{"id":25,"date":"2024-06-12T16:27:29","date_gmt":"2024-06-12T16:27:29","guid":{"rendered":"https:\/\/lab.dev.vanderbilt.edu\/karbstein-lab\/?page_id=25"},"modified":"2024-06-12T20:17:08","modified_gmt":"2024-06-12T20:17:08","slug":"publications","status":"publish","type":"page","link":"https:\/\/lab.dev.vanderbilt.edu\/karbstein-lab\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"

Click here to view publications listed on PubMed.<\/a><\/strong><\/p>\n

Yang, Y.-M. & Karbstein, K. <\/strong>(2024) Ribosome Assembly and Repair. Annu. Rev. Cell Dev. Biol. 2024. 40:5.1\u20135.24<\/em><\/p>\n

Parker, M.P., Brunk, E.S., Getzler, A. & Karbstein, K.<\/strong> (2024) The kinase Rio1 and a ribosome collision-dependent decay pathway survey the integrity of 18S rRNA cleavage. PloS Biology e3001767<\/em> [Preview<\/strong> by Gordon&Stanley (2024) PloS Biology<\/em>].<\/p>\n

Blomqvist, K.E., Huang, H. & Karbstein, K. <\/strong>(2023) A disease associated mutant reveals how Ltv1 orchestrates RP assembly and rRNA folding of the small ribosomal subunit head. PLoS Genetics<\/em> 19(11):e1010862.<\/p>\n

Parker, M.P. & Karbstein, K.<\/strong> (2023) Quality control ensures the fidelity of ribosome assembly and human health. J Cell Biol<\/em>. 222(4):e202209115<\/p>\n

Yang, Y-M., Jung, Y., Abegg, D., Adebekian, A., Carroll, K.S. & Karbstein, K. <\/strong>(2023) Chaperone-directed ribosome repair after oxidative stress.Molecular Cell <\/em>83(9):1527-1537 [Preview<\/strong> by Spiri&Brar (2023) Mol Cell<\/em> 83(9):1374-1376]<\/p>\n

Karbstein, K. <\/strong>(2022) The cost of ribosome heterogeneity. Molecular Cell<\/em> 82(12):2179-2184.<\/p>\n

Yang, Y-M. & Karbstein, K. <\/strong>(2022) The chaperone Tsr2 regulates Rps26 release and reincorporation from mature ribosomes to enable a reversible, ribosome-mediated response to stress. Science Advances <\/em>8(8):eable4386.<\/p>\n

Huang, H., Parker, M.D. & Karbstein, K. <\/strong>(2022) The rRNA modifying enzyme Tsr3 coordinates the activity of the Rio1 and Rio2 kinases during 40S ribosome assembly. RNA <\/em>doi: 10.1261\/rna.078994.121<\/p>\n

Karbstein, K. (2022) Attacking a DEAD Problem: The Role of DEAD-box ATPases in Ribosome Assembly and beyond. Methods in Enzymology <\/em><\/p>\n

Liu, X., Huang, H. & Karbstein, K. <\/strong>(2022) Using DMS-MaPseq to Uncover the Roles of DEAD-box Proteins in Ribosome Assembly. Methods <\/em>204: 249-257.<\/p>\n

Huang, H. & Karbstein, K. <\/strong>(2021) Assembly factors chaperone rRNA folding by isolating helical junctions that are prone to misfolding. Proceedings of the National Academy of Sciences<\/em> 118(25):e2101164118.<\/p>\n

Rai, J.*, Parker, M.P.*, Huang, H., Choy, S.,<\/u> Ghalei, H., Johnson, M.C., Karbstein, K.<\/strong> & Stroupe, M.E. (2021) An open interface in the pre-80S ribosome coordinated by ribosome assembly factors Tsr1 and Dim1 enables temporal regulation of Fap7. RNA <\/em>27(2): 221-233.<\/p>\n

Huang, H., Ghalei, H & Karbstein, K. <\/strong>(2020) Quality control during head assembly ensures scanning competence J Cell Biol.<\/em> 219(11):e202004161.<\/p>\n

Parker, M.P., Collins, J.C., Korona, B., Ghalei, H. & Karbstein, K.<\/strong> (2019) A kinase-dependent checkpoint prevents escape of immature ribosomes into the translating pool. PloS Biology <\/em>17(12):e3000329<\/p>\n

Yin, Z., Liu, X., Jin, M, Ariosa, A., Huang, H., Karbstein<\/strong>, K<\/strong>. & Klionsky, D. (2019) Psp2, a novel regulator of autophagy that promotes autophagy-related protein translation. Cell Research<\/em> 29:994-1008.<\/p>\n

Karbstein, K. <\/strong>(2019) Mitochondria Teach Ribosome Assembly. Science<\/em> 365 (6458), 1077-1078.<\/p>\n

Khoshnevis, S., Dattolo, M.D<\/u>.<\/u> & Karbstein, K.<\/strong> (2019) Rrp5 Establishes a Checkpoint for 60S Assembly During 40S Maturation to Ensure Balanced Levels of Ribosomal Subunits for Translational Control. RNA<\/em> 25(9)1164-1176. PMID: 31217256.<\/p>\n

Ferretti, M.B. & Karbstein, K. (2019) Does Functional Specialization of Ribosomes Really Exist? RNA<\/em> 25, 521-538. PMID:30733326<\/p>\n

Karbstein, K.<\/strong> (2018) Responsible Peer Review. ACS Chemical Biology<\/em> 13(12)3217-18. PMID: 30993984<\/p>\n

Collins, J.C.*, Ghalei, H.*, Doherty, J.R., Culver, R.N.<\/u> & Karbstein, K.<\/strong> (2018) Quality Control During Small Ribosomal Subunit Maturation: Ltv1 Chaperones Assembly of the Head. J Cell Biol.<\/em> 217(12): 4141-4154. PMID: 30348748<\/p>\n

Ferretti, M.B., Barre, J.L. <\/u>& Karbstein, K.<\/strong> (2018) Translational Reprogramming Provides a Blueprint for Cellular Adaptation. Cell Chem. Biol.<\/em>25(11)1372-79. PMID: 3017431<\/p>\n

Ghalei, H., Trepreau, J., Collins, J.C., Bhaskaran, H., Strunk, B.S. and Karbstein, K.<\/strong> (2017) The ATPase Fap7 Tests the Ability to Carry Out Translocation-Like Conformational Changes and Releases Dim1 During 40S Ribosome Maturation. Mol. Cell<\/em> 67(6):990-1000. PMID: 2889033<\/p>\n

Ferretti, M.B., Ghalei, H., Ward, E.A., Potts, E.L.<\/u>, & Karbstein, K.<\/strong> (2017) Rps26 directs mRNA-specific translation by recognition of Kozak sequence elements. Nature Structure and Molecular Biology <\/em>24(9):700-709. PMID: 28759050<\/p>\n

Johnson, M.C.*, Ghalei, H.*, Doxtader, K.<\/u>, Karbstein, K.<\/strong> & Stroupe, M.E. Structural heterogeneity of pre-40S ribosomes. (2017) Structure 25(2):329-340. PMID: 28111018 [Preview<\/strong> by Hartwick&Wimberly (2017) Structure<\/em> 25(2):261-219]<\/p>\n

Khoshnevis, S., Askenazy, I., Johnson, M.C., Dattolo, M.D.<\/u>, Young-Erdos, C.L., Stroupe, M.E. & Karbstein, K.<\/strong> (2016) The DEAD-box protein Rok1 Orchestrates 40S and 60S Ribosome Assembly by Promoting the Release of Rrp5 from Pre-40S Ribosomes to Allow for 60S Maturation. PLoS Biol<\/em>.<\/em> 2016 Jun 9;14(6):e1002480. PMID: 27280440<\/p>\n

Karbstein, K. <\/strong>*, What Will the Future Hold? RNP quality Control and Degradation. (2015) RNA<\/em> 21(4):657-658. PMID: 25780179<\/p>\n

De la Cruz, J.*, Karbstein, K.<\/strong> * and Woolford, J.L.*, Functions of Ribosomal Proteins in Assembly of Eukaryotic Ribosomes In Vivo. (2015) Annual Reviews Biochemistry<\/em> 84: 93-129 * corresponding authors<\/p>\n

Tyagi R., Shahani N., Gorgen L., Ferretti M., Pryor W., Chen P.Y., Swarnkar S., Worley P.F., Karbstein, K.<\/strong>, Snyder, S.H., Subramaniam, S. Rheb Inhibits Protein Synthesis by Activating the PERK-elF2\u03b1 Signaling Cascade. (2015) Cell Rep<\/em>orts<\/em> 10(5) 684-693.\u00a0 PMID: 25660019<\/p>\n

Ghalei, H., Schaub, F.X., Doherty, J.R., Noguchi, Y., Roush, W.R., Cleveland, J.L., Stroupe, M.E. & Karbstein, K. \u00a0<\/sup><\/strong>(2015). Hrr25\/CK1d-directed release of Ltv1 from pre-40S ribosomes is necessary for ribosome assembly and cell growth. Journal of Cell Biology<\/em> 208(6):745-59. PMCID: PMC4362465<\/p>\n

Young, C.L., Khoshnevis, S., and Karbstein, K.<\/strong> (2013). Co-factor dependent specificity of a DEAD-box protein. Proceedings of the National Academy of Sciences<\/em> 110, E2668-2676. PMCID: PMC3718167<\/p>\n

Karbstein, K. <\/strong>(2013). Quality Control Mechanisms During Ribosome Maturation. Trends in Cell Biology <\/em>23, 242-250. PMCID: PMC3640646<\/p>\n

Strunk, B.S., Novak, M.N.<\/u>, Young, C.L. and Karbstein, K. <\/strong>(2012). Joining of 60S subunits and a translation-like cycle in 40S ribosome maturation. Cell<\/em> 150(1):111-21. [Preview<\/strong> by Schutz & Panse (2012) Nature Structural and Molecular Biology 19(9):861-2; cited in Faculty of 1000]<\/p>\n

Young, C.L. and Karbstein, K. <\/strong>(2012). Analysis of cofactor effects on RNA helicases. Methods in Enzymology<\/em> 511:213-37.<\/p>\n

Karbstein, K.<\/strong> (2011). Inside the 40S Assembly Machinery. Current Opinions in Chemical Biology<\/em> 5(5):657-63.<\/p>\n

Horn, D.H., Mason, S.E.<\/u> & Karbstein, K.<\/strong> (2011). Rcl1 protein, a novel nuclease for 18S ribosomal RNA production. <\/em>Journal of Biological Chemistry<\/em>286(39):34082-7.<\/p>\n

Strunk, B.S., Loucks, C.E., Su, M., Vashtish, H., Cheng, S., Schilling, J., Brooks, C.L. III, Karbstein, K.<\/strong># and Skiniotis, G.# (2011) Ribosome Assembly Factors Prevent Premature Translation Initiation by 40S Assembly Intermediates. Science<\/em> 333(6048), 1449-53. # corresponding authors<\/p>\n

Young, C.L. and Karbstein, K. <\/strong>(2011). The Roles of S1 RNA-Binding Domains in Rrp5’s Interactions with pre-rRNA.\u00a0 RNA<\/em> 17, 512-21.<\/p>\n

Campbell, M.G.<\/u> and Karbstein, K.<\/strong> (2011). Protein-Protein Interactions in Late Pre-40S Ribosomes.\u00a0 PLoS One<\/em> 6(1):e16194.<\/p>\n

Woolls, H.A., Lamanna, A.C. and Karbstein, K.<\/strong> (2011). Roles of DIM2 In Ribosome Assembly.\u00a0 Journal of Biological Chemistry<\/em> 286, 2578-2586.<\/p>\n

Lamanna, A.C. and Karbstein, K. <\/strong>(2011). An RNA Conformational Switch Regulates Pre-18S rRNA Cleavage. Journal of Molecular Biology <\/em>405, 3-17, featured on the cover [Preview<\/strong> by Warner J.R. (2010) Journal of Molecular Biology 405, 1-2]<\/p>\n

Karbstein, K. <\/strong>(2010). Chaperoning Ribosome Assembly. J. Cell Biol. <\/em>181, 11-12.<\/p>\n

Strunk, B.S. and Karbstein, K. <\/strong>(2009) Powering Through Ribosome Assembly. RNA<\/em> 15, 2083-2104.<\/p>\n

Lamanna, A.C. & Karbstein, K.<\/strong> (2009) Nob1 Uses its PIN domain to Directly Bind the Single Stranded Cleavage Site D at the 3\u2019-end of 18S rRNA. Proceedings of the National Academy of Sciences <\/em>106, 14259-14264<\/p>\n

Karbstein, K.<\/strong> (2009) Eukaryotic Ribosome Assembly. Wiley Encyclopedia of Chemical Biology<\/em> 4, 222-230.<\/p>\n

Todd, G.C. and Karbstein, K.<\/strong> (2007) RNA takes center stage. Biopolymers<\/em> 87, 275-278.<\/p>\n

Coppola BP, Banaszak Holl MM, Karbstein, K.<\/strong> (2007) Closing the gap between interdisciplinary research and disciplinary teaching. ACS Chem. Biol.<\/em> 2, 518-20.<\/p>\n

Karbstein, K. <\/strong>(2007) Role of GTPases in ribosome assembly. Biopolymers<\/em> 87 1-11.<\/p>\n

Karbstein, K.<\/strong>, Lee, J. and Herschlag, D. (2007) Probing the Role of a Secondary Structure Element at the 5′- and 3′-Splice Sites in Group I Intron Self-splicing: The Tetrahymena L-16 ScaI Ribozyme Reveals a New Role of the G\u2022U Pair in Self-splicing. Biochemistry 46, 4861-75.<\/p>\n

Karbstein, K.<\/strong> and Doudna, J. A. (2006) GTP-Dependent Formation of a Ribonucleoprotein Subcomplex Required for Ribosome Biogenesis. Journal of Molecular Biology<\/em> 356, 432-443.<\/p>\n

Karbstein, K.<\/strong>, Jonas, S. and Doudna, J. A. (2005) An essential GTPase promotes assembly of preribosomal RNA processing complexes. Molecular Cell<\/em> 20, 633-643. [Preview by Dutca & Culver Molecular Cell 20, 497-499.]<\/p>\n

Karbstein, K.<\/strong>, Tang, K. H. and Herschlag, D. (2004) A Base Triple in the Tetrahymena Group I Core Affects the Reaction Equilibirum via a Threshold Effect. RNA<\/em> 10, 1730-1739.<\/p>\n

Karbstein, K.<\/strong>, and Doudna, J. A. (2004) RNA: Primed for Packing? Chemistry & Biology<\/em> 11, 149-151.<\/p>\n

Karbstein, K.<\/strong>, and Herschlag, D. (2003) Extraordinarily Slow Binding of Guanosine to the Tetrahymena Group I Ribozyme: Implications for RNA Preorganization and Function. Proceedings of the National Academy of Sciences<\/em> 100, 2300-2305.<\/p>\n

Karbstein, K.<\/strong>, Carroll, K.S., and Herschlag, D. (2002) Probing the Tetrahymena Group I Ribozyme Reaction in Both Directions. Biochemistry<\/em> 41, 11171-11183.<\/p>\n

Wang, S.L.*, Karbstein, K.<\/strong> *, Peracchi, A., Beigelman, L., and Herschlag, D. (1999) Identification of the Hammerhead Ribozyme Metal Ion Binding Site that Rescues the Deleterious Effect of a Cleavage Site Phosphorothioate. Biochemistry<\/em> 38, 14363-14378.\u00a0\u00a0\u00a0 * These authors contributed equally to this work.<\/p>\n

 <\/p>\n

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Click here to view publications listed on PubMed. Yang, Y.-M. & Karbstein, K. (2024) Ribosome Assembly and Repair. Annu. Rev. Cell Dev. Biol. 2024. 40:5.1\u20135.24 Parker, M.P., Brunk, E.S., Getzler, A. & Karbstein, K. (2024) The kinase Rio1 and a ribosome collision-dependent decay pathway survey the integrity of 18S rRNA cleavage. PloS Biology e3001767 [Preview…<\/p>\n","protected":false},"author":11,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"_acf_changed":false,"footnotes":""},"tags":[],"class_list":["post-25","page","type-page","status-publish","hentry"],"acf":[],"jetpack_shortlink":"https:\/\/wp.me\/PfQecJ-p","jetpack_sharing_enabled":true,"_links":{"self":[{"href":"https:\/\/lab.dev.vanderbilt.edu\/karbstein-lab\/wp-json\/wp\/v2\/pages\/25","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/lab.dev.vanderbilt.edu\/karbstein-lab\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/lab.dev.vanderbilt.edu\/karbstein-lab\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/lab.dev.vanderbilt.edu\/karbstein-lab\/wp-json\/wp\/v2\/users\/11"}],"replies":[{"embeddable":true,"href":"https:\/\/lab.dev.vanderbilt.edu\/karbstein-lab\/wp-json\/wp\/v2\/comments?post=25"}],"version-history":[{"count":4,"href":"https:\/\/lab.dev.vanderbilt.edu\/karbstein-lab\/wp-json\/wp\/v2\/pages\/25\/revisions"}],"predecessor-version":[{"id":82,"href":"https:\/\/lab.dev.vanderbilt.edu\/karbstein-lab\/wp-json\/wp\/v2\/pages\/25\/revisions\/82"}],"wp:attachment":[{"href":"https:\/\/lab.dev.vanderbilt.edu\/karbstein-lab\/wp-json\/wp\/v2\/media?parent=25"}],"wp:term":[{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/lab.dev.vanderbilt.edu\/karbstein-lab\/wp-json\/wp\/v2\/tags?post=25"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}