{"entity": "researcher", "timestamp": "2026-08-20T20:40:08.993Z", "family": "Kudva", "given": "Renuka", "initials": "R", "orcid": "0000-0003-0426-3716", "affiliations": ["Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/a8f164c44cca4540965f66c2829f624e.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/a8f164c44cca4540965f66c2829f624e"}}, "publications": [{"entity": "publication", "iuid": "af3012effc7e4c12972453056d7e8de4", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/af3012effc7e4c12972453056d7e8de4.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/af3012effc7e4c12972453056d7e8de4"}}, "title": "Single-residue effects on the behavior of a nascent polypeptide chain inside the ribosome exit tunnel.", "authors": [{"family": "Pardo-Avila", "given": "F\u00e1tima", "initials": "F", "orcid": "0009-0002-9040-4684", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/edb6b877440e40f0a4f0272a7ac4f5a7.json"}}, {"family": "Kudva", "given": "Renuka", "initials": "R", "orcid": "0000-0003-0426-3716", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/a8f164c44cca4540965f66c2829f624e.json"}}, {"family": "Levitt", "given": "Michael", "initials": "M", "orcid": "0000-0002-8414-7397", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/ea8efb5af79543d4ab9a357b889abe37.json"}}, {"family": "von Heijne", "given": "Gunnar", "initials": "G", "orcid": "0000-0002-4490-8569", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/529a460e668a479ca7d9b9271375ef9f.json"}}], "type": "journal article", "published": "2024-08-20", "journal": {"title": "bioRxiv", "issn": "2692-8205", "issn-l": null}, "abstract": "Nascent polypeptide chains (NCs) are extruded from the ribosome through an exit tunnel (ET) traversing the large ribosomal subunit. The ET's irregular and chemically complex wall allows for various NC-ET interactions. Translational arrest peptides (APs) bind in the ET to induce translational arrest, a property that can be exploited to study NC-ET interactions by Force Profile Analysis (FPA). We employed FPA and molecular dynamics (MD) simulations to investigate how individual residues placed in a glycine-serine repeat segment within an AP-stalled NC interact with the ET to exert a pulling force on the AP and release stalling. Our results indicate that large and hydrophobic residues generate a pulling force on the NC when placed \u227310 residues away from the peptidyl transfer center (PTC). Moreover, an asparagine placed 12 residues from the PTC makes a specific stabilizing interaction with the tip of ribosomal protein uL22 that reduces the pulling force on the NC, while a lysine or leucine residue in the same position increases the pulling force. Finally, the MD simulations suggest how the Mannheimia succiniproducens SecM AP interacts with the ET to promote translational stalling.", "doi": "10.1101/2024.08.20.608737", "pmid": "39229094", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC11370347"}, {"db": "pii", "key": "2024.08.20.608737"}], "notes": [], "created": "2026-08-20T10:56:12.120Z", "modified": "2026-08-20T10:56:12.255Z"}, {"entity": "publication", "iuid": "50434f6df5c34d5597aab002b6098324", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/50434f6df5c34d5597aab002b6098324.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/50434f6df5c34d5597aab002b6098324"}}, "title": "The ribosome modulates folding inside the ribosomal exit tunnel.", "authors": [{"family": "Wruck", "given": "Florian", "initials": "F"}, {"family": "Tian", "given": "Pengfei", "initials": "P"}, {"family": "Kudva", "given": "Renuka", "initials": "R", "orcid": "0000-0003-0426-3716", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/a8f164c44cca4540965f66c2829f624e.json"}}, {"family": "Best", "given": "Robert B", "initials": "RB", "orcid": "0000-0002-7893-3543", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/36c5cc15e14e412fb8798666bd48f00f.json"}}, {"family": "von Heijne", "given": "Gunnar", "initials": "G"}, {"family": "Tans", "given": "Sander J", "initials": "SJ"}, {"family": "Katranidis", "given": "Alexandros", "initials": "A", "orcid": "0000-0002-1785-1659", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/4b148b128428419ba9b2e759ca159691.json"}}], "type": "journal article", "published": "2021-05-05", "journal": {"title": "Commun Biol", "issn": "2399-3642", "volume": "4", "issue": "1", "pages": "523", "issn-l": "2399-3642"}, "abstract": "Proteins commonly fold co-translationally at the ribosome, while the nascent chain emerges from the ribosomal exit tunnel. Protein domains that are sufficiently small can even fold while still located inside the tunnel. However, the effect of the tunnel on the folding dynamics of these domains is not well understood. Here, we combine optical tweezers with single-molecule FRET and molecular dynamics simulations to investigate folding of the small zinc-finger domain ADR1a inside and at the vestibule of the ribosomal tunnel. The tunnel is found to accelerate folding and stabilize the folded state, reminiscent of the effects of chaperonins. However, a simple mechanism involving stabilization by confinement does not explain the results. Instead, it appears that electrostatic interactions between the protein and ribosome contribute to the observed folding acceleration and stabilization of ADR1a.", "doi": "10.1038/s42003-021-02055-8", "pmid": "33953328", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC8100117"}, {"db": "pii", "key": "10.1038/s42003-021-02055-8"}], "notes": [], "created": "2026-08-20T09:24:59.112Z", "modified": "2026-08-20T09:24:59.214Z"}, {"entity": "publication", "iuid": "f045bb18c2a748879939f71c6872f94c", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/f045bb18c2a748879939f71c6872f94c.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/f045bb18c2a748879939f71c6872f94c"}}, "title": "Cotranslational folding of a periplasmic protein domain in Escherichia coli", "authors": [{"family": "Sandhu", "given": "Hena", "initials": "H"}, {"family": "Hedman", "given": "Rickard", "initials": "R"}, {"family": "Cymer", "given": "Florian", "initials": "F"}, {"family": "Kudva", "given": "Renuka", "initials": "R", "orcid": "0000-0003-0426-3716", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/a8f164c44cca4540965f66c2829f624e.json"}}, {"family": "Ismail", "given": "Nurzian", "initials": "N"}, {"family": "von Heijne", "given": "Gunnar", "initials": "G", "orcid": "0000-0002-4490-8569", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/529a460e668a479ca7d9b9271375ef9f.json"}}], "type": "posted-content", "published": "2021-02-06", "journal": {"issn-l": null}, "abstract": null, "doi": "10.1101/2021.02.06.430026", "pmid": null, "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T10:02:33.167Z", "modified": "2026-08-20T10:02:33.225Z"}, {"entity": "publication", "iuid": "71f0280c5fa44aff85961bc6c771cbd5", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/71f0280c5fa44aff85961bc6c771cbd5.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/71f0280c5fa44aff85961bc6c771cbd5"}}, "title": "Cotranslational folding of alkaline phosphatase in the periplasm of Escherichia coli.", "authors": [{"family": "Elfageih", "given": "Rageia", "initials": "R", "orcid": "0000-0003-0506-1470", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/a76db32fb3f44bd992423d22ebef0293.json"}}, {"family": "Karyolaimos", "given": "Alexandros", "initials": "A", "orcid": "0000-0003-2264-3958", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/4d43d202f8684c09a3e34ca0d26cabc4.json"}}, {"family": "Kemp", "given": "Grant", "initials": "G", "orcid": "0000-0001-5125-2740", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d715b8af2972418aa144b2ca11487ce4.json"}}, {"family": "de Gier", "given": "Jan-Willem", "initials": "JW", "orcid": "0000-0001-5537-4358", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/5868d65a24344c5da61ca3cacd29a558.json"}}, {"family": "von Heijne", "given": "Gunnar", "initials": "G", "orcid": "0000-0002-4490-8569", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/529a460e668a479ca7d9b9271375ef9f.json"}}, {"family": "Kudva", "given": "Renuka", "initials": "R", "orcid": "0000-0003-0426-3716", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/a8f164c44cca4540965f66c2829f624e.json"}}], "type": "journal article", "published": "2020-10-00", "journal": {"title": "Protein Sci.", "issn": "1469-896X", "volume": "29", "issue": "10", "pages": "2028-2037", "issn-l": "0961-8368"}, "abstract": "Cotranslational protein folding studies using Force Profile Analysis, a method where the SecM translational arrest peptide is used to detect folding-induced forces acting on the nascent polypeptide, have so far been limited mainly to small domains of cytosolic proteins that fold in close proximity to the translating ribosome. In this study, we investigate the cotranslational folding of the periplasmic, disulfide bond-containing Escherichia coli protein alkaline phosphatase (PhoA) in a wild-type strain background and a strain background devoid of the periplasmic thiol: disulfide interchange protein DsbA. We find that folding-induced forces can be transmitted via the nascent chain from the periplasm to the polypeptide transferase center in the ribosome, a distance of ~160 \u00c5, and that PhoA appears to fold cotranslationally via at least two disulfide-stabilized folding intermediates. Thus, Force Profile Analysis can be used to study cotranslational folding of proteins in an extra-cytosolic compartment, like the periplasm.", "doi": "10.1002/pro.3927", "pmid": "32790204", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC7513700"}], "notes": [], "created": "2026-08-20T06:35:05.418Z", "modified": "2026-08-20T06:35:05.625Z"}, {"entity": "publication", "iuid": "4a7cb3934b1f44359966f38a422fae00", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/4a7cb3934b1f44359966f38a422fae00.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/4a7cb3934b1f44359966f38a422fae00"}}, "title": "Cotranslational folding of alkaline phosphatase in the periplasm of Escherichia coli", "authors": [{"family": "Elfageih", "given": "Rageia", "initials": "R"}, {"family": "Karyolaimos", "given": "Alexandros", "initials": "A", "orcid": "0000-0003-2264-3958", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/4d43d202f8684c09a3e34ca0d26cabc4.json"}}, {"family": "Kemp", "given": "Grant", "initials": "G", "orcid": "0000-0001-5125-2740", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d715b8af2972418aa144b2ca11487ce4.json"}}, {"family": "de Gier", "given": "Jan Willem", "initials": "JW", "orcid": "0000-0001-5537-4358", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/5868d65a24344c5da61ca3cacd29a558.json"}}, {"family": "von Heijne", "given": "Gunnar", "initials": "G", "orcid": "0000-0002-4490-8569", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/529a460e668a479ca7d9b9271375ef9f.json"}}, {"family": "Kudva", "given": "Renuka", "initials": "R", "orcid": "0000-0003-0426-3716", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/a8f164c44cca4540965f66c2829f624e.json"}}], "type": "posted-content", "published": "2020-07-06", "journal": {"issn-l": null}, "abstract": null, "doi": "10.1101/2020.07.06.189464", "pmid": null, "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T09:58:02.348Z", "modified": "2026-08-20T09:58:02.461Z"}, {"entity": "publication", "iuid": "811141c16e52452d9cf2acf9eab6ddba", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/811141c16e52452d9cf2acf9eab6ddba.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/811141c16e52452d9cf2acf9eab6ddba"}}, "title": "The ribosome modulates folding inside the ribosomal exit tunnel", "authors": [{"family": "Wruck", "given": "Florian", "initials": "F"}, {"family": "Tian", "given": "Pengfei", "initials": "P", "orcid": "0000-0003-0255-8692", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/2c8345e3930e4a52b396837a1c099e3f.json"}}, {"family": "Kudva", "given": "Renuka", "initials": "R", "orcid": "0000-0003-0426-3716", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/a8f164c44cca4540965f66c2829f624e.json"}}, {"family": "Best", "given": "Robert B", "initials": "RB", "orcid": "0000-0002-7893-3543", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/36c5cc15e14e412fb8798666bd48f00f.json"}}, {"family": "von Heijne", "given": "Gunnar", "initials": "G", "orcid": "0000-0002-4490-8569", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/529a460e668a479ca7d9b9271375ef9f.json"}}, {"family": "Tans", "given": "Sander J", "initials": "SJ", "orcid": "0000-0002-7131-2568", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/89eebe8050034729afe2d4063e767582.json"}}, {"family": "Katranidis", "given": "Alexandros", "initials": "A", "orcid": "0000-0002-1785-1659", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/4b148b128428419ba9b2e759ca159691.json"}}], "type": "posted-content", "published": "2020-07-01", "journal": {"issn-l": null}, "abstract": null, "doi": "10.1101/2020.06.30.180224", "pmid": null, "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T09:57:41.544Z", "modified": "2026-08-20T09:57:41.643Z"}, {"entity": "publication", "iuid": "199ee9afcd994a54ada42a2d15d7e615", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/199ee9afcd994a54ada42a2d15d7e615.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/199ee9afcd994a54ada42a2d15d7e615"}}, "title": "Membrane integration and topology of RIFIN and STEVOR proteins of the Plasmodium falciparum parasite.", "authors": [{"family": "Andersson", "given": "Annika", "initials": "A"}, {"family": "Kudva", "given": "Renuka", "initials": "R", "orcid": "0000-0003-0426-3716", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/a8f164c44cca4540965f66c2829f624e.json"}}, {"family": "Magoulopoulou", "given": "Anastasia", "initials": "A"}, {"family": "Lejarre", "given": "Quentin", "initials": "Q"}, {"family": "Lara", "given": "Patricia", "initials": "P"}, {"family": "Xu", "given": "Peibo", "initials": "P"}, {"family": "Goel", "given": "Suchi", "initials": "S"}, {"family": "Pissi", "given": "Jennifer", "initials": "J"}, {"family": "Ru", "given": "Xing", "initials": "X"}, {"family": "Hessa", "given": "Tara", "initials": "T"}, {"family": "Wahlgren", "given": "Mats", "initials": "M"}, {"family": "von Heijne", "given": "Gunnar", "initials": "G"}, {"family": "Nilsson", "given": "IngMarie", "initials": "I", "orcid": "0000-0002-7981-3201", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/9df508868ae34871b53cec2d912dd44a.json"}}, {"family": "Tellgren-Roth", "given": "\u00c5sa", "initials": "\u00c5"}], "type": "journal article", "published": "2020-07-00", "journal": {"title": "FEBS J.", "issn": "1742-4658", "volume": "287", "issue": "13", "pages": "2744-2762", "issn-l": "1742-464X"}, "abstract": "The malarial parasite Plasmodium exports its own proteins to the cell surfaces of red blood cells (RBCs) during infection. Examples of exported proteins include members of the repetitive interspersed family (RIFIN) and subtelomeric variable open reading frame (STEVOR) family of proteins from Plasmodium falciparum. The presence of these parasite-derived proteins on surfaces of infected RBCs triggers the adhesion of infected cells to uninfected cells (rosetting) and to the vascular endothelium potentially obstructing blood flow. While there is a fair amount of information on the localization of these proteins on the cell surfaces of RBCs, less is known about how they can be exported to the membrane and the topologies they can adopt during the process. The first step of export is plausibly the cotranslational insertion of proteins into the endoplasmic reticulum (ER) of the parasite, and here, we investigate the insertion of three RIFIN and two STEVOR proteins into the ER membrane. We employ a well-established experimental system that uses N-linked glycosylation of sites within the protein as a measure to assess the extent of membrane insertion and the topology it assumes when inserted into the ER membrane. Our results indicate that for all the proteins tested, transmembranes (TMs) 1 and 3 integrate into the membrane, so that the protein assumes an overall topology of Ncyt-Ccyt. We also show that the segment predicted to be TM2 for each of the proteins likely does not reside in the membrane, but is translocated to the lumen.", "doi": "10.1111/febs.15171", "pmid": "31821735", "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T11:17:56.377Z", "modified": "2026-08-20T11:17:56.443Z"}, {"entity": "publication", "iuid": "29364defa7344e85803c5a50536254b9", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/29364defa7344e85803c5a50536254b9.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/29364defa7344e85803c5a50536254b9"}}, "title": "Membrane integration and topology of RIFIN and STEVOR proteins of the Plasmodium falciparum parasite", "authors": [{"family": "Andersson", "given": "Annika", "initials": "A"}, {"family": "Kudva", "given": "Renuka", "initials": "R", "orcid": "0000-0003-0426-3716", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/a8f164c44cca4540965f66c2829f624e.json"}}, {"family": "Magoulopoulou", "given": "Anastasia", "initials": "A"}, {"family": "Lejarre", "given": "Quentin", "initials": "Q"}, {"family": "Lara", "given": "Patricia", "initials": "P"}, {"family": "Xu", "given": "Peibo", "initials": "P"}, {"family": "Goel", "given": "Suchi", "initials": "S"}, {"family": "Pissi", "given": "Jennifer", "initials": "J"}, {"family": "Ru", "given": "Xing", "initials": "X"}, {"family": "Hessa", "given": "Tara", "initials": "T"}, {"family": "Wahlgren", "given": "Mats", "initials": "M"}, {"family": "von Heijne", "given": "Gunnar", "initials": "G", "orcid": "0000-0002-4490-8569", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/529a460e668a479ca7d9b9271375ef9f.json"}}, {"family": "Nilsson", "given": "IngMarie", "initials": "I", "orcid": "0000-0002-7981-3201", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/9df508868ae34871b53cec2d912dd44a.json"}}, {"family": "Tellgren-Roth", "given": "\u00c5sa", "initials": "\u00c5"}], "type": "posted-content", "published": "2019-05-29", "journal": {"issn-l": null}, "abstract": null, "doi": "10.1101/653998", "pmid": null, "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T11:13:53.210Z", "modified": "2026-08-20T11:13:53.278Z"}, {"entity": "publication", "iuid": "3d2666aeab594f11941415b21465d48d", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/3d2666aeab594f11941415b21465d48d.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/3d2666aeab594f11941415b21465d48d"}}, "title": "The shape of the bacterial ribosome exit tunnel affects cotranslational protein folding.", "authors": [{"family": "Kudva", "given": "Renuka", "initials": "R", "orcid": "0000-0003-0426-3716", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/a8f164c44cca4540965f66c2829f624e.json"}}, {"family": "Tian", "given": "Pengfei", "initials": "P"}, {"family": "Pardo-Avila", "given": "F\u00e1tima", "initials": "F"}, {"family": "Carroni", "given": "Marta", "initials": "M", "orcid": "0000-0002-7697-6427", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/55fa4ba347a34d7ca80d214e8d718e44.json"}}, {"family": "Best", "given": "Robert B", "initials": "RB", "orcid": "0000-0002-7893-3543", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/36c5cc15e14e412fb8798666bd48f00f.json"}}, {"family": "Bernstein", "given": "Harris D", "initials": "HD", "orcid": "0000-0002-4941-3741", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/fb6371b33ef4475083cedc5d0a0fe8c4.json"}}, {"family": "von Heijne", "given": "Gunnar", "initials": "G", "orcid": "0000-0002-4490-8569", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/529a460e668a479ca7d9b9271375ef9f.json"}}], "type": "journal article", "published": "2018-11-26", "journal": {"title": "Elife", "issn": "2050-084X", "volume": "7", "issn-l": "2050-084X"}, "abstract": "The E. coli ribosome exit tunnel can accommodate small folded proteins, while larger ones fold outside. It remains unclear, however, to what extent the geometry of the tunnel influences protein folding. Here, using E. coli ribosomes with deletions in loops in proteins uL23 and uL24 that protrude into the tunnel, we investigate how tunnel geometry determines where proteins of different sizes fold. We find that a 29-residue zinc-finger domain normally folding close to the uL23 loop folds deeper in the tunnel in uL23 \u0394loop ribosomes, while two ~ 100 residue proteins normally folding close to the uL24 loop near the tunnel exit port fold at deeper locations in uL24 \u0394loop ribosomes, in good agreement with results obtained by coarse-grained molecular dynamics simulations. This supports the idea that cotranslational folding commences once a protein domain reaches a location in the exit tunnel where there is sufficient space to house the folded structure.", "doi": "10.7554/eLife.36326", "pmid": "30475203", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC6298777"}, {"db": "pii", "key": "36326"}], "notes": [], "created": "2026-08-20T13:52:24.997Z", "modified": "2026-08-20T13:52:25.126Z"}, {"entity": "publication", "iuid": "cfb2a1f4aaf94da59ddda22ae2c8f22e", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/cfb2a1f4aaf94da59ddda22ae2c8f22e.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/cfb2a1f4aaf94da59ddda22ae2c8f22e"}}, "title": "Author response: The shape of the bacterial ribosome exit tunnel affects cotranslational protein folding", "authors": [{"family": "Kudva", "given": "Renuka", "initials": "R", "orcid": "0000-0003-0426-3716", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/a8f164c44cca4540965f66c2829f624e.json"}}, {"family": "Tian", "given": "Pengfei", "initials": "P"}, {"family": "Pardo-Avila", "given": "F\u00e1tima", "initials": "F"}, {"family": "Carroni", "given": "Marta", "initials": "M", "orcid": "0000-0002-7697-6427", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/55fa4ba347a34d7ca80d214e8d718e44.json"}}, {"family": "Best", "given": "Robert B", "initials": "RB", "orcid": "0000-0002-7893-3543", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/36c5cc15e14e412fb8798666bd48f00f.json"}}, {"family": "Bernstein", "given": "Harris D", "initials": "HD", "orcid": "0000-0002-4941-3741", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/fb6371b33ef4475083cedc5d0a0fe8c4.json"}}, {"family": "von Heijne", "given": "Gunnar", "initials": "G", "orcid": "0000-0002-4490-8569", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/529a460e668a479ca7d9b9271375ef9f.json"}}], "type": "peer-review", "published": "2018-06-13", "journal": {"issn-l": null}, "abstract": null, "doi": "10.7554/elife.36326.028", "pmid": null, "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T13:52:27.102Z", "modified": "2026-08-20T13:52:27.148Z"}]}