Molecular chaperone targeting and regulation by BAG family proteins

Structure of Bcl-x L -Bak Peptide Complex: Recognition Between Regulators of Apoptosis

Sattler, M., Liang, H., Nettesheim, D., Meadows, R. P., Harlan, J. E., Eberstadt, M., Yoon, H. S., Shuker, S. B., Chang, B. S., Minn, A. J., et al. (1997) · Science · doi:10.1126/science.275.5302.983 · Cited by 1,476

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 1,173

Cloning and functional analysis of BAG-1: A novel Bcl-2-binding protein with anti-cell death activity

Takayama, S., Sato, T., Krajewski, S., Kochel, K., Irie, S., Milian, J. A., & Reed, J. C. (1995) · Cell · doi:10.1016/0092-8674(95)90410-7 · Cited by 857

Three-dimensional structure of the neuronal-Sec1–syntaxin 1a complex

Misura, K. M. S., Scheller, R. H., & Weis, W. I. (2000) · Nature · doi:10.1038/35006120 · Cited by 785

Function of WW Domains as Phosphoserine- or Phosphothreonine-Binding Modules

Lu, P.-J., Zhou, X. Z., Shen, M., & Lu, K. P. (1999) · Science · doi:10.1126/science.283.5406.1325 · Cited by 682

Siah-1, SIP, and Ebi Collaborate in a Novel Pathway for β-Catenin Degradation Linked to p53 Responses

Matsuzawa, S.-I., & Reed, J. C. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00242-8 · Cited by 587

An Evolutionarily Conserved Family of Hsp70/Hsc70 Molecular Chaperone Regulators

Takayama, S., Xie, Z., & Reed, J. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.2.781 · Cited by 517

BAG-1 modulates the chaperone activity of Hsp70/Hsc70

Takayama, S. (1997) · The EMBO Journal · doi:10.1093/emboj/16.16.4887 · Cited by 514

Crystal Structure of the Nucleotide Exchange Factor GrpE Bound to the ATPase Domain of the Molecular Chaperone DnaK

Harrison, C. J., Hayer-Hartl, M., Liberto, M. D., Hartl, F.-U., & Kuriyan, J. (1997) · Science · doi:10.1126/science.276.5311.431 · Cited by 497

The Ubiquitin-related BAG-1 Provides a Link between the Molecular Chaperones Hsc70/Hsp70 and the Proteasome

Lüders, J., Demand, J., & Höhfeld, J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.7.4613 · Cited by 489

Stress management – heat shock protein-70 and the regulation of apoptosis

Beere, H. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01874-2 · Cited by 435

Structure of a Bag/Hsc70 Complex: Convergent Functional Evolution of Hsp70 Nucleotide Exchange Factors

Sondermann, H., Scheufler, C., Schneider, C., Höhfeld, J., Hartl, F.-U., & Moarefi, I. (2001) · Science · doi:10.1126/science.1057268 · Cited by 435

Prevention of Constitutive TNF Receptor 1 Signaling by Silencer of Death Domains

Jiang, Y., Woronicz, J. D., Liu, W., & Goeddel, D. V. (1999) · Science · doi:10.1126/science.283.5401.543 · Cited by 417

GrpE-like regulation of the Hsc70 chaperone by the anti-apoptotic protein BAG-1

Hohfeld, J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.20.6209 · Cited by 393

DAP kinase activates a p19ARF/p53-mediated apoptotic checkpoint to suppress oncogenic transformation

Raveh, T., Droguett, G., Horwitz, M. S., DePinho, R. A., & Kimchi, A. (2001) · Nature Cell Biology · doi:10.1038/35050500 · Cited by 361

Bcl-2 interacting protein, BAG-1, binds to and activates the kinase Raf-1.

Wang, H. G., Takayama, S., Rapp, U. R., & Reed, J. C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.14.7063 · Cited by 361

Three-Dimensional Structure of an Evolutionarily Conserved N-Terminal Domain of Syntaxin 1A

Fernandez, I., Ubach, J., Dulubova, I., Zhang, X., Südhof, T. C., & Rizo, J. (1998) · Cell · doi:10.1016/s0092-8674(00)81742-0 · Cited by 346

HGF receptor associates with the anti-apoptotic protein BAG-1 and prevents cell death.

Bardelli, A., Longati, P., Albero, D., Goruppi, S., Schneider, C., Ponzetto, C., & Comoglio, P. M. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01009.x · Cited by 312

Chaperones get in touch: the Hip-Hop connection

Frydman, J., & Höhfeld, J. (1997) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(97)01005-0 · Cited by 291

Bag1–Hsp70 mediates a physiological stress signalling pathway that regulates Raf-1/ERK and cell growth

Song, J., Takeda, M., & Morimoto, R. I. (2001) · Nature Cell Biology · doi:10.1038/35060068 · Cited by 284

Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange.

Brehmer, D., Rüdiger, S., Gässler, C. S., Klostermeier, D., Packschies, L., Reinstein, J., Mayer, M. P., & Bukau, B. (2001) · Nature Structural Biology · doi:10.1038/87588 · Cited by 231

Expression and location of Hsp70/Hsc-binding anti-apoptotic protein BAG-1 and its variants in normal tissues and tumor cell lines.

Takayama, S.-I. J., Krajewski, S., Krajewska, M., Kitada, S., Zapata, J. M., Kochel, K., Knee, D. A., Scudiero, D. A., Tudor, G., Miller, G. J., et al. (1998) · PubMed · Cited by 215

Molecular Chaperone Interactions with Steroid Receptors: an Update

Cheung, J. C. Y., & Smith, D. F. (2000) · Molecular Endocrinology · doi:10.1210/me.14.7.939 · Cited by 207

p53-inducible human homologue of Drosophila seven in absentia (Siah) inhibits cell growth: suppression by BAG-1

Matsuzawa, S.-I. (1998) · The EMBO Journal · doi:10.1093/emboj/17.10.2736 · Cited by 203

Bis, a Bcl-2-binding protein that synergizes with Bcl-2 in preventing cell death

Lee, J.-H., Takahashi, T., Yasuhara, N., Inazawa, J., Kamada, S., & Tsujimoto, Y. (1999) · Oncogene · doi:10.1038/sj.onc.1203043 · Cited by 197

BAG-1L Protein Enhances Androgen Receptor Function

Froesch, B. A., Takayama, S., & Reed, J. C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.19.11660 · Cited by 193

Mammalian cells express two differently localized Bag-1 isoforms generated by alternative translation initiation

PACKHAM, G., BRIMMELL, M., & CLEVELAND, L. J. (1997) · Biochemical Journal · doi:10.1042/bj3280807 · Cited by 188

A protein that interacts with members of the nuclear hormone receptor family: identification and cDNA cloning.

Zeiner, M., & Gehring, U. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.25.11465 · Cited by 185

BAG-1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release

Bimston, D., Song, J., Winchester, D., Takayama, S., Reed, J. C., & Morimoto, R. I. (1998) · The EMBO Journal · doi:10.1093/emboj/17.23.6871 · Cited by 180

Bag-1M Accelerates Nucleotide Release for Human Hsc70 and Hsp70 and Can Act Concentration-dependent as Positive and Negative Cofactor

Gässler, C. S., Wiederkehr, T., Brehmer, D., Bukau, B., & Mayer, M. P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105328200 · Cited by 164

CAIR-1/BAG-3 forms an EGF-regulated ternary complex with phospholipase C-γ and Hsp70/Hsc70

Doong, H., Price, J., Kim, Y. S., Gasbarre, C., Probst, J., Liotta, L. A., Blanchette, J., Rizzo, K., & Kohn, E. (2000) · Oncogene · doi:10.1038/sj.onc.1203797 · Cited by 163

Mammalian protein RAP46: an interaction partner and modulator of 70 kDa heat shock proteins

Zeiner, M., Gebauer, M., & Gehring, U. (1997) · The EMBO Journal · doi:10.1093/emboj/16.18.5483 · Cited by 152

Structural analysis of BAG1 cochaperone and its interactions with Hsc70 heat shock protein.

Briknarová, K., Takayama, S.-I. J., Brive, L., Havert, M. L., Knee, D. A., Velasco, J., Homma, S. T., Cabezas, E., Stuart, J., Hoyt, D. W., et al. (2001) · Nature Structural Biology · doi:10.1038/86236 · Cited by 150

Human BAG-1/RAP46 protein is generated as four isoforms by alternative translation initiation and overexpressed in cancer cells

Yang, X., Chernenko, G. A., Hao, Y., Ding, Z., Pater, M. M., Pater, A., & Tang, S. (1998) · Oncogene · doi:10.1038/sj.onc.1202032 · Cited by 145

RAP46 Is a Negative Regulator of Glucocorticoid Receptor Action and Hormone-induced Apoptosis

Kullmann, M. K., Schneikert, J., Moll, J., Heck, S., Zeiner, M., Gehring, U., & Cato, A. C. B. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.23.14620 · Cited by 140

Interaction of BAG-1 with Retinoic Acid Receptor and Its Inhibition of Retinoic Acid-induced Apoptosis in Cancer Cells

Liu, R., Takayama, S.-I. J., Zheng, Y., Froesch, B. A., Chen, G., Zhang, X., Reed, J. C., & Zhang, X.-K. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.27.16985 · Cited by 127

Scythe: a novel reaper‐binding apoptotic regulator

Thress, K. S., Henzel, W. J., Shillinglaw, W., & Kornbluth, S. A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.21.6135 · Cited by 126

A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE

Buchberger, A., Schröder, H., Büttner, M., Valencia, A., & Bukau, B. (1994) · Nature Structural & Molecular Biology · doi:10.1038/nsb0294-95 · Cited by 122

Human DnaJ Homologs dj2 and dj3, and bag-1 Are Positive Cochaperones of hsc70

Terada, K., & Mori, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002021200 · Cited by 121

Molecular chaperones and the art of recognizing a lost cause

McClellan, A. J., & Frydman, J. (2001) · Nature Cell Biology · doi:10.1038/35055162 · Cited by 117

BAG-1: A Novel Biomarker Predicting Long-Term Survival in Early-Stage Breast Cancer

Turner, B. C., Krajewski, S., Krajewska, M., Takayama, S.-I. J., Gumbs, A. A., Carter, D., Rebbeck, T. R., Haffty, B. G., & Reed, J. C. (2001) · Journal of Clinical Oncology · doi:10.1200/jco.2001.19.4.992 · Cited by 105

Characterization of Interactions between the Anti-apoptotic Protein BAG-1 and Hsc70 Molecular Chaperones

Stuart, J. K., Myszka, D. G., Joss, L., Mitchell, R. S., McDonald, S. M., Xie, Z., Takayama, S.-I. J., Reed, J. C., & Ely, K. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.35.22506 · Cited by 103

Reversible inhibition of Hsp70 chaperone function by Scythe and Reaper

Thress, K. S., Song, J., Morimoto, R. I., & Kornbluth, S. (2001) · The EMBO Journal · doi:10.1093/emboj/20.5.1033 · Cited by 101

Role of Bag-1 in the Survival and Proliferation of the Cytokine-Dependent Lymphocyte Lines, Ba/F3 and Nb2

Clevenger, C. V., Thickman, K. R., Ngo, W., Chang, W., Takayama, S.-I. J., & Reed, J. C. (1997) · Molecular Endocrinology · doi:10.1210/mend.11.5.9925 · Cited by 97

A Nuclear Action of the Eukaryotic Cochaperone Rap46 in Downregulation of Glucocorticoid Receptor Activity

Schneikert, J., Hübner, S., Martin, E., & Cato, A. C. B. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.146.5.929 · Cited by 94

Apoptosis: Silencing the death receptors

Tschopp, J., Martinon, F., & Hofmann, K. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80233-4 · Cited by 92

The hsp70-associating protein Hap46 binds to DNA and stimulates transcription

Zeiner, M., Niyaz, Y., & Gehring, U. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.10194 · Cited by 83

Expression of BAG-1 in Invasive Breast Carcinomas

Tang, S.-C., Shaheta, N., Chernenko, G. A., Khalifa, M., & Wang, X. (1999) · Journal of Clinical Oncology · doi:10.1200/jco.1999.17.6.1710 · Cited by 76

Structure-Function Analysis of Bag1 Proteins

Knee, D. A., Froesch, B. A., Nuber, U. A., Takayama, S.-I. J., & Reed, J. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010841200 · Cited by 74

High level expression of differentially localized BAG-1 isoforms in some oestrogen receptor-positive human breast cancers

Brimmell, M., Burns, J. S., Munson, P., McDonald, L., O'Hare, M. J., Lakhani, S. R., & Packham, G. (1999) · British Journal of Cancer · doi:10.1038/sj.bjc.6690805 · Cited by 73

Enhanced Expression of Silencer of Death Domains (SODD/BAG-4) in Pancreatic Cancer

Ozawa, F., Friess, H., Zimmermann, A., Kleeff, J. H., & Büchler, M. W. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.2610 · Cited by 56

BAG1L Enhances Trans-activation Function of the Vitamin D Receptor

Güzey, M., Takayama, S.-I. J., & Reed, J. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004977200 · Cited by 55

Transcriptional activation by the human Hsp70-associating protein Hap50

Niyaz, Y., Zeiner, M., & Gehring, U. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.10.1839 · Cited by 33

Nuclear BAG-1 localization and the risk of recurrence after radiation therapy in laryngeal carcinomas

Yamauchi, H., Adachi, M., Sakata, K., Hareyama, M., Satoh, M., Himi, T., Takayama, S.-I. J., Reed, J. C., & Imai, K. (2001) · Cancer Letters · doi:10.1016/s0304-3835(01)00397-4 · Cited by 32

The HSP70 chaperone machinery: J proteins as drivers of functional specificity

Kampinga, H. H., & Craig, E. A. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2941 · Cited by 1,755

Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3

Gamerdinger, M., Hajieva, P., Kaya, A. M., Wolfrum, U., Hartl, F. U., & Behl, C. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.29 · Cited by 522

Molecular chaperones and the stress of oncogenesis

Mosser, D. D., & Morimoto, R. I. (2004) · Oncogene · doi:10.1038/sj.onc.1207529 · Cited by 502

Mutation in BAG3 causes severe dominant childhood muscular dystrophy

Selcen, D., Muntoni, F., Burton, B. K., Pegoraro, E., Sewry, C., Bite, A. V., & Engel, A. G. (2009) · Annals of Neurology · doi:10.1002/ana.21553 · Cited by 357

HspB8 Chaperone Activity toward Poly(Q)-containing Proteins Depends on Its Association with Bag3, a Stimulator of Macroautophagy

Carra, S., Seguin, S. J., Lambert, H., & Landry, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706304200 · Cited by 349