The interaction network of the chaperonin CCT

Functional organization of the yeast proteome by systematic analysis of protein complexes

Gavin, A., Böesche, M., Krause, R., Grandi, P., Marzioch, M., Bauer, A., Schultz, J., Rick, J. M., Michon, A., Cruciat, C., et al. (2002) · Nature · doi:10.1038/415141a · Cited by 4,729 · see citing works

Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry

Ho, Y., Gruhler, A., Heilbut, A. M., Bader, G. D., Moore, L., Adams, S., Millar, A., Taylor, P. P., Bennett, K. L., Boutilier, K., et al. (2002) · Nature · doi:10.1038/415180a · Cited by 3,573 · see citing works

Global landscape of protein complexes in the yeast Saccharomyces cerevisiae

Krogan, N. J., Cagney, G., Yu, H., Zhong, G., Guo, X., Ignatchenko, A., Li, J., Pu, S., Datta, N., Tikuisis, A., et al. (2006) · Nature · doi:10.1038/nature04670 · Cited by 2,915 · see citing works

Proteome survey reveals modularity of the yeast cell machinery

Gavin, A., Aloy, P., Grandi, P., Krause, R., Böesche, M., Marzioch, M., Rau, C., Jensen, L. J., Bastuck, S., Dümpelfeld, B., et al. (2006) · Nature · doi:10.1038/nature04532 · Cited by 2,544 · see citing works

Systematic Genetic Analysis with Ordered Arrays of Yeast Deletion Mutants

Tong, A. H. Y., Evangelista, M., Parsons, A. B., Xu, H., Bader, G. D., Pagé, N., Robinson, M., Raghibizadeh, S., Hogue, C. W. V., Bussey, H., et al. (2001) · Science · doi:10.1126/science.1065810 · Cited by 2,138 · see citing works

Global Mapping of the Yeast Genetic Interaction Network

Tong, A. H. Y., Lesage, G., Bader, G. D., Ding, H., Xu, H., Xin, X., Young, J., Berriz, G. F., Brost, R. L., Chang, M., et al. (2004) · Science · doi:10.1126/science.1091317 · Cited by 2,070 · 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

Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi

Katinka, M., Duprat, S., Cornillot, E., Méténier, G., Thomarat, F., Prensier, G., Barbe, V., Peyretaillade, E., Brottier, P., Wincker, P., et al. (2001) · Nature · doi:10.1038/35106579 · Cited by 1,051 · see citing works

Global analysis of protein phosphorylation in yeast

Ptacek, J., Devgan, G., Michaud, G. A., Zhu, H., Zhu, X., Fasolo, J., Guo, H., Jona, G., Breitkreutz, A., Sopko, R., et al. (2005) · Nature · doi:10.1038/nature04187 · Cited by 970 · see citing works

Logic of the Yeast Metabolic Cycle: Temporal Compartmentalization of Cellular Processes

Tu, B. P., Kudlicki, A. S., Rowicka, M., & McKnight, S. L. (2005) · Science · doi:10.1126/science.1120499 · Cited by 889 · see citing works

Functional dissection of protein complexes involved in yeast chromosome biology using a genetic interaction map

Collins, S. R., Miller, K. M., Maas, N. L., Roguev, A., Fillingham, J., Chu, C. S., Schuldiner, M., Gebbia, M., Recht, J., Shales, M., et al. (2007) · Nature · doi:10.1038/nature05649 · Cited by 869 · see citing works

Navigating the Chaperone Network: An Integrative Map of Physical and Genetic Interactions Mediated by the Hsp90 Chaperone

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

Toward a protein–protein interaction map of the budding yeast: A comprehensive system to examine two-hybrid interactions in all possible combinations between the yeast proteins

Ito, T., Tashiro, K., Muta, S., Ozawa, R., Chiba, T., Nishizawa, M., Yamamoto, K., Kuhara, S., & Sakaki, Y. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.3.1143 · Cited by 814 · see citing works

Genome-wide analysis of mRNA translation profiles in <i>Saccharomyces</i> <i>cerevisiae</i>

Arava, Y., Wang, Y., Storey, J. D., Liu, C. L., Brown, P. O., & Herschlag, D. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0635171100 · Cited by 663 · see citing works

Prefoldin, a Chaperone that Delivers Unfolded Proteins to Cytosolic Chaperonin

Vainberg, I. E., Lewis, S. A., Rommelaere, H., Ampè, C., Vandekerckhove, J. S., Klein, H. L., & Cowan, N. J. (1998) · Cell · doi:10.1016/s0092-8674(00)81446-4 · Cited by 567 · see citing works

Osprey: a network visualization system

Breitkreutz, B., Stark, C., & Tyers, M. (2003) · Genome biology · doi:10.1186/gb-2003-4-3-r22 · Cited by 472 · see citing works

Structure-Based Assembly of Protein Complexes in Yeast

Aloy, P., Böttcher, B., Ceulemans, H., Leutwein, C., Mellwig, C., Fischer, S., Gavin, A.-C., Bork, P., Superti-Furga, G., Serrano, L., et al. (2004) · Science · doi:10.1126/science.1092645 · Cited by 383 · see citing works

Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets

Spiess, C., Meyer, A. S., Reißmann, S., & Frydman, J. (2004) · Trends in Cell Biology · doi:10.1016/j.tcb.2004.09.015 · Cited by 377 · see citing works

In vivo newly translated polypeptides are sequestered in a protected folding environment

Thulasiraman, V., Yang, C., & Frydman, J. (1999) · The EMBO Journal · doi:10.1093/emboj/18.1.85 · Cited by 350 · see citing works

The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo

Sternlicht, H., Farr, G. W., Sternlicht, M. L., Driscoll, J. K., Willison, K., & Yaffe, M. B. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.20.9422 · Cited by 341 · see citing works

A novel protein complex promoting formation of functional α‐ and γ‐tubulin

Geissler, S., Siegers, K., & Schiebel, E. (1998) · The EMBO Journal · doi:10.1093/emboj/17.4.952 · Cited by 334 · see citing works

T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol

Lewis, V. A., Hynes, G. M., Dong, Z., Saibil, H. R., & Willison, K. R. (1992) · Nature · doi:10.1038/358249a0 · Cited by 308 · see citing works

The GRID: The General Repository for Interaction Datasets

Breitkreutz, B., Stark, C., & Tyers, M. (2003) · Genome biology · doi:10.1186/gb-2003-4-3-r23 · Cited by 294 · see citing works

Methods in yeast genetics : a Cold Spring Harbor Laboratory course manual

Adams, A. E. (1998) · Medical Entomology and Zoology · Cited by 293 · see citing works

The <i>S. cerevisiae</i> SET3 complex includes two histone deacetylases, Hos2 and Hst1, and is a meiotic-specific repressor of the sporulation gene program

Pijnappel, W. W. M. P., Schaft, D., Roguev, A., Shevchenko, A., Tekotte, H., Wilm, M., Rigaut, G., Séraphin, B., Aasland, R., & Stewart, A. F. (2001) · Genes &amp; Development · doi:10.1101/gad.207401 · Cited by 265 · see citing works

A Proteome-wide Approach Identifies Sumoylated Substrate Proteins in Yeast

Panse, V. G., Hardeland, U., Werner, T., Küster, B., & Hurt, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407950200 · Cited by 254 · see citing works

Metabolic cycles as an underlying basis of biological oscillations.

Tu, B. P., & McKnight, S. L. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1980 · Cited by 229 · see citing works

Structure and function of a protein folding machine: the eukaryotic cytosolic chaperonin CCT

Valpuesta, J., Martín‐Benito, J., Gómez‐Puertas, P., Carrascosa, J. L., & Willison, K. R. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03180-0 · Cited by 229 · see citing works

Some assembly required: yeast septins provide the instruction manual

Versele, M., & Thorner, J. W. (2005) · Trends in Cell Biology · doi:10.1016/j.tcb.2005.06.007 · Cited by 227 · see citing works

Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae

Haslbeck, M., Braun, N., Stromer, T., Richter, B., Model, N., Weinkauf, S., & Büchner, J. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600080 · Cited by 216 · see citing works

The CCT Chaperonin Promotes Activation of the Anaphase-Promoting Complex through the Generation of Functional Cdc20

Camasses, A., Bogdanova, A. I., Shevchenko, A., & Zachariae, W. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00244-2 · Cited by 209 · see citing works

Prefoldin–Nascent Chain Complexes in the Folding of Cytoskeletal Proteins

Hansen, W. J., Cowan, N. J., & Welch, W. J. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.145.2.265 · Cited by 205 · see citing works

Doc1 mediates the activity of the anaphase‐promoting complex by contributing to substrate recognition

Passmore, L. A., McCormack, E. A., Au, S. W. N., Paul, A., Willison, K. R., Harper, J. W., & Barford, D. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg084 · Cited by 201 · see citing works

Applicability of Tandem Affinity Purification MudPIT to Pathway Proteomics in Yeast

Graumann, J., Dunipace, L., Seol, J. H., McDonald, W. H., Yates, J. R., Wold, B. J., & Deshaies, R. J. (2003) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m300099-mcp200 · Cited by 139 · see citing works

Assembly of the SMRT–histone deacetylase 3 repression complex requires the TCP-1 ring complex

Guenther, M. G., Yu, J., Kao, G. D., Yen, T. J., & Lazar, M. A. (2002) · Genes &amp; Development · doi:10.1101/gad.1037502 · Cited by 138 · see citing works

A yeast TCP-1-like protein is required for actin function in vivo.

Vinh, D. B. N., & Drubin, D. G. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.19.9116 · Cited by 136 · see citing works

Mutation in the epsilon subunit of the cytosolic chaperonin-containing t-complex peptide-1 (Cct5) gene causes autosomal recessive mutilating sensory neuropathy with spastic paraplegia

Bouhouche, A., Benomar, A., Bouslam, N., Chkili, T., & Yahyaoui, M. (2006) · Journal of Medical Genetics · doi:10.1136/jmg.2005.039230 · Cited by 130 · see citing works

Substantial CCT activity is required for cell cycle progression and cytoskeletal organization in mammalian cells

Grantham, J., Brackley, K. I., & Willison, K. R. (2006) · Experimental Cell Research · doi:10.1016/j.yexcr.2006.03.028 · Cited by 129 · see citing works

Two yeast genes with similarity to TCP-1 are required for microtubule and actin function in vivo.

Chen, X., Sullivan, D. S., & Huffaker, T. C. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.19.9111 · Cited by 127 · see citing works

Cytosolic Chaperonin Is Up-regulated during Cell Growth

Yokota, S., Yanagi, H., Yura, T., & KUBOTA, H. Y. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.37070 · Cited by 119 · see citing works

Characterization and over‐expression of chaperonin t‐complex proteins in colorectal cancer

Coghlin, C., Carpenter, B., Dundas, S. R., Lawrie, L. C., Telfer, C., & Murray, G. I. (2006) · The Journal of Pathology · doi:10.1002/path.2056 · Cited by 111 · see citing works

Facilitated Folding of Actins and Tubulins Occurs via a Nucleotide-Dependent Interaction between Cytoplasmic Chaperonin and Distinctive Folding Intermediates

Melki, R., & Cowan, N. J. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.5.2895 · Cited by 110 · see citing works

The essential yeast Tcp1 protein affects actin and microtubules.

Ursic, D., Sedbrook, J. C., Himmel, K. L., & Culbertson, M. R. (1994) · Molecular Biology of the Cell · doi:10.1091/mbc.5.10.1065 · Cited by 106 · see citing works

Mechanism of Assembly of G Protein βγ Subunits by Protein Kinase CK2-phosphorylated Phosducin-like Protein and the Cytosolic Chaperonin Complex

Lukov, G. L., Baker, C. M., Ludtke, P. J., Hu, T., Carter, M. D., Hackett, R. A., Thulin, C. D., & Willardson, B. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601590200 · Cited by 83 · see citing works

PhLP3 Modulates CCT-mediated Actin and Tubulin Folding via Ternary Complexes with Substrates

Stirling, P. C., Cuéllar, J., Alfaro, G., Khadali, F. E., Beh, C. T., Valpuesta, J., Melki, R., & Leroux, M. R. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513235200 · Cited by 79 · see citing works

Cytosolic chaperonin protects folding intermediates of Gβ from aggregation by recognizing hydrophobic β-strands

Kubota, S., KUBOTA, H. Y., & Nagata, K. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600195103 · Cited by 77 · see citing works

Regulatory interaction of phosducin-like protein with the cytosolic chaperonin complex

McLaughlin, J. N., Thulin, C. D., Hart, S. J., Resing, K. A., Ahn, N. G., & Willardson, B. M. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.112075699 · Cited by 76 · see citing works

Quantitative actin folding reactions using yeast CCT purified via an internal tag in the CCT3/gamma subunit.

Pappenberger, G., Mccormack, E. A., & Willison, K. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.05.003 · Cited by 75 · see citing works

Deciphering Protein Complexes and Protein Interaction Networks by Tandem Affinity Purification and Mass Spectrometry

Shevchenko, A., Schaft, D., Roguev, A., Pijnappel, W. W. M. P., Stewart, A. F., & Shevchenko, A. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m200005-mcp200 · Cited by 69 · see citing works

Type II chaperonns, prefoldin, and the tubulin-specific chaperones

Cowan, N. J., & Lewis, S. A. (2001) · Advances in protein chemistry · doi:10.1016/s0065-3233(01)59003-8 · Cited by 68 · see citing works

The cytosolic chaperonin CCT associates to cytoplasmic microtubular structures during mammalian spermiogenesis and to heterochromatin in germline and somatic cells

Souès, S. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(03)00248-9 · Cited by 63 · see citing works

ATP-Induced Allostery in the Eukaryotic Chaperonin CCT Is Abolished by the Mutation G345D in CCT4 that Renders Yeast Temperature-Sensitive for Growth

Shimon, L., Hynes, G. M., McCormack, E. A., Willison, K. R., & Horovitz, A. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.01.011 · Cited by 58 · see citing works

Alf1p, a CLIP-170 Domain-containing Protein, Is Functionally and Physically Associated with α-Tubulin

Feierbach, B., Nogales, E., Downing, K. H., & Stearns, T. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.144.1.113 · Cited by 58 · see citing works

Functional Interaction between Phosducin-like Protein 2 and Cytosolic Chaperonin Is Essential for Cytoskeletal Protein Function and Cell Cycle Progression

Stirling, P. C., Srayko, M., Takhar, K. S., Pozniakovsky, A., Hyman, A. A., & Leroux, M. R. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-01-0069 · Cited by 53 · see citing works

Physiological effects of unassembled chaperonin Cct subunits in the yeastSaccharomyces cerevisiae

Kabir, M. A., Kamińska, J., Segel, G. B., Bethlendy, G., Lin, P., Seta, F. D., Blegen, C., Swiderek, K. M., dek, T. O., Arndt, K. T., et al. (2005) · Yeast · doi:10.1002/yea.1210 · Cited by 47 · see citing works

SCEPTRANS: an online tool for analyzing periodic transcription in yeast

Kudlicki, A. S., Rowicka, M., & Otwinowski, Z. (2007) · Bioinformatics · doi:10.1093/bioinformatics/btm126 · Cited by 36 · see citing works

Structure and Function of the Cytosolic Chaperonin CCT

Valpuesta, J., Carrascosa, J. L., & Willison, K. R. (2005) · doi:10.1002/9783527619498.ch54 · Cited by 28 · see citing works

What Does the Microsporidian E. cuniculi Tell Us About the Origin of the Eukaryotic Cell?

Fedorov, A. N., & Hartman, H. (2004) · Journal of Molecular Evolution · doi:10.1007/s00239-003-0085-1 · Cited by 17 · see citing works

The roles of the cytosolic chaperonin, CCT, in normal eukaryotic cell growth

Willison, K. R., & Grantham, J. (2001) · doi:10.1093/oso/9780199638680.003.0004 · Cited by 13 · see citing works

Molecular Chaperone Functions in Protein Folding and Proteostasis

Kim, Y., Hipp, M. S., Bracher, A., Hayer-Hartl, M. K., & Hartl, F. U. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060208-092442 · Cited by 1,468 · see citing works

Converging concepts of protein folding in vitro and in vivo

Hartl, F. U., & Hayer-Hartl, M. K. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1591 · Cited by 1,186 · see citing works

Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies

Yam, A. Y.-W., Xia, Y., Lin, H. J., Burlingame, A. L., Gerstein, M., & Frydman, J. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1515 · Cited by 413 · see citing works

Affinity-purification coupled to mass spectrometry: basic principles and strategies

Dunham, W. H., Mullin, M., & Gingras, A. (2012) · PROTEOMICS · doi:10.1002/pmic.201100523 · Cited by 368 · see citing works

Capturing the phosphorylation and protein interaction landscape of the plant TOR kinase

Leene, J. V., Han, C., Gadeyne, A., Eeckhout, D., Matthijs, C., Cannoot, B., Winne, N. D., Persiau, G., Slijke, E. V. D., van de Cotte, B., et al. (2019) · Nature Plants · doi:10.1038/s41477-019-0378-z · Cited by 269 · see citing works

An atlas of chaperone–protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell

Gong, Y., Kakihara, Y., Krogan, N. J., Greenblatt, J. F., Emili, A., Zhang, Z., & Houry, W. A. (2009) · Molecular Systems Biology · doi:10.1038/msb.2009.26 · Cited by 222 · see citing works

Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis

Finka, A., & Goloubinoff, P. (2013) · Cell Stress and Chaperones · doi:10.1007/s12192-013-0413-3 · Cited by 218 · see citing works

Septin functions in organ system physiology and pathology

Dolat, L., Hu, Q., & Spiliotis, E. T. (2013) · Biological Chemistry · doi:10.1515/hsz-2013-0233 · Cited by 187 · see citing works

A Direct Regulatory Interaction between Chaperonin TRiC and Stress-Responsive Transcription Factor HSF1

Neef, D. W., Jaeger, A. M., Gómez‐Pastor, R., Willmund, F., Frydman, J., & Thiele, D. J. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.09.056 · Cited by 163 · see citing works

Chaperonins: two rings for folding

Yébenes, H., Mesa, P., Muñoz, I. G., Montoya, G., & Valpuesta, J. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.05.003 · Cited by 162 · see citing works

The Genome of the Obligate Intracellular Parasite Trachipleistophora hominis: New Insights into Microsporidian Genome Dynamics and Reductive Evolution

Heinz, E., Williams, T. A., Nakjang, S., Noël, C. J., Swan, D., Goldberg, A. V., Harris, S. R., Weinmaier, T., Markert, S., Becher, D., et al. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002979 · Cited by 154 · see citing works

Vitagenes, cellular stress response, and acetylcarnitine: Relevance to hormesis

Calabrese, V., Cornelius, C., Dinkova‐Kostova, A. T., & Calabrese, E. J. (2009) · BioFactors · doi:10.1002/biof.22 · Cited by 147 · see citing works

The Broad-Spectrum Antiviral Protein ZAP Restricts Human Retrotransposition

Goodier, J. L., Pereira, G., Cheung, L. E., Rose, R. J., & Kazazian, H. H. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005252 · Cited by 131 · see citing works

The Chaperonin Containing TCP1 Complex (CCT/TRiC) Is Involved in Mediating Sperm-Oocyte Interaction

Dun, M. D., Smith, N. D., Baker, M. A., Lin, M., Aitken, R. J., & Nixon, B. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.188888 · Cited by 126 · see citing works

Genetics and Expression Profile of the Tubulin Gene Superfamily in Breast Cancer Subtypes and Its Relation to Taxane Resistance

Nami, B., & Wang, Z. (2018) · Cancers · doi:10.3390/cancers10080274 · Cited by 124 · see citing works

Extracellular Vesicles Derived from Human Umbilical Cord Mesenchymal Stem Cells Protect Liver Ischemia/Reperfusion Injury by Reducing CD154 Expression on CD4+ T Cells via CCT2

Zheng, J., Lu, T., Zhou, C., Cai, J., Zhang, X., Liang, J., Sui, X. Y., Chen, X., Chen, L., Sun, Y., et al. (2020) · Advanced Science · doi:10.1002/advs.201903746 · Cited by 119 · see citing works

The role of the molecular chaperone CCT in protein folding and mediation of cytoskeleton-associated processes: implications for cancer cell biology

Vallin, J., & Grantham, J. (2018) · Cell stress & chaperones (Print) · doi:10.1007/s12192-018-0949-3 · Cited by 96 · see citing works

Biogenesis of multisubunit RNA polymerases

Wild, T., & Cramer, P. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.12.001 · Cited by 116 · see citing works

Antarctic notothenioid fish: what are the future consequences of ‘losses’ and ‘gains’ acquired during long-term evolution at cold and stable temperatures?

Beers, J. M., & Jayasundara, N. (2015) · Journal of Experimental Biology · doi:10.1242/jeb.116129 · Cited by 113 · see citing works

Quality control of cytoskeletal proteins and human disease

Lundin, V. F., Leroux, M. R., & Stirling, P. C. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.12.007 · Cited by 108 · see citing works

The Protein Interaction Network of the Human Transcription Machinery Reveals a Role for the Conserved GTPase RPAP4/GPN1 and Microtubule Assembly in Nuclear Import and Biogenesis of RNA Polymerase II

Forget, D., Lacombe, A.-A., Cloutier, P., Al‐Khoury, R., Bouchard, A., Lavallée‐Adam, M., Faubert, D., Jerónimo, C., Blanchette, M., & Coulombe, B. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.003616 · Cited by 105 · see citing works

The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins

Dekker, C., Roe, S. M., McCormack, E. A., Beuron, F., Pearl, L. H., & Willison, K. R. (2010) · The EMBO Journal · doi:10.1038/emboj.2011.208 · Cited by 102 · see citing works

Equivalent Mutations in the Eight Subunits of the Chaperonin CCT Produce Dramatically Different Cellular and Gene Expression Phenotypes

Amit, M., Weisberg, S. J., Nadler-Holly, M., McCormack, E. A., Feldmesser, E., Kaganovich, D., Willison, K. R., & Horovitz, A. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.06.037 · Cited by 94 · see citing works

Parallel global profiling of plant TOR dynamics reveals a conserved role for LARP1 in translation

Scarpin, M. R., Leiboff, S., & Brunkard, J. O. (2020) · eLife · doi:10.7554/elife.58795 · Cited by 90 · see citing works

Pathway of Actin Folding Directed by the Eukaryotic Chaperonin TRiC

Balchin, D., Miličić, G., Strauss, M., Hayer-Hartl, M. K., & Hartl, F. U. (2018) · Cell · doi:10.1016/j.cell.2018.07.006 · Cited by 90 · see citing works

Cmr1/WDR76 defines a nuclear genotoxic stress body linking genome integrity and protein quality control

Gallina, I., Colding, C., Henriksen, P., Beli, P., Nakamura, K., Offman, J., Mathiasen, D. P., Silva, S. D. R., Hoffmann, E. R., Groth, A., et al. (2015) · Nature Communications · doi:10.1038/ncomms7533 · Cited by 87 · see citing works

Allosteric Mechanisms in Chaperonin Machines

Gruber, R., & Horovitz, A. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00556 · Cited by 86 · see citing works

Thermal Shock Induces Host Proteostasis Disruption and Endoplasmic Reticulum Stress in the Model Symbiotic CnidarianAiptasia

Oakley, C. A., Durand, E., Wilkinson, S., Peng, L., Weis, V. M., Grossman, A. R., & Davy, S. K. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00797 · Cited by 85 · see citing works

Nuclear functions of prefoldin

Millán-Zambrano, G., & Chávez, S. (2014) · Open Biology · doi:10.1098/rsob.140085 · Cited by 86 · see citing works

Association of the Influenza Virus RNA Polymerase Subunit PB2 with the Host Chaperonin CCT

Fislová, T., Thomas, B., Graef, K. M., & Fodor, E. (2010) · Journal of Virology · doi:10.1128/jvi.00813-10 · Cited by 85 · see citing works

Essential Genetic Interactors of SIR2 Required for Spatial Sequestration and Asymmetrical Inheritance of Protein Aggregates

Song, J. M., Yang, Q., Yang, J., Larsson, L., Hao, X., Zhu, X., Hill, S. M., Cvijović, M., Fernández-Rodrı́guez, J., Grantham, J., et al. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004539 · Cited by 84 · see citing works

Contribution of the Type II Chaperonin, TRiC/CCT, to Oncogenesis

Roh, S., Kasembeli, M. M., Bakthavatsalam, D., Chiu, W., & Tweardy, D. J. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms161125975 · Cited by 80 · see citing works

Chapter 4 Ciliary Tubulin and Its Post-Translational Modifications

Gaertig, J., & Włoga, D. (2008) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(08)00804-1 · Cited by 79 · see citing works

Spatial Guidance of Cell Asymmetry: Septin GTP ases Show the Way

Spiliotis, E. T., & Gladfelter, A. S. (2011) · Traffic · doi:10.1111/j.1600-0854.2011.01268.x · Cited by 78 · see citing works

Structural and functional analysis of the role of the chaperonin CCT in mTOR complex assembly

Cuéllar, J., Ludlam, W. G., Tensmeyer, N. C., Aoba, T., Dhavale, M., Santiago, C. A., Bueno-Carrasco, M. T., Mann, M. J., Plimpton, R. L., Makaju, A., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10781-1 · Cited by 77 · see citing works

Liver proteome response of pre-harvest Atlantic salmon following exposure to elevated temperature

Nuez‐Ortín, W. G., Carter, C. G., Nichols, P. D., Cooke, I., & Wilson, R. (2018) · BMC Genomics · doi:10.1186/s12864-018-4517-0 · Cited by 76 · see citing works

Subunits of the chaperonin CCT interact with F-actin and influence cell shape and cytoskeletal assembly

Brackley, K. I., & Grantham, J. (2009) · Experimental Cell Research · doi:10.1016/j.yexcr.2009.11.003 · Cited by 70 · see citing works

Folding of large multidomain proteins by partial encapsulation in the chaperonin TRiC/CCT

Rüßmann, F., Stemp, M. J., Mönkemeyer, L., Etchells, S. A., Bracher, A., & Hartl, F. U. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218836109 · Cited by 69 · see citing works

Overexpression of chaperonin containing TCP1, subunit 3 predicts poor prognosis in hepatocellular carcinoma

Cui, X. (2015) · World Journal of Gastroenterology · doi:10.3748/wjg.v21.i28.8588 · Cited by 68 · see citing works

The Prefoldin Complex Regulates Chromatin Dynamics during Transcription Elongation

Millán-Zambrano, G., Rodríguez‐Gil, A., Peñate, X., de Miguel-Jiménez, L., Morillo‐Huesca, M., Krogan, N. J., & Chávez, S. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003776 · Cited by 63 · see citing works

The substrate specificity of eukaryotic cytosolic chaperonin CCT

Willison, K. R. (2018) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2017.0192 · Cited by 65 · see citing works

A TRPV1‐to‐secretagogin regulatory axis controls pancreatic β‐cell survival by modulating protein turnover

Maleńczyk, K., Girach, F., Szodorai, E., Storm, P., Segerstolpe, Å., Tortoriello, G., Schnell, R., Mulder, J., Romanov, R., Borók, E., et al. (2017) · EMBO Journal · doi:10.15252/embj.201695347 · Cited by 60 · see citing works

Features of the Chaperone Cellular Network Revealed through Systematic Interaction Mapping

Rizzolo, K., Huen, J., Kumar, A., Phanse, S., Vlasblom, J., Kakihara, Y., Zeineddine, H. A., Minić, Z., Snider, J. D., Wang, W., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.08.074 · Cited by 62 · see citing works

The human protein coevolution networkPreprint

Tillier, E. R. M., & Charlebois, R. L. (2009) · Genome Research · doi:10.1101/gr.092452.109 · Cited by 61 · see citing works

Functional Genomic Screening Reveals Core Modulators of Echinocandin Stress Responses in Candida albicans

Caplan, T., Polvi, E. J., Xie, J. L., Buckhalter, S., Leach, M. D., Robbins, N., & Cowen, L. E. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.084 · Cited by 56 · see citing works

Quantitative proteome profiling of respiratory virus-infected lung epithelial cells

van Diepen, A., Brand, H. K., Sama, I. E., Lambooy, L. H. J., van den Heuvel, L. P., van der Well, L., Huynen, M. A., Osterhaus, A. D. M. E., Andeweg, A. C., & Hermans, P. W. M. (2010) · Journal of Proteomics · doi:10.1016/j.jprot.2010.04.008 · Cited by 55 · see citing works

GroEL dependency affects codon usage—support for a critical role of misfolding in gene evolution

Warnecke, T., & Hurst, L. D. (2010) · Molecular Systems Biology · doi:10.1038/msb.2009.94 · Cited by 53 · see citing works

Caenorhabditiseleganschaperonin CCT/TRiC is required for actin and tubulin biogenesis and microvillus formation in intestinal epithelial cells

Saegusa, K., Sato, M., Sato, K., Nakajima‐Shimada, J., Harada, A., & Sato, K. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-09-0530 · Cited by 53 · see citing works

Differential HDAC1/2 network analysis reveals a role for prefoldin/CCT in HDAC1/2 complex assembly

Banks, C. A. S., Miah, S., Adams, M. K., Kempf, C. G., Thornton, J. L., Florens, L. A., & Washburn, M. P. (2018) · Scientific Reports · doi:10.1038/s41598-018-32009-w · Cited by 51 · see citing works

Management of cytoskeleton architecture by molecular chaperones and immunophilins

Quintá, H. R., Galigniana, N. M., Erlejman, A. G., Lagadari, M., Pilipuk, G. P., & Galigniana, M. D. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.07.023 · Cited by 50 · see citing works

Transcriptome of Atlantic Cod (Gadus morhua L.) Early Embryos from Farmed and Wild Broodstocks

Lanes, C. F. C., Bizuayehu, T. T., Fernandes, J. M. O., Kiron, V., & Babiak, I. (2013) · Marine Biotechnology · doi:10.1007/s10126-013-9527-y · Cited by 49 · see citing works

CCT2 Mutations Evoke Leber Congenital Amaurosis due to Chaperone Complex Instability

Minegishi, Y., Sheng, X., Yoshitake, K., Sergeev, Y. V., Iejima, D., Shibagaki, Y., Monma, N., Ikeo, K., Furuno, M., Zhuang, W., et al. (2016) · Scientific Reports · doi:10.1038/srep33742 · Cited by 49 · see citing works

Biogenesis of RNA Polymerases II and III Requires the Conserved GPN Small GTPases in Saccharomyces cerevisiae

Minaker, S. W., Filiatrault, M. C., Ben‐Aroya, S., Hieter, P., & Stirling, P. C. (2012) · Genetics · doi:10.1534/genetics.112.148726 · Cited by 48 · see citing works

Effect of TBCD and its regulatory interactor Arl2 on tubulin and microtubule integrity

Tian, G., Thomas, S., & Cowan, N. J. (2010) · Cytoskeleton · doi:10.1002/cm.20480 · Cited by 47 · see citing works

Differential substrate specificity of group I and group II chaperonins in the archaeon Methanosarcina mazei

Hirtreiter, A., Calloni, G., Forner, F., Scheibe, B., Puype, M., Vandekerckhove, J. S., Mann, M., Hartl, F. U., & Hayer-Hartl, M. K. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06924.x · Cited by 45 · see citing works

Yeast Genome Maintenance by the Multifunctional PIF1 DNA Helicase Family

Muellner, J., & Schmidt, K. H. (2020) · Genes · doi:10.3390/genes11020224 · Cited by 42 · see citing works

Over-Expression Analysis of All Eight Subunits of the Molecular Chaperone CCT in Mammalian Cells Reveals a Novel Function for CCTdelta

Spiess, M., Echbarthi, M., Svanström, A., Karlsson, R., & Grantham, J. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.06.007 · Cited by 42 · see citing works

mChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases

MITCHELL, L. A., Huard, S., Cotrut, M., Pourhanifeh-Lemeri, R., Steunou, A., Hamza, A., Lambert, J., Zhou, H., Ning, Z., Basu, A. B., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218515110 · Cited by 41 · see citing works

Physical and functional interaction between yeast Pif1 helicase and Rim1 single-stranded DNA binding protein

Ramanagoudr-Bhojappa, R., Blair, L. P., Tackett, A., & Raney, K. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1088 · Cited by 43 · see citing works

Functional Subunits of Eukaryotic Chaperonin CCT/TRiC in Protein Folding

Kabir, M. A., Uddin, W., Narayanan, A., Reddy, P. K., Jairajpuri, M. A., Sherman, F., & Ahmad, Z. (2011) · Journal of Amino Acids · doi:10.4061/2011/843206 · Cited by 39 · see citing works

Chaperone Function of Hgh1 in the Biogenesis of Eukaryotic Elongation Factor 2

Mönkemeyer, L., Klaips, C. L., Balchin, D., Körner, R., Hartl, F. U., & Bracher, A. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.01.034 · Cited by 38 · see citing works

The TRiC/CCT Chaperonin and Its Role in Uncontrolled Proliferation

Wang, D. Y., Kamuda, K., Montoya, G., & Mesa, P. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-40204-4_2 · Cited by 37 · see citing works

Clinicopathological features and CCT2 and PDIA2 expression in gallbladder squamous/adenosquamous carcinoma and gallbladder adenocarcinoma

Zou, Q., Yang, Z., Yuan, Y., Li, J.-H., Liang, L., Zeng, G.-X., & Chen, S. (2013) · World Journal of Surgical Oncology · doi:10.1186/1477-7819-11-143 · Cited by 38 · see citing works

Chaperonin Mechanisms: Multiple and (Mis)Understood?

Horovitz, A., Reingewertz, T. H., Cuéllar, J., & Valpuesta, J. (2022) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-082521-113418 · Cited by 38 · see citing works

Regulation of Nuclear Factor κB (NF-κB) Transcriptional Activity via p65 Acetylation by the Chaperonin Containing TCP1 (CCT)

Pejanovic, N., Hochrainer, K., Liu, T., Aerne, B. L., Soares, M. P., & Anrather, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042020 · Cited by 38 · see citing works

Interactions of subunit CCT3 in the yeast chaperonin CCT/TRiC with Q/N-rich proteins revealed by high-throughput microscopy analysis

Nadler-Holly, M., Breker, M., Gruber, R., Azia, A., Gymrek, M., Eisenstein, M., Willison, K. R., Schuldiner, M., & Horovitz, A. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1209277109 · Cited by 37 · see citing works

The structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring

Willison, K. R. (2018) · Biochemical Journal · doi:10.1042/bcj20170378 · Cited by 38 · see citing works

Proteomic analysis of A2780/S ovarian cancer cell response to the cytotoxic organogold(III) compound Aubipyc

Gamberi, T., Massai, L., Magherini, F., Landini, I., Fiaschi, T., Scaletti, F., Gabbiani, C., Bianchi, L., Bini, L., Nobili, S., et al. (2014) · Journal of Proteomics · doi:10.1016/j.jprot.2014.03.032 · Cited by 37 · see citing works

Disruption of the Chaperonin Containing TCP-1 Function Affects Protein Networks Essential for Rod Outer Segment Morphogenesis and Survival

Posokhova, E. N., Song, H., Belcastro, M., Higgins, L., Bigley, L. R., Michaud, N. A., Martemyanov, K. A., & Sokolov, M. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.000570 · Cited by 36 · see citing works

A Comparative Perspective on Wnt/β-Catenin Signalling in Cell Fate Determination

Garcin, C. L., & Habib, S. J. (2017) · Results and problems in cell differentiation · doi:10.1007/978-3-319-53150-2_15 · Cited by 36 · see citing works

Yeast Phosducin-Like Protein 2 Acts as a Stimulatory Co-Factor for the Folding of Actin by the Chaperonin CCT via a Ternary Complex

McCormack, E. A., Altschuler, G. M., Dekker, C., Filmore, H., & Willison, K. R. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.06.003 · Cited by 36 · see citing works

The diversity of protein turnover and abundance under nitrogen-limited steady-state conditions in <i>Saccharomyces cerevisiae</i>

Helbig, A. O., Daran-Lapujade, P., van Maris, A. J. A., de Hulster, E. A. F., de Ridder, D., Pronk, J. T., Heck, A. J. R., & Slijper, M. (2011) · Molecular BioSystems · doi:10.1039/c1mb05250k · Cited by 33 · see citing works

Structure of GPN-Loop GTPase Npa3 and Implications for RNA Polymerase II Assembly

Niesser, J., Wagner, F., Kostrewa, D., Mühlbacher, W., & Cramer, P. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.01009-15 · Cited by 34 · see citing works

Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin

Altschuler, G. M., & Willison, K. R. (2008) · Journal of The Royal Society Interface · doi:10.1098/rsif.2008.0185 · Cited by 34 · see citing works

Cytosolic chaperones mediate quality control of higher-order septin assembly in budding yeast

Johnson, C. R., Weems, A. D., Brewer, J. M., Thorner, J. W., & McMurray, M. A. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-11-1531 · Cited by 33 · see citing works

CCTα and CCTδ Chaperonin Subunits Are Essential and Required for Cilia Assembly and Maintenance in Tetrahymena

Seixas, C., Cruto, T., Tavares, A., Gaertig, J., & Soares, H. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010704 · Cited by 33 · see citing works

Regulation of GPCR expression through an interaction with CCT7, a subunit of the CCT/TRiC complex

Génier, S., Degrandmaison, J., Moreau, P., Labrecque, P., Hébert, T. E., & Parent, J. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-04-0224 · Cited by 32 · see citing works

Carbon nanopowder acts as a Trojan-horse for benzo(α)pyrene in Danio rerio embryos

Binelli, A., Giacco, L. D., Santo, N., Bini, L., Magni, S., Parolini, M., Madaschi, L., Ghilardi, A., Maggioni, D., Ascagni, M., et al. (2017) · Nanotoxicology · doi:10.1080/17435390.2017.1306130 · Cited by 32 · see citing works

Chaperone Networks in Fungal Pathogens of Humans

Horianopoulos, L. C., & Kronstad, J. W. (2021) · Journal of Fungi · doi:10.3390/jof7030209 · Cited by 29 · see citing works

Chaperones and multitasking proteins in the nucleolus: networking together for survival?

Bański, P., Kodiha, M., & Stochaj, U. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.02.010 · Cited by 32 · see citing works

The one thousand and one chaperones of the NF-κB pathway

Fusella, F., Seclì, L., Cannata, C., & Brancaccio, M. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03402-z · Cited by 32 · see citing works

Molecular and Genetic Analysis of the Drosophila Model of Fragile X Syndrome

Tessier, C. R., & Broadie, K. S. (2011) · Results and problems in cell differentiation · doi:10.1007/978-3-642-21649-7_7 · Cited by 31 · see citing works

In situ analysis reveals the TRiC duty cycle and PDCD5 as an open-state cofactor

Xing, H., Rosenkranz, R. R. E., Rodriguez-Aliaga, P., Lee, T.-T., Majtner, T., Böhm, S., Turoňová, B., Frydman, J., & Beck, M. (2024) · Nature · doi:10.1038/s41586-024-08321-z · Cited by 29 · see citing works

Interactions between monomeric CCTδ and p150Glued: A novel function for CCTδ at the cell periphery distinct from the protein folding activity of the molecular chaperone CCT

Echbarthi, M., Vallin, J., & Grantham, J. (2018) · Experimental Cell Research · doi:10.1016/j.yexcr.2018.06.018 · Cited by 30 · see citing works

Protein interactome of the deamidase phosphoribosylformylglycinamidine synthetase (PFAS) by LC-MS/MS

Ai, L., Disoma, C., Zhou, Y., Chen, Z., Zhang, L., Shen, Y., Zhou, M., Du, A., Zheng, R., Li, S., et al. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.04.039 · Cited by 30 · see citing works

Silencing Mediated by the Schizosaccharomyces pombe HIRA Complex Is Dependent upon the Hpc2-Like Protein, Hip4

Anderson, H., Kagansky, A., Wardle, J., Rappsilber, J., Allshire, R., & Whitehall, S. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013488 · Cited by 33 · see citing works

The interactome of CCT complex—a computational analysis

Narayanan, A., Pullepu, D., & Kabir, M. A. (2016) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2016.09.002 · Cited by 29 · see citing works

Mapping the Spatial Proteome of Metastatic Cells in Colorectal Cancer

Mendes, M. L., Peláez‐García, A., López-Lucendo, M. F., Bartolomé, R. A., Calviño, E., Barderas, R., & Casal, J. I. (2017) · PROTEOMICS · doi:10.1002/pmic.201700094 · Cited by 29 · see citing works

Quantitative and integrated proteome and microRNA analysis of endothelial replicative senescence

Yentrapalli, R., Azimzadeh, O., Kraemer, A., Malinowsky, K., Sarioglu, H., Becker, K., Atkinson, M. J., Moertl, S., & Tapio, S. (2015) · Journal of Proteomics · doi:10.1016/j.jprot.2015.05.023 · Cited by 29 · see citing works

A Two-step Mechanism for the Folding of Actin by the Yeast Cytosolic Chaperonin

Stuart, S. F., Leatherbarrow, R. J., & Willison, K. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.166256 · Cited by 28 · see citing works

On the evolutionary origin of the chaperonins

Dekker, C., Willison, K. R., & Taylor, W. R. (2010) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22952 · Cited by 28 · see citing works

Interactions between the actin filament capping and severing protein gelsolin and the molecular chaperone CCT: evidence for nonclassical substrate interactions

Brackley, K. I., & Grantham, J. (2010) · Cell Stress and Chaperones · doi:10.1007/s12192-010-0230-x · Cited by 28 · see citing works

Assisted protein folding at low temperature: evolutionary adaptation of the Antarctic fish chaperonin CCT and its client proteins

Cuéllar, J., Yébenes, H., Parker, S. K., Carranza, G., Serna, M., Valpuesta, J., Zabala, J. C., & Detrich, H. W. (2014) · Biology Open · doi:10.1242/bio.20147427 · Cited by 27 · see citing works

Functional characterization of chaperonin containing T-complex polypeptide-1 and its conserved and novel substrates in Arabidopsis

Ahn, H.-K., Yoon, J.-T., Choi, I., Kim, S. M., Lee, H., & Pai, H. (2019) · Journal of Experimental Botany · doi:10.1093/jxb/erz099 · Cited by 27 · see citing works

Compensatory growth renders Tcf7l1a dispensable for eye formation despite its requirement in eye field specification

Young, R., Hawkins, T. A., Cavodeassi, F., Stickney, H. L., Schwarz, Q., Lawrence, L. M., Wierzbicki, C., Cheng, B. Y.-L., Luo, J., Ambrosio, E. M., et al. (2019) · eLife · doi:10.7554/elife.40093 · Cited by 27 · see citing works

Targeting β-tubulin:CCT-β complexes incurs Hsp90- and VCP-related protein degradation and induces ER stress-associated apoptosis by triggering capacitative Ca2+ entry, mitochondrial perturbation and caspase overactivation

Lin, Y., Lee, Y.-F., & Liang, P.-H. (2012) · Cell Death and Disease · doi:10.1038/cddis.2012.173 · Cited by 27 · see citing works

Protein folding, misfolding and quality control: the role of molecular chaperones

Papsdorf, K., & Richter, K. (2014) · Essays in Biochemistry · doi:10.1042/bse0560053 · Cited by 27 · see citing works

The nucleotide-binding proteins Nubp1 and Nubp2 are negative regulators of ciliogenesis

Kypri, E., Christodoulou, A., Maimaris, G., Lethan, M., Markaki, M., Lysandrou, C., Lederer, C. W., Tavernarakis, N., Geimer, S., Pedersen, L. B., et al. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1401-6 · Cited by 27 · see citing works

Chaperonin Containing T-Complex Polypeptide Subunit Eta (CCT-eta) Is a Specific Regulator of Fibroblast Motility and Contractility

Satish, L., Johnson, S. L., Wang, J. H., Post, J. C., Ehrlich, G. D., & Kathju, S. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010063 · Cited by 27 · see citing works

The substrate specificity of eukaryotic cytosolic chaperonin CCT

Willison, K. R. (2018) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2017.0192 · Cited by 65 · see citing works

Activities of the chaperonin containing TCP-1 (CCT): implications for cell cycle progression and cytoskeletal organisation.

Brackley, K. I., & Grantham, J. (2008) · Cell Stress and Chaperones · doi:10.1007/s12192-008-0057-x · Cited by 169 · see citing works

The interactome of CCT complex—a computational analysis

Narayanan, A., Pullepu, D., & Kabir, M. A. (2016) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2016.09.002 · Cited by 29 · see citing works

Eukaryotic chaperonin CCT: Prolonged interaction with cytoskeletal components

Roobol, A., Grantham, J., King, M. D. A., Alami, W. E., Wilson, S. J., Yuan, A., Bray, J. J., & Carden, M. J. (2000) · Biochemical Society Transactions · doi:10.1042/bst028a415

The malaria parasite chaperonin containing TCP-1 (CCT) complex: Data integration with other CCT proteomes

Wilkinson, M. D., Ferreira, J. L., Beeby, M., Baum, J., & Willison, K. R. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.1057232 · Cited by 4 · see citing works