Quality Control of Orphaned Proteins
Open accessAbstract
The billions of proteins inside a eukaryotic cell are organized among dozens of sub-cellular compartments, within which they are further organized into protein complexes. The maintenance of both levels of organization is crucial for normal cellular function. Newly made proteins that fail to be segregated to the correct compartment or assembled into the appropriate complex are defined as orphans. In this review, we discuss the challenges faced by a cell of minimizing orphaned proteins, the quality control systems that recognize orphans, and the consequences of excess orphans for protein homeostasis and disease.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Other RNA exosome subunits with reduced abundance by global proteomics had thermal stability largely unaffected, indicating their depletion may occur through mechanisms independent of protein destabilization, such as altered synthesis or degradation pathways including orphan protein decay.
“In contrast, while other subunits of the RNA exosome exhibited reduced abundance by global proteomics, their thermal stability remained largely unaffected, indicating that their depletion may occur through mechanisms independent of protein destabilization, such as altered synthesis or degradation pathways that could include orphan protein decay89.”
From EXOSC3 G191 Variants Trigger System-Wide Recalibration of RNA Processing Machinery (2026) · cites this paper as [89]
Split into 2 atoms — 1 confirmed, 0 partially supported, 0 disputed, 0 misattributed, 1 unverifiable. Expand the claim to see per-atom verdicts.
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
UniProt: the Universal Protein knowledgebase
Apweiler, R. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkh131 · Cited by 7,535 · 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
Locating proteins in the cell using TargetP, SignalP and related tools
Emanuelsson, O., Brunak, S., von HEIJNE, G., & Nielsen, H. (2007) · Nature Protocols · doi:10.1038/nprot.2007.131 · Cited by 2,746 · 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
UniProt: the universal protein knowledgebase
The UniProt Consortium (2018) · Nucleic Acids Research · doi:10.1093/nar/gky092 · Cited by 2,043 · see citing works
A brave new world of RNA-binding proteins
Hentze, M. W., Castelló, A., Schwarzl, T., & Preiß, T. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.130 · Cited by 1,727 · see citing works
Kulak, N. A., Pichler, G., Paron, I., Nagaraj, N., & Mann, M. (2014) · Nature Methods · doi:10.1038/nmeth.2834 · Cited by 1,719 · see citing works
Intracellular protein topogenesis
Blobel, G. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.3.1496 · Cited by 1,393 · see citing works
Perutz, M. F., Rossmann, M. G., Cullis, A. F., Muirhead, H., Will, G., & North, A. C. T. (1960) · Nature · doi:10.1038/185416a0 · Cited by 1,351 · see citing works
One step at a time: endoplasmic reticulum-associated degradation
Vembar, S. S., & Brodsky, J. L. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2546 · Cited by 1,299 · see citing works
Li, G., Burkhardt, D. H., Gross, C. A., & Weissman, J. S. (2014) · Cell · doi:10.1016/j.cell.2014.02.033 · Cited by 1,218 · see citing works
Weatherall, D. J., & Clegg, J. B. (2001) · Wiley eBooks · doi:10.1002/9780470696705 · Cited by 1,077 · see citing works
Mitochondrial Import Efficiency of ATFS-1 Regulates Mitochondrial UPR Activation
Nargund, A. M., Pellegrino, M., Fiorese, C. J., Baker, B. M., & Haynes, C. M. (2012) · Science · doi:10.1126/science.1223560 · Cited by 1,027 · see citing works
A SMALL PARTICULATE COMPONENT OF THE CYTOPLASM
Palade, G. E. (1955) · The Journal of Cell Biology · doi:10.1083/jcb.1.1.59 · Cited by 1,014 · see citing works
Mitochondrial Machineries for Protein Import and Assembly
Wiedemann, N., & Pfanner, N. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014352 · Cited by 894 · see citing works
Bole, D. G., Hendershot, L. M., & Kearney, J. F. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.102.5.1558 · Cited by 876 · see citing works
Immunoglobulin heavy chain binding protein
Haas, I. G., & Wabl, M. R. (1983) · Nature · doi:10.1038/306387a0 · Cited by 854 · see citing works
A Census of Human Soluble Protein Complexes
Havugimana, P. C., Hart, T., Nepusz, T., Yang, H., Turinsky, A. L., Li, Z., Wang, P. I., Boutz, D. R., Fong, V., Phanse, S., et al. (2012) · Cell · doi:10.1016/j.cell.2012.08.011 · Cited by 843 · see citing works
(1973) · The Medical Journal of Australia · doi:10.5694/j.1326-5377.1973.tb111034.x · Cited by 812 · see citing works
AAA+ Proteases: ATP-Fueled Machines of Protein Destruction
Sauer, R. T., & Baker, T. A. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060408-172623 · Cited by 763 · see citing works
Using Gene Expression Noise to Understand Gene Regulation
Munsky, B., Neuert, G., & van Oudenaarden, A. (2012) · Science · doi:10.1126/science.1216379 · Cited by 745 · see citing works
Rajagopalan, H., & Christoph Lengauer, C. (2004) · Nature · doi:10.1038/nature03099 · Cited by 730 · see citing works
Olivieri, N. F. (1999) · New England Journal of Medicine · doi:10.1056/nejm199907083410207 · Cited by 718 · see citing works
Comprehensive Characterization of Genes Required for Protein Folding in the Endoplasmic Reticulum
Jonikas, M. C., Collins, S. R., Denic, V., Oh, E., Toyama, E. Q., Schmid, V., Weibezahn, J., Schwappach, B., Walter, P., Weissman, J. S., et al. (2009) · Science · doi:10.1126/science.1167983 · Cited by 713 · see citing works
Aneuploidy Affects Proliferation and Spontaneous Immortalization in Mammalian Cells
Williams, B. R., Prabhu, V. R., Hunter, K. E., Glazier, C. M., Whittaker, C. A., Housman, D. E., & Amon, A. (2008) · Science · doi:10.1126/science.1160058 · Cited by 665 · see citing works
The Signal Recognition Particle
Keenan, R. J., Freymann, D. M., Stroud, R. M., & Walter, P. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.755 · Cited by 639 · see citing works
Global, quantitative and dynamic mapping of protein subcellular localization
Itzhak, D. N., Tyanova, S., Cox, J., & Borner, G. H. H. (2016) · eLife · doi:10.7554/elife.16950 · Cited by 595 · see citing works
Dual role of autophagy in hallmarks of cancer
Singh, S. S., Vats, S., Chia, A. Y.-Q., Tan, T. Z., Deng, S., Ong, M. S., Arfuso, F., Yap, C. T., Goh, B. C., Sethi, G., et al. (2018) · Oncogene · doi:10.1038/s41388-017-0046-6 · Cited by 542 · see citing works
Histone chaperone networks shaping chromatin function
Hammond, C. M., Strømme, C. B., Huang, H., Patel, D. J., & Groth, A. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.159 · Cited by 528 · see citing works
Jäkel, S., & Görlich, D. (1998) · The EMBO Journal · doi:10.1093/emboj/17.15.4491 · Cited by 527 · see citing works
The GET Complex Mediates Insertion of Tail-Anchored Proteins into the ER Membrane
Schuldiner, M., Metz, J., Schmid, V., Denic, V., Rakwalska, M., Schmitt, H. D., Schwappach, B., & Weissman, J. S. (2008) · Cell · doi:10.1016/j.cell.2008.06.025 · Cited by 522 · see citing works
Murphy, M. E. (2013) · Carcinogenesis · doi:10.1093/carcin/bgt111 · Cited by 505 · see citing works
Degradation from the endoplasmic reticulum: Disposing of newly synthesized proteins
Lippincott‐Schwartz, J. (1988) · Cell · doi:10.1016/0092-8674(88)90553-3 · Cited by 494 · see citing works
Signal sequences specify the targeting route to the endoplasmic reticulum membrane.
Ng, D., Brown, J. D., & Walter, P. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.134.2.269 · Cited by 473 · see citing works
A novel ER α‐mannosidase‐like protein accelerates ER‐associated degradation
Hosokawa, N., Wada, I., Hasegawa, K., Yorihuzi, T., Tremblay, L. O., Herscovics, A. A., & Nagata, K. (2001) · EMBO Reports · doi:10.1093/embo-reports/kve084 · Cited by 467 · see citing works
Protein translocation across biological membranes
Wickner, W., & Schekman, R. (2005) · Science · doi:10.1126/science.1113752 · Cited by 458 · see citing works
Mistargeted mitochondrial proteins activate a proteostatic response in the cytosol
Wróbel, L., Topf, U., Brągoszewski, P., Wiese, S., Sztolsztener, M. E., Oeljeklaus, S., Varabyova, A., Lirski, M., Chrościcki, P., Mroczek, S., et al. (2015) · Nature · doi:10.1038/nature14951 · Cited by 458 · see citing works
Stingele, S., Stoehr, G., Peplowska, K., Cox, J., Mann, M., & Štorchová, Z. (2012) · Molecular Systems Biology · doi:10.1038/msb.2012.40 · Cited by 449 · see citing works
Matlack, K. E. S., Misselwitz, B., Plath, K., & Rapoport, T. A. (1999) · Cell · doi:10.1016/s0092-8674(00)80767-9 · Cited by 447 · see citing works
Crystallographic structure studies of an IgG molecule and an Fc fragment
Huber, R., Deisenhofer, J., Colman, P. M., Matsushima, M., & Palm, W. (1976) · Nature · doi:10.1038/264415a0 · Cited by 422 · see citing works
A protein complex required for signal-sequence-specific sorting and translocation
Wiedmann, B., Sakai, H., Davis, T. A., & Wiedmann, M. (1994) · Nature · doi:10.1038/370434a0 · Cited by 421 · see citing works
Structure of the signal recognition particle interacting with the elongation-arrested ribosome
Halić, M., Becker, T. A., Pool, M., Spahn, C. M. T., Grassucci, R. A., Frank, J., & Beckmann, R. (2004) · Nature · doi:10.1038/nature02342 · Cited by 418 · see citing works
Translation drives mRNA quality control
Shoemaker, C. J., & Green, R. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2301 · Cited by 397 · see citing works
Unpolymerized tubulin modulates the level of tubulin mRNAs
Cleveland, D. W., Lopata, M. A., SHERLINE, P., & Kirschner, M. W. (1981) · Cell · doi:10.1016/0092-8674(81)90072-6 · Cited by 393 · see citing works
Piel, F. B., & Weatherall, D. J. (2014) · New England Journal of Medicine · doi:10.1056/nejmra1404415 · Cited by 393 · see citing works
Kikkert, M., Doolman, R., Dai, M., Avner, R., Hassink, G., van Voorden, S., Thanedar, S., Roitelman, J., Chau, V., & Wiertz, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307453200 · Cited by 384 · see citing works
Tasaki, T., Sriram, S. M., Park, K. S., & Kwon, Y. T. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-051710-093308 · Cited by 382 · see citing works
A cytosolic network suppressing mitochondria-mediated proteostatic stress and cell death
Wang, X., & Chen, X. J. (2015) · Nature · doi:10.1038/nature14859 · Cited by 366 · see citing works
Laboratory Investigation of Hemoglobinopathies and Thalassemias: Review and Update
Clarke, G. M., & Higgins, T. (2000) · Clinical Chemistry · doi:10.1093/clinchem/46.8.1284 · Cited by 352 · see citing works
Structural and Mechanistic Insights into Protein Translocation
Rapoport, T. A., Li, L., & Park, E. (2017) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100616-060439 · Cited by 344 · see citing works
MitoCPR—A surveillance pathway that protects mitochondria in response to protein import stress
Weidberg, H., & Amon, A. (2018) · Science · doi:10.1126/science.aan4146 · Cited by 344 · see citing works
Hendershot, L., Bole, D., Köhler, G., & Kearney, J. F. (1987) · The Journal of cell biology · doi:10.1083/jcb.104.3.761 · Cited by 340 · see citing works
Jäkel, S., Mingot, J. M., Schwarzmaier, P., Hartmann, E., & Görlich, D. (2002) · The EMBO Journal · doi:10.1093/emboj/21.3.377 · Cited by 324 · see citing works
The Eukaryotic Proteome Is Shaped by E3 Ubiquitin Ligases Targeting C-Terminal Degrons
Koren, I., Timms, R. T., Kula, T., Xu, Q., Li, M. Z., & Elledge, S. J. (2018) · Cell · doi:10.1016/j.cell.2018.04.028 · Cited by 320 · see citing works
Aneuploidy causes proteotoxic stress in yeastPreprint
Oromendia, A. B., Dodgson, S. E., & Amon, A. (2012) · Genes & Development · doi:10.1101/gad.207407.112 · Cited by 307 · see citing works
Ma, J., & Lindquist, S. L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.011578098 · Cited by 295 · see citing works
Kinetic Analysis of Protein Stability Reveals Age-Dependent Degradation
McShane, E., Sin, C., Zauber, H., Wells, J. N., Donnelly, N., Wang, X., Hou, J., Chen, W., Štorchová, Z., Marsh, J. A., et al. (2016) · Cell · doi:10.1016/j.cell.2016.09.015 · Cited by 291 · see citing works
Kang, S., Rane, N. S., Kim, S. J., Garrison, J. L., Taunton, J., & Hegde, R. S. (2006) · Cell · doi:10.1016/j.cell.2006.10.032 · Cited by 290 · see citing works
Self-citationFRACTIONATION OF MAMMALIAN LIVER CELLS BY DIFFERENTIAL CENTRIFUGATION
Claude, A. (1946) · The Journal of Experimental Medicine · doi:10.1084/jem.84.1.61 · Cited by 288 · see citing works
Membrane Protein Insertion at the Endoplasmic Reticulum
Shao, S., & Hegde, R. S. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154125 · Cited by 287 · see citing works
Self-citationAn abundant erythroid protein that stabilizes free α-haemoglobin
Kihm, A. J., Kong, Y., Wei, H., Russell, J., Rouda, S., Adachi, K., Simon, M. C., Blobel, G. A., & Weiss, M. J. (2002) · Nature · doi:10.1038/nature00803 · Cited by 276 · see citing works
Control of Protein Quality and Stoichiometries by N-Terminal Acetylation and the N-End Rule Pathway
Shemorry, A., Hwang, C., & Varshavsky, A. J. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.03.018 · Cited by 276 · see citing works
Protein targeting and degradation are coupled for elimination of mislocalized proteins
Hessa, T., Sharma, A., Mariappan, M., Eshleman, H. D., Gutierrez, E., & Hegde, R. S. (2011) · Nature · doi:10.1038/nature10181 · Cited by 272 · see citing works
Self-citationN-linked sugar-regulated protein folding and quality control in the ER
Tannous, A., Pisoni, G. B., Hebert, D. N., & Molinari, M. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2014.12.001 · Cited by 269 · see citing works
Fons, R. D., Bogert, B. A., & Hegde, R. S. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200210095 · Cited by 268 · see citing works
Self-citationQuantitative proteomic analysis reveals posttranslational responses to aneuploidy in yeast
Dephoure, N., Hwang, S., O'Sullivan, C., Dodgson, S. E., Gygi, S. P., Amon, A., & Torres, E. M. (2014) · eLife · doi:10.7554/elife.03023 · Cited by 263 · see citing works
Brodsky, J. L., Goeckeler-Fried, J. L., & Schekman, R. W. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.21.9643 · Cited by 260 · see citing works
Tail-anchored membrane protein insertion into the endoplasmic reticulum
Hegde, R. S., & Keenan, R. J. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3226 · Cited by 258 · see citing works
Self-citationUbiquilins Chaperone and Triage Mitochondrial Membrane Proteins for Degradation
Itakura, E., Zavodszky, E., Shao, S., Wohlever, M. L., Keenan, R. J., & Hegde, R. S. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.020 · Cited by 255 · see citing works
Self-citationInteraction landscape of membrane-protein complexes in Saccharomyces cerevisiae
Babu, M., Vlasblom, J., Pu, S., Guo, X., Graham, C., Bean, B. D. M., Burston, H. E., Vizeacoumar, F. J., Snider, J. D., Phanse, S., et al. (2012) · Nature · doi:10.1038/nature11354 · Cited by 251 · see citing works
Protein Complexes Are under Evolutionary Selection to Assemble via Ordered Pathways
Marsh, J. A., Hernández, H., Hall, Z., Ahnert, S. E., Perica, T., Robinson, C. V., & Teichmann, S. A. (2013) · Cell · doi:10.1016/j.cell.2013.02.044 · Cited by 245 · see citing works
Regulation of mitochondrial protein import by cytosolic kinases.
Schmidt, O., Harbauer, A. B., Rao, S., Eyrich, B., Zahedi, R., Stojanovski, D., Schönfisch, B., Guiard, B., Sickmann, A., Pfanner, N., et al. (2011) · Cell · doi:10.1016/j.cell.2010.12.015 · Cited by 244 · see citing works
Eukaryotic ribosome assembly, transport and quality control
Peña, C., Hurt, E., & Panse, V. G. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3454 · Cited by 244 · see citing works
An Unfolded CH1 Domain Controls the Assembly and Secretion of IgG Antibodies
Feige, M. J., Groscurth, S., Marcinowski, M., Shimizu, Y., Kessler, H., Hendershot, L. M., & Büchner, J. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.04.028 · Cited by 237 · see citing works
Membrane protein association by potential intrarnembrane charge pairs
Cosson, P., Lankford, S. P., Bonifacino, J. S., & Klausner, R. D. (1991) · Nature · doi:10.1038/351414a0 · Cited by 237 · see citing works
KOHNE, E. (2011) · Deutsches Ärzteblatt international · doi:10.3238/arztebl.2011.0532 · Cited by 234 · see citing works
Proteome complexity and the forces that drive proteome imbalance
Harper, J. W., & Bennett, E. J. (2016) · Nature · doi:10.1038/nature19947 · Cited by 234 · see citing works
The Constitution of Protoplasm
Claude, A. (1943) · Science · doi:10.1126/science.97.2525.451 · Cited by 233 · see citing works
Braunger, K., Pfeffer, S., Shrimal, S., Gilmore, R., Berninghausen, O., Mandon, E. C., Becker, T. A., Förster, F. G., & Beckmann, R. (2018) · Science · doi:10.1126/science.aar7899 · Cited by 229 · see citing works
Drisaldi, B., Stewart, R. S., Adles, C., Stewart, L. R., Quaglio, E., Biasini, E., Fioriti, L., Chiesa, R., & Harris, D. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m213247200 · Cited by 228 · see citing works
Principles of Cotranslational Ubiquitination and Quality Control at the Ribosome
Duttler, S., Pechmann, S., & Frydman, J. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.03.010 · Cited by 226 · see citing works
Bonifacino, J. S., Suzuki, C. K., Lippincott‐Schwartz, J., Weissman, A. M., & Klausner, R. D. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.109.1.73 · Cited by 226 · see citing works
The race to decipher the top secrets of TOP mRNAs
Meyuhas, O., & Kahan, T. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.08.015 · Cited by 224 · see citing works
The separation and characterization of subcellular particles.
Duve, C. D. (1965) · PubMed · Cited by 222 · see citing works
The conserved AAA-ATPase Msp1 confers organelle specificity to tail-anchored proteins
Okreglak, V., & Walter, P. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1405755111 · Cited by 219 · see citing works
Chen, Y., Umanah, G. K. E., Dephoure, N., Andrabi, S. A., Gygi, S. P., Dawson, T. M., Dawson, V. L., & Rutter, J. P. (2014) · The EMBO Journal · doi:10.15252/embj.201487943 · Cited by 217 · see citing works
Defining the physiological role of SRP in protein-targeting efficiency and specificity
Boydston, E. A., Subramanian, K., Nunnari, J. M., & Weissman, J. S. (2018) · Science · doi:10.1126/science.aar3607 · Cited by 216 · see citing works
Transmembrane Helical Interactions and the Assembly of the T Cell Receptor Complex
Manolios, N., Bonifacino, J. S., & Klausner, R. D. (1990) · Science · doi:10.1126/science.2142801 · Cited by 216 · see citing works
Fundamental relationship between operon organization and gene expression
Lim, H. N., Lee, Y., & Hussein, R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1105692108 · Cited by 214 · see citing works
Shen, Y., & Hendershot, L. M. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-05-0434 · Cited by 211 · see citing works
Bonifacino, J. S., Cosson, P., Shah, N., & Klausner, R. D. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07827.x · Cited by 210 · see citing works
Wang, Q., Liu, Y., Soetandyo, N., Baek, K., Hegde, R. S., & Ye, Y. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.05.010 · Cited by 210 · see citing works
Self-citationSato, B. K., Schulz, D., Do, P. H., & Hampton, R. Y. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.03.010 · Cited by 210 · see citing works
Chen, L., & Madura, K. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-0201 · Cited by 207 · see citing works
Cryo-EM structure of the protein-conducting ERAD channel Hrd1 in complex with Hrd3
Schoebel, S., Mi, W., Stein, A., Ovchinnikov, S., Pavlovicz, R. E., DiMaio, F., Baker, D. A., Chambers, M. G., Su, H., Li, D., et al. (2017) · Nature · doi:10.1038/nature23314 · Cited by 196 · see citing works
A conserved quality-control pathway that mediates degradation of unassembled ribosomal proteins
Sung, M., Porras-Yakushi, T. R., Reitsma, J. M., Huber, F. M., Sweredoski, M. J., Hoelz, A., Hess, S. Y., & Deshaies, R. J. (2016) · eLife · doi:10.7554/elife.19105 · Cited by 195 · see citing works
Degradation of proteins within the endoplasmic reticulum
Bonifacio, J. S., & Lippincott‐Schwartz, J. (1991) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(91)90028-w · Cited by 193 · see citing works
Ben-David, U., Arad, G., Weissbein, U., Mandefro, B., Maimon, A., Golan-lev, T., Narwani, K., Clark, A., Andrews, P., Benvenisty, N., et al. (2014) · Nature Communications · doi:10.1038/ncomms5825 · Cited by 189 · see citing works
Warner, J. R., Mitra, G., Schwindinger, W. F., Studeny, M., & Fried, H. M. (1985) · Molecular and Cellular Biology · doi:10.1128/mcb.5.6.1512 · Cited by 188 · see citing works
Cytosolic Quality Control of Mislocalized Proteins Requires RNF126 Recruitment to Bag6
Rodrigo-Brenni, M. C., Gutierrez, E., & Hegde, R. S. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.05.025 · Cited by 186 · see citing works
Self-citationVoigt, S., Jungnickel, B., Hartmann, E., & Rapoport, T. A. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.134.1.25 · Cited by 184 · see citing works
A Cotranslational Ubiquitination Pathway for Quality Control of Misfolded Proteins
Wang, F., Durfee, L. A., & Huibregtse, J. M. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.03.009 · Cited by 179 · see citing works
Palmitoylated calnexin is a key component of the ribosome–translocon complex
Lakkaraju, A. K., Abrami, L., Lemmin, T., Blašković, S., Kunz, B., Kihara, A., Peraro, M. D., & van der Goot, F. G. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.15 · Cited by 178 · see citing works
Cotranslational signal-independent SRP preloading during membrane targeting
Chartron, J. W., Hunt, K. C. L., & Frydman, J. (2016) · Nature · doi:10.1038/nature19309 · Cited by 176 · see citing works
C-Terminal End-Directed Protein Elimination by CRL2 Ubiquitin Ligases
Lin, H.-C., Yeh, C., Chen, Y., Lee, T.-T., Hsieh, P.-Y., Rusnac, D. V., Lin, S.-Y., Elledge, S. J., Zheng, N., & Yen, H.-C. S. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.04.006 · Cited by 172 · see citing works
The α Chain of the T Cell Antigen Receptor Is Degraded in the Cytosol
Huppa, J. B., & Ploegh, H. L. (1997) · Immunity · doi:10.1016/s1074-7613(00)80514-2 · Cited by 168 · see citing works
The submicroscopic morphology of protoplasm.
Kr, P. (2002) · PubMed · Cited by 167 · see citing works
Park, S.-H., Bolender, N., Eisele, F., Kostova, Z., Takeuchi, J. S., Coffino, P., & Wolf, D. H. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-04-0338 · Cited by 165 · see citing works
UBE2O remodels the proteome during terminal erythroid differentiation
Nguyen, A. T., Prado, M. A., Schmidt, P. J., Sendamarai, A. K., Wilson‐Grady, J., Min, M., Campagna, D. R., Tian, G., Shi, Y., Dederer, V., et al. (2017) · Science · doi:10.1126/science.aan0218 · Cited by 164 · see citing works
Autoregulatory control of beta-tubulin mRNA stability is linked to translation elongation.
Gay, D. A., Sisodia, S. S., & Cleveland, D. W. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.15.5763 · Cited by 160 · see citing works
A substrate-specific inhibitor of protein translocation into the endoplasmic reticulum
Garrison, J. L., Kunkel, E. J., Hegde, R. S., & Taunton, J. (2005) · Nature · doi:10.1038/nature03821 · Cited by 159 · see citing works
Self-citationMolecular Mechanism of AHSP-Mediated Stabilization of α-Hemoglobin
Feng, L., Gell, D. A., Zhou, S., Gu, L., Kong, Y., Li, J., Hu, M., Yan, N., Lee, C., Rich, A. M., et al. (2004) · Cell · doi:10.1016/j.cell.2004.11.025 · Cited by 157 · see citing works
Horie, C., Suzuki, H., Sakaguchi, M., & Mihara, K. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-12-0570 · Cited by 154 · see citing works
A sweet code for glycoprotein folding
Caramelo, J. J., & Parodi, A. J. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.07.021 · Cited by 146 · see citing works
Using hyperLOPIT to perform high-resolution mapping of the spatial proteome
Mulvey, C. M., Breckels, L. M., Geladaki, A., Britovšek, N. K., Nightingale, D. J. H., Christoforou, A., Elzek, M., Deery, M. J., Gatto, L., & Lilley, K. S. (2017) · Nature Protocols · doi:10.1038/nprot.2017.026 · Cited by 141 · see citing works
Protection from cytosolic prion protein toxicity by modulation of protein translocation
Rane, N. S., Yonkovich, J. L., & Hegde, R. S. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600462 · Cited by 139 · see citing works
Self-citationBAG-6 is essential for selective elimination of defective proteasomal substrates
Minami, R., Hayakawa, A., Kagawa, H., Yanagi, Y., Yokosawa, H., & Kawahara, H. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200908092 · Cited by 139 · see citing works
Structures of the scanning and engaged states of the mammalian SRP-ribosome complex
Voorhees, R. M., & Hegde, R. S. (2015) · eLife · doi:10.7554/elife.07975 · Cited by 138 · see citing works
Self-citationCell cycle–dependent regulation of mitochondrial preprotein translocase
Harbauer, A. B., Opalińska, M., Gerbeth, C., Herman, J. S., Rao, S., Schönfisch, B., Guiard, B., Schmidt, O., Pfanner, N., & Meisinger, C. (2014) · Science · doi:10.1126/science.1261253 · Cited by 137 · see citing works
Mechanistic basis for a molecular triage reaction
Shao, S., Rodrigo-Brenni, M. C., Kivlen, M. H., & Hegde, R. S. (2017) · Science · doi:10.1126/science.aah6130 · Cited by 135 · see citing works
Self-citationHeterogeneity of Tubulin Subunits
Feit, H. W., Slusarek, L., & Shelanski, M. L. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.9.2028 · Cited by 134 · see citing works
The principle of antagonism ensures protein targeting specificity at the endoplasmic reticulum
Gamerdinger, M., Hanebuth, M. A., Frickey, T., & Deuerling, E. (2015) · Science · doi:10.1126/science.aaa5335 · Cited by 134 · see citing works
Predictable tuning of protein expression in bacteria
Bonde, M., Pedersen, M., Klausen, M. S., Jensen, S. I., Wulff, T., Harrison, S. J., Nielsen, A. T., Herrgård, M. J., & Sommer, M. O. A. (2016) · Nature Methods · doi:10.1038/nmeth.3727 · Cited by 133 · see citing works
Reduced Translocation of Nascent Prion Protein During ER Stress Contributes to Neurodegeneration
Rane, N. S., Kang, S., Chakrabarti, O., Feigenbaum, L., & Hegde, R. S. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.06.015 · Cited by 132 · see citing works
Self-citationUBE2O is a quality control factor for orphans of multiprotein complexes
Yanagitani, K., Juszkiewicz, S., & Hegde, R. S. (2017) · Science · doi:10.1126/science.aan0178 · Cited by 132 · see citing works
Self-citationWidespread Cotranslational Formation of Protein Complexes
Duncan, C. D. S., & Mata, J. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002398 · Cited by 131 · see citing works
Selective inhibition of cotranslational translocation of vascular cell adhesion molecule 1
Besemer, J., Harant, H., Wang, S. V., Oberhauser, B., Marquardt, K., Foster, C. A., Schreiner, E. P., de Vries, J. E., Dascher-Nadel, C., & Lindley, I. J. D. (2005) · Nature · doi:10.1038/nature03670 · Cited by 131 · see citing works
A UBE2O-AMPKα2 Axis that Promotes Tumor Initiation and Progression Offers Opportunities for Therapy
Vila, I. K., Yao, Y., Kim, G., Xia, W., Kim, H.-J., Kim, S.-J., Park, M.-K., Hwang, J. P., González‐Billalabeitia, E., Hung, M., et al. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.01.003 · Cited by 129 · see citing works
Biochemical Aspects of Genetics: The Operon
Ames, B. N., & Martin, R. G. (1964) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.33.070164.001315 · Cited by 129 · see citing works
Berndt, U., Oellerer, S., Zhang, Y., Johnson, A. E., & Rospert, S. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808584106 · Cited by 128 · see citing works
Signal Sequences Control Gating of the Protein Translocation Channel in a Substrate-Specific Manner
Kim, S. J., Mitra, D., Salerno, J. R., & Hegde, R. S. (2002) · Developmental Cell · doi:10.1016/s1534-5807(01)00120-4 · Cited by 127 · see citing works
Self-citationThe Efficiency of Protein Compartmentalization into the Secretory Pathway
Levine, C. G., Mitra, D., Sharma, A., Smith, C. L., & Hegde, R. S. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-06-0508 · Cited by 124 · see citing works
Self-citationTherapeutic Targeting of MLL Degradation Pathways in MLL-Rearranged Leukemia
Liang, K., Volk, A. G., Haug, J. S., Marshall, S. A., Woodfin, A. R., Bartom, E. T., Gilmore, J. M., Florens, L. A., Washburn, M. P., Sullivan, K. D., et al. (2017) · Cell · doi:10.1016/j.cell.2016.12.011 · Cited by 124 · see citing works
Vanhove, M., Usherwood, Y.-K., & Hendershot, L. M. (2001) · Immunity · doi:10.1016/s1074-7613(01)00163-7 · Cited by 120 · see citing works
Physical Evidence for Cotranslational Regulation of β-Tubulin mRNA Degradation
Theodorakis, N. D., & Cleveland, D. W. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.2.791-799.1992 · Cited by 119 · see citing works
Transmembrane Domain Recognition during Membrane Protein Biogenesis and Quality Control
Guna, A., & Hegde, R. S. (2018) · Current Biology · doi:10.1016/j.cub.2018.02.004 · Cited by 118 · see citing works
Self-citationMsp1 Is a Membrane Protein Dislocase for Tail-Anchored Proteins
Wohlever, M. L., Mateja, A., McGilvray, P. T., Day, K. J., & Keenan, R. J. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.06.019 · Cited by 115 · see citing works
Building an antibody factory: a job for the unfolded protein response
Brewer, J. W., & Hendershot, L. M. (2004) · Nature Immunology · doi:10.1038/ni1149 · Cited by 112 · see citing works
Structure of oxidized α-haemoglobin bound to AHSP reveals a protective mechanism for haem
Feng, L., Zhou, S., Gu, L., Gell, D. A., Mackay, J. P., Weiss, M. J., Gow, A. J., & Shi, Y. (2005) · Nature · doi:10.1038/nature03609 · Cited by 109 · see citing works
Oxidative Stress Inhibits the Mitochondrial Import of Preproteins and Leads to Their Degradation
Wright, G. L., Terada, K., Yano, M., Sergeev, I. N., & Mori, M. (2001) · Experimental Cell Research · doi:10.1006/excr.2000.5096 · Cited by 108 · see citing works
Karaplis, A. C., Lim, S., Baba, H., Arnold, A., & Kronenberg, H. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.4.1629 · Cited by 108 · see citing works
Mayor, T., Lipford, J. R., Graumann, J., Smith, G. T., & Deshaies, R. J. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m400220-mcp200 · Cited by 101 · see citing works
Effect of RP51 gene dosage alterations on ribosome synthesis in Saccharomyces cerevisiae.
Abovich, N., Gritz, L. R., Tung, L. W., & Rosbash, M. (1985) · Molecular and Cellular Biology · doi:10.1128/mcb.5.12.3429 · Cited by 97 · see citing works
Mayor, T., Graumann, J., Bryan, J., MacCoss, M. J., & Deshaies, R. J. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700264-mcp200 · Cited by 96 · see citing works
Mancini, R., Fagioli, C., Fra, A., Maggioni, C., & Sitia, R. (2000) · The FASEB Journal · doi:10.1096/fasebj.14.5.769 · Cited by 96 · see citing works
Inefficient SRP Interaction with a Nascent Chain Triggers a mRNA Quality Control Pathway
Karamyshev, A. L., Patrick, A. E., Karamysheva, Z. N., Griesemer, D. S., Hudson, H., Tjon‐Kon‐Sang, S., Nilsson, I., Otto, H., Liu, Q., Rospert, S., et al. (2014) · Cell · doi:10.1016/j.cell.2013.12.017 · Cited by 90 · see citing works
Bag6 complex contains a minimal tail-anchor–targeting module and a mock BAG domain
Mock, J., Chartron, J. W., Zaslaver, M., Xu, Y., Ye, Y., & Clemons, W. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402745112 · Cited by 89 · see citing works
Warner, J. R., Mitra, G., Schwindinger, W. F., Studeny, M., & Fried, H. M. (1985) · Molecular and Cellular Biology · doi:10.1128/mcb.5.6.1512-1521.1985 · Cited by 84 · see citing works
Quality Control of Integral Membrane Proteins by Assembly-Dependent Membrane Integration
Feige, M. J., & Hendershot, L. M. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.07.013 · Cited by 83 · see citing works
Structure and function of DNA-binding proteins
Nelson, H. C. M. (1995) · Current Opinion in Genetics & Development · doi:10.1016/0959-437x(95)80006-9 · Cited by 82 · see citing works
Pittenger, M. F., & Cleveland, D. W. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.101.5.1941 · Cited by 81 · see citing works
Weir, N. R., Kamber, R. A., Martenson, J. S., & Denic, V. (2017) · eLife · doi:10.7554/elife.28507 · Cited by 81 · see citing works
Induction of ubiquitin-conjugating enzymes during terminal erythroid differentiation.
Wefes, I., Mastrandrea, L. D., Haldeman, M. T., Koury, S. T., Tamburlin, J. H., Pickart, C. M., & Finley, D. J. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.11.4982 · Cited by 79 · see citing works
Signal sequence insufficiency contributes to neurodegeneration caused by transmembrane prion protein
Rane, N. S., Chakrabarti, O., Feigenbaum, L., & Hegde, R. S. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200911115 · Cited by 79 · see citing works
Self-citationBachurski, C. J., Theodorakis, N. D., Coulson, R., & Cleveland, D. W. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.6.4076 · Cited by 79 · see citing works
Seppen, J., Steenken, E., Lindhout, D., Bosma, P. J., & Elferink, R. P. J. O. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00677-1 · Cited by 76 · see citing works
The HECT domain ubiquitin ligase HUWE1 targets unassembled soluble proteins for degradation
Xu, Y., Anderson, D. E., & Ye, Y. (2016) · Cell Discovery · doi:10.1038/celldisc.2016.40 · Cited by 75 · see citing works
Physical evidence for cotranslational regulation of beta-tubulin mRNA degradation.
Theodorakis, N. D., & Cleveland, D. W. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.2.791 · Cited by 71 · see citing works
Abnormal Haem Binding and Globin SH Group Blockade in Unstable Haemoglobins
Jacob, H. S., Brain, M. C., Dacie, J. V., Carrell, R. W., & Lehmann, H. (1968) · Nature · doi:10.1038/2181214a0 · Cited by 63 · see citing works
Suzuki, R., & Kawahara, H. (2016) · EMBO Reports · doi:10.15252/embr.201541402 · Cited by 62 · see citing works
SYNTHESIS, ASSEMBLY, AND SECRETION OF GAMMA GLOBULIN BY MOUSE MYELOMA CELLS
Baumal, R., Potter, M. J., & Scharff, M. D. (1971) · The Journal of Experimental Medicine · doi:10.1084/jem.134.5.1316 · Cited by 61 · see citing works
López, M. D., Guerra, J. J. M., & Samuelsson, T. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010654 · Cited by 58 · see citing works
Vitali, D. G., Sinzel, M., Bulthuis, E. P., Kolb, A., Zabel, S., Mehlhorn, D. G., Costa, B. F., Farkas, Á., Clancy, A., Schuldiner, M., et al. (2018) · Journal of Cell Science · doi:10.1242/jcs.211110 · Cited by 51 · see citing works
Pfeffer, S., Dudek, J., Zimmermann, R., & Förster, F. G. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.06.024 · Cited by 46 · see citing works
Chromosome-Specific and Global Effects of Aneuploidy inSaccharomyces cerevisiae
Dodgson, S. E., Kim, S. H., Costanzo, M., Baryshnikova, A., Morse, D. L., Kaiser, C. A., Boone, C. M., & Amon, A. (2016) · Genetics · doi:10.1534/genetics.115.185660 · Cited by 43 · see citing works
Effect of RP51 Gene Dosage Alterations on Ribosome Synthesis in Saccharomyces cerevisiae
Abovich, N., Gritz, L. R., Tung, L. W., & Rosbash, M. (1985) · Molecular and Cellular Biology · doi:10.1128/mcb.5.12.3429-3435.1985 · Cited by 40 · see citing works
Williams, N. K., & Dichtl, B. (2018) · Biochemical Society Transactions · doi:10.1042/bst20170451 · Cited by 36 · see citing works
Cytosolic aggregates perturb the degradation of nontranslocated secretory and membrane proteins
Chakrabarti, O., Rane, N. S., & Hegde, R. S. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-07-0638 · Cited by 31 · see citing works
Self-citationMiyazaki, Y., Chen, L., Chu, B. W., Swigut, T., & Wandless, T. J. (2015) · eLife · doi:10.7554/elife.07687 · Cited by 28 · see citing works
Wattenberg, B. W., Clark, D., & Brock, S. E. (2007) · Bioscience Reports · doi:10.1007/s10540-007-9061-0 · Cited by 28 · see citing works
Quality Control of a Cytoplasmic Protein Complex
Scazzari, M., Amm, I., & Wolf, D. H. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.596064 · Cited by 27 · see citing works
Human hemoglobin stability and instability: molecular mechanisms and some clinical correlations.
Rieder, R. F. (1974) · PubMed · Cited by 22 · see citing works
Bachurski, C. J., Theodorakis, N. D., Coulson, R., & Cleveland, D. W. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.6.4076-4086.1994 · Cited by 21 · see citing works
THE BIOSYNTHESIS OF HEMOGLOBIN
Benz, E. J., & Forget, B. G. (1952) · JAMA · doi:10.1001/jama.1952.03680120059014 · Cited by 18 · see citing works
Cassanelli, S., Bertolini, S., Rolleri, M., Stefano, F. D., Casarino, L., Elicio, N., Naselli, A., & Calandra, S. (1998) · Clinical Genetics · doi:10.1111/j.1399-0004.1998.tb02752.x · Cited by 15 · see citing works
Protein sorting signals: Simple peptides with complex functions
von HEIJNE, G. (1995) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-9061-8_4 · Cited by 10 · see citing works
Systems-Level Evidence of Transcriptional Co-Regulation of Yeast Protein Complexes
Lee, H., Żemojtel, T., & Shakhnovich, E. I. (2009) · Journal of Computational Biology · doi:10.1089/cmb.2008.17tt · Cited by 7 · see citing works
The Biosynthesis of Hemoglobin*
Orten, J. M. (1972) · School Science and Mathematics · doi:10.1111/j.1949-8594.1972.tb08895.x · Cited by 5 · see citing works
Flagged first, then by citations
3 of the 181 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
mRNAs, proteins and the emerging principles of gene expression control
Buccitelli, C., & Selbach, M. (2020) · Nature Reviews Genetics · doi:10.1038/s41576-020-0258-4 · Cited by 1,243 · see citing works
The mechanisms of integral membrane protein biogenesis
Hegde, R. S., & Keenan, R. J. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00413-2 · Cited by 244 · see citing works
Self-citationHakai is required for stabilization of core components of the m6A mRNA methylation machinery
Bawankar, P., Lenče, T., Paolantoni, C., Haussmann, I. U., Kazlauskiene, M., Jacob, D., Heidelberger, J. B., Richter, F. M., Nallasivan, M. P., Morı́n, V., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23892-5 · Cited by 162 · see citing works
Msp1 Clears Mistargeted Proteins by Facilitating Their Transfer from Mitochondria to the ER
Matsumoto, S., Nakatsukasa, K., Kakuta, C., Tamura, Y., Esaki, M., & Endo, T. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.07.006 · Cited by 111 · see citing works
Alternative lengthening of telomeres in childhood neuroblastoma from genome to proteome
Hartlieb, S., Sieverling, L., Nadler-Holly, M., Ziehm, M., Toprak, U. H., Herrmann, C., Ishaque, N., Okonechnikov, K., Gartlgruber, M., Park, Y.-G., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21247-8 · Cited by 114 · see citing works
Schmidt, O., Weyer, Y., Baumann, V., Widerin, M. A., Eising, S., Angelova, M., Schleiffer, A., Kremser, L., Lindner, H., Peter, M., et al. (2019) · The EMBO Journal · doi:10.15252/embj.2018101433 · Cited by 110 · see citing works
Stress response silencing by an E3 ligase mutated in neurodegeneration
Haakonsen, D. L., Heider, M., Ingersoll, A. J., Vodehnal, K., Witus, S. R., Uenaka, T., Wernig, M., & Rapé, M. (2024) · Nature · doi:10.1038/s41586-023-06985-7 · Cited by 107 · see citing works
Ribosome Abundance Control Via the Ubiquitin–Proteasome System and Autophagy
An, H., & Harper, J. W. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.06.001 · Cited by 98 · see citing works
Keeping the Proportions of Protein Complex Components in Check
Taggart, J., Zauber, H., Selbach, M., Li, G., & McShane, E. (2020) · Cell Systems · doi:10.1016/j.cels.2020.01.004 · Cited by 94 · see citing works
Microtubules orchestrate local translation to enable cardiac growth
Scarborough, E. A., Uchida, K., Vogel, M. C., Erlitzki, N., Iyer, M., Phyo, S. A., Bogush, A. I., Kehat, I., & Prosser, B. L. (2021) · Nature Communications · doi:10.1038/s41467-021-21685-4 · Cited by 99 · see citing works
Protein quality control in the endoplasmic reticulum
Phillips, B. P., Gómez‐Navarro, N., & Miller, E. A. (2020) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2020.04.002 · Cited by 96 · see citing works
Taggart, J., & Li, G. (2018) · Cell Systems · doi:10.1016/j.cels.2018.11.003 · Cited by 94 · see citing works
Cooperation of mitochondrial and ER factors in quality control of tail-anchored proteins
Dederer, V., Khmelinskii, A., Huhn, A. G., Okreglak, V., Knop, M., & Lemberg, M. K. (2019) · eLife · doi:10.7554/elife.45506 · Cited by 88 · see citing works
The proteomic landscape of genome-wide genetic perturbations
Messner, C. B., Demichev, V., Muenzner, J., Aulakh, S. K., Barthel, N., Röhl, A., Herrera-Domínguez, L., Egger, A.-S., Kamrad, S., Hou, J., et al. (2023) · Cell · doi:10.1016/j.cell.2023.03.026 · Cited by 84 · see citing works
Quality Control of Protein Complex Assembly by a Transmembrane Recognition Factor
Natarajan, N., Foresti, O., Wendrich, K., Stein, A., & Carvalho, P. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.10.003 · Cited by 76 · see citing works
The Benefits of Cotranslational Assembly: A Structural Perspective
Schwarz, A., & Beck, M. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.07.006 · Cited by 72 · see citing works
Coupling of import and assembly pathways in mitochondrial protein biogenesis
Grevel, A., Pfanner, N., & Becker, T. (2019) · Biological Chemistry · doi:10.1515/hsz-2019-0310 · Cited by 71 · see citing works
Defining E3 ligase–substrate relationships through multiplex CRISPR screening
Timms, R. T., Mena, E. L., Leng, Y., Li, M. Z., Tchasovnikarova, I. A., Koren, I., & Elledge, S. J. (2023) · Nature Cell Biology · doi:10.1038/s41556-023-01229-2 · Cited by 69 · see citing works
Functional interdependence of N6-methyladenosine methyltransferase complex subunits in Arabidopsis
Shen, L. (2023) · The Plant Cell · doi:10.1093/plcell/koad070 · Cited by 68 · see citing works
The Multiple Levels of Mitonuclear Coregulation
Isaac, R. S., McShane, E., & Churchman, L. S. (2018) · Annual Review of Genetics · doi:10.1146/annurev-genet-120417-031709 · Cited by 62 · see citing works
Recognition and Degradation of Mislocalized Proteins in Health and DiseasePreprint
Hegde, R. S., & Zavodszky, E. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033902 · Cited by 62 · see citing works
Self-citationCotranslational Mechanisms of Protein Biogenesis and Complex Assembly in Eukaryotes
Morales-Polanco, F., Lee, J. H., Barbosa, N. M., & Frydman, J. (2022) · Annual Review of Biomedical Data Science · doi:10.1146/annurev-biodatasci-121721-095858 · Cited by 58 · see citing works
Orphan quality control shapes network dynamics and gene expression
Mark, K. G., Kolla, S., Aguirre, J. D., Garshott, D. M., Schmitt, S., Haakonsen, D. L., Xu, C., Kater, L., Kempf, G., Martínez-González, B., et al. (2023) · Cell · doi:10.1016/j.cell.2023.06.015 · Cited by 58 · see citing works
Adaptive preservation of orphan ribosomal proteins in chaperone-dispersed condensates
Ali, A., Garde, R., Schaffer, O., Bard, J. A. M., Husain, K. B., Kik, S. K., Davis, K. A., Luengo-Woods, S., Igarashi, M. G., Drummond, D. A., et al. (2023) · Nature Cell Biology · doi:10.1038/s41556-023-01253-2 · Cited by 55 · see citing works
Leo, I. R., Aswad, L., Stahl, M. M. S., Kunold, E., Post, F., Erkers, T., Struyf, N., Mermelekas, G., Joshi, R. N., Villacampa, E. G., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-29224-5 · Cited by 53 · see citing works
Degrons: defining the rules of protein degradation
Zhang, Z., Mena, E. L., Timms, R. T., Koren, I., & Elledge, S. J. (2025) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-025-00870-z · Cited by 57 · see citing works
Tune instead of destroy: How proteolysis keeps OXPHOS in shape
Szczepanowska, K., & Trifunović, A. (2021) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2020.148365 · Cited by 51 · see citing works
Elucidation of E3 ubiquitin ligase specificity through proteome-wide internal degron mapping
Zhang, Z., Sie, B. M., Chang, A., Leng, Y., Nardone, C., Timms, R. T., & Elledge, S. J. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.08.022 · Cited by 49 · see citing works
mRNA Editing, Processing and Quality Control in Caenorhabditis elegans
Arribere, J. A., Kuroyanagi, H., & Hundley, H. A. (2020) · Genetics · doi:10.1534/genetics.119.301807 · Cited by 46 · see citing works
Mitochondrial protein import stress
Pfanner, N., den Brave, F., & Becker, T. (2025) · Nature Cell Biology · doi:10.1038/s41556-024-01590-w · Cited by 52 · see citing works
Knopf, J. D., Landscheidt, N., Pegg, C. L., Schulz, B. L., Kühnle, N., Chao, C.-W., Huck, S., & Lemberg, M. K. (2020) · Journal of Cell Science · doi:10.1242/jcs.243790 · Cited by 43 · see citing works
Quality control of protein complex composition
Padovani, C., Jevtić, P., & Rapé, M. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.02.029 · Cited by 43 · see citing works
A nanobody-based strategy for rapid and scalable purification of human protein complexes
Stevens, T. A., Tomaleri, G. P., Hazu, M., Wei, S., Nguyen, V. N., DeKalb, C., Voorhees, R. M., & Pleiner, T. (2023) · Nature Protocols · doi:10.1038/s41596-023-00904-w · Cited by 41 · see citing works
Ferguson, R., Goold, R., Coupland, L. A., Flower, M. D., & Tabrizi, S. J. (2024) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2024.04.015 · Cited by 41 · see citing works
WNK1 is an assembly factor for the human ER membrane protein complex
Pleiner, T., Hazu, M., Tomaleri, G. P., Januszyk, K., Oania, R. S., Sweredoski, M. J., Moradian, A., Guna, A., & Voorhees, R. M. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.04.013 · Cited by 40 · see citing works
Bacterial rhomboid proteases mediate quality control of orphan membrane proteins
Liu, G., Beaton, S. E., Grieve, A. G., Evans, R. M., Rogers, M., Střı́šovský, K., Armstrong, F. A., Freeman, M., Exley, R. M., & Tang, C. M. (2020) · The EMBO Journal · doi:10.15252/embj.2019102922 · Cited by 39 · see citing works
Mechanisms of Cotranslational Protein Maturation in Bacteria
Koubek, J., Schmitt, J. L., Galmozzi, C. V., & Krämer, G. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.689755 · Cited by 35 · see citing works
Physiological Functions of Intracellular Protein Degradation
McShane, E., & Selbach, M. (2022) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-120420-091943 · Cited by 39 · see citing works
Rhomboid protease RHBDL4 promotes retrotranslocation of aggregation-prone proteins for degradation
Bock, J., Kühnle, N., Knopf, J. D., Landscheidt, N., Lee, J., Ye, Y., & Lemberg, M. K. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111175 · Cited by 38 · see citing works
Ribosome-associated quality control of membrane proteins at the endoplasmic reticulum
Phillips, B. P., & Miller, E. A. (2020) · Journal of Cell Science · doi:10.1242/jcs.251983 · Cited by 36 · see citing works
Perez, J. D., Fusco, C. M., & Schuman, E. M. (2021) · Annual Review of Genetics · doi:10.1146/annurev-genet-030321-054851 · Cited by 36 · see citing works
Differential Modes of Orphan Subunit Recognition for the WRB/CAML Complex
Inglis, A. J., Page, K. R., Guna, A., & Voorhees, R. M. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.02.084 · Cited by 33 · see citing works
Translational Control of Secretory Proteins in Health and Disease
Karamyshev, A. L., Tikhonova, E. B., & Karamysheva, Z. N. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21072538 · Cited by 35 · see citing works
A selectivity filter in the ER membrane protein complex limits protein misinsertion at the ER
Pleiner, T., Hazu, M., Tomaleri, G. P., Nguyen, V. N., Januszyk, K., & Voorhees, R. M. (2023) · The Journal of Cell Biology · doi:10.1083/jcb.202212007 · Cited by 33 · see citing works
O'Neill, J. S., Hoyle, N. P., Robertson, J. B., Edgar, R. S., Beale, A. D., Peak‐Chew, S., Day, J., Costa, A. S. H., Frezza, C., & Causton, H. C. (2020) · Nature Communications · doi:10.1038/s41467-020-18330-x · Cited by 34 · see citing works
Cytoplasmic control of Rab family small GTPases through BAG6
Takahashi, T., Minami, S., Tsuchiya, Y., Tajima, K., Sakai, N., Suga, K., Hisanaga, S., Ohbayashi, N., Fukuda, M., & Kawahara, H. (2019) · EMBO Reports · doi:10.15252/embr.201846794 · Cited by 33 · see citing works
Trip, D. S. L., van Oostrum, M., Memon, D., Frommelt, F., Baptista, D., Panneerselvam, K., Bradley, G., Licata, L., Hermjakob, H., Orchard, S. E., et al. (2025) · Nature Biotechnology · doi:10.1038/s41587-025-02659-z · Cited by 39 · see citing works
Protein quality control at the Golgi
Schwabl, S., & Teis, D. (2022) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2022.02.008 · Cited by 31 · see citing works
Large protein complex interfaces have evolved to promote cotranslational assembly
Badonyi, M., & Marsh, J. A. (2022) · eLife · doi:10.7554/elife.79602 · Cited by 29 · see citing works
Mechanism of orphan subunit recognition during assembly quality control
Yagita, Y., Zavodszky, E., Peak-Chew, S.-Y., & Hegde, R. S. (2023) · Cell · doi:10.1016/j.cell.2023.06.016 · Cited by 30 · see citing works
Self-citationControl of mRNA fate by its encoded nascent polypeptide
Höpfler, M., & Hegde, R. S. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.07.014 · Cited by 31 · see citing works
Self-citationCRYPTOCHROMES promote daily protein homeostasis
Wong, D. C. S., Seinkmane, E., Zeng, A., Stangherlin, A., Rzechorzek, N. M., Beale, A. D., Day, J., Reed, M., Peak‐Chew, S. Y., Styles, C. T., et al. (2022) · The EMBO Journal · doi:10.15252/embj.2021108883 · Cited by 30 · see citing works
Kamikubo, K., Kato, H., Kioka, H., Yamazaki, S., Tsukamoto, O., Nishida, Y., Asano, Y., Imamura, H., Kawahara, H., Shintani, Y., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.008544 · Cited by 29 · see citing works
The human signal peptidase complex acts as a quality control enzyme for membrane proteins
Zanotti, A., Coelho, J. P. L., Kaylani, D., Singh, G., Tauber, M., Hitzenberger, M., Avci, D., Zacharias, M., Russell, R. B., Lemberg, M. K., et al. (2022) · Science · doi:10.1126/science.abo5672 · Cited by 29 · see citing works
CCPG1 recognizes endoplasmic reticulum luminal proteins for selective ER-phagy
Ishii, S., Chino, H., Ode, K. L., Kurikawa, Y., Ueda, H. R., Matsuura, A., Mizushima, N., & Itakura, E. (2023) · Molecular Biology of the Cell · doi:10.1091/mbc.e22-09-0432 · Cited by 28 · see citing works
Influence of Subcellular Localization and Functional State on Protein Turnover
Yousefi, R., Jevdokimenko, K., Kluever, V., Pacheu‐Grau, D., & Fornasiero, E. F. (2021) · Cells · doi:10.3390/cells10071747 · Cited by 25 · see citing works
Mechanism of client selection by the protein quality-control factor UBE2O
Yip, M. C. J., Sedor, S. F., & Shao, S. (2022) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00807-6 · Cited by 23 · see citing works
Signal sequences encode information for protein folding in the endoplasmic reticulum
Sun, S., Li, X., & Mariappan, M. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202203070 · Cited by 22 · see citing works
Carvalho, H. J. F., Bondio, A. D., Maltecca, F., Colombo, S. F., & Borgese, N. (2019) · Scientific Reports · doi:10.1038/s41598-019-48363-2 · Cited by 23 · see citing works
Ubiquitin-dependent translation control mechanisms: Degradation and beyond
Ford, P. W., Narasimhan, M., & Bennett, E. J. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.115050 · Cited by 22 · see citing works
Transmembrane dislocases: a second chance for protein targeting
Dederer, V., & Lemberg, M. K. (2021) · Trends in Cell Biology · doi:10.1016/j.tcb.2021.05.007 · Cited by 22 · see citing works
Multilayered regulation of proteome stoichiometry
Ishikawa, K. (2021) · Current Genetics · doi:10.1007/s00294-021-01205-z · Cited by 21 · see citing works
A hierarchical assembly pathway directs the unique subunit arrangement of TRiC/CCT
Moreira, K. E., Collier, M. P., Leitner, A., Li, K. H., Lachapel, I. L. S., McCarthy, F., Opoku-Nsiah, K., Morales-Polanco, F., Barbosa, N., Gestaut, D. R., et al. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.07.031 · Cited by 21 · see citing works
Architecture of the UBR4 complex, a giant E4 ligase central to eukaryotic protein quality control
Grabarczyk, D. B., Ehrmann, J. F., Murphy, P. V., Yang, W. S., Kurzbauer, R., Bell, L., Deszcz, L., Neuhold, J., Schleiffer, A., Shulkina, A., et al. (2025) · Science · doi:10.1126/science.adv9309 · Cited by 20 · see citing works
Self-citationThe molecular basis of chaperone-mediated interleukin 23 assembly control
Meier, S., Bohnacker, S., Klose, C. J., López, A., Choe, C. A., Schmid, P. W. N., Bloemeke, N., Rührnößl, F., Haslbeck, M., Bieren, J. E., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12006-x · Cited by 21 · see citing works
Rawat, S., Valpadashi, A., Jha, M., Sreedurgalakshmi, K., & Raychaudhuri, S. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.01.022 · Cited by 21 · see citing works
Proteomics Identifies Substrates and a Novel Component in hSnd2-Dependent ER Protein Targeting
Tirincsi, A., O’Keefe, S., Nguyen, D., Sicking, M., Dudek, J., Förster, F., Jung, M., Hadzibeganovic, D., Helms, V., High, S., et al. (2022) · Cells · doi:10.3390/cells11182925 · Cited by 20 · see citing works
Mitochondrial-derived compartments remove surplus proteins from the outer mitochondrial membrane
Wilson, Z. N., Balasubramaniam, S. S., Wong, S., Schuler, M.-H., Wopat, M. J., & Hughes, A. L. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202307036 · Cited by 20 · see citing works
AAA+ Protein-Based Technologies to Counter Neurodegenerative Disease
March, Z. M., Mack, K. L., & Shorter, J. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2019.03.007 · Cited by 20 · see citing works
Convergence of orphan quality control pathways at a ubiquitin chain-elongating ligase
Roas, S. C., Yagita, Y., Murphy, P. V., Kurzbauer, R., Clausen, T., Zavodszky, E., & Hegde, R. S. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.01.002 · Cited by 19 · see citing works
Self-citationEspinoza, M. F., Nguyen, K. K., Sycks, M. M., Lyu, Z., Quanrud, G. M., Montoya, M. R., & Genereux, J. C. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102597 · Cited by 19 · see citing works
It's not just a phase; ubiquitination in cytosolic protein quality control
Baker, H. A., & Bernardini, J. P. (2021) · Biochemical Society Transactions · doi:10.1042/bst20200694 · Cited by 19 · see citing works
The m6A-YTH regulatory system in plants: A status
Brodersen, P., & Arribas‐Hernández, L. (2024) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2024.102650 · Cited by 19 · see citing works
Collier, M. P., Moreira, K. E., Li, K. H., Chen, Y., Itzhak, D. N., Samant, R. S., Leitner, A., Burlingame, A. L., & Frydman, J. (2021) · Scientific Reports · doi:10.1038/s41598-021-91086-6 · Cited by 17 · see citing works
Bernardini, A., & Tora, L. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168382 · Cited by 15 · see citing works
Role of Mitochondrial Protein Import in Age-Related Neurodegenerative and Cardiovascular Diseases
Bogorodskiy, A. O., Okhrimenko, I. S., Burkatovskii, D., Jakobs, P., Maslov, I., Gordeliy, V., Dencher, N. A., Gensch, T., Voos, W., Altschmied, J., et al. (2021) · Cells · doi:10.3390/cells10123528 · Cited by 17 · see citing works
An AAGAB-to-CCDC32 handover mechanism controls the assembly of the AP2 adaptor complex
Wan, C., Puscher, H., Ouyang, Y., Wu, J., Tian, Y., Li, S., Yin, Q., & Shen, J. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2409341121 · Cited by 16 · see citing works
C-terminal tail length guides insertion and assembly of membrane proteins
Sun, S., & Mariappan, M. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.012992 · Cited by 16 · see citing works
Maintaining Golgi Homeostasis: A Balancing Act of Two Proteolytic Pathways
Benyair, R., Eisenberg‐Lerner, A., & Merbl, Y. (2022) · Cells · doi:10.3390/cells11050780 · Cited by 16 · see citing works
Accessing Mitochondrial Protein Import in Living Cells by Protein Microinjection
Bogorodskiy, A. O., Okhrimenko, I. S., Maslov, I., Maliar, N. L., Burkatovskii, D., von Ameln, F., Schulga, A. A., Jakobs, P., Altschmied, J., Haendeler, J., et al. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.698658 · Cited by 15 · see citing works
Teyssonnière, É., Shichino, Y., Mito, M., Friedrich, A., Iwasaki, S., & Schacherer, J. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae030 · Cited by 14 · see citing works
Protein and RNA Quality Control by Autophagy in Plant Cells.
Yoon, S. H., & Chung, T. (2019) · PubMed Central · doi:10.14348/molcells.2019.0011 · Cited by 14 · see citing works
Jeran, N., Mercier, M., Pesaresi, P., & Tadini, L. (2025) · Journal of Experimental Botany · doi:10.1093/jxb/eraf182 · Cited by 13 · see citing works
Orphan quality control by an SCF ubiquitin ligase directed to pervasive C-degrons
Kong, K.-Y. E., Shankar, S., Rühle, F., & Khmelinskii, A. (2023) · Nature Communications · doi:10.1038/s41467-023-44096-z · Cited by 12 · see citing works
Dipeptidyl peptidases and E3 ligases of N-degron pathways cooperate to regulate protein stability
Shimshon, A., Dahan, K., Israel-Gueta, M., Olmayev-Yaakobov, D., Timms, R. T., Bekturova, A., Makaros, Y., Elledge, S. J., & Koren, I. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202311035 · Cited by 14 · see citing works
Siebert, V., Silber, M., Heuten, E., Muhle‐Goll, C., & Lemberg, M. K. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102321 · Cited by 13 · see citing works
BAG6 deficiency induces mis‐distribution of mitochondrial clusters under depolarization
Hayashishita, M., Kawahara, H., & Yokota, N. (2019) · FEBS Open Bio · doi:10.1002/2211-5463.12677 · Cited by 13 · see citing works
C9orf72 protein quality control by UBR5‐mediated heterotypic ubiquitin chains
Jülg, J., Edbauer, D., & Behrends, C. (2023) · EMBO Reports · doi:10.15252/embr.202255895 · Cited by 11 · see citing works
Weyer, Y., Schwabl, S., Tang, X., Purwar, A., Siegmann, K. A., Ruepp, A., Dunzendorfer-Matt, T., Widerin, M. A., Niedrist, V., Mutsters, N. J. M., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-53676-6 · Cited by 12 · see citing works
Circadian Control of Protein Synthesis
James, N. R., & O'Neill, J. S. (2024) · BioEssays · doi:10.1002/bies.202300158 · Cited by 11 · see citing works
Bailey, M., Ivanauskaite, A., Grimmer, J., Akintewe, O., Payne, A. C., Osborne, R., Labandera, A., Etherington, R. D., Rantala, M., Baginsky, S., et al. (2021) · Nature Communications · doi:10.1038/s41467-020-20506-4 · Cited by 12 · see citing works
RetractedOborská‐Oplová, M., Geiger, A. G., Michel, E., Klingauf‐Nerurkar, P., Dennerlein, S., Bykov, Y. S., Amodeo, S., Schneider, A., Schuldiner, M., Rehling, P., et al. (2025) · Nature Cell Biology · doi:10.1038/s41556-024-01588-4 · Cited by 11 · see citing works
FKBP39 controls nutrient dependent Nprl3 expression and TORC1 activity in Drosophila
Zhou, Y., Guo, J., Wang, X.-Y., Cheng, Y., Guan, J., Barman, P., Sun, M.-A., Fu, Y., Wei, W.-H., Feng, C.-J., et al. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03860-z · Cited by 8 · see citing works
UBXN1 maintains ER proteostasis and represses UPR activation by modulating translation
Ahlstedt, B. A., Ganji, R., Mukkavalli, S., Paulo, J. A., Gygi, S. P., & Raman, M. (2024) · EMBO Reports · doi:10.1038/s44319-023-00027-z · Cited by 11 · see citing works
The role of RNF149 in the pre-emptive quality control substrate ubiquitination
Legesse, A., Kaushansky, N., Braunstein, I., Saad, H., Lederkremer, G. Z., Navon, A., & Stanhill, A. (2023) · Communications Biology · doi:10.1038/s42003-023-04763-9 · Cited by 10 · see citing works
Cosma, G. L., Lobby, J. L., Fay, E. J., Siciliano, N. A., Langlois, R. A., & Eisenlohr, L. C. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2004372117 · Cited by 10 · see citing works
Temporal alterations of the nascent proteome in response to mitochondrial stress
Stępkowski, T. M., Linke, V., Stadnik, D., Zakrzewski, M., Zawada, A. E., Serwa, R. A., & Chacińska, A. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114803 · Cited by 9 · see citing works
Ishikawa, K., Ishihara, A., & Moriya, H. (2020) · PLoS Genetics · doi:10.1371/journal.pgen.1009091 · Cited by 9 · see citing works
Sun, G., DeFelice, M. M., Gillies, T. E., Ahn-Horst, T. A., Andrews, C. J., Krummenacker, M., Karp, P. D., Morrison, J. H., & Covert, M. W. (2024) · Cell Systems · doi:10.1016/j.cels.2024.02.002 · Cited by 9 · see citing works
- Authors
- Juszkiewicz, S., & Hegde, R. S.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Corresponding author
- Hegde, Ramanujan S.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2018-08
- Volume
- 71
- Issue
- 3
- Pages
- 443-457
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC6624128
- OpenAlex
- W2886379694
- Cited by
- 165
- References
- 181
- Citations by year
- 2026: 18 · 2025: 17 · 2024: 23 · 2023: 28 · 2022: 22 · 2021: 22 · 2020: 16 · 2019: 17 · 2018: 2
- FWCI
- 1.44
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Research Councils UK (MC_UP_A022_1007)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Keywords
- orphan proteins, protein quality control, protein complex formation, proteostasis, protein misfolding, disease
- MeSH terms
- Proteostasis, Proteins, Protein Biosynthesis, Protein Transport, Proteolysis
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
