170276797 · Cited by 967 · see citing works
Benjamin, I. J., & McMillan, D. R. (1998) · Circulation Research · doi:10.1161/01.res.83.2.117 · Cited by 840 · see citing works
Zhao, R., Davey, M., Hsu, Y.-C., Kaplanek, P., Tong, A., Parsons, A. B., Krogan, N., Cagney, G., Mai, D., Greenblatt, J., et al. (2005) · Cell · doi:10.1016/j.cell.2004.12.024 · Cited by 819 · see citing works
HSP104 Required for Induced Thermotolerance
Sánchez, Y., & Lindquist, S. L. (1990) · Science · doi:10.1126/science.2188365 · Cited by 832 · see citing works
Self-citationReduced levels of hsp90 compromise steroid receptor action in vivo
Picard, D., Khursheed, B., Garabedian, M. J., Fortin, M. G., Lindquist, S., & Yamamoto, K. R. (1990) · Nature · doi:10.1038/348166a0 · Cited by 787 · see citing works
Self-citationHeat-shock protein 90, a chaperone for folding and regulation
Picard, D. (2002) · Cellular and Molecular Life Sciences · doi:10.1007/pl00012491 · Cited by 797 · see citing works
ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
Panaretou, B., Prodromou, C., Roe, S. M., O'Brien, R., Ladbury, J. E., Piper, P. W., & Pearl, L. H. (1998) · The EMBO Journal · doi:10.1093/emboj/17.16.4829 · Cited by 735 · see citing works
Cell Wall and Secreted Proteins of<i>Candida albicans</i>: Identification, Function, and Expression
Chaffin, W. L., López-Ribot, J. L., Casanova, M., Gozalbo, D., & Martínez, J. P. (1998) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.62.1.130-180.1998 · Cited by 726 · see citing works
Heat shock proteins: molecular chaperones of protein biogenesis
Craig, E. A., Gambill, B. D., & Nelson, R. J. (1993) · Microbiological Reviews · doi:10.1128/mr.57.2.402-414.1993 · Cited by 670 · see citing works
The Response to Heat Shock and Oxidative Stress in Saccharomyces cerevisiae
Morano, K. A., Grant, C. M., & Moye-Rowley, S. (2011) · Genetics · doi:10.1534/genetics.111.128033 · Cited by 655 · see citing works
Stationary phase in the yeast Saccharomyces cerevisiae
Werner‐Washburne, M., Braun, E. L., Johnston, G. C., & Singer, R. A. (1993) · Microbiological Reviews · doi:10.1128/mr.57.2.383-401.1993 · Cited by 650 · see citing works
Hsp90 & Co. – a holding for folding
Büchner, J. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01373-0 · Cited by 625 · see citing works
Verghese, J., Abrams, J., Wang, Y., & Morano, K. A. (2012) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.05018-11 · Cited by 575 · see citing works
Hsp70 and Hsp90—a relay team for protein folding
Wegele, H., Müller, L., & Büchner, J. (2004) · Springer eBooks · doi:10.1007/s10254-003-0021-1 · Cited by 603 · see citing works
In Vivo Function of Hsp90 Is Dependent on ATP Binding and ATP Hydrolysis
Obermann, W. M. J., Sondermann, H., Russo, A. A., Pavletich, N. P., & Hartl, F. U. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.4.901 · Cited by 593 · see citing works
Hsp90: Chaperoning signal transduction
Richter, K., & Büchner, J. (2001) · Journal of Cellular Physiology · doi:10.1002/jcp.1131 · Cited by 570 · see citing works
Hsp104 is required for tolerance to many forms of stress.
Sánchez, Y., Taulien, J., Borkovich, K. A., & Lindquist, S. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05295.x · Cited by 565 · see citing works
Self-citationHeat‐shock proteins as molecular chaperones
Becker, J. D., & Craig, E. A. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb19910.x · Cited by 557 · see citing works
Krobitsch, S., & Lindquist, S. L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.4.1589 · Cited by 546 · see citing works
Self-citationPlant disease resistance protein signaling: NBS–LRR proteins and their partners
Belkhadir, Y., Subramaniam, R., & Dangl, J. L. (2004) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2004.05.009 · Cited by 535 · see citing works
Cryptic genetic variation: evolution's hidden substrate
Paaby, A. B., & Rockman, M. V. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3688 · Cited by 500 · see citing works
Heat shock proteins in toxicology: How close and how far?
Gupta, S. C., Sharma, A., Mishra, M., Mishra, R. K., & Chowdhuri, D. K. (2010) · Life Sciences · doi:10.1016/j.lfs.2009.12.015 · Cited by 502 · see citing works
The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones
Li, J., Soroka, J., & Buchner, J. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.09.003 · Cited by 498 · see citing works
Lavoie, J. N., Gingras-Breton, G., Tanguay, R. M., & Landry, J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53711-x · Cited by 487 · see citing works
Mutational Analysis of Hsp90 Function: Interactions with a Steroid Receptor and a Protein Kinase
Nathan, D. F., & Lindquist, S. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.7.3917 · Cited by 423 · see citing works
Self-citationStructure, Function and Regulation of the Hsp90 Machinery
Büchner, J., & Li, J. (2013) · Biomedical Journal · doi:10.4103/2319-4170.113230 · Cited by 421 · see citing works
Heat-shock protein hsp90 governs the activity of pp60v-src kinase.
Xu, Y., & Lindquist, S. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.15.7074 · Cited by 416 · see citing works
Self-citationPharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90
Schneider, C. B., Sepp‐Lorenzino, L., Nimmesgern, E., Ouerfelli, O., Danishefsky, S. J., Rosen, N. X., & Hartl, F. U. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.25.14536 · Cited by 405 · see citing works
Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease resistance protein
Hubert, D. A., Tornero, P., Belkhadir, Y., Krishna, P., Takahashi, A., Shirasu, K., & Dangl, J. L. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg547 · Cited by 398 · see citing works
The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative Diseases
Lackie, R. E., Maciejewski, A., Ostapchenko, V. G., Marques-Lopes, J., Choy, W., Duennwald, M. L., Prado, V. F., & Prado, M. A. M. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00254 · Cited by 375 · see citing works
<i>In vivo</i> functions of the <i>Saccharomyces cerevisiae</i> Hsp90 chaperone
Nathan, D. F., Vos, M. H., & Lindquist, S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.24.12949 · Cited by 364 · see citing works
Self-citationHsp90 Governs Echinocandin Resistance in the Pathogenic Yeast Candida albicans via Calcineurin
Singh, S. D., Robbins, N., Zaas, A. K., Schell, W. A., Perfect, J. R., & Cowen, L. E. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000532 · Cited by 362 · see citing works
Stress-induced transcriptional activation
Mager, W. H., & Kruijff, A. J. D. (1995) · Microbiological Reviews · doi:10.1128/mr.59.3.506-531.1995 · Cited by 351 · see citing works
Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability
Randow, F., & Seed, B. (2001) · Nature Cell Biology · doi:10.1038/ncb1001-891 · Cited by 351 · see citing works
Hsp90 and Environmental Stress Transform the Adaptive Value of Natural Genetic Variation
Jarosz, D. F., & Lindquist, S. (2010) · Science · doi:10.1126/science.1195487 · Cited by 346 · see citing works
Self-citationExperimental illumination of a fitness landscape
Hietpas, R. T., Jensen, J. D., & Bolon, D. N. A. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016024108 · Cited by 336 · see citing works
Birnby, D., Link, E. M., Vowels, J. J., Tian, H., Colacurcio, P. L., & Thomas, J. H. (2000) · Genetics · doi:10.1093/genetics/155.1.85 · Cited by 328 · see citing works
Fitness Trade-offs Restrict the Evolution of Resistance to Amphotericin B
Vincent, B. M., Lancaster, A. K., Scherz-Shouval, R., Whitesell, L., & Lindquist, S. (2013) · PLoS Biology · doi:10.1371/journal.pbio.1001692 · Cited by 322 · see citing works
Self-citationAneuploidy causes proteotoxic stress in yeastPreprint
Oromendia, A. B., Dodgson, S. E., & Amon, A. (2012) · Genes & Development · doi:10.1101/gad.207407.112 · Cited by 307 · see citing works
The evolution of fungal drug resistance: modulating the trajectory from genotype to phenotype.
Cowen, L. E. (2008) · Nature Reviews Microbiology · doi:10.1038/nrmicro1835 · Cited by 311 · see citing works
Miyata, Y., & Yahara, I. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50533-6 · Cited by 311 · see citing works
Structure, Function, and Regulation of the Hsp90 MachineryPreprint
Biebl, M. M., & Büchner, J. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a034017 · Cited by 308 · see citing works
Karagöz, G. E., Acosta‐Alvear, D., & Walter, P. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033886 · Cited by 302 · see citing works
Evolution and function of diverse Hsp90 homologs and cochaperone proteins
Johnson, J. L. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.09.020 · Cited by 283 · see citing works
The Hsp70–Hsp90 Chaperone Cascade in Protein Folding
Luengo, T. M., Mayer, M. P., & Rüdiger, S. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.10.004 · Cited by 276 · see citing works
Mice lacking HSP90β fail to develop a placental labyrinth
Voss, A. K., Thomas, T., & Gruß, P. (2000) · Development · doi:10.1242/dev.127.1.1 · Cited by 282 · see citing works
Bagatell, R., Paine-Murrieta, G. D., Taylor, C. W., Pulcini, E. J., Akinaga, S., Benjamin, I. J., & Whitesell, L. J. (2000) · PubMed · Cited by 270 · see citing works
An, W. G., Schulte, T. W., & Neckers, L. Μ. (2000) · PubMed · Cited by 265 · see citing works
Geller, R., Vignuzzi, M., Andino, R., & Frydman, J. (2007) · Genes & Development · doi:10.1101/gad.1505307 · Cited by 260 · see citing works
Aligue, R., Akhavan‐Niak, H., & Russell, P. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06956.x · Cited by 261 · see citing works
p50cdc37 Acting in Concert with Hsp90 Is Required for Raf-1 Function
Grammatikakis, N., Lin, J.-H., Grammatikakis, A., Tsichlis, P. N., & Cochran, B. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.3.1661 · Cited by 262 · see citing works
The native structure of the activated Raf protein kinase is a membrane-bound multi-subunit complex.
Wartmann, M., & Davis, R. J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37431-8 · Cited by 261 · see citing works
Under cover: causes, effects and implications of Hsp90‐mediated genetic capacitance
Sangster, T. A., Lindquist, S., & Queitsch, C. (2004) · BioEssays · doi:10.1002/bies.20020 · Cited by 251 · see citing works
Self-citationSorger, P. K. (1990) · Cell · doi:10.1016/0092-8674(90)90123-v · Cited by 241 · see citing works
Antagonistic Interactions between Yeast Chaperones Hsp104 and Hsp70 in Prion Curing
Newnam, G. P., Wegrzyn, R. D., Lindquist, S. L., & Chernoff, Y. O. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.2.1325 · Cited by 245 · see citing works
Self-citationNadeau, K. C., Das, A., & Walsh, C. T. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54100-4 · Cited by 245 · see citing works
Nucleotides and Two Functional States of hsp90
Sullivan, W., Stensgard, B. A., Caucutt, G., Bartha, B. B., McMahon, N., Alnemri, E. S., Litwack, G., & Toft, D. O. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.12.8007 · Cited by 235 · see citing works
Molecular events associated with acquisition of heat tolerance by the yeast Saccharomyces cerevisiae
Piper, P. W. (1993) · FEMS Microbiology Reviews · doi:10.1016/0168-6445(93)90005-t · Cited by 237 · see citing works
Firefly luciferase mutants as sensors of proteome stress
Gupta, R., Kasturi, P., Bracher, A., Loew, C., Zheng, M., Villella, A., Garza, D., Hartl, F. U., & Raychaudhuri, S. (2011) · Nature Methods · doi:10.1038/nmeth.1697 · Cited by 219 · see citing works
Organelle-Based Aggregation and Retention of Damaged Proteins in Asymmetrically Dividing Cells
Zhou, C., Slaughter, B. D., Unruh, J. R., Guo, F., Yu, Z., Mickey, K., Narkar, A., Trimble, R., McClain, M. L., & Li, R. (2014) · Cell · doi:10.1016/j.cell.2014.09.026 · Cited by 228 · see citing works
Role of the Protein Chaperone YDJ1 in Establishing Hsp90-Mediated Signal Transduction Pathways
Kimura, Y., Yahara, I., & Lindquist, S. L. (1995) · Science · doi:10.1126/science.7761857 · Cited by 228 · see citing works
Self-citationHeat Shock Protein 90 Function Is Essential for Plasmodium falciparum Growth in Human Erythrocytes
Gowrishankar, B., Singh, V., Pavithra, S. R., & Tatu, U. S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211309200 · Cited by 225 · see citing works
A Cyclophilin Function in Hsp90-Dependent Signal Transduction
Duina, A. A., Foreman, H.-C. C., Marsh, J. A., Lindquist, S. L., & Gaber, R. F. (1996) · Science · doi:10.1126/science.274.5293.1713 · Cited by 224 · see citing works
Self-citationGrenert, J. P., Johnson, B. D., & Toft, D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.25.17525 · Cited by 238 · see citing works
Heat-shock protein 104 expression is sufficient for thermotolerance in yeast.
Lindquist, S., & Kim, G. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.11.5301 · Cited by 223 · see citing works
Self-citationIn Vivo Analysis of the Hsp90 Cochaperone Sti1 (p60)
Foreman, H.-C. C., Nathan, D. F., & Lindquist, S. L. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.1.318 · Cited by 214 · see citing works
Self-citationActivation of stress signaling pathways by electrophilic oxidized and nitrated lipids
Kansanen, E., Jyrkkänen, H.-K., & Levonen, A. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.11.038 · Cited by 208 · see citing works
Mager, W. H., & Ferreira, P. M. (1993) · Biochemical Journal · doi:10.1042/bj2900001 · Cited by 204 · see citing works
Cdc37 is a molecular chaperone with specific functions in signal transduction.Preprint
Kimura, Y., Rutherford, S. L., Miyata, Y., Yahara, I., Freeman, B. C., Yue, L., Morimoto, R. I., & Lindquist, S. (1997) · Genes & Development · doi:10.1101/gad.11.14.1775 · Cited by 206 · see citing works
Self-citationStructure, function, and mechanism of the Hsp90 molecular chaperone
Pearl, L. H., & Prodromou, C. (2001) · Advances in protein chemistry · doi:10.1016/s0065-3233(01)59005-1 · Cited by 199 · see citing works
Isolation of Hsp90 mutants by screening for decreased steroid receptor function.
Bohen, S. P., & Yamamoto, K. R. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.11424 · Cited by 195 · see citing works
Molecular Chaperones: Biology and Prospects for Pharmacological Intervention
Smith, D. F., Whitesell, L. J., & Katsanis, E. (1998) · Pharmacological Reviews · doi:10.1016/s0031-6997(24)01380-2 · Cited by 197 · see citing works
Microbial molecular chaperones
Lund, P. A. (2001) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/s0065-2911(01)44012-4 · Cited by 194 · see citing works
Constitutive expression of heat‐shock protein 70 in mammalian cells confers thermoresistance
Angelidis, C. E., Lazaridis, I., & Pagoulatos, G. N. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb16088.x · Cited by 193 · see citing works
The role of Hsp90 in protein complex assembly
Makhnevych, T., & Houry, W. A. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.09.001 · Cited by 184 · see citing works
Xu, Y., Singer, M. A., & Lindquist, S. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.1.109 · Cited by 184 · see citing works
Self-citationPraekelt, U. M., & Meacock, P. A. (1990) · Molecular and General Genetics MGG · doi:10.1007/bf00315801 · Cited by 182 · see citing works
Protein Homeostasis and the Phenotypic Manifestation of Genetic Diversity: Principles and Mechanisms
Jarosz, D. F., Taipale, M., & Lindquist, S. (2010) · Annual Review of Genetics · doi:10.1146/annurev.genet.40.110405.090412 · Cited by 179 · see citing works
Self-citationDeshaies, R. J., & Schekman, R. W. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.109.6.2653 · Cited by 181 · see citing works
Li, Y., Zhang, T., Schwartz, S. J., & Sun, D. (2009) · Drug Resistance Updates · doi:10.1016/j.drup.2008.12.002 · Cited by 176 · see citing works
Mechanism of Dimer Formation of the 90‐kDa Heat‐Shock Protein
Nemoto, T., Ohara‐Nemoto, Y., Ota, M., Takagi, T., & Yokoyama, K. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.001_1.x · Cited by 176 · see citing works
Carbone, D. L., Doorn, J. A., Kiebler, Z., Ickes, B. R., & Petersen, D. R. (2005) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.105.088088 · Cited by 175 · see citing works
The Carboxy-Terminal Region of Mammalian HSP90 Is Required for Its Dimerization and Function In Vivo
Minami, Y., Kimura, Y., Kawasaki, H., Suzuki, K., & Yahara, I. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.2.1459-1464.1994 · Cited by 172 · see citing works
Heat Shock Protein 90 as a Drug Target against Protozoan Infections
Pallavi, R., Roy, N., Nageshan, R. K., Talukdar, P., Pavithra, S. R., Reddy, R., Sivaramakrishnan, V., Kumar, R., Gupta, A. K., Singh, R. K., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.155317 · Cited by 167 · see citing works
Youker, R. T., Walsh, P., Beilharz, T. H., Lithgow, T. J., & Brodsky, J. L. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-07-0584 · Cited by 167 · see citing works
Cold-Induced Accumulation of hsp90 Transcripts in Brassica napus
Krishna, P., Sacco, M. A., Cherutti, J. F., & Hill, S. (1995) · PLANT PHYSIOLOGY · doi:10.1104/pp.107.3.915 · Cited by 167 · see citing works
Stress proteins and myocardial protection
Yellon, D. M. (1992) · Journal of Molecular and Cellular Cardiology · doi:10.1016/0022-2828(92)93148-d · Cited by 167 · see citing works
Hoepfner, D., Helliwell, S. B., Sadlish, H., Schuierer, S., Filipuzzi, I., Brachat, S., Bhullar, B., Plikat, U., Abraham, Y., Altorfer, M., et al. (2014) · Microbiological Research · doi:10.1016/j.micres.2013.11.004 · Cited by 166 · see citing works
Role of Heat Shock Proteins (HSP70 and HSP90) in Viral Infection
Lubkowska, A., Pluta, W. W., Strońska-Pluta, A., & Lalko, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179366 · Cited by 168 · see citing works
The Hsp90 complex—a super-chaperone machine as a novel drug target
Scheibel, T., & Büchner, J. (1998) · Biochemical Pharmacology · doi:10.1016/s0006-2952(98)00120-8 · Cited by 164 · see citing works
Physical and functional association of RNA polymerase II and the proteasome.
Gillette, T., Gonzalez, F., Delahodde, A., Johnston, S. A., & Kodadek, T. (2004) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0305411101 · Cited by 182 · see citing works
The Charged Linker Region Is an Important Regulator of Hsp90 Function*
Hainzl, O., Lapina, M. C., Buchner, J., & Richter, K. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.031658 · Cited by 150 · see citing works
- Authors
- Borkovich, K. A., Farrelly, F. W., Finkelstein, D. B., Taulien, J., & Lindquist, S.
- Affiliations
- Howard Hughes Medical Institute (US)
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 1989-09
- Volume
- 9
- Issue
- 9
- Pages
- 3919-3930
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC362454
- OpenAlex
- W1956379070
- Cited by
- 641
- References
- 54
- Citations by year
- 2026: 1 · 2025: 5 · 2024: 22 · 2023: 11 · 2022: 19 · 2021: 16 · 2020: 15 · 2019: 23 · 2018: 16 · 2017: 16 · 2016: 18 · 2015: 11 · 2014: 32 · 2013: 26 · 2012: 24
- FWCI
- 5.41
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular and Cellular Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (GM 11223, GM3582, GM25829)
- 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 › Ubiquitin and proteasome pathways
- Keywords
- Hsp82, heat shock proteins, Saccharomyces cerevisiae, heat tolerance, gene copy number, site-directed mutagenesis, protein-protein complex formation, molecular chaperones, constitutive expression
- MeSH terms
- Amino Acid Sequence, Base Sequence, DNA, Fungal, Gene Expression Regulation, Genes, Fungal, Multigene Family, Hot Temperature, Heat-Shock Proteins, Molecular Sequence Data, Mutation, Saccharomyces cerevisiae, Spores, Fungal
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review