Genetic and Biochemical Analysis of p23 and Ansamycin Antibiotics in the Function of Hsp90-Dependent Signaling Proteins

A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae.

Sikorski, R. S., & Hieter, P. (1989) · Genetics · doi:10.1093/genetics/122.1.19 · Cited by 8,685 · see citing works

The Steroid and Thyroid Hormone Receptor Superfamily

Evans, R. M. (1988) · Science · doi:10.1126/science.3283939 · Cited by 7,442 · see citing works

Getting started with yeast

Sherman, F. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)94004-v · Cited by 4,078 · see citing works

Improved method for high efficiency transformation of intact yeast cells.

Gietz, D., Jean, A. S., Woods, R. A., & Schiestl, R. (1992) · Nucleic Acids Research · doi:10.1093/nar/20.6.1425 · Cited by 3,379 · see citing works

STEROID RECEPTOR REGULATED TRANSCRIPTION OF SPECIFIC GENES AND GENE NETWORKS

Yamamoto, K. R. (1985) · Annual Review of Genetics · doi:10.1146/annurev.ge.19.120185.001233 · Cited by 1,872 · see citing works

Multifunctional yeast high-copy-number shuttle vectors

Christianson, T., Sikorski, R. S., Dante, M., Shero, J. H., & Hieter, P. (1992) · Gene · doi:10.1016/0378-1119(92)90454-w · Cited by 1,660 · see citing works

Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation.

Whitesell, L., Mimnaugh, E. G., De Costa, B., Myers, C. E., & Neckers, L. M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8324 · Cited by 1,444 · see citing works

Crystal Structure of an Hsp90–Geldanamycin Complex: Targeting of a Protein Chaperone by an Antitumor Agent

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

Identification and Structural Characterization of the ATP/ADP-Binding Site in the Hsp90 Molecular Chaperone

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

The Biology of heat shock proteins and molecular chaperones.

Morimoto, R. I., Tissieres, A., & Georgopoulos, C. P. (1994) · Cited by 1,244 · see citing works

Reduced 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

hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures.

Borkovich, K. A., Farrelly, F. W., Finkelstein, D. B., Taulien, J., & Lindquist, S. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.9.3919 · Cited by 641 · see citing works

The Amino-terminal Domain of Heat Shock Protein 90 (hsp90) That Binds Geldanamycin Is an ATP/ADP Switch Domain That Regulates hsp90 Conformation

Grenert, J. P., Sullivan, W. P., Fadden, P., Haystead, T., Clark, J., Mimnaugh, E. G., Krutzsch, H. C., Ochel, H.-J., Schulte, T. W., Sausville, E. A., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.38.23843 · Cited by 568 · see citing works

Steroid receptors and their associated proteins

Smith, D. F., & Toft, D. O. (1993) · Molecular Endocrinology · doi:10.1210/mend.7.1.8446107 · Cited by 549 · see citing works

The common 90‐kd protein component of non‐transformed ‘8S’ steroid receptors is a heat‐shock protein.

CATELLI, M. G., Binart, N., Jung‐Testas, I., Renoir, J., Baulieu, E. E., Feramisco, J. R., & Wj, W. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb04055.x · Cited by 516 · see citing works

Preclinical pharmacologic evaluation of geldanamycin as an antitumor agent

Supko, J. G., Hickman, R. L., Grever, M. R., & Malspeis, L. (1995) · Cancer Chemotherapy and Pharmacology · doi:10.1007/bf00689048 · Cited by 512 · see citing works

The translation machinery and 70 kd heat shock protein cooperate in protein synthesis

Nelson, R., Ziegelhoffer, T., Nicolet, C. M., Werner‐Washburne, M., & Craig, E. A. (1992) · Cell · doi:10.1016/0092-8674(92)90269-i · Cited by 512 · see citing works

Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein.

Sánchez, E. R., Toft, D. O., Schlesinger, M. J., & Pratt, W. B. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38886-5 · Cited by 482 · see citing works

Disruption of the Raf-1-Hsp90 Molecular Complex Results in Destabilization of Raf-1 and Loss of Raf-1-Ras Association

Schulte, T. W., Blagosklonny, M. V., Ingui, C., & Neckers, L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.41.24585 · Cited by 457 · see citing works

Glucocorticoid receptor mutants that are constitutive activators of transcriptional enhancement

Godowski, P. J., Rusconi, S., Miesfeld, R. L., & Yamamoto, K. R. (1987) · Nature · doi:10.1038/325365a0 · Cited by 420 · 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

Evidence That the 90-kDa Heat Shock Protein Is Necessary for the Steroid Binding Conformation of the L Cell Glucocorticoid Receptor

Bresnick, E. H., Dalman, F. C., Sánchez, E. R., & Pratt, W. B. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83689-4 · Cited by 384 · see citing works

The mechanism of RU486 antagonism is dependent on the conformation of the carboxy-terminal tail of the human progesterone receptor

Vegeto, E., Allan, G. F., Schrader, W. T., Tsai, M., McDonnell, D. P., & O’Malley, B. W. (1992) · Cell · doi:10.1016/0092-8674(92)90234-4 · Cited by 376 · see citing works

Complete DNA sequence of yeast chromosome XI

Dujon, B., Alexandraki, D., André, B., Ansorge, W. J., Baladrón, V., Ballesta, J. P. G., Bánrévi, A., Bolle, P. A., Bolotin‐Fukuhara, M., Bossier, P., et al. (1994) · Nature · doi:10.1038/369371a0 · Cited by 374 · see citing works

Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90.

Blagosklonny, M. V., Toretsky, J. A., Bohen, S. P., & Neckers, L. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.16.8379 · Cited by 315 · see citing works

Mammalian Glucocorticoid Receptor Derivatives Enhance Transcription in Yeast

Schena, M., & Yamamoto, K. R. (1988) · Science · doi:10.1126/science.3043665 · Cited by 309 · see citing works

Dynamics of heat shock protein 90–progesterone receptor binding and the disactivation loop model for steroid receptor complexes

Smith, D. F. (1993) · Molecular Endocrinology · doi:10.1210/me.7.11.1418 · Cited by 300 · see citing works

Progesterone Receptor Structure and Function Altered by Geldanamycin, an hsp90-Binding Agent

Smith, D. F., Whitesell, L. J., Nair, S. C., Chen, S., Prapapanich, V., & Rimerman, R. A. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.12.6804 · Cited by 289 · see citing works

Folding of the Glucocorticoid Receptor by the Heat Shock Protein (hsp) 90-based Chaperone Machinery

Dittmar, K. D., Demady, D. R., Stancato, L., Krishna, P., & Pratt, W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.34.21213 · Cited by 288 · see citing works

Mutations in Hsp83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila

Cutforth, T. (1994) · Cell · doi:10.1016/0092-8674(94)90442-1 · Cited by 287 · see citing works

Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells

Whitesell, L. J., & Cook, P. (1996) · Molecular Endocrinology · doi:10.1210/mend.10.6.8776730 · Cited by 263 · see citing works

A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90.

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

Quantitation and Intracellular Localization of the 85K Heat Shock Protein by Using Monoclonal and Polyclonal Antibodies

Lai, B.-T., Chin, N. W., Stanek, A. E., Keh, W., & Lanks, K. W. (1984) · Molecular and Cellular Biology · doi:10.1128/mcb.4.12.2802 · Cited by 243 · 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

Binding of p23 and hsp90 during assembly with the progesterone receptor.

Johnson, J. L., & Toft, D. O. (1995) · Molecular Endocrinology · doi:10.1210/mend.9.6.8592513 · Cited by 233 · see citing works

A novel chaperone complex for steroid receptors involving heat shock proteins, immunophilins, and p23.

Johnson, J. L., & Toft, D. O. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31487-4 · Cited by 229 · 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

Interaction of the Rous Sarcoma Virus Protein pp60 src with the Cellular Proteins pp50 and pp90

Brugge, J. S. (1986) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-70810-7_1 · 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

[31] Use and selectivity of herbimycin A as inhibitor of protein-tyrosine kinases

Uehara, Y., & Fukazawa, H. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)01033-x · Cited by 216 · see citing works

In 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

Functional Specificity Among Hsp70 Molecular Chaperones

James, P. M., Pfund, C., & Craig, E. A. (1997) · Science · doi:10.1126/science.275.5298.387 · Cited by 202 · see citing works

The specific DNA binding activity of the dioxin receptor is modulated by the 90 kd heat shock protein.

Wilhelmsson, A., Cuthill, S., Denis, M. G., Wikström, A., Gustafsson, J.-Å., & Poellinger, L. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb08081.x · Cited by 198 · see citing works

Characterization of a Novel 23-Kilodalton Protein of Unactive Progesterone Receptor Complexes

Johnson, J. L., Beito, T. G., Krco, C. J., & Toft, D. O. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.3.1956 · Cited by 197 · see citing works

Hold 'em and Fold 'em: Chaperones and Signal Transduction

Bohen, S. P., Kralli, A., & Yamamoto, K. R. (1995) · Science · doi:10.1126/science.7761850 · Cited by 196 · 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

Folding of the Glucocorticoid Receptor by the Reconstituted hsp90-based Chaperone Machinery

Dittmar, K. D., & Pratt, W. B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.20.13047 · Cited by 184 · see citing works

Assembly of progesterone receptor with heat shock proteins and receptor activation are ATP mediated events.

Smith, D. F., Stensgard, B. A., Welch, W. J., & Toft, D. O. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48438-4 · Cited by 174 · see citing works

Proof that hsp70 is required for assembly of the glucocorticoid receptor into a heterocomplex with hsp90.

Hutchison, K. A., Dittmar, K. D., Czar, M. J., & Pratt, W. B. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37651-2 · Cited by 165 · see citing works

The Function of Steroid Hormone Receptors Is Inhibited by the hsp90-specific Compound Geldanamycin

Segnitz, B., & Gehring, U. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.30.18694 · Cited by 161 · see citing works

LEM1, an ATP-binding-cassette transporter, selectively modulates the biological potency of steroid hormones.

Kralli, A., Bohen, S. P., & Yamamoto, K. R. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.10.4701 · Cited by 160 · see citing works

Conservation of Hsp90 macromolecular complexes in Saccharomyces cerevisiae.

Chang, H.-C., & Lindquist, S. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31486-2 · Cited by 158 · see citing works

Suppression of c-Src activity by C-terminal Src kinase involves the c-Src SH2 and SH3 domains: analysis with Saccharomyces cerevisiae.

Murphy, S. M., Bergman, M., & Morgan, D. O. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.9.5290 · Cited by 130 · see citing works

The 23-kDa Acidic Protein in Reticulocyte Lysate Is the Weakly Bound Component of the hsp Foldosome That Is Required for Assembly of the Glucocorticoid Receptor into a Functional Heterocomplex with hsp90

Hutchison, K. A., Stancato, L. F., Owens-Grillo, J. K., Johnson, J. L., Krishna, P., Toft, D. O., & Pratt, W. B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.32.18841 · Cited by 125 · see citing works

An FK506-sensitive Transporter Selectively Decreases Intracellular Levels and Potency of Steroid Hormones

Kralli, A., & Yamamoto, K. R. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.29.17152 · Cited by 123 · see citing works

Genetic dissection of the signaling domain of a mammalian steroid receptor in yeast.

Garabedian, M. J., & Yamamoto, K. R. (1992) · Molecular Biology of the Cell · doi:10.1091/mbc.3.11.1245 · Cited by 103 · see citing works

Retinoic acid receptor belongs to a subclass of nuclear receptors that do not form "docking" complexes with hsp90

Dalman, F. C., Sturzenbecker, L. J., Levin, A. A., Lucas, D. A., Perdew, G. H., Petkovitch, M., Chambon, P., Grippo, J. F., & Pratt, W. B. (1991) · Biochemistry · doi:10.1021/bi00236a038 · Cited by 90 · see citing works

Protein components of the nonactivated glucocorticoid receptor.

Rexin, M., Busch, W., & Gehring, U. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54271-x · Cited by 82 · see citing works

A role for Hsp90 in retinoid receptor signal transduction.

Holley, S., & Yamamoto, K. R. (1995) · Molecular Biology of the Cell · doi:10.1091/mbc.6.12.1833 · Cited by 82 · see citing works

The viral erbA oncogene protein, a constitutive repressor in animal cells, is a hormone-regulated activator in yeast

Privalsky, M. L., Sharif, M., & Yamamoto, K. R. (1990) · Cell · doi:10.1016/0092-8674(90)90423-c · Cited by 75 · see citing works

[Experimental study of glucocorticoid in the treatment of acute respiratory distress syndrome induced by E.coli].

Song, Z.-F., Xie, W., Shan, H.-M., Guo, X.-H., & Sun, B. (2006) · PubMed · doi:10.1101/087969427.26.313 · Cited by 66 · see citing works

Growth inhibition of virus transformed cells in vitro and antitumor activity in vivo of geldanamycin and its derivatives.

Sasaki, K., Yasuda, H., & Onodera, K. (1979) · The Journal of Antibiotics · doi:10.7164/antibiotics.32.849 · Cited by 65 · see citing works

Reconstitution of retinoid X receptor function and combinatorial regulation of other nuclear hormone receptors in the yeast Saccharomyces cerevisiae.

Hall, B. L., Smit‐McBride, Z., & Privalsky, M. L. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.15.6929 · Cited by 64 · see citing works

A model of glucocorticoid receptor unfolding and stabilization by a heat shock protein complex

Pratt, W. B., Scherrer, L. C., Hutchison, K. A., & Dalman, F. C. (1992) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/0960-0760(92)90348-m · Cited by 60 · see citing works

Macbecins I and II, new antitumor antibiotics. I. Producing organism, fermentation and antimicrobial activities.

TANIDA, S., HASEGAWA, T., & Higashide, E. (1980) · The Journal of Antibiotics · doi:10.7164/antibiotics.33.199 · Cited by 52 · see citing works

A heat shock protein complex isolated from rabbit reticulocyte lysate can reconstitute a functional glucocorticoid receptor-Hsp90 complex

Scherrer, L. C., Hutchison, K. A., Sánchez, E. R., Randall, S. K., & Pratt, W. B. (1992) · Biochemistry · doi:10.1021/bi00147a017 · Cited by 49 · see citing works

Hsp90 Mutants Disrupt Glucocorticoid Receptor Ligand Binding and Destabilize Aporeceptor Complexes

Bohen, S. P. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.49.29433 · Cited by 45 · see citing works

Macbecins I and II, new antitumor antibiotics. II. Isolation and characterization.

Muroi, M., Izawa, M., KOSAI, Y., & Asai, M. (1980) · The Journal of Antibiotics · doi:10.7164/antibiotics.33.205 · Cited by 43 · see citing works

Heterotetrameric structure of the human progesterone receptor.

Rehberger, P. A., Rexin, M., & Gehring, U. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.17.8001 · Cited by 36 · see citing works

Antitumor and cytocidal activities of a newly isolated benzenoid ansamycin, macbecin I.

Ono, Y., Kozai, Y., & Ootsu, K. (1982) · PubMed · Cited by 10 · see citing works

Regulation of Signaling Protein Function and Trafficking by the hsp90/hsp70-Based Chaperone Machinery 1

Pratt, W., & Toft, D. (2003) · Experimental biology and medicine · doi:10.1177/153537020322800201 · Cited by 1,539 · see citing works

Folding of Newly Translated Proteins In Vivo: The Role of Molecular Chaperones

Frydman, J. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.603 · Cited by 1,170 · see citing works

Heat-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

Molecular Identification of Cytosolic Prostaglandin E2 Synthase That Is Functionally Coupled with Cyclooxygenase-1 in Immediate Prostaglandin E2Biosynthesis

Tanioka, T., Nakatani, Y., Semmyo, N., Murakami, M., & Kudo, I. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003504200 · Cited by 708 · 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

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

Diverse Cellular Functions of the Hsp90 Molecular Chaperone Uncovered Using Systems Approaches

McClellan, A. J., Xia, Y., Deutschbauer, A. M., Davis, R. W., Gerstein, M., & Frydman, J. (2007) · Cell · doi:10.1016/j.cell.2007.07.036 · Cited by 474 · see citing works

Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement

Pratt, W. B., Galigniana, M. D., Harrell, J. M., & DeFranco, D. B. (2004) · Cellular Signalling · doi:10.1016/j.cellsig.2004.02.004 · Cited by 285 · see citing works

Hsp90 stress potentiates rapid cellular adaptation through induction of aneuploidy

Chen, G., Bradford, W. D., Seidel, C. W., & Li, R. (2012) · Nature · doi:10.1038/nature10795 · Cited by 274 · see citing works

Folding and Quality Control of the VHL Tumor Suppressor Proceed through Distinct Chaperone Pathways

McClellan, A. J., Scott, M. D., & Frydman, J. (2005) · Cell · doi:10.1016/j.cell.2005.03.024 · Cited by 260 · see citing works

Chaperoning of Glucocorticoid Receptors

Pratt, W. B., Morishima, Y., Murphy, M. N., & Harrell, M. (2005) · Springer eBooks · doi:10.1007/3-540-29717-0_5 · Cited by 247 · see citing works

The Assembly of Progesterone Receptor-hsp90 Complexes Using Purified Proteins*

Kosano, H., Stensgard, B., Charlesworth, M., McMahon, N., & Toft, D. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.49.32973 · Cited by 251 · see citing works

Aha1 Binds to the Middle Domain of Hsp90, Contributes to Client Protein Activation, and Stimulates the ATPase Activity of the Molecular Chaperone

Lotz, G. P., Lin, H., Harst, A., & Obermann, W. M. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212761200 · Cited by 236 · see citing works

Hsp-90-associated oncoproteins: multiple targets of geldanamycin and its analogs

Blagosklonny, M. V. (2002) · Leukemia · doi:10.1038/sj.leu.2402415 · Cited by 235 · see citing works

Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co‐chaperone p23

Young, J. C., & Hartl, F. U. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5930 · Cited by 230 · see citing works

Structure, 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

Hsp90's secrets unfold: new insights from structural and functional studies

Caplan, A. J. (1999) · Trends in Cell Biology · doi:10.1016/s0962-8924(99)01580-9 · Cited by 178 · see citing works

The Co-chaperone p23 Arrests the Hsp90 ATPase Cycle to Trap Client Proteins

McLaughlin, S. H., Sobott, F., Yao, Z.-P., Zhang, W., Nielsen, P. R., Grossmann, J. G., Laue, E. D., Robinson, C. V., & Jackson, S. E. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.11.085 · Cited by 196 · see citing works

The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies

Freeman, B. C., Felts, S. J., Toft, D. O., & Yamamoto, K. R. (2000) · Genes & Development · doi:10.1101/gad.14.4.422 · Cited by 168 · see citing works

Distinct Roles for the Hsp40 and Hsp90 Molecular Chaperones during Cystic Fibrosis Transmembrane Conductance Regulator Degradation in Yeast

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

Structure of Hsp90–p23–GR reveals the Hsp90 client-remodelling mechanism

Noddings, C. M., Wang, R. Y.-R., Johnson, J. L., & Agard, D. A. (2022) · Nature · doi:10.1038/s41586-021-04236-1 · Cited by 165 · see citing works

A model for the cytoplasmic trafficking of signalling proteins involving the hsp90-binding immunophilins and p50cdc37.

Pratt, W., Silverstein, A., & Galigniana, M. (1999) · Cellular Signalling · doi:10.1016/s0898-6568(99)00064-9 · Cited by 171 · see citing works

Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90.

Chadli, A., Bouhouche, I., Sullivan, W. J., Stensgard, B., McMahon, N., Catelli, M., & Toft, D. (2000) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.220430297 · Cited by 159 · see citing works

Fungal heat-shock proteins in human disease

Burnie, J., Carter, T. L., Hodgetts, S. J., & Matthews, R. (2005) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2005.00001.x · Cited by 158 · see citing works

Crystal Structure and Activity of Human p23, a Heat Shock Protein 90 Co-chaperone

Weaver, A. J., Sullivan, W. P., Felts, S. J., Owen, B. A. L., & Toft, D. O. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003410200 · Cited by 136 · see citing works

The Yeast Hsp110 Family Member, Sse1, Is an Hsp90 Cochaperone

Liu, X., Morano, K. A., & Thiele, D. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.38.26654 · Cited by 133 · see citing works

Heat shock factor function and regulation in response to cellular stress, growth, and differentiation signals.

Morano, K. A., & Thiele, D. J. (1999) · Europe PMC (PubMed Central) · Cited by 134 · see citing works

Role for Hsp90-Associated Cochaperone p23 in Estrogen Receptor Signal Transduction

Knoblauch, R., & Garabedian, M. J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.5.3748 · Cited by 126 · see citing works

The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA‐dependent kinase PKR

Donzé, O., Abbas‐Terki, T., & Picard, D. (2001) · The EMBO Journal · doi:10.1093/emboj/20.14.3771 · Cited by 126 · see citing works

p23, a simple protein with complex activities

Felts, S. J., & Toft, D. O. (2003) · Cell Stress and Chaperones · doi:10.1379/1466-1268(2003)008 · Cited by 116 · see citing works

Estrogen Receptor-α Hinge-Region Lysines 302 and 303 Regulate Receptor Degradation by the Proteasome

Berry, N. B., Fan, M., & Nephew, K. P. (2008) · Molecular Endocrinology · doi:10.1210/me.2007-0449 · Cited by 112 · see citing works

In Vitro Reconstitution of Functional Hepadnavirus Reverse Transcriptase with Cellular Chaperone Proteins

Hu, J., Toft, D. O., Anselmo, D., & Wang, X. (2002) · Journal of Virology · doi:10.1128/jvi.76.1.269-279.2002 · Cited by 106 · see citing works

The Hsp Organizer Protein Hop Enhances the Rate of but Is Not Essential for Glucocorticoid Receptor Folding by the Multiprotein Hsp90-based Chaperone System

Morishima, Y., Kanelakis, K. C., Silverstein, A. M., Dittmar, K. D., Estrada, L., & Pratt, W. B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.10.6894 · Cited by 106 · see citing works

The heat shock protein 90 of Plasmodium falciparum and antimalarial activity of its inhibitor, geldanamycin

Kumar, R., Musiyenko, A., & Barik, S. (2003) · Malaria Journal · doi:10.1186/1475-2875-2-30 · Cited by 105 · see citing works

Antifungal Activities of Antineoplastic Agents: Saccharomyces cerevisiae as a Model System To Study Drug Action

Cardenas, M. E., Cruz, M. C., Poeta, M. D., Chung, N., Perfect, J. R., & Heitman, J. (1999) · Clinical Microbiology Reviews · doi:10.1128/cmr.12.4.583 · Cited by 103 · see citing works

An unstructured C-terminal region of the hsp90 co-chaperone p23 is important for its chaperone function 1 1Edited by R. Huber

Weikl, T., Abelmann, K., & Buchner, J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3172 · Cited by 97 · see citing works

The Hsp90 Cochaperone p23 Is the Limiting Component of the Multiprotein Hsp90/Hsp70-based Chaperone System in Vivo Where It Acts to Stabilize the Client Protein·Hsp90 Complex

Morishima, Y., Kanelakis, K. C., Murphy, P. J. M., Lowe, E. R., Jenkins, G. J., Osawa, Y., Sunahara, R. K., & Pratt, W. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m309814200 · Cited by 97 · see citing works

The Hsp90 Cochaperone p23 Is Essential for Perinatal Survival

Grad, I., McKee, T., Ludwig, S. M., Hoyle, G. W., Ruíz, P., Wurst, W., Floß, T., Miller, C. A., & Picard, D. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00734-06 · Cited by 91 · see citing works

Hsp104 Interacts with Hsp90 Cochaperones in Respiring Yeast

Abbas‐Terki, T., Donzé, O., Briand, P.-A., & Picard, D. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.22.7569-7575.2001 · Cited by 94 · see citing works

Chaperoning Checkpoint Kinase 1 (Chk1), an Hsp90 Client, with Purified Chaperones

Arlander, S. J. H., Felts, S. J., Wagner, J. M., Stensgard, B. A., Toft, D. O., & Karnitz, L. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508687200 · Cited by 92 · see citing works

CNS1 Encodes an Essential p60/Sti1 Homolog in Saccharomyces cerevisiae That Suppresses Cyclophilin 40 Mutations and Interacts with Hsp90

Dolinski, K. J., Cardenas, M. E., & Heitman, J. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.12.7344 · Cited by 87 · see citing works

Sti1 and Cdc37 Can Stabilize Hsp90 in Chaperone Complexes with a Protein Kinase

Lee, P. C., Shabbir, A., Cardozo, C. P., & Caplan, A. J. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-07-0480 · Cited by 85 · see citing works

p23/Sba1p protects against Hsp90 inhibitors independently of its intrinsic chaperone activity

Forafonov, F., Toogun, O. A., Grad, I., Suslova, E., Freeman, B. C., & Picard, D. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.02246-07 · Cited by 84 · see citing works

Hsp90 Binds and Regulates the Ligand-Inducible α Subunit of Eukaryotic Translation Initiation Factor Kinase Gcn2

Donzé, O., & Picard, D. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.12.8422 · Cited by 79 · see citing works

Aryl hydrocarbon (Ah) receptor levels are selectively modulated by hsp90-associated immunophilin homolog XAP2

Meyer, B. K., Petrulis, J. R., & Perdew, G. H. (2000) · Cell Stress and Chaperones · doi:10.1379/1466-1268(2000)005 · Cited by 105 · see citing works

The Biochemical Role of the Heat Shock Protein 90 Chaperone Complex in Establishing Human Telomerase Activity

Keppler, B. R., Grady, A. T., & Jarstfer, M. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511067200 · Cited by 75 · see citing works

Ligand-independent activation of oestrogen receptor α by caveolin-1

Schlegel, A., Chenguang, W. A. N. G., Pestell, R. G., & Lisanti, M. P. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3590203 · Cited by 74 · see citing works

The Cdc37 protein kinase–binding domain is sufficient for protein kinase activity and cell viability

Lee, P. C., Rao, J., Fliss, A., Yang, E., Garrett, S., & Caplan, A. J. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200210121 · Cited by 69 · see citing works

Hsp90 chaperone complexes are required for the activity and stability of yeast protein kinases Mik1, Wee1 and Swe1

Goes, F. S., & Martin, J. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02105.x · Cited by 64 · see citing works

Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle

Biebl, M. M., Lopez, A., Rehn, A., Freiburger, L., Lawatscheck, J., Blank, B., Sattler, M., & Buchner, J. (2021) · Nature Communications · doi:10.1038/s41467-021-21063-0 · Cited by 58 · see citing works

High levels of Hsp90 co-chaperone p23 promotes tumor progression and poor prognosis in breast cancer by increasing lymph node metastases and drug resistance

Simpson, N., Lambert, W. M., Watkins, R. A., Giashuddin, S., Huang, S., Oxelmark, E., Arju, R., Hochman, T., Goldberg, J. D., Schneider, R. J., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-1590 · Cited by 11 · see citing works

The Sch9 protein kinase regulates Hsp90 chaperone complex signal transduction activity in vivo

Morano, K. A., & Thiele, D. J. (1999) · The EMBO Journal · doi:10.1093/emboj/18.21.5953 · Cited by 62 · see citing works

BAG-1 family of cochaperones in the modulation of nuclear receptor action

Cato, A. C. B., & Mink, S. (2001) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/s0960-0760(01)00114-5 · Cited by 60 · see citing works

A Role for the Hsp40 Ydj1 in Repression of Basal Steroid Receptor Activity in Yeast

Johnson, J. L., & Craig, E. A. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.9.3027-3036.2000 · Cited by 56 · see citing works

The Right Tool for the Job: An Overview of Hsp90 Inhibitors

Koren, J., & Blagg, B. S. J. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-40204-4_9 · Cited by 51 · see citing works

Cns1 Is an Activator of the Ssa1 ATPase Activity

Hainzl, O., Wegele, H., Richter, K., & Büchner, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402189200 · Cited by 51 · see citing works

Hsp90 Nuclear Accumulation in Quiescence Is Linked to Chaperone Function and Spore Development in Yeast

Tapia, H., & Morano, K. A. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-05-0376 · Cited by 50 · see citing works

Functional Interactions between Hsp90 and the Co-chaperones Cns1 and Cpr7 in Saccharomyces cerevisiae

Tesic, M., Marsh, J. A., Cullinan, S. B., & Gaber, R. F. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304315200 · Cited by 50 · see citing works

The Hsp90 Co-Chaperones Cdc37 and Sti1 Interact Physically and Genetically

Abbas‐Terki, T., Briand, P.-A., Donzé, O., & Picard, D. (2002) · Biological Chemistry · doi:10.1515/bc.2002.152 · Cited by 47 · see citing works

Investigating the protein-protein interactions of the yeast Hsp90 chaperone system by two-hybrid analysis: potential uses and limitations of this approach

Millson, S. H., Truman, A. W., Wolfram, F., King, V., Panaretou, B., Prodromou, C., Pearl, L. H., & Piper, P. W. (2004) · Cell Stress and Chaperones · doi:10.1379/csc-29r1.1 · Cited by 46 · see citing works

Inhibition of GR‐mediated transcription by p23 requires interaction with Hsp90

Wochnik, G. M., Young, J. C., Schmidt, U., Holsboer, F., Hartl, F. U., & Rein, T. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00066-3 · Cited by 46 · see citing works

Fused Thiopyrano[2,3-d]thiazole Derivatives as Potential Anticancer Agents

Kryshchyshyn‐Dylevych, A. (2012) · Scientia Pharmaceutica · doi:10.3797/scipharm.1204-02 · Cited by 45 · see citing works

The p23 co-chaperone facilitates dioxin receptor signaling in a yeast model system

Cox, M. B., & Miller, C. A. (2002) · Toxicology Letters · doi:10.1016/s0378-4274(01)00465-9 · Cited by 43 · see citing works

The yeast response to heat shock

Trott, A. E., & Morano, K. A. (2007) · Springer eBooks · doi:10.1007/3-540-45611-2_3 · Cited by 43 · see citing works

The Identification of Wos2, a p23 Homologue That Interacts With Wee1 and Cdc2 in the Mitotic Control of Fission Yeasts

Muñoz, M. J., Bejarano, E. R., Daga, R. R., & Jiménez, J. (1999) · Genetics · doi:10.1093/genetics/153.4.1561 · Cited by 43 · see citing works

The Heat Shock Protein 70 Cochaperone YDJ1 Is Required for Efficient Membrane-Specific Flock House Virus RNA Replication Complex Assembly and Function in Saccharomyces cerevisiae

Weeks, S. A., & Miller, D. J. (2007) · Journal of Virology · doi:10.1128/jvi.02017-07 · Cited by 40 · see citing works

Identification and Characterization of Harc, a Novel Hsp90-associating Relative of Cdc37

Scholz, G. M., Cartledge, K., & Hall, N. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103889200 · Cited by 40 · see citing works

Genetic Dissection of p23, an Hsp90 Cochaperone, Reveals a Distinct Surface Involved in Estrogen Receptor Signaling

Oxelmark, E., Knoblauch, R. E., Arnal, S. M., Su, L. F., Schapira, M., & Garabedian, M. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305960200 · Cited by 38 · see citing works

The Molecular Chaperone Hsp90 Mediates Heme Activation of the Yeast Transcriptional Activator Hap1

Lee, H. C., Hon, T., & Li, Z. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106951200 · Cited by 38 · see citing works

General Structural and Functional Features of Molecular Chaperones

Edkins, A. L., & Boshoff, A. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-78397-6_2 · Cited by 36 · see citing works

The conserved NxNNWHW motif in Aha-type co-chaperones modulates the kinetics of Hsp90 ATPase stimulation

Mercier, R., Wolmarans, A., Schubert, J., Neuweiler, H., Johnson, J. L., & LaPointe, P. (2019) · Nature Communications · doi:10.1038/s41467-019-09299-3 · Cited by 31 · see citing works

The Hsp90 Molecular Chaperone Complex Regulates Maltose Induction and Stability of the Saccharomyces MAL Gene Transcription Activator Mal63p

Bali, M., Zhang, B., Morano, K. A., & Michels, C. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m309536200 · Cited by 30 · see citing works

The Hsp90 of Candida albicans can confer Hsp90 functions in Saccharomyces cerevisiae: a potential model for the processes that generate immunogenic fragments of this molecular chaperone in C. albicans infections

Panaretou, B., SINCLAIR, K. E., Prodromou, C., Johal, J., Pearl, L. H., & Piper, P. W. (1999) · Microbiology · doi:10.1099/00221287-145-12-3455 · Cited by 30 · see citing works

The C-terminal region of the human p23 chaperone modulates its structure and function

Seraphim, T. V., Gava, L. M., Mokry, D. Z., Cagliari, T. C., Barbosa, L. R. S., Ramos, C. H. I., & Borges, J. C. (2015) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.10.015 · Cited by 27 · see citing works

Regulation of Glucocorticoid Receptor Ligand-Binding Activity by the hsp90/hsp70-based Chaperone Machinery

Kanelakis, K. C., & Pratt, W. B. (2003) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(03)64010-3 · Cited by 25 · see citing works

A Mutation in the Catalytic Loop of Hsp90 Specifically Impairs ATPase Stimulation by Aha1p, But Not Hch1p

Horvat, N. K., Armstrong, H., Lee, B. L., Mercier, R., Wolmarans, A., Knowles, J., Spyracopoulos, L., & LaPointe, P. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.04.002 · Cited by 24 · see citing works

The sperm outer dense fiber protein is the 10th member of the superfamily of mammalian small stress proteins

Fontaine, J., Rest, J. S., Welsh, M. J., & Benndorf, R. (2003) · Cell Stress and Chaperones · doi:10.1379/1466-1268(2003)8 · Cited by 145 · see citing works

Pharmacological and Genetic Analysis of 90-kDa Heat Shock Isoprotein-Aryl Hydrocarbon Receptor Complexes

Cox, M. B., & Miller, C. A. (2003) · Molecular Pharmacology · doi:10.1124/mol.64.6.1549 · Cited by 22 · see citing works

Geldanamycin derivative inhibition of HGF/SF-mediated Met tyrosine kinase receptor-dependent urokinase-plasminogen activation

Shen, Y., Xie, Q. R., Norberg, M., Sausville, E. A., Woude, G. V., & Wenkert, D. (2005) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2005.05.038 · Cited by 20 · see citing works

Evidence for Hsp90 Co-chaperones in Regulating Hsp90 Function and Promoting Client Protein Folding

Cox, M. B., & Johnson, J. L. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7477-1_28 · Cited by 20 · see citing works

Chemo-signal therapy, an emerging new approach to modify drug resistance in breast cancer

Pusztai, L., Esteva, F. J., Cristofanilli, M., & Hung, M. (1999) · Cancer Treatment Reviews · doi:10.1053/ctrv.1999.0132 · Cited by 20 · see citing works

Computational aided mechanistic understanding of Camellia sinensis bioactive compounds against co‐chaperone p23 as potential anticancer agent

Bharadwaj, S., Lee, K. E., Dwivedi, V., Yadava, U., & Kang, S.-G. (2019) · Journal of Cellular Biochemistry · doi:10.1002/jcb.29229 · Cited by 18 · see citing works

Heat shock protein 90 inhibitors repurposed against Entamoeba histolytica

Shahinas, D., Debnath, A., Benedict, C., McKerrow, J. H., & Pillai, D. R. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00368 · Cited by 19 · see citing works

Leishmania donovani P23 protects parasites against HSP90 inhibitor-mediated growth arrest

Hombach, A., Ommen, G., Sattler, V., & Clos, J. (2015) · Cell Stress and Chaperones · doi:10.1007/s12192-015-0595-y · Cited by 18 · see citing works

Detection of changes in gene regulatory patterns, elicited by perturbations of the Hsp90 molecular chaperone complex, by visualizing multiple experiments with an animation

Echeverria, P. C., Forafonov, F., Pandey, D., Muhlebach, G., & Picard, D. (2011) · BioData Mining · doi:10.1186/1756-0381-4-15 · Cited by 15 · see citing works

Hsp90 Co-chaperones as Drug Targets in Cancer: Current Perspectives

Edkins, A. L. (2016) · Topics in medicinal chemistry · doi:10.1007/7355_2015_99 · Cited by 13 · see citing works

Transgenic overexpression of p23 induces spontaneous hydronephrosis in mice

Lee, J., Kim, H. J., Moon, J. A., Sung, Y. H., Baek, I., Roh, J.-I., Ha, N. Y., Kim, S.-Y., Bahk, Y. Y., Lee, J. E., et al. (2011) · International Journal of Experimental Pathology · doi:10.1111/j.1365-2613.2011.00762.x · Cited by 12 · see citing works

p23 and Aha1: Distinct Functions Promote Client Maturation

Biebl, M. M., & Büchner, J. (2022) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-14740-1_6 · Cited by 9 · see citing works

Heat-induced degradation of overexpressed glucocorticoid receptor

Siriani, D., Mitsiou, D. J., & Alexis, Μ. N. (2005) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2005.01.013 · Cited by 9 · see citing works

The Hsp90/Cdc37p chaperone system is a determinant of molybdate resistance in Saccharomyces cerevisiae

Millson, S. H., Nuttall, J. M., Mollapour, M., & Piper, P. W. (2009) · Yeast · doi:10.1002/yea.1670 · Cited by 9 · see citing works

Potentiometric flow-injection determination of vitamin C and glutathione with a chemically prepared tubular silver electrode.

Kolar, M., Dobčnik, D., & Radić, N. (2000) · PubMed · Cited by 9 · see citing works

Chaperones and Their Role in Telomerase Ribonucleoprotein Biogenesis and Telomere Maintenance

Viviescas, M. A., Cano, M. I. N., & Segatto, M. (2018) · Current Proteomics · doi:10.2174/1570164615666180713103133 · Cited by 5 · see citing works

Chemogenomic Analysis Identifies Macbecin II as a Compound Specific for SMAD4‐Negative Colon Cancer Cells

Kaiser, C. E., Meurice, N., Gonzales, I. M., Arora, S., Beaudry, C. E., Bisanz, K. M., Robeson, A. C., Petit, J. L., & Azorsa, D. O. (2010) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2010.00949.x · Cited by 4 · see citing works

Yeast-Based Reporter Assays for the Functional Characterization of Cochaperone Interactions with Steroid Hormone Receptors

Balsiger, H. A., & Cox, M. B. (2009) · Methods in molecular biology · doi:10.1007/978-1-60327-575-0_8 · Cited by 4 · see citing works

Identifying functional interactions with molecular chaperones

Johnson, J. L., & Craig, E. A. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)51863-2 · Cited by 4 · see citing works

Design, synthesis, in silico and in vitro investigation of 4-cyano-2-phenyl-1,3-oxazole-5-sulfonamide derivatives

Pilyo, S. G., Kachaeva, M. V., Severin, O. O., Kozachenko, O. P., Zhirnov, V. V., & Броварец, В. С. (2024) · Ukrainica Bioorganica Acta · doi:10.15407/bioorganica2024.01.030 · Cited by 3 · see citing works

HSP90 Co-Chaperones in Saccharomyces Cerevisiae

Tesic, M., & Gaber, R. F. (2007) · Springer eBooks · doi:10.1007/978-1-4020-5963-6_6 · Cited by 1 · see citing works

Emergence and Characterization of the p23 Molecular Chaperone

Echtenkamp, F., & Freeman, B. (2014) · Springer eBooks · doi:10.1007/978-1-4939-1130-1_9 · Cited by 1 · see citing works

General Structural and Functional Features of Molecular Chaperones.

Edkins, A., & Boshoff, A. (2021) · Advances in Experimental Medicine and Biology · doi:10.1007/978-94-007-7438-4_2 · Cited by 32 · see citing works

Hsp90 and p23 facilitate steroid hormone receptor signaling in yeast

Tan, X., Wilson, M. J., & Miller, C. A. (2009) · The FASEB Journal · doi:10.1096/fasebj.23.1_supplement.673.7

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

p23/Sba1p Protects against Hsp90 Inhibitors Independently of Its Intrinsic Chaperone Activity‡

Freeman, B. C., & Picard, D. (2008)

The Hsp90 Cochaperone p23 Is the Limiting Component of the Multiprotein Hsp90/Hsp70-based Chaperone System in Vivo Where It Acts to Stabilize the Client Protein·Hsp90 Complex

Morishima, Y., Kanelakis, K. C., Murphy, P. J. M., Lowe, E. R., Jenkins, G. J., Osawa, Y., Sunahara, R. K., & Pratt, W. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m309814200 · Cited by 97 · see citing works

Cooperation of heat shock protein 90 and p23 in aryl hydrocarbon receptor signaling

Cox, M. B., & Miller, C. A. (2004) · Cell Stress and Chaperones · doi:10.1379/460.1 · Cited by 29 · see citing works