{"id":27,"date":"2015-12-16T12:58:22","date_gmt":"2015-12-16T12:58:22","guid":{"rendered":"http:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/?page_id=27"},"modified":"2026-03-07T12:00:11","modified_gmt":"2026-03-07T12:00:11","slug":"publications","status":"publish","type":"page","link":"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"<p>Notes: * co-first authors; # co-corresponding authors<\/p>\n<p><strong>2025<\/strong><\/p>\n<ul>\n<li><span class=\"docsum-authors full-authors\"><span class=\"docsum-authors full-authors\">Sundaram, A., Li. Q., Wan, Y., Tang, J., Wu, H., Smalinskaite, L., <strong>Hegde, R.S.<\/strong>, Ji, Z., Keenan, R.J. (2025) <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/41116047\/\" target=\"_blank\" rel=\"noopener\">Global analysis of translocon remodeling during protein synthesis at the ER<\/a>. <em>Nat. Struct. Mol. Biol.<\/em>, <\/span><\/span><span class=\"cit\">32(12):2517-2525.<\/span><\/li>\n<li>Grabarczyk, D.B., Ehrmann, J.F., Murphy, P., Yang, W.S., Kurzbauer, R., Bell, L.E., Deszcz, L., Neuhold, J., Schleiffer, A., Shulkina, A., Lee, J., Shin, J.S., Meinhart, A., Versteeg, G.A., Zavodszky, E., Song, H.K., <strong>Hegde, R.S.<\/strong>, Clausen, T. (2025) <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/40875847\/\" target=\"_blank\" rel=\"noopener\">Architecture of the UBR4 complex, a giant E4 ligase central to eukaryotic protein quality control.<\/a> <em>Science<\/em>, 389(6763):909-914.<\/li>\n<li>Carrillo Roas, S., Yagita, Y., Murphy, P., Kurzbauer, R., Clausen, T., <sup>#<\/sup>Zavodszky, E., <sup>#<\/sup><strong>Hegde, R.S.<\/strong> (2025) <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/39879985\/\" target=\"_blank\" rel=\"noopener\">Convergence of orphan quality control pathways at a ubiquitin chain-elongating ligase.<\/a> <em>Mol Cell, <\/em><span class=\"docsum-journal-citation full-journal-citation\">85(4):815-828<\/span>.<\/li>\n<li><sup>#<\/sup><span class=\"docsum-authors full-authors\"><span class=\"docsum-authors full-authors\">Juszkiewicz, S., Peak-Chew, S.Y., <\/span><\/span><sup>#<\/sup><span class=\"docsum-authors full-authors\"><span class=\"docsum-authors full-authors\"><b>Hegde RS<\/b> (2025) <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/39878680\/\" target=\"_blank\" rel=\"noopener\">Mechanism of chaperone recruitment and retention on mitochondrial precursors<\/a>. <em>Mol. Biol. Cell<\/em>, <\/span><\/span><span class=\"cit\">36(4):ar39.<\/span><\/li>\n<\/ul>\n<p><strong>2024<\/strong><\/p>\n<ul>\n<li><span class=\"docsum-authors full-authors\">Wang, H., <b>Hegde, R.S.<\/b><\/span> (2024) <a class=\"docsum-title\" href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/39607913\/\" data-ga-category=\"result_click\" data-ga-action=\"1\" data-ga-label=\"39607913\" data-full-article-url=\"from_term=Hegde+RS&amp;from_sort=pubdate&amp;from_pos=1\" data-article-id=\"39607913\">Identification of a factor that accelerates substrate release from the signal recognition particle.<\/a> <em>Science<\/em>, <span class=\"docsum-journal-citation full-journal-citation\">386(6725):996-1003. <\/span><\/li>\n<li><span class=\"docsum-authors full-authors\">Batiuk, A., H\u00f6pfler, M., Almeida, A.C., Teoh En-Jie, D., Vadas, O., Vartholomaiou, E., <b>Hegde, R.S.<\/b>, Lin, Z., Gasic, I. (2024) <a class=\"docsum-title\" href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/39551769\/\" data-ga-category=\"result_click\" data-ga-action=\"2\" data-ga-label=\"39551769\" data-full-article-url=\"from_term=Hegde+RS&amp;from_sort=pubdate&amp;from_pos=2\" data-article-id=\"39551769\">Soluble \u03b1\u03b2-tubulins reversibly sequester TTC5 to regulate tubulin mRNA decay. <\/a><em>Nat. Commun.,<\/em> <span class=\"docsum-journal-citation full-journal-citation\">15(1):9963. doi: 10.1038\/s41467-024-54036-0.<\/span><\/span><\/li>\n<li>Lewis, A.J.O., Zhong, F., Keenan, R.J., <strong>Hegde, R.S.<\/strong> (2024) <a href=\"https:\/\/elifesciences.org\/articles\/95814\" target=\"_blank\" rel=\"noopener\">Structural analysis of the dynamic ribosome-translocon complex<\/a>. <em>eLife<\/em>, <span class=\"docsum-journal-citation full-journal-citation\">13:RP95814.<\/span><\/li>\n<li><strong>Hegde, R.S.<\/strong> and Keenan, R.J. (2024) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-content\/uploads\/sites\/8\/2024\/08\/NSMB_2024.pdf\" target=\"_blank\" rel=\"noopener\">A unifying model for membrane protein biogenesis<\/a>. <em>Nat. Struct. Mol. Biol.<\/em>, <span class=\"docsum-journal-citation full-journal-citation\">31:1009-1017.<\/span><\/li>\n<li><strong>Hegde, R.S.<\/strong> (2024) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-content\/uploads\/sites\/8\/2024\/08\/Mol_Cell_2024_preview.pdf\" target=\"_blank\" rel=\"noopener\">Getting membrane proteins into shape<\/a>. <em>Mol. Cell<\/em>, 84:1821-1823.<\/li>\n<li><strong>Hegde, R.S.<\/strong> (2024) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-content\/uploads\/sites\/8\/2024\/08\/TICB_2024b.pdf\" target=\"_blank\" rel=\"noopener\">How to enjoy and thrive in graduate school<\/a>. <em>Trends Cell Biol.<\/em>, 34:349-351.<\/li>\n<li><strong>Hegde, R.S.<\/strong> (2024) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-content\/uploads\/sites\/8\/2024\/08\/TICB_2024a.pdf\" target=\"_blank\" rel=\"noopener\">Things you should learn in graduate school<\/a>. <em>Trends Cell Biol.<\/em>, 34:269-271.<\/li>\n<li>Wu, H., Smalinskaite, L., <strong>Hegde, R.S.<\/strong> (2024) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-content\/uploads\/sites\/8\/2024\/08\/NSMB_2023.pdf\" target=\"_blank\" rel=\"noopener\">EMC rectifies the topology of multipass membrane proteins<\/a>. <em>Nat. Struct. Mol. Biol.<\/em>, <span class=\"docsum-journal-citation full-journal-citation\">31:32-41.<\/span><\/li>\n<\/ul>\n<p><strong>2023<\/strong><\/p>\n<ul>\n<li>H\u00f6pfler, M. and <strong>Hegde, R.S.<\/strong> (2023) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-content\/uploads\/sites\/8\/2023\/08\/Mol_Cell_2023c.pdf\" target=\"_blank\" rel=\"noopener\">Control of mRNA fate by its encoded nascent polypeptide<\/a>. <em>Mol. Cell<\/em>, 83:2840-2855.<\/li>\n<li>Yagita, Y., Zavodszky, E., Peak-Chew, S.Y., and <strong>Hegde, R.S.<\/strong> (2023) <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/37480851\/\" target=\"_blank\" rel=\"noopener\">Mechanism of orphan subunit recognition during assembly quality control<\/a>. <em>Cell<\/em>, 186:3443-3459.<\/li>\n<li>H\u00f6pfler, M., Absmeier, E., Peak-Chew, S.Y., Vartholomaiou, E., Passmore, L.A., Gasic, I., <strong>Hegde, R.S.<\/strong> (2023) <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/37295431\/\" target=\"_blank\" rel=\"noopener\">Mechanism of ribosome-associated mRNA degradation during tubulin autoregulation.<\/a> <em>Mol. Cell<\/em>, 83:2290-2302.<\/li>\n<li>Lemus, L., <strong>Hegde, R.S.<\/strong>, Goder, V. (2023) <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/37231113\/\" target=\"_blank\" rel=\"noopener\">New frontiers in quality control: the case of GPI-anchored proteins.<\/a> <em>Nat. Rev. Mol. Cell Biol.<\/em>, doi: 10.1038\/s41580-023-00616-9.<\/li>\n<li>Wu, H. and <strong>Hegde, R.S.<\/strong> (2023) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-content\/uploads\/sites\/8\/2023\/08\/Mol_Cell_2023a.pdf\" target=\"_blank\" rel=\"noopener\">Mechanism of signal-anchor triage during early steps of membrane protein insertion.<\/a> <em>Mol. Cell<\/em>, <span class=\"docsum-journal-citation full-journal-citation\">83:961-973.<\/span><\/li>\n<li>Smalinskait\u0117, L. and <strong>Hegde, R.S.<\/strong> (2023) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-content\/uploads\/sites\/8\/2023\/08\/CSHL_Persp_2022.pdf\" target=\"_blank\" rel=\"noopener\">The biogenesis of multipass membrane proteins.<\/a> <em>Cold Spring Harb. Perspect Biol.<\/em>, 15: a041251.<\/li>\n<\/ul>\n<p><strong>2022<\/strong><\/p>\n<ul>\n<li><sup>*<\/sup>Smalinskait\u0117, L., <sup>*<\/sup>Kim, M.K., Lewis, A.J.O., Keenan, R.J., and <strong>Hegde, R.S.<\/strong> (2022) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-content\/uploads\/sites\/8\/2023\/08\/Nature_2022a.pdf\" target=\"_blank\" rel=\"noopener\">Mechanism of an intramembrane chaperone for multipass membrane proteins.<\/a> <em>Nature<\/em>, 611:161-166.<\/li>\n<li><sup>*<\/sup>Sundaram, A., <sup>*<\/sup>Yamsek, M., <sup>*<\/sup>Zhong, F., Hooda, Y., <strong>Hegde, R.S.,<\/strong> Keenan, R.J. (2022) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-content\/uploads\/sites\/8\/2023\/08\/Nature_2022b.pdf\" target=\"_blank\" rel=\"noopener\">Substrate-driven assembly of a translocon for multipass protein biosynthesis.<\/a> <em>Nature<\/em>, 611:167-172.<\/li>\n<li><strong>Hegde, R.S.<\/strong> (2022) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-content\/uploads\/sites\/8\/2023\/08\/Annual_Rev_Biochem_2022.pdf\" target=\"_blank\" rel=\"noopener\">The function, structure, and origins of the ER membrane protein complex.<\/a> <em>Annu. Rev. Biochem.<\/em>, 91:651-678.<\/li>\n<li>Neal, S., Ohtake, F., Cuervo, A.M., <strong>Hegde R.S.<\/strong>, Jakob, U., Lazarou, M., Gilbert, W.V., Chen, Z.J., Tooze, S.A., Haber, J.E., Walters, K.J., and Hartl, F.U. (2022) <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/35452608\/\" target=\"_blank\" rel=\"noopener\">Quality Control: Maintaining molecular order and preventing cellular chaos.<\/a> <em>Mol. Cell<\/em>, 82:1390-1397.<\/li>\n<li><sup>*<\/sup>Jomaa, A., <sup>*<\/sup>Gamerdinger, M., <sup>*<\/sup>Hsieh, H.H., Wallisch, A., Chandrasekaran, V., Ulusoy, Z., Scaiola, A., <strong>Hegde, R.S.<\/strong>, Shan, S.O., Ban, N., and Deuerling, E. (2022) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-content\/uploads\/sites\/8\/2023\/08\/Science_2022.pdf\" target=\"_blank\" rel=\"noopener\">Mechanism of signal sequence handover from NAC to SRP on ribosomes during ER-protein targeting.<\/a> <em>Science<\/em>, 375:839-844.<\/li>\n<li><strong>Hegde, R.S.<\/strong> and Keenan, R.J. (2022) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-content\/uploads\/sites\/8\/2023\/08\/NRMCB_2021.pdf\" target=\"_blank\" rel=\"noopener\">The mechanisms of integral membrane protein biogenesis.<\/a> <em>Nat. Rev. Mol. Cell Biol.<\/em>, 23:107-124.<\/li>\n<\/ul>\n<p><strong>2021<\/strong><\/p>\n<ul>\n<li>Lewis, A.J.O. and <strong>Hegde, R.S.<\/strong> (2021) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-content\/uploads\/sites\/8\/2023\/08\/BMC_Biology_2021.pdf\" target=\"_blank\" rel=\"noopener\">A unified evolutionary origin for the ubiquitous protein transporters SecY and YidC.<\/a> <em>BMC Biol.<\/em>, 19:266<\/li>\n<li>Zavodszky, E., Peak-Chew, S.-Y., Juszkiewicz, S., Narvaez, A.J. and <strong>Hegde, R.S.<\/strong> (2021) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-content\/uploads\/sites\/8\/2023\/08\/Science_2021.pdf\" target=\"_blank\" rel=\"noopener\">Identification of a quality-control factor that monitors failures during proteasome assembly.<\/a> <em>Science,<\/em> <span class=\"docsum-journal-citation full-journal-citation\">373, 998-1004.<\/span><\/li>\n<li>Wan, L., Juszkiewicz, S., <span class=\"docsum-authors full-authors\">Blears, D., Bajpe, P.K., Han, Z., Faull, P., Mitter, R., Stewart, A., Snijders, A.P., <strong>Hegde, R.S.<\/strong>, and Svejstrup, J.Q. <\/span>(2021) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-content\/uploads\/sites\/8\/2023\/08\/Mol_Cell_2021.pdf\" target=\"_blank\" rel=\"noopener\">Translation stress and collided ribosomes are co-activators of cGAS.<\/a> <em>Mol. Cell,<\/em> <span class=\"docsum-journal-citation full-journal-citation\">81, 2808-2822.<\/span><\/li>\n<\/ul>\n<p><strong>2020<\/strong><\/p>\n<ul>\n<li>Chitwood, P. and <strong>Hegde, R.S.<\/strong> (2020) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-content\/uploads\/sites\/8\/2020\/09\/Nature_2020.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">An intramembrane chaperone complex facilitates membrane protein biogenesis<\/a>. <em>Nature,<\/em> 584, 630-634.<\/li>\n<li>Juszkiewicz, S., Slodkowicz, G., Lin, Z., Freire-Pritchett, P., Peak-Chew, S.Y., and <strong>Hegde, R.S.<\/strong> (2020) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-content\/uploads\/sites\/8\/2020\/09\/eLife_2020b.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">Ribosome collisions trigger cis-acting feedback inhibition of translation initiation.<\/a> <em>eLife,<\/em> doi: 10.7554\/eLife.60038.<\/li>\n<li>Juszkiewicz, S., Speldewinde, S.H., Wan, L., Svejstrup, J.Q., and <strong>Hegde, R.S.<\/strong> (2020) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-content\/uploads\/sites\/8\/2020\/09\/Mol_Cell_2020.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">The ASC-1 complex disassembles collided ribosomes.<\/a> <em>Mol. Cell,<\/em> doi: 10.1016\/j.molcel.2020.06.006.<\/li>\n<li>*O&#8217;Donnell, J.P., *Phillips, B.P., *Yagita, Y., Juszkiewicz, S., Wagner, A., Malinverni, D., Keenan, R.J., Miller, E.A., and <strong>Hegde, R.S.<\/strong> (2020) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-content\/uploads\/sites\/8\/2020\/09\/eLife_2020.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">The architecture of EMC reveals a path for membrane protein insertion.<\/a> <em>eLife,<\/em> doi: 10.7554\/eLife.57887.<\/li>\n<\/ul>\n<p><strong>2019<\/strong><\/p>\n<ul>\n<li>*Chandrasekaran, V., *Juszkiewicz, S., Choi, J., Puglisi, J.D., Brown, A., Shao, S., Ramakrishnan, V., and <strong>Hegde, R.S.<\/strong> (2019) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/NSMB_2019.pdf\" >Mechanism of ribosome stalling during translation of a poly(A) tail<\/a>. <em>Nat. Struct. Mol. Biol.,<\/em> doi: 10.1038\/s41594-019-0331-x.<\/li>\n<li>Lin, Z., Gasic, I., Chandrasekaran, V., Peters, N., Shao, S., Mitchison, T.J., and <strong>Hegde, R.S.<\/strong> (2019) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/Science_2019.pdf\" >TTC5 mediates autoregulation of tubulin via mRNA degradation.<\/a> <em>Science,<\/em> doi: 10.1126\/science.aaz4352.<\/li>\n<li>Verhagen, J.M.A. et al. (2019) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/CircGen_2019.pdf\" >Biallelic Variants in ASNA1, Encoding a Cytosolic Targeting Factor of Tail-Anchored Proteins, Cause Rapidly Progressive Pediatric Cardiomyopathy.<\/a> <em>Circ. Genome Precision Med.,<\/em> 12:397-406.<\/li>\n<li>Zavodszky, E. and <strong>Hegde, R.S.<\/strong> (2019) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/elife_2019.pdf\" >Misfolded GPI-anchored proteins are escorted through the secretory pathway by ER-derived factors.<\/a> <em>eLife,<\/em> 8:e46740.<\/li>\n<li><strong>Hegde, R.S.<\/strong> and Zavodszky, E. (2019) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/CSHL_Persp_2019.pdf\" >Recognition and Degradation of Mislocalized Proteins in Health and Disease.<\/a>. <em>Cold Spring Harb Perspect Biol.<\/em> doi: 10.1101\/cshperspect.a033902<\/li>\n<li>Chitwood, P.J. and <strong>Hegde, R.S.<\/strong> (2019) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/TCB_2019.pdf\" >The Role of EMC during Membrane Protein Biogenesis.<\/a>. <em>Trends Cell Biol.<\/em> doi:10.1016\/j.tcb.2019.01.007<\/li>\n<li>Inglis, A.J., Masson, G.R., Shao, S., Perisic, O., McLaughlin, S.H., <strong>Hegde, R.S.<\/strong>, and Williams, R.L. (2019) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/PNAS_2019.pdf\" >Activation of GCN2 by the ribosomal P-stalk.<\/a>. <em>Proc Natl Acad Sci U S A.<\/em> doi: 10.1073\/pnas.1813352116<\/li>\n<li>Volkmar, N., Thezenas, M.-L., Louie, S.M., Juszkiewicz, S., Nomura, D.K., <strong>Hegde, R.S.<\/strong>, Kessler, B.M., and Christianson, J.C. (2019) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/JCS_2019.pdf\" >The ER membrane protein complex promotes biogenesis of sterol-related enzymes maintaining cholesterol homeostasis<\/a>. <em>J. Cell Sci.<\/em> doi:10.1242\/jcs.223453<\/li>\n<\/ul>\n<p><strong>2018<\/strong><\/p>\n<ul>\n<li>Chitwood, P.J., Juszkiewicz, S., Guna, A., Shao, S., and <strong>Hegde, R.S.<\/strong> (2018) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/Cell_2018.pdf\" >EMC is required to initiate accurate membrane protein topogenesis<\/a>. <em>Cell<\/em> 175:1507-1519.<\/li>\n<li>*Juszkiewicz, S., *#Chandrasekaran, V., Lin, Z., Kraaz, S., Ramakrishnan, V., and <strong>Hegde, R.S.<\/strong> (2018) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/Mol_Cell_2018b.pdf\" >ZNF598 is a quality control sensor of ribosome collisions<\/a>. <em>Mol. Cell<\/em> 72:469-481<\/li>\n<li>Juszkiewicz, S. and <strong>Hegde, R.S.<\/strong> (2018) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/Mol_Cell_2018.pdf\" >Quality control of orphaned proteins<\/a>. <em>Mol. Cell<\/em> 71:443-457.<\/li>\n<li>Guna, A. and <strong>Hegde, R.S.<\/strong> (2018) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/Current_Biology_2018.pdf\" >Transmembrane domain recognition during membrane protein biogenesis and quality control<\/a>. <em>Current Biology<\/em> 28:R498-R511.<\/li>\n<li>Guna, A., Volkmar, N., Christianson, J.C. and <strong>Hegde, R.S.<\/strong> (2018) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/Science_2017c.pdf\" >The ER membrane protein complex is a transmembrane domain insertase<\/a>. <em>Science<\/em> 359:470-473.<\/li>\n<\/ul>\n<p><strong>2017<\/strong><\/p>\n<ul>\n<li>Anghel, S.A., McGilvray, P.T., <strong>Hegde, R.S.<\/strong> and Keenan, R.J. (2017) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/Cell_Reports_2017.pdf\" >Identification of Oxa1 homologs operating in the eukaryotic endoplasmic reticulum<\/a>. <em>Cell Reports<\/em> 21:3708-3716.<\/li>\n<li>Yanagitani, K., Juszkiewicz, S., and <strong>Hegde, R.S.<\/strong> (2017) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/Science_2017b.pdf\" >UBE2O is a quality control factor for orphans of multi-protein complexes<\/a>. <em>Science<\/em> 357: 472-475.<\/li>\n<li>Shao, S., Rodrigo-Brenni, M.C., Kivlen, M.H., and <strong>Hegde, R.S.<\/strong> (2017) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/Science_2017.pdf\" >Mechanistic basis for a molecular triage reaction<\/a>. <em>Science<\/em>, 355(6322):298-302.<\/li>\n<li>Chen, C., Itakura, E., Nelson, G.M., Sheng, M., Laurent, P., <strong>Hegde, R.S<\/strong>., and de Bono, M. (2017) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/Nature_2017.pdf\" >IL-17 is a neuromodulator of <em>Caenorhabditis elegans <\/em>sensory responses<\/a>. <em>Nature<\/em>, doi:10.1038\/nature20818.<\/li>\n<li>Juszkiewicz, S. and <strong>Hegde, R.S.<\/strong> (2017) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/Mol_Cell_2017.pdf\" >Initiation of Quality Control during Poly(A) Translation Requires Site-Specific Ribosome Ubiquitination<\/a>. <em>Mol. Cell<\/em>, doi:10.1016\/j.molcel.2016.11.039.<\/li>\n<\/ul>\n<p><strong>2016<\/strong><\/p>\n<ul>\n<li>Shao, S., Murray, J., Brown, A., Taunton, J., <sup>#<\/sup>Ramakrishnan, V., and <sup>#<\/sup><strong>Hegde, R.S.<\/strong> (2016) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/Cell_2016.pdf\" >Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes<\/a>. <em>Cell<\/em>, 167(5):1229-1240.<\/li>\n<li>Itakura, E., Zavodszky, E., Shao, S., Wohlever, M.L., Keenan, R.J., and <strong>Hegde, R.S.<\/strong> (2016) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/Mol_Cell_2016.pdf\" >Ubiquilins chaperone and triage mitochondrial membrane proteins for degradation<\/a>. <em>Mol. Cell<\/em>, 63(1):21-33.<\/li>\n<li>Brandman, O. and <strong>Hegde, R.S. <\/strong>(2016) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/98_Brandman_O_NSMB_2016.pdf\" >Ribosome-associated protein quality control<\/a>. <em>Nat Struct Mol Biol,<\/em> 23(1):7-15.<\/li>\n<li>Voorhees, R.M. and <strong>Hegde, R.S.<\/strong> (2016) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/97_Voorhees_RM_Science_2016.pdf\" >Structure of the Sec61 channel opened by a signal sequence<\/a>. <em>Science,<\/em> 351(6268):88-91.<\/li>\n<li>Shao, S. and <strong>Hegde, R. S. <\/strong>(2016) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/96_Shao_S_TIBS_2016.pdf\" >Target Selection during Protein Quality Control<\/a>. <em>Trends Biochem,<\/em> 41(2):124-37.<\/li>\n<\/ul>\n<p><strong>2015<\/strong><\/p>\n<ul>\n<li>Brown, A., <sup>*<\/sup>Shao, S., Murray, J., <strong><sup>#<\/sup>Hegde, R. S.<\/strong>, and <sup>#<\/sup>Ramakrishnan, V. (2015) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/95_Brown_A_Nature_2015.pdf\" >Structural basis for stop codon recognition in eukaryotes<\/a>. <em>Nature<\/em>, 524:493-6.<\/li>\n<li>Voorhees, R.M., and <strong>Hegde, R.S.<\/strong> (2015) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/94_Voorhees_RM_eLife_2015.pdf\" >Structures of the scanning and engaged states of the mammalian SRP-ribosome complex.<\/a> <em>Elife<\/em>, 4:e07975.<\/li>\n<li>von der Malsburg, K., Shao, S., and <strong>Hegde, R.S.<\/strong> (2015) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/93_vonderMalsburg-_K_MBC_2015.pdf\" >The Ribosome Quality Control Pathway can Access Nascent Polypeptides Stalled at the Sec61 Translocon.<\/a> <em>Mol Biol Cell,<\/em> 26:2168-80.<\/li>\n<li>Mateja, A. Paduch, M., Chang, H.-Y., Szydlowska, A., Kossiakoff, A.A., <strong><sup>#<\/sup>Hegde, R.S.<\/strong>, and <sup>#<\/sup>Keenan, R.J. (2015) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/92_Mateja_A_Science_2015.pdf\" >Structure of the Get3 targeting factor in complex with its membrane protein cargo.<\/a> <em>Science<\/em>, 347:1152-5.<\/li>\n<li>Shao, S., Brown, A., Santhanam, B., and <strong>Hegde, R.S.<\/strong> (2015) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/91_Shao_S_Mol_Cell_2015.pdf\" >Structure and assembly pathway of the ribosome quality control complex.<\/a> <em>Mol. Cell<\/em>, 57:433-44.<\/li>\n<\/ul>\n<p><strong>2014<\/strong><\/p>\n<ul>\n<li>Shao, S. and <strong>Hegde, R.S.<\/strong> (2014) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/90_Shao_S_Science_2014.pdf\" >Local synthesis and disposal.<\/a> <em>Science<\/em>, 346:701-2.<\/li>\n<li>Shao, S. and <strong>Hegde, R.S.<\/strong> (2014) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/89_Shao_S_Mol_Cell_2014b.pdf\" >Reconstitution of a Minimal Ribosome-Associated Ubiquitination Pathway with Purified Factors.<\/a> <em>Mol. Cell<\/em>, 55:880-90.<\/li>\n<li>Satpute-Krishnan, P., Ajinkya, M., Bhat, S., Itakura, E., <sup>#<\/sup><strong>Hegde R.S.<\/strong>, and <sup>#<\/sup>Lippincott-Schwartz, J. (2014) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/88_SatputeKrishnan_P_Cell_2014b.pdf\" >ER stress-induced clearance of misfolded GPI-anchored proteins via the secretory pathway.<\/a> <em>Cell<\/em>, 158:522-533<\/li>\n<li><sup>*#<\/sup>Voorhees, R.M., <sup>*<\/sup>Fernandez, I.S., Scheres, S.H.W., and <sup>#<\/sup><strong>Hegde, R.S.<\/strong> (2014) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/87_Voorhees_RM_Cell_2014.pdf\" >Structure of the mammalian-Sec61 complex to 3.4 \u0081 resolution<\/a>. <em>Cell<\/em>, 157:1632-43.<\/li>\n<li><strong>Hegde, R.S.<\/strong> (2014) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/86_Hegde_RS_EMBO_2014.pdf\" >Msp1: patrolling mitochondria for lost proteins.<\/a> <em>EMBO J<\/em>, 33:1509-10.<\/li>\n<li>Rodrigo-Brenni, M.C., Gutierrez, E., and <strong>Hegde, R.S.<\/strong> (2014) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/85_RodrigoBrenni_MC_Mol_Cell_2014.pdf\" >Cytosolic quality control of mislocalized proteins requires RNF126 recruitment to Bag6.<\/a> <em>Mol. Cell<\/em>, 55:227-237.<\/li>\n<li>Chen, C., Itakura, E., Weber, K.P., <strong>Hegde, R.S.<\/strong>, and de Bono, M. (2014) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/84_Chen_C_PlosGen_2014.pdf\" >An ER complex of ODR-4 and ODR-8\/Ufm1 specific protease 2 promotes GPCR maturation by a Ufm1-independent mechanism.<\/a> <em>PLoS Genetics<\/em>, 10(3):e1004082.<\/li>\n<li><sup>*<\/sup>MacKinnon, A.L., <sup>*<\/sup>Paavilainen, V.O., Sharma, A., <strong>Hegde, R.S.<\/strong>, and Taunton, J. (2014) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/83_MacKinnon_AL_eLife_2014.pdf\" >An allosteric Sec61 inhibitor traps nascent transmembrane helices at the lateral gate.<\/a> <em>eLife<\/em>, 3:e01483.<\/li>\n<\/ul>\n<p><strong>2013<\/strong><\/p>\n<ul>\n<li>Zhang, Z.R., Bonifacino, J.S., and <strong>Hegde, R.S.<\/strong> (2013) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/82_Zhang_ZR_Cell_2013.pdf\" >Deubiquitinases sharpen substrate discrimination during membrane protein degradation from the ER.<\/a> <em>Cell<\/em>, 154, 609-22.<\/li>\n<li><sup>*<\/sup>Shao, S., <sup>*<\/sup>von der Malsburg, K., and <strong>Hegde, R.S.<\/strong> (2013) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/81_Shao_S_Mol_Cell_2013.pdf\" >Listerin-dependent nascent protein ubiquitination relies on ribosome subunit dissociation.<\/a> <em>Mol. Cell<\/em> 50:637-48.<\/li>\n<\/ul>\n<p><strong>2012<\/strong><\/p>\n<ul>\n<li>Rodrigo-Brenni, M.C. and <strong>Hegde, R.S.<\/strong> (2012) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/80_RodrigoBrenni_MC_DevCell_2012.pdf\" >Design principles of protein biosynthesis-coupled quality control.<\/a> <em>Dev. Cell<\/em>, 23:896-907.<\/li>\n<li>Basseville, A., Tamaki, A., Ierano, C., Trostel, S., Ward, Y., Robey, R.W., <strong>Hegde, R.S.<\/strong>, and Bates, S.E. (2012) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/79_Basseville_A_CanRes_2012.pdf\" >Histone deacetylase inhibitors influence chemotherapy transport by modulating expression and trafficking of a common polymorphic variant of the ABCG2 efflux transporter.<\/a> <em>Cancer Res.<\/em> 72:3642-51.<\/li>\n<\/ul>\n<p><strong>2011<\/strong><\/p>\n<ul>\n<li>Shao, S. and <strong>Hegde, R.S.<\/strong> (2011) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/78_Shao_S_Cell_2011b.pdf\" >A calmodulin-dependent translocation pathway for small secretory proteins.<\/a> <em>Cell<\/em> 147:1576-88.<\/li>\n<li><strong>Hegde, R.S.<\/strong> and Keenan, R.J. (2011) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/77_Hegde_RS_NRMCB_2011.pdf\" >Tail-anchored membrane protein insertion into the endoplasmic reticulum.<\/a> <em>Nat. Rev. Mol. Cell Biol.<\/em> 12:787-98.<\/li>\n<li>Maifeld, S.V., MacKinnon, A.L., Garrison, J.L., Sharma, A., <strong>Hegde, R.S.<\/strong>, Kunkel, E.J., and Taunton, J. (2011) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/76_Maifeld_SV_Chem_Biol_2011.pdf\" >Secretory protein profiling reveals TNF_ inactivation by selective and promiscuous Sec61 modulators. <\/a> <em>Chem. Biol.,<\/em> 18:1082-8.<\/li>\n<li>Shao, S. and <strong>Hegde, R.S.<\/strong> (2011) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/75_Shao_S_Ann_Rev_2011.pdf\" >Membrane protein insertion at the endoplasmic reticulum.<\/a> <em>Ann. Rev. Cell Dev. Biol.<\/em>, 27:25-56.<\/li>\n<li><sup>*<\/sup>Mariappan, M., <sup>*<\/sup>Mateja, A., Dobosz, M., Bove, E., <sup>#<\/sup><strong>Hegde, R.S.<\/strong>, and <sup>#<\/sup>Keenan, R.J. (2011) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/74_Mariappan_M_Nature_2011b.pdf\" >The mechanism of membrane-associated steps in tail-anchored protein insertion.<\/a> <em>Nature<\/em> 477:61-6.<\/li>\n<li>Hessa, T., Sharma, A., Mariappan, M., Eshleman, H.D., Gutierrez, E., and <strong>Hegde, R.S.<\/strong> (2011) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/73_Hessa_T_Nature_2011.pdf\" >Protein targeting and degradation are coupled for elimination of mislocalized proteins.<\/a> <em>Nature<\/em>, 475:394-7.<\/li>\n<li>Wang, Q., Liu, Y., Soetandyo, N., Baek, K., Hegde, R.S., and Ye, Y. (2011) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/72_Wang_Q_Mol_Cell_2011.pdf\" >A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasomal degradation.<\/a> <em>Mol. Cell<\/em> 42:758-70.<\/li>\n<li>Shao, S. and <strong>Hegde, R.S.<\/strong> (2011) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/71_Shao_S_Cell_2011.pdf\" >A flip turn for membrane protein insertion.<\/a> <em>Cell<\/em>, 146:13-15.<\/li>\n<li>Sherrill, J., Mariappan, M., Dominik, P., <strong>Hegde, R.S.<\/strong>, and Keenan, R.J. (2011) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/70_Sherrill_J_Traffic_2011.pdf\" >A conserved archaeal pathway for tail-anchored membrane protein insertion.<\/a> <em>Traffic<\/em>, doi: 10.1111\/j.1600-0854.2011.01229.x.<\/li>\n<li>Chakrabarti, O., Rane, N.S., and <strong>Hegde, R.S.<\/strong> (2011) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/69_Chakrabarti_O_MBC_2011.pdf\" >Cytosolic aggregates perturb the degradation of non-translocated secretory and membrane proteins.<\/a> <em>Mol. Biol. Cell<\/em>, 22:1625-37.<\/li>\n<li>Morimoto, R.I., Driessen, A.J., <strong>Hegde, R.S.<\/strong>, and Langer, T. (2011) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/68_Morimoto_RI_NSMB_2011.pdf\" >The life of proteins: the good, the mostly good and the ugly.<\/a> <em>Nat. Struct. Mol. Biol. <\/em>18:1-4.<\/li>\n<\/ul>\n<p><strong>2010<\/strong><\/p>\n<ul>\n<li>Emerman, A.E., Zhang, Z.R., Chakrabarti, O., and <strong>Hegde, R.S.<\/strong> (2010) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/67_Emerman_AE_MBC_2010.pdf\" >Compartment-restricted biotinylation reveals novel features of prion protein metabolism in vivo.<\/a> <em>Mol. Biol. Cell <\/em>21:4325-37.<\/li>\n<li>Mariappan, M., Li, X., Sharma, A., Mateja, A., Keenan, R.J., and <strong>Hegde, R.S.<\/strong> (2010) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/66_Mariappan_M_Nature_2010.pdf\" >A ribosome-associating factor chaperones tail-anchored membrane proteins.<\/a> <em>Nature<\/em>, 466:1120-4.<\/li>\n<li><strong>Hegde, R.S.<\/strong> and Ploegh, H.L. (2010) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/65_Hegde_RS_COCB_2010.pdf\" >Quality and Quantity Control at the Endoplasmic Reticulum.<\/a> <em>Curr. Opin. Cell Biol.<\/em> 10.1016\/j.ceb.2010.05.005.<\/li>\n<li>Rutkowski, D.T. and <strong>Hegde, R.S.<\/strong> (2010) <a>Regulation of basal cellular physiology by the homeostatic unfolded protein response.<\/a> <em>J. Cell Biol.<\/em> 189:783-94.<\/li>\n<li>Rane, N.S., Chakrabarti, O., Feigenbaum, L., and <strong>Hegde, R.S. <\/strong>(2010) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/63_Rane_NS_JCB_2010.pdf\" >Signal sequence insufficiency contributes to neurodegeneration caused by transmembrane prion protein.<\/a> <em>J. Cell Biol<\/em>. 188:515-26.<\/li>\n<li>Sharma, A.S., Mariappan, M., Appathurai, S., and <strong>Hegde, R.S.<\/strong> (2010) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/62_Sharma_AS_MMB_2010.pdf\" >In vitro dissection of protein translocation into the mammalian endoplasmic reticulum.<\/a> <em>Methods Mol. Biol.<\/em> 619:339-63.<\/li>\n<\/ul>\n<p><strong>2009<\/strong><\/p>\n<ul>\n<li>Mateja, A., Szlachcic, A., Downing, M.E., Dobosz, M., Mariappan, M., <strong>Hegde, R.S.<\/strong>, and Keenan, R.J. (2009) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/61_Mateja_A_Nature_2009.pdf\" >The structural basis of tail-anchored membrane protein recognition by Get3.<\/a> <em>Nature<\/em>, 461:361-6.<\/li>\n<li>Ashok, A. and <strong>Hegde, R.S.<\/strong> (2009) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/60_Ashok_A_PLoS_Path_2009.pdf\" >Selective Processing and Metabolism of Disease-Causing Mutant Prion Proteins.<\/a> <em>PLoS Pathogens<\/em>, 5:e1000479.<\/li>\n<li>Chakrabarti, O. and <strong>Hegde, R.S.<\/strong> (2009) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/59_Chakrabarti_O_Cell_2009.pdf\" >Functional depletion of Mahogunin by cytosolically exposed prion protein contributes to neurodegeneration.<\/a> <em>Cell<\/em>, 137:1136-1147.<\/li>\n<li>Chakrabarti, O., Ashok, A., and <strong>Hegde, R.S.<\/strong> (2009) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/58_Chakrabarti_O_TIBS_2009.pdf\" >Prion protein biosynthesis and its emerging role in neurodegeneration.<\/a> <em>Trends Biochem. Sci.<\/em>, 34:287-95.<\/li>\n<li><strong>Hegde, R.S.<\/strong> (2009) <a>Protein maturation and processing at the endoplasmic reticulum. In: The Liver: Biology and Pathobiology.<\/a> <em>5<sup>th<\/sup> Edition. Edited by I. A. Arias et al., Wiley-Blackwell.<\/em><\/li>\n<li>Polgar, O., Ediriwickrema, L.S., Robey, R.W., Sharma, A., <strong>Hegde, R.S.<\/strong>, Li, Y., Xia, D., Ward, Y., Dean, M., Ozvegy-Laczka, C., Sarkadi, B., and Bates, S.E. (2009) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/56_Polgar_O_BBA_2009.pdf\" >Arginine 383 is a crucial residue in ABCG2 biogenesis.<\/a> <em>Biochim. Biophy. Acta,<\/em> 1788(7):1434-43.<\/li>\n<li>Kang, S.W. and <strong>Hegde, R.S.<\/strong> (2008) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/55_Kang_SW_Cell_2008.pdf\" >Lighting up the stressed ER.<\/a> <em>Cell<\/em>, 135(5):787-9.<\/li>\n<\/ul>\n<p><strong>2008<\/strong><\/p>\n<ul>\n<li>Rane, N.S., Kang, S.W., Chakrabarti, O., Feigenbaum, L., and <strong>Hegde, R.S.<\/strong> (2008) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/54_Rane_NS_DevCell_2008.pdf\" >Chronic prion protein degradation via pre-emptive quality control causes neurodegeneration.<\/a> <em>Dev. Cell<\/em>, 15:359-370.<\/li>\n<li><strong>Hegde, R.S.<\/strong> and Kang, S.W. (2008) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/53_Hegde_RS_JCB_2008.pdf\" >The concept of translocational regulation.<\/a> <em>J. Cell Biol. <\/em>182:225-232.<\/li>\n<li>Menetret, J.F., <strong>Hegde, R.S.<\/strong>, Aguiar, M., Gygi, S.P., Park, E., Rapoport, T.A., and Akey, C.W. (2008) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/52_Menetret_JF_Structure_2008.pdf\" >Single copies of Sec61 and TRAP associate with a non-translating mammalian ribosome.<\/a> <em>Structure<\/em>, 16:1126-1137.<\/li>\n<li>Ashok, A. and <strong>Hegde, R.S.<\/strong> (2008) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/51_Ashok_A_MBC_2008.pdf\" >Retrotranslocation of prion proteins from the ER by inhibition of GPI signal sequence transamidation.<\/a> <em>Mol. Biol. Cell<\/em>. 19:3463-3476.<\/li>\n<li>Ashok, A. and <strong>Hegde, R.S.<\/strong> (2008) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/50_Ashok_A_ELS_2008.pdf\" >Cytotoxicity of aberrant proteins.<\/a> <em>In: Encyclopedia of Life Sciences (ELS). John Wiley &amp; Sons, Ltd:<\/em> DOI: 10.1002\/9780470015902.a0020887.<\/li>\n<\/ul>\n<p><strong>2007<\/strong><\/p>\n<ul>\n<li>MacKinnon, A.L., Garrison, J.L., <strong>Hegde, R.S.<\/strong>, and Taunton J. (2007) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/49_MacKinnon_AL_JACS_2007.pdf\" >Photo-leucine incorporation reveals the target of a cyclodepsipeptide inhibitor of cotranslational translocation.<\/a> <em>J. Am. Chem. Soc.<\/em> 129:14560-1.<\/li>\n<li><sup>*<\/sup>Rutkowski, D.T., <sup>*<\/sup>Kang, S.W., Goodman, A.G., Garrison, J.L., Taunton, J., Katze, M.G., Kaufman, R.J., and <strong>Hegde, R.S.<\/strong> (2007) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/48_Rutkowski_DT_MBC_2007.pdf\" >The Role of p58IPK in Protecting the Stressed Endoplasmic Reticulum.<\/a> <em>Mol. Biol. Cell,<\/em> 18:3681-91.<\/li>\n<li>Ong, H. L., Liu, X., Tsaneva-Atanasova, K., Singh, B. B., Bandyopadhyay, B. C., Swaim, W. D., Russell, J. T., <strong>Hegde, R. S.<\/strong>, Sherman, A., and Ambudkar, I. S. (2007) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/47_Ong_HL_JBC_2007.pdf\" >Relocalization of STIM1 for activation of store-operated Ca2+ entry is determined by the depletion of subplasma membrane endoplasmic reticulum Ca2+ store.<\/a> <em>J. Biol. Chem.<\/em>, 282:12176-85.<\/li>\n<li>Stefanovic, S. and <strong>Hegde, R. S.<\/strong> (2007) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/46_Stefanovic_S_Cell_2007.pdf\" >Identification of a targeting factor for post-translational membrane protein insertion into the ER.<\/a> <em>Cell<\/em>, 128:1147-1159.<\/li>\n<li>Alken, M. and <strong>Hegde, R. S.<\/strong> (2007) <a>The translocation apparatus of the endoplasmic reticulum. In: Molecular machines involved in protein transport across cellular membranes, ed. R. Dalbey, C. Koehler, and F. Tamanoi.<\/a> <em>Academic press\/Elsevier.<\/em><\/li>\n<li>Ong, H. L., Liu, X., Sharma, A., <strong>Hegde, R. S.<\/strong>, and Ambudkar, I. (2007) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/44_Ong_HL_Pflug_Arch_2007.pdf\" >Intracellular Ca2+ release via the ER translocon activates store-operated calcium entry.<\/a> <em>Pflugers Arch.<\/em> 453:797-808.<\/li>\n<\/ul>\n<p><strong>2006<\/strong><\/p>\n<ul>\n<li><sup>*<\/sup>Kang, S. W., <sup>*<\/sup>Rane, N. S., Kim, S. J., Garrison, J. L., Taunton, J., and <strong>Hegde, R. S.<\/strong> (2006) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/43_Kang_SW_Cell_2006.pdf\" >Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway.<\/a> <em>Cell<\/em>, 127:999-1013.<\/li>\n<li>Bernstein, H. D. and <strong>Hegde, R. S.<\/strong> (2006) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/42_Bernstein_HD_TIBS_2006.pdf\" >The surprising complexity of signal sequences.<\/a> <em>Trends Biochem. Sci.<\/em> 31:563-71.<\/li>\n<li>Ashok, A. and <strong>Hegde, R. S.<\/strong> (2006) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/41_Ashok_A_EMBORep_2006.pdf\" >Prions and retroviruses: an endosomal rendezvous? <\/a> <em>EMBO Rep.<\/em> 7:685-687.<\/li>\n<li>Snapp, E. L. and <strong>Hegde, R. S.<\/strong> (2006) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/40_Snapp_EL_Curr_Prot_2006.pdf\" >Rational design and evaluation of FRET experiments to measure protein proximities in cells. In<\/a> <em>Curr. Prot. in Cell Biol.<\/em>, ed. J. S. Bonifacino et al., Chapter 17:Unit 17.9, Wiley.<\/li>\n<li>Snapp, E. L., Sharma, A., Lippincott-Schwartz, J., and <strong>Hegde, R. S.<\/strong> (2006) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/39_Snapp_EL_PNAS_2006.pdf\" >Monitoring chaperone engagement of substrates in the endoplasmic reticulum of live cells.<\/a> <em>Proc. Natl. Acad. Sci.<\/em>, 103(17):6536-6541.<\/li>\n<li>Chakrabarti, O. and <strong>Hegde, R. S.<\/strong> (2006) <a>Trafficking of the cellular Prion protein and its role in neurodegeneration.<\/a> <em>In: Protein trafficking in the neuron, ed. A. Bean, Elsevier<\/em>, 413-436.<\/li>\n<\/ul>\n<p><strong>2005<\/strong><\/p>\n<ul>\n<li><sup>*<\/sup>Shaffer, K. L., <sup>*<\/sup>Sharma, A., Snapp, E. L., and <strong>Hegde, R. S.<\/strong> (2005) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/37_Shaffer_KL_DevCell_2005.pdf\" >Regulation of protein compartmentalization expands the diversity of protein function.<\/a> <em>Dev. Cell,<\/em> 9:545-554.<\/li>\n<li>Brambillasca, S., Yabal, M., Soffientini, P., Stefanovic, S., Makarow, M., <strong><sup>#<\/sup>Hegde, R. S.<\/strong>, and <sup>#<\/sup>Borgese, N. (2005) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/36_Brambillasca_S_EMBO_2005.pdf\" >Transmembrane topogenesis of a tail-anchored protein is modulated by membrane lipid composition.<\/a> <em>EMBO J.<\/em>, 24:2533-2542.<\/li>\n<li>Garrison, J. L., Kunkel, E. J., <strong><sup>#<\/sup>Hegde, R. S.<\/strong>, and <sup>#<\/sup>Taunton, J. (2005) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/35_Garrison_JL_Nature_2005.pdf\" >A substrate-specific inhibitor of protein translocation into the endoplasmic reticulum.<\/a> <em>Nature<\/em>, 436:285-289.<\/li>\n<li><sup>*<\/sup>Menetret, J. F., <strong><sup>*<\/sup>Hegde, R. S.<\/strong>, Heinrich, S. U., Chandramouli, P., Ludtke, S. J., Rapoport, T. A., and Akey, C. W. (2005) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/34_Menetret_JF_JMB_2005.pdf\" >Architecture of the ribosome-channel complex derived from native membranes. <\/a> <em>J. Mol. Biol.<\/em>, 348:445-457.<\/li>\n<li><strong>Hegde, R. S.<\/strong> (2005) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/33_Hegde_RS_Chapter_2005.pdf\" >Protein translocation across the endoplasmic reticulum. In: Protein movement across membranes, pp. 1-18. ed. J. Eichler, Landes Bioscience, Georgetown, TX.<\/a><\/li>\n<li>Levine, C. G., Mitra, D., Sharma, A., Smith, C. L., and <strong>Hegde, R. S.<\/strong> (2005) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/32_Levine_CG_MBC_2005.pdf\" >The efficiency of protein compartmentalization into the secretory pathway.<\/a> <em>Mol. Biol. Cell<\/em>, 16:279-291.<\/li>\n<li><strong>Hegde, R. S.<\/strong> and Rane, N. S. (2005) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/31_Rane_Chapter_2005.pdf\" >The molecular basis of prion protein-mediated neuronal damage.<\/a> <em>In: Neurodegeneration and Prion Disease<\/em>, pp. 407-450, ed. D. R. Brown, Springer, NY, NY.<\/li>\n<\/ul>\n<p><strong>2004<\/strong><\/p>\n<ul>\n<li>Rane, N., Yonkovich, J., and <strong>Hegde, R. S.<\/strong> (2004) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/30_Rane_N_EMBO_2004.pdf\" >Protection from cytosolic prion protein toxicity by modulation of protein translocation.<\/a> <em>EMBO J.<\/em>, 23:4550-4559.<\/li>\n<li><sup>*<\/sup>Karsten, V., <strong><sup>*<\/sup>Hegde, R. S.<\/strong>, Sinai, A. P., Yang, M., and Joiner, K. (2004) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/29_Karsten_V_JBC_2004.pdf\" >Transmembrane domain modulates sorting of membrane proteins in toxoplasma gondii.<\/a> <em>J. Biol. Chem<\/em>. 279:26052-26057.<\/li>\n<li>Snapp, E. L., Reinhart, G. A., Bogert, B. A., Lippincott-Schwartz, J., and <strong>Hegde, R. S.<\/strong> (2004) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/28_Snapp_EL_JCB_2004.pdf\" >The organization of engaged and quiescent translocons in the endoplasmic reticulum of mammalian cells.<\/a> <em>J. Cell Biol.<\/em> 164:997-1007.<\/li>\n<li>Tremblay P., Ball, H. L., Kaneko, K., Groth, D., <strong>Hegde, R. S.<\/strong>, Cohen, F. E., DeArmond, S. J., Prusiner, S. B., and Safar, J. G. (2004) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/27_Tremblay_P_JV_2004.pdf\" >Mutant PrPSc conformers induced by a synthetic peptide and various prion strains.<\/a> <em>J. Virol.,<\/em> 78:2088-2099.<\/li>\n<\/ul>\n<p><strong>2003<\/strong><\/p>\n<ul>\n<li>Snapp, E. L., <strong>Hegde, R. S.<\/strong>, Francolini, M., Lombardo, F., Colombo, S., Pedrazzini, E., Borgese, N., and Lippincott-Schwartz, J. (2003) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/26_Snapp_EL_JCB_2003.pdf\" >Formation of stacked ER cisternae by low affinity protein interactions.<\/a> <em>J. Cell Biol.<\/em>,163:257-69.<\/li>\n<li><strong>Hegde, R. S.<\/strong> and Rane, N. S. (2003) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/25_Hegde_RS_TINS_2003.pdf\" >Prion protein trafficking and the development of neurodegeneration.<\/a> <em>Trends Neurol. Sci.<\/em> 26:337-339.<\/li>\n<li>Fons, R. D., Bogert, B. A., and <strong>Hegde, R. S.<\/strong> (2003) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/24_Fons_RD_JCB_2003.pdf\" >Substrate-specific function of the translocon-associated protein complex during translocation across the ER membrane.<\/a> <em>J. Cell Biol.<\/em> 160:529-539.<\/li>\n<\/ul>\n<p><strong>2002<\/strong><\/p>\n<ul>\n<li><strong>Hegde, R. S.<\/strong> (2002) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/23_Hegde_RS_Mol_Cell-2002.pdf\" >Targeting and beyond: new roles for old signal sequences.<\/a> <em>Mol. Cell,<\/em> 10:697-698.<\/li>\n<li>Kim, S. J. and <strong>Hegde, R. S.<\/strong> (2002) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/22_Kim_SJ_MBC_2002.pdf\" >Cotranslational partitioning of nascent prion protein into multiple populations at the translocation channel.<\/a> <em>Mol. Biol. Cell,<\/em> 13:3775-3786.<\/li>\n<li>Lingappa, V. R., Rutkowski, D. T., <strong>Hegde, R. S.<\/strong>, and Andersen, O. S. (2002) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/21_Lingappa_VR_BioEssays_2002.pdf\" >Conformational control through translocational regulation: a new view of secretory and membrane protein folding.<\/a> <em>Bioessays<\/em>, 24:741-748.<\/li>\n<li>Kim, S. J., Mitra, D., Salerno, J. S., and <strong>Hegde, R. S.<\/strong> (2002) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/20_Kim_SJ_DevCell_2002.pdf\" >Signal sequences control gating of the protein translocation channel in a substrate-specific manner.<\/a> <em>Dev. Cell,<\/em>2:207-217.<\/li>\n<\/ul>\n<p><strong>2001<\/strong><\/p>\n<ul>\n<li>Lingappa, V. R. and <strong>Hegde, R. S.<\/strong> (2001) <a>Prion Protein Biogenesis: Implications for Neurodegeneration.<\/a> <em>In &#8216;Research and Perspectives in Alzheimer&#8217;s Diseases&#8217;. Beyreuther\/Christen\/Masters (Eds.) copyright Springer-Verlag Berlin Heidelberg.<\/em><\/li>\n<li>Kim, S. J., Rahbar, R., and <strong>Hegde, R. S.<\/strong> (2001) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/18_Kim_SJ_JBC_2001.pdf\" >Combinatorial control of prion protein biogenesis by the signal sequence and transmembrane domain. <\/a> <em>J. Biol. Chem. <\/em>276:26132-26140 <em>.<\/em><\/li>\n<li>Rutkowski, D. T., Lingappa, V. R. and <strong>Hegde, R. S.<\/strong> (2001) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/17_Rutkowski_DT_PNAS_2001.pdf\" >Substrate-specific regulation of the ribosome-translocon junction by N-terminal signal sequences.<\/a> <em>Proc. Natl. Acad. Sci. <\/em>98:7823-7828.<\/li>\n<\/ul>\n<p><strong>1990 to 2000 [publications as a student]<\/strong><\/p>\n<ul>\n<li>Wilhelm, J. E., Vale, R. D., and <strong>Hegde, R. S.<\/strong> (2000) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/16_Wilhelm_JE_PNAS_2000.pdf\" >Coordinate control of translation and localization of Vg1 mRNA in Xenopus oocytes.<\/a> <em>Proc. Natl. Acad. Sci.<\/em>, 97:13132-13137.<\/li>\n<li><strong>Hegde, R. S.<\/strong>, Tremblay, P., Groth, D., DeArmond, S. J., Prusiner, S. B. and Lingappa, V.R. (1999) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/15_Hegde_RS_Nature_1999.pdf\" >Transmissible and genetic prion diseases share a common pathway of neurodegeneration.<\/a> <em>Nature<\/em>, 402:822-826.<\/li>\n<li><strong>Hegde, R. S.<\/strong> and Lingappa, V. R. (1999) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/14_Hegde_RS_TCB_1999.pdf\" >Regulation of protein biogenesis at the endoplasmic reticulum membrane.<\/a> <em>Trends Cell Biol<\/em>., 9:132-137.<\/li>\n<li><strong>Hegde, R. S.<\/strong>, Voigt, S., and Lingappa, V. R. (1998) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/13_Hegde_RS_MolCell_1998.pdf\" >Regulation of protein topology by <\/a> <em>trans<\/em>-acting factors at the endoplasmic reticulum. <em>Mol. Cell<\/em>, 2:85-91.<\/li>\n<li><strong>Hegde, R. S.<\/strong>, Voigt, S., Rapoport, T. A., and Lingappa, V. R. (1998) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/12_Hegde_RS_Cell_1998.pdf\" >TRAM regulates the exposure of nascent secretory proteins to the cytosol during translocation into the endoplasmic reticulum.<\/a> <em>Cell<\/em>, 92:621-631.<\/li>\n<li><strong>Hegde, R. S.<\/strong>, Mastrianni, J. A., Scott, M. R., DeFea, K. A., Tremblay, P., Torchia, M., DeArmond, S. J., Prusiner, S. B., and Lingappa, V. R. (1998) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/11_Hegde_RS_Science_1998.pdf\" >A transmembrane form of the prion protein in neurodegenerative disease.<\/a> <em>Science<\/em>, 279:827-834.<\/li>\n<li>Rusinol, A. E., <strong>Hegde, R. S.<\/strong>, Chuck, S. L., Lingappa, V. R., and Vance, J. E. (1998) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/10_Rusinol_AE_JLR_1998.pdf\" >Translocational pausing of apolipoprotein can be regulated by membrane lipid composition.<\/a> <em>J. Lipid. Res.,<\/em> 39:1287-1294.<\/li>\n<li><strong>Hegde, R. S.<\/strong> and Lingappa, V. R. (1997) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/9_Hegde_RS_Cell_1997.pdf\" >Membrane protein biogenesis: regulated complexity at the endoplasmic reticulum.<\/a> <em>Cell<\/em>, 91: 575-582.<\/li>\n<li>Lingappa, J. R., Hill, R. L., Wong, M. L. and <strong>Hegde, R. S.<\/strong> (1997) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/8_Lingappa_JE_JCB_1997.pdf\" >A multi-step, ATP-dependent pathway for assembly of human Immunodeficiency (HIV) capsids in a cell-free system.<\/a> <em>J. Cell Biol.<\/em>, 136:567-581.<\/li>\n<li>Lingappa, V. R. and <strong>Hegde, R.<\/strong> (1997) <a>Translocational pausing and the regulation of membrane protein biogenesis. in<\/a> <em>Membrane Proteins: structure, function and expression control.<\/em> Edited by Naotaka Hamasaki and Katsuyoshi Mihara. Kyushu University Press (Japan), S. Karger AG (Switzerland).<\/li>\n<li>Kivlen, M. H., Dorsey, C. A., Lingappa, V. R. and <strong>Hegde, R. S.<\/strong> (1997) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/6_Kivlen_MH_JLR_1997.pdf\" >Asymmetric distribution of pause transfer sequences in apolipoprotein B-100.<\/a> <em>J. Lipid Res<\/em>., 38: 1149-1162.<\/li>\n<li><strong>Hegde, R. S.<\/strong> and Lingappa, V. R. (1996) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/5_Hegde_RS_Cell_1996.pdf\" >Sequence-specific alteration of the ribosome-membrane junction exposes nascent secretory proteins to the cytosol.<\/a> <em>Cell<\/em>, 85:217-228.<\/li>\n<li><strong>Hegde, R. S.<\/strong>, Zuo, J., Voellmy, R. and Welch, W. J. (1995) Short circuiting stress protein expression via a tyrosine kinase inhibitor, Herbimycin A. <em>J. Cellular Physiology<\/em>, 165:186-200.<\/li>\n<li><strong>Hegde, R. S.<\/strong> and Palfrey, H. C. (1991) Ionic effects on bumetanide binding to the activated Na\/K\/2Cl Cotransporter: Selectivity and Kinetic properties of ion binding sites. <em>J. Membrane Biology<\/em>, 126:27-37.<\/li>\n<li>Pewitt, E. B., <strong>Hegde, R. S.<\/strong>, Haas, M., and Palfrey, H. C. (1990) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/2_Pewitt_EB_JBC_1990b.pdf\" >The Regulation of Na\/K\/2Cl cotransport and bumetanide binding by protein phosphorylation and dephosphorylation.<\/a> <em>J. Biol. Chem.<\/em>, 265:20747-20756.<\/li>\n<li>Pewitt, E. B., <strong>Hegde, R. S.<\/strong>, and Palfrey, H. C. (1990) <a href=\"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/download\/1_Pewitt_EB_JBC_1990a.pdf\" >3H Bumetanide binding to avian erythrocyte membranes.<\/a> <em>J. Biol. Chem<\/em>., 265:14364-14370.<\/li>\n<\/ul>\n","protected":false},"excerpt":{"rendered":"<p>Notes: * co-first authors; # co-corresponding authors 2025 Sundaram, A., Li. Q., Wan, Y., Tang, J., Wu, H., Smalinskaite, L., Hegde, R.S., Ji, Z., Keenan, R.J. (2025) Global analysis of translocon remodeling during protein synthesis at the ER. Nat. Struct. Mol. Biol., 32(12):2517-2525. Grabarczyk, D.B., Ehrmann, J.F., Murphy, P., Yang, W.S., Kurzbauer, R., Bell, L.E., [&hellip;]<\/p>\n","protected":false},"author":6,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"_genesis_hide_title":false,"_genesis_hide_breadcrumbs":false,"_genesis_hide_singular_image":false,"_genesis_hide_footer_widgets":false,"_genesis_custom_body_class":"","_genesis_custom_post_class":"","_genesis_layout":"","footnotes":""},"class_list":{"0":"post-27","1":"page","2":"type-page","3":"status-publish","5":"entry"},"_links":{"self":[{"href":"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-json\/wp\/v2\/pages\/27","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-json\/wp\/v2\/users\/6"}],"replies":[{"embeddable":true,"href":"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-json\/wp\/v2\/comments?post=27"}],"version-history":[{"count":86,"href":"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-json\/wp\/v2\/pages\/27\/revisions"}],"predecessor-version":[{"id":567,"href":"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-json\/wp\/v2\/pages\/27\/revisions\/567"}],"wp:attachment":[{"href":"https:\/\/www2.mrc-lmb.cam.ac.uk\/groups\/hegde\/wp-json\/wp\/v2\/media?parent=27"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}