Biological and Chemical Approaches to Diseases of Proteostasis Deficiency

Principles that Govern the Folding of Protein Chains

Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096 · see citing works

Autophagy in the Pathogenesis of Disease

Levine, B., & Kroemer, G. (2008) · Cell · doi:10.1016/j.cell.2007.12.018 · Cited by 7,069 · see citing works

Origin and physiological roles of inflammation

Medzhitov, R. (2008) · Nature · doi:10.1038/nature07201 · Cited by 6,618 · see citing works

Signal integration in the endoplasmic reticulum unfolded protein response

Ron, D., & Walter, P. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2199 · Cited by 6,308 · see citing works

Mechanisms linking obesity to insulin resistance and type 2 diabetes

Kahn, S. E., Hull, R. L., & Utzschneider, K. M. (2006) · Nature · doi:10.1038/nature05482 · Cited by 5,448 · see citing works

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide

Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744 · see citing works

Network pharmacology: the next paradigm in drug discovery

Hopkins, A. L. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.118 · Cited by 4,622 · see citing works

A gene atlas of the mouse and human protein-encoding transcriptomes

Su, A. I., Wiltshire, T., Batalov, S., Lapp, H., Ching, K. A., Block, D., Zhang, J., Soden, R., Hayakawa, M., Kreiman, G., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400782101 · Cited by 3,475 · see citing works

The human disease network

Goh, K.-I., Cusick, M. E., Valle, D., Childs, B., Vidal, M., & Barabási, A.-L. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701361104 · Cited by 3,242 · see citing works

Adapting Proteostasis for Disease Intervention

Balch, W. E., Morimoto, R. I., Dillin, A., & Kelly, J. W. (2008) · Science · doi:10.1126/science.1141448 · Cited by 2,495 · see citing works

Chemical Chaperones Reduce ER Stress and Restore Glucose Homeostasis in a Mouse Model of Type 2 Diabetes

Özcan, U., Yilmaz, E., Özcan, L., Furuhashi, M., Vaillancourt, E., Smith, R. O., Görgün, C. Z., & Hotamisligil, G. S. (2006) · Science · doi:10.1126/science.1128294 · Cited by 2,413 · see citing works

Macromolecular Crowding and Confinement: Biochemical, Biophysical, and Potential Physiological Consequences

Zhou, H., Rivas, G., & Minton, A. P. (2008) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.37.032807.125817 · Cited by 2,130 · see citing works

From endoplasmic-reticulum stress to the inflammatory response

Zhang, K., & Kaufman, R. J. (2008) · Nature · doi:10.1038/nature07203 · Cited by 2,010 · see citing works

Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes

Milne, J. C., Lambert, P. D., Schenk, S., Carney, D. P., Smith, J. J., Gagne, D. J., Jin, L., Boss, O., Perni, R. B., Vu, C. B., et al. (2007) · Nature · doi:10.1038/nature06261 · Cited by 1,707 · see citing works

Molecular Chaperones and Protein Quality Control

Bukau, B., Weissman, J. S., & Horwich, A. L. (2006) · Cell · doi:10.1016/j.cell.2006.04.014 · Cited by 1,556 · see citing works

Histone deacetylase inhibitors: molecular mechanisms of action

Xu, W. S., Parmigiani, R. B., & Marks, P. A. (2007) · Oncogene · doi:10.1038/sj.onc.1210620 · Cited by 1,542 · see citing works

Intrinsically Disordered Proteins in Human Diseases: Introducing the D 2 Concept

Uversky, V. N., Oldfield, C. J., & Dunker, A. K. (2008) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.37.032807.125924 · Cited by 1,406 · see citing works

A Selective Inhibitor of eIF2α Dephosphorylation Protects Cells from ER Stress

Boyce, M., Bryant, K. F., Jousse, C., Long, K., Harding, H. P., Scheuner, D. L., Kaufman, R. J., Ma, D., Coen, D. M., Ron, D., et al. (2005) · Science · doi:10.1126/science.1101902 · Cited by 1,403 · see citing works

HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS.

Pandey, U. B., Nie, Z., Batlevi, Y., McCray, B. A., Ritson, G. P., Nedelsky, N. B., Schwartz, S. L., DiProspero, N. A., Knight, M. A., Schuldiner, O., et al. (2007) · Nature · doi:10.1038/nature05853 · Cited by 1,234 · see citing works

The Role for Endoplasmic Reticulum Stress in Diabetes Mellitus

Eizirik, D. L., Cardozo, A. K., & Cnop, M. (2008) · Endocrine Reviews · doi:10.1210/er.2007-0015 · Cited by 1,173 · see citing works

The Protein Folding Problem

Dill, K. A., Ozkan, S. B., Shell, M. S., & Weikl, T. R. (2008) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.37.092707.153558 · Cited by 1,163 · see citing works

Astrocytes as determinants of disease progression in inherited amyotrophic lateral sclerosis

Yamanaka, K., Chun, S. J., Boillee, S., Fujimori-Tonou, N., Yamashita, H., Gutmann, D. H., Takahashi, R., Misawa, H., & Cleveland, D. W. (2008) · Nature Neuroscience · doi:10.1038/nn2047 · Cited by 1,140 · 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

Histone acetyltransferase complexes: one size doesn't fit all

Lee, K. K. W., & Workman, J. L. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2145 · Cited by 1,091 · see citing works

Mistranslation-Induced Protein Misfolding as a Dominant Constraint on Coding-Sequence Evolution

Drummond, D. A., & Wilke, C. O. (2008) · Cell · doi:10.1016/j.cell.2008.05.042 · Cited by 1,041 · see citing works

Macromolecular Modeling with Rosetta

Das, R., & Baker, D. A. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.062906.171838 · Cited by 995 · see citing works

The endoplasmic reticulum and the unfolded protein response

Malhotra, J. D., & Kaufman, R. J. (2007) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2007.09.003 · Cited by 984 · see citing works

The Chemical Genomic Portrait of Yeast: Uncovering a Phenotype for All Genes

Hillenmeyer, M. E., Fung, E., Wildenhain, J., Pierce, S. E., Hoon, S. S., Lee, W., Proctor, M. J., St.Onge, R. P., Tyers, M., Koller, D., et al. (2008) · Science · doi:10.1126/science.1150021 · Cited by 978 · see citing works

Misfolded proteins partition between two distinct quality control compartments

Kaganovich, D., Kopito, R., & Frydman, J. (2008) · Nature · doi:10.1038/nature07195 · Cited by 932 · see citing works

Direct inhibition of the longevity-promoting factor SKN-1 by insulin-like signaling in C. elegans

Tullet, J. M. A., Hertweck, M., An, J. H., Baker, J., Hwang, J. Y., Liu, S., Oliveira, R. P., Baumeister, R., & Blackwell, T. K. (2008) · Cell · doi:10.1016/j.cell.2008.01.030 · Cited by 923 · see citing works

Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging

Morimoto, R. I. (2008) · Genes & Development · doi:10.1101/gad.1657108 · Cited by 872 · see citing works

Opposing activities protect against age-onset proteotoxicity

Cohen, E., Bieschke, J., Perciavalle, R. M., Kelly, J. W., & Dillin, A. (2006) · Science · doi:10.1126/science.1124646 · Cited by 843 · see citing works

Protein networks in disease

Ideker, T., & Sharan, R. (2008) · Genome Research · doi:10.1101/gr.071852.107 · Cited by 817 · see citing works

Endoplasmic Reticulum Stress in Disease Pathogenesis

Lin, J. H., Walter, P., & Yen, T. S. B. (2007) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathmechdis.3.121806.151434 · Cited by 814 · see citing works

Gut hormones and the regulation of energy homeostasis

Murphy, K. G., & Bloom, S. R. (2006) · Nature · doi:10.1038/nature05484 · Cited by 778 · see citing works

ER chaperones in mammalian development and human diseases

Ni, M., & Lee, A. S. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.04.045 · Cited by 736 · see citing works

Dissection of mechanisms of Chinese medicinal formula Realgar- Indigo naturalis as an effective treatment for promyelocytic leukemia

Wang, L., Zhou, G., Liu, P., Song, J.-H., Liang, Y., Yan, X.-J., Xu, F., Wang, B., Mao, J., Shen, Z.-X., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0712365105 · Cited by 729 · see citing works

Stress-Inducible Regulation of Heat Shock Factor 1 by the Deacetylase SIRT1

Westerheide, S. D., Anckar, J., Stevens, S. M., Sistonen, L., & Morimoto, R. I. (2009) · Science · doi:10.1126/science.1165946 · Cited by 722 · see citing works

Hsp90 Potentiates the Rapid Evolution of New Traits: Drug Resistance in Diverse Fungi

Cowen, L. E., & Lindquist, S. (2005) · Science · doi:10.1126/science.1118370 · Cited by 698 · see citing works

Chop deletion reduces oxidative stress, improves β cell function, and promotes cell survival in multiple mouse models of diabetes

Song, B., Scheuner, D. L., Ron, D., Pennathur, S., & Kaufman, R. J. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34587 · Cited by 693 · see citing works

Epigenetics and aging: the targets and the marks

Fraga, M. F., & Esteller, M. (2007) · Trends in Genetics · doi:10.1016/j.tig.2007.05.008 · Cited by 690 · see citing works

Molecular Understanding and Modern Application of Traditional Medicines: Triumphs and Trials

Corson, T. W., & Crews, C. M. (2007) · Cell · doi:10.1016/j.cell.2007.08.021 · Cited by 656 · see citing works

Progressive disruption of cellular protein folding in models of polyglutamine diseases

Gidalevitz, T., Ben-Zvi, A., Ho, K. H., Brignull, H. R., & Morimoto, R. I. (2006) · Science · doi:10.1126/science.1124514 · Cited by 643 · see citing works

Accelerated transport and maturation of lysosomal α–galactosidase A in Fabry lymphoblasts by an enzyme inhibitor

Fan, J., Ishii, S., Asano, N., & Suzuki, Y. (1999) · Nature Medicine · doi:10.1038/4801 · Cited by 616 · see citing works

The Endoplasmic Reticulum: Folding, Calcium Homeostasis, Signaling, and Redox Control

Görlach, A., Klappa, P., & Kietzmann, T. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1391 · Cited by 616 · see citing works

Islet Amyloid in Type 2 Diabetes, and the Toxic Oligomer Hypothesis

Haataja, L., Gurlo, T., Huang, C. J., & Butler, P. C. (2008) · Endocrine Reviews · doi:10.1210/er.2007-0037 · Cited by 612 · see citing works

Aging and Survival: The Genetics of Life Span Extension by Dietary Restriction

Mair, W. B., & Dillin, A. G. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.061206.171059 · Cited by 600 · see citing works

Islet Amyloid: A Critical Entity in the Pathogenesis of Type 2 Diabetes

Hull, R. L., Westermark, G. T., Westermark, P., & Kahn, S. E. (2004) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2004-0405 · Cited by 586 · see citing works

Thematic review series: Adipocyte Biology. Adipocyte stress: the endoplasmic reticulum and metabolic disease

Gregor, M. F., & Hotamisligil, G. S. (2007) · Journal of Lipid Research · doi:10.1194/jlr.r700007-jlr200 · Cited by 586 · see citing works

Intrinsic Disorder Is a Common Feature of Hub Proteins from Four Eukaryotic Interactomes

Haynes, C. A., Oldfield, C. J., Ji, F., Klitgord, N., Cusick, M. E., Predrag Radivojac, A., Uversky, V. N., Vidal, M., & Iakoucheva, L. M. (2006) · PLoS Computational Biology · doi:10.1371/journal.pcbi.0020100 · Cited by 583 · see citing works

Rapamycin and mTOR-independent autophagy inducers ameliorate toxicity of polyglutamine-expanded huntingtin and related proteinopathies

Sarkar, S., Ravikumar, B., Floto, R. A., & Rubinsztein, D. C. (2009) · Cell Death & Differentiation · doi:10.1038/cdd.2008.110 · Cited by 578 · see citing works

Chaperone-Mediated Autophagy

Dice, J. F. (2007) · Autophagy · doi:10.4161/auto.4144 · Cited by 569 · see citing works

Small-molecule correctors of defective F508-CFTR cellular processing identified by high-throughput screening

Pedemonte, N. (2005) · Journal of Clinical Investigation · doi:10.1172/jci24898 · Cited by 542 · see citing works

New Genes Tied to Endocrine, Metabolic, and Dietary Regulation of Lifespan from a Caenorhabditis elegans Genomic RNAi Screen

Hansen, M., Hsu, A., Dillin, A. G., & Kenyon, C. J. (2005) · PLoS Genetics · doi:10.1371/journal.pgen.0010017 · Cited by 533 · see citing works

Prevention of Transthyretin Amyloid Disease by Changing Protein Misfolding Energetics

Hammarström, P., Wiseman, R. L., Powers, E. T., & Kelly, J. W. (2003) · Science · doi:10.1126/science.1079589 · Cited by 526 · see citing works

The Unfolded Protein Response: A Pathway That Links Insulin Demand with β-Cell Failure and Diabetes

Scheuner, D., & Kaufman, R. J. (2008) · Endocrine Reviews · doi:10.1210/er.2007-0039 · Cited by 525 · see citing works

Autophagy: Basic Principles and Relevance to Disease

Kundu, M., & Thompson, C. B. (2008) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev.pathmechdis.2.010506.091842 · Cited by 523 · see citing works

Regulation of macroautophagy by mTOR and Beclin 1 complexes

Pattingre, S., Espert, L., Biard‐Piechaczyk, M., & Codogno, P. (2007) · Biochimie · doi:10.1016/j.biochi.2007.08.014 · Cited by 521 · see citing works

Chemical chaperones increase the cellular activity of N370S β-glucosidase: A therapeutic strategy for Gaucher disease

Sawkar, A. R., Cheng, W., Beutler, E., Wong, C., Balch, W. E., & Kelly, J. W. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.192582899 · Cited by 508 · see citing works

HDAC6: a key regulator of cytoskeleton, cell migration and cell–cell interactions

Valenzuela-Fernández, A., Cabrero, J. R., Serrador, J. M., & Sánchez‐Madrid, F. (2008) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.04.003 · Cited by 500 · see citing works

The Biological and Chemical Basis for Tissue-Selective Amyloid Disease

Sekijima, Y., Wiseman, R. L., Matteson, J., Hammarström, P., Miller, S. R., Sawkar, A. R., Balch, W. E., & Kelly, J. W. (2005) · Cell · doi:10.1016/j.cell.2005.01.018 · Cited by 490 · see citing works

Heat Shock Response Modulators as Therapeutic Tools for Diseases of Protein Conformation

Westerheide, S. D., & Morimoto, R. I. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.r500010200 · Cited by 481 · see citing works

The Hsp90 molecular chaperone: an open and shut case for treatment

Pearl, L. H., Prodromou, C., & Workman, P. (2008) · Biochemical Journal · doi:10.1042/bj20071640 · Cited by 447 · see citing works

Loss of the Tuberous Sclerosis Complex Tumor Suppressors Triggers the Unfolded Protein Response to Regulate Insulin Signaling and Apoptosis

Özcan, U., Özcan, L., Yılmaz, E., Düvel, K., Şahin, M., Manning, B. D., & Hotamışlıgil, G. S. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.12.023 · Cited by 434 · see citing works

Two Families of Chaperonin: Physiology and Mechanism

Horwich, A. L., Fenton, W. A., Chapman, E., & Farr, G. W. (2007) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.23.090506.123555 · Cited by 422 · see citing works

The human PDI family: Versatility packed into a single fold

Appenzeller‐Herzog, C., & Ellgaard, L. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2007.11.010 · Cited by 416 · see citing works

Arsenical-based cancer drugs

Dilda, P. J., & Hogg, P. J. (2007) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2007.05.001 · Cited by 389 · see citing works

Sorting, recognition and activation of the misfolded protein degradation pathways through macroautophagy and the proteasome

Ding, W., & Yin, X.-M. (2008) · Autophagy · doi:10.4161/auto.5190 · Cited by 383 · see citing works

Sirtuins in Aging and DiseasePreprint

Guarente, L. (2007) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2007.72.024 · Cited by 371 · see citing works

A novel Hsp90 inhibitor to disrupt Hsp90/Cdc37 complex against pancreatic cancer cells

Zhang, T., Hamza, A., Cao, X., Wang, B., Yu, S., Zhan, C., & Sun, D. (2008) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-07-0484 · Cited by 365 · see citing works

Heat shock protein 90: The cancer chaperone

Neckers, L. (2007) · Journal of Biosciences · doi:10.1007/s12038-007-0051-y · Cited by 363 · see citing works

Regulation of the Cellular Heat Shock Response in Caenorhabditis elegans by Thermosensory Neurons

Prahlad, V., Cornelius, T., & Morimoto, R. I. (2008) · Science · doi:10.1126/science.1156093 · Cited by 359 · see citing works

Chemical and Biological Approaches Synergize to Ameliorate Protein-Folding Diseases

Mu, T., Ong, D. S. T., Wang, Y., Balch, W. E., Yates, J. R., Segatori, L., & Kelly, J. W. (2008) · Cell · doi:10.1016/j.cell.2008.06.037 · Cited by 359 · see citing works

Inhibitors of the heat shock response: Biology and pharmacology

Powers, M. V., & Workman, P. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.05.040 · Cited by 320 · see citing works

Native State Kinetic Stabilization as a Strategy To Ameliorate Protein Misfolding Diseases: A Focus on the Transthyretin Amyloidoses

Johnson, S. M., Wiseman, R. L., Sekijima, Y., Green, N. S., Adamski‐Werner, S. L., & Kelly, J. W. (2005) · Accounts of Chemical Research · doi:10.1021/ar020073i · Cited by 306 · see citing works

Dietary histone deacetylase inhibitors: From cells to mice to man

Dashwood, R. H., & HO, E. (2007) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2007.04.001 · Cited by 299 · see citing works

The HDAC inhibitor 4b ameliorates the disease phenotype and transcriptional abnormalities in Huntington's disease transgenic mice

Thomas, E. A., Coppola, G., Desplats, P., Tang, B., Soragni, E., Burnett, R., Gao, F., Fitzgerald, K. M., Borok, J. F., Herman, D., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804249105 · Cited by 291 · see citing works

Targeting Hsp90: small-molecule inhibitors and their clinical development

Taldone, T., Gozman, A., Maharaj, R., & Chiosis, G. (2008) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2008.06.015 · Cited by 284 · see citing works

Polyglutamine diseases: emerging concepts in pathogenesis and therapy

Shao, J., & Diamond, M. I. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm213 · Cited by 284 · see citing works

Role of insulin-like signalling in Drosophila lifespan

Giannakou, M. E., & PARTRIDGE, L. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.02.007 · Cited by 283 · see citing works

Genetics of familial amyotrophic lateral sclerosis

Valdmanis, P. N., & Rouleau, G. A. (2008) · Neurology · doi:10.1212/01.wnl.0000296811.19811.db · Cited by 280 · see citing works

The experimental survey of protein-folding energy landscapes

Oliveberg, M., & Wolynes, P. G. (2005) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583506004185 · Cited by 275 · see citing works

The Sirtuin family: therapeutic targets to treat diseases of aging

Milne, J. C., & Denu, J. M. (2008) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2008.01.019 · Cited by 271 · see citing works

Oxidative activation of antioxidant defence

Winyard, P. G., Moody, C. J., & Jacob, C. (2005) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.06.001 · Cited by 254 · see citing works

An elt-3/elt-5/elt-6 GATA transcription circuit guides aging in C. elegans

Budovskaya, Y. V., Wu, K., Southworth, L. K., Jiang, M., Tedesco, P., Johnson, T. E., & Kim, S. K. (2008) · Cell · doi:10.1016/j.cell.2008.05.044 · Cited by 253 · see citing works

Development and application of Hsp90 inhibitors

Solit, D. B., & Chiosis, G. (2007) · Drug Discovery Today · doi:10.1016/j.drudis.2007.10.007 · Cited by 251 · see citing works

Molecular Physiology of Preconditioning-Induced Brain Tolerance to Ischemia

Obrenovitch, T. P. (2008) · Physiological Reviews · doi:10.1152/physrev.00039.2006 · Cited by 250 · see citing works

Class IIa histone deacetylases: regulating the regulators

Martin, M., Kettmann, R., & Dequiedt, F. (2007) · Oncogene · doi:10.1038/sj.onc.1210613 · Cited by 243 · see citing works

G Protein-Coupled Receptor Trafficking in Health and Disease: Lessons Learned to Prepare for Therapeutic Mutant Rescue in Vivo

Conn, P. M., Ulloa‐Aguirre, A., Ito, J., & Janovick, J. A. (2007) · Pharmacological Reviews · doi:10.1124/pr.59.3.2 · Cited by 242 · see citing works

Calcium signalling: Past, present and future

Petersen, O. H., Michalak, M., & Verkhratsky, A. (2005) · Cell Calcium · doi:10.1016/j.ceca.2005.06.023 · Cited by 238 · see citing works

Regulation of Pancreatic β Cell Mass by Neuronal Signals from the Liver

Imai, J., Katagiri, H., Yamada, T., Ishigaki, Y., Suzuki, T., Kudo, H., Uno, K., Hasegawa, Y., Gao, J., Kaneko, K., et al. (2008) · Science · doi:10.1126/science.1163971 · Cited by 236 · see citing works

Intraluminal calcium as a primary regulator of endoplasmic reticulum function

Burdakov, D., Petersen, O. H., & Verkhratsky, A. (2005) · Cell Calcium · doi:10.1016/j.ceca.2005.06.010 · Cited by 228 · see citing works

The Tumor Proteasome Is a Primary Target for the Natural Anticancer Compound Withaferin A Isolated from “Indian Winter Cherry”

Yang, H., Shi, G., & Dou, Q. P. (2006) · Molecular Pharmacology · doi:10.1124/mol.106.030015 · Cited by 227 · see citing works

Regulation of protein turnover by acetyltransferases and deacetylases

Sadoul, K., Boyault, C., Pabion, M., & Khochbin, S. (2007) · Biochimie · doi:10.1016/j.biochi.2007.06.009 · Cited by 223 · see citing works

Activation of Heat Shock and Antioxidant Responses by the Natural Product Celastrol: Transcriptional Signatures of a Thiol-targeted Molecule

Trott, A. E., West, J. D., Klaić, L., Westerheide, S. D., Silverman, R. B., Morimoto, R. I., & Morano, K. A. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-10-1004 · Cited by 223 · see citing works

Polyglutamine Proteins at the Pathogenic Threshold Display Neuron-Specific Aggregation in a Pan-NeuronalCaenorhabditis elegansModel

Brignull, H. R., Moore, F. E., Tang, S. J., & Morimoto, R. I. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.0990-06.2006 · Cited by 213 · see citing works

Hsp70 Molecular Chaperones: Emerging Roles in Human Disease and Identification of Small Molecule Modulators

Brodsky, J. L., & Chiosis, G. (2006) · Current Topics in Medicinal Chemistry · doi:10.2174/156802606777811997 · Cited by 202 · see citing works

Transcriptional targets of sirtuins in the coordination of mammalian physiology

Feige, J. N., & Auwerx, J. H. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.03.012 · Cited by 202 · see citing works

New insights into the mechanism of heat shock response activation

Shamovsky, I., & Nudler, E. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-7458-y · Cited by 197 · see citing works

Common molecular signature in SOD1 for both sporadic and familial amyotrophic lateral sclerosis

Gruzman, A., Wood, W. L., Alpert, E., Prasad, M. D., Miller, R. G., Rothstein, J. D., Bowser, R. P., Hamilton, R. L., Wood, T. D., Cleveland, D. W., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705044104 · Cited by 190 · see citing works

SIR2: a potential target for calorie restriction mimetics

Chen, D., & Guarente, L. (2007) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2006.12.004 · Cited by 185 · see citing works

Reversal of a full-length mutant huntingtin neuronal cell phenotype by chemical inhibitors of polyglutamine-mediated aggregation

Wang, J., Ginés, S., MacDonald, M. E., & Gusella, J. F. (2005) · BMC Neuroscience · doi:10.1186/1471-2202-6-1 · Cited by 179 · see citing works

Role of Proteasomes in Cellular Regulation

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Protein misfolding and disease: from the test tube to the organism

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