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Puig-Segui, M.S., Decker, C., Barlit, H., Labunskyy, V.M., Parker, R., and Puig, S. ÌýRegulation of translation in response to iron deficiency in human cells. Scientific Reports (2024) Apr 11;14(1):8451.Ìýdoi: 10.1038/s41598-024-59003-9.ÌýÌý

Ripin, N., Macedo de Vasconcelos, L., Ugay, D.A. and R. Parker. DDX6 modulates P-body and stress granule assembly composition and docking. Journal of Cell BiologyÌýJun 3;223(6):e202306022. Ìýdoi: 10.1083/jcb.202306022.ÌýEpub 2024 Mar 27.Ìý

Burke, J.M., Ratnayake, O.C., Watkins, J.M., Perera, R., and R. Parker. (2024) G3BP1-dependent condensation of translationally inactive viral RNAs antagonizes infection. Science Advances Feb 2;10(5):eadk8152. doi: 10.1126/sciadv.adk8152. Epub 2024 Jan 31.

Book Chapters & Invited Reviews

Parker, D.M., Bublitz, G.R., and Parker, R. (2024) Shining light on DHX9: UV-induced stress granules illuminate protective mechanisms for daughter cell resilience. Molecular Cell Apr 18;84(8):1403-1405.Ìýdoi: 10.1016/j.molcel.2024.03.027.

Shehata, S.I., Watkins, J.M, Burke, J.M., and R. Parker. (2024) Mechanisms and consequences of mRNA destabilization during viral infections. Virology Journal Feb 6;21(1):38. doi: 10.1186/s12985-024-02305-1.

Yang, Q., Meyerson, N.R., Paige, C.L., Morrison, J.H., Clark, S.K., Fattor, W.T., Decker, C.J., Steiner, H.R., Lian, E., Larremore, D.B., Perera, R., Poeschla, E.M., Parker, R., Dowell, R.D., and S. Sawyer. (2023) Human mRNA in Saliva can correctly identify individuals harboring acute infection. mBio

Shehata, S. and R. Parker. (2023) SARS-CoV-2 Nsp1 mediated mRNA degradation requires mRNA interaction with the ribosome. RNA Biology 20(1): 444–456.

Currie, S.L., Xing, W., Muhlrad, D., Decker, C.J., Parker, R., and M. K. Rosen. (2023) Quantitative reconstitution of yeast RNA processing bodies. Proceedings of the National Academy of Sciences https://doi.org/10.1073/pnas.2214064120

Liang, Q., Chan, Y.-C., Toscano, J., Bjorkman, K.K., Leinwand, L.A., R. Parker, Nozik, E.S., Nesbitt, D.J., and J. Ye. (2023) Breath analysis by ultra-sensitive broadband laser spectroscopy detects SARS-CoV-2 infection. Journal of Breath Research Apr 5;17(3). doi: 10.1088/1752-7163/acc6e4

Jeong, H-C., Shukla, S., Fok, W.C., Huynh, T.H., Batista, L.F.Z., and R. Parker. (2023) USB1 is a miRNA deadenylase that regulates hematopoietic development. Science 379, 901-907.

Lester, E., Van Alstyne, M., McCann, K.L., Reddy, S., Cheng L., Kuo, J., Pratt, J., and R. Parker. (2023) Cytosolic condensates rich in polyserine define subcellular sites of tau aggregation. Proceedings of the National Academy of Sciences 120(3) doi.org/10.1073/pnas.2217759120

Book Chapters & Invited Reviews

Ripin, N. and R. Parker. (2023) Formation, Function, and Pathology of RNP Granules. Cell 186(22): 4737-4756.

Huynh, T.N. and R. Parker. (2023) The PARN, TOE1, and USB1 RNA deadenylases and their roles in non-coding RNA regulation. Journal of Biological Chemistry Aug 4;105139. doi:

Lester, E. and R. Parker. (2023) Tau, RNA, and RNA binding proteins: complex interactions in health and neurodegenerative diseases. The Neuroscientist Mar 9;10738584231154551. doi: 10.1177/10738584231154551

Huynh, T.N., Shukla, S., Reigan, P., and R. Parker. (2022) Identification of PARN nuclease activity inhibitors by computational-based docking and high-throughput screening. Scientific Reports Mar 31. doi:Ìý

Corbet, G.A., Burke, J.M., Bublitz, G.R., Tay, J.W. and R. Parker. (2022) dsRNA-induced condensation of antiviral proteins promotes PKR activation. PNAS Aug 8; 119(33)

Wheeler, J.R., Whitney, O.N., Vogler, T.O., Nguyen, E.D., Pawlikowski, B., Lester, E., Cutler, A., Elston, T., Betta, N.D., Parker, K.R., Yost, K.E., Vogel, H., Rando, T.A., Chang, H.Y., Johnson, A.M., Parker, R., and B.B. Olwin. (2022) RNA-binding proteins direct myogenic cell fate decisions. eLife Jun 13;11:e75844. doi: 10.7554/eLife.75844Ìý

Burke, J.M., Ripin, N., Ferretti, M.B., St. Clair, L.A., Worden-Sapper, E.R., Sawyer, S.L., Perera, R., Lynch, K.W. and R. Parker. (2022) RNase L-mediated RNA decay alters 3' end formation and splicing of host mRNAs. bioRxiv doi:

Iadevaia, V., Burke, J.M., Eke, L., Moller-Levet, C., Parker, R. and N. Locker. (2022) Novel stress granules-like structures are induced via a paracrine mechanism during viral infection. Journal of Cell Science Feb 15;135(4):jcs259194. doi: 10.1242/jcs.259194

Bubar, K.M., Middleton, C.E., Bjorkman, K.K., R. Parker and D.B. Larremore. (2022) SARS-CoV-2 transmission and impacts of unvaccinated-only testing in populations of mixed vaccination status. Nature Communications May 19;13(1):2777. doi: 10.1038/s41467-022-30144-7

Khong, A., Matheny, T., Huynh, T.N., Babl, V. and Roy Parker. (2022) Limited effects of m⁶A modification on mRNA partitioning into stress granules. Nature CommunicationsÌý Jun 29;13(1):3735.

Decker, C.J., Burke, J.M., Mulvaney, P.K. and R. Parker. (2022) RNA is required for the maintenance of multiple cytoplasmic and nuclear membrane-less organelles. EMBO Journal May 2;41(9):e110137. doi: 10.15252/embj.2021110137

Book Chapters & Invited Reviews

Batista, L.F.Z., Dokal, I., and R. Parker. (2022) Telomere biology disorders: time for moving towards the clinic? Trends in Molecular Medicine October;28(10):882-891.

Ripin, N. and R. Parker. (2022) Are stress granules the RNA analogs of misfolded protein aggregates? RNA 28(1)67-75. doi:

Corbet, G.A., Burke, J.M. and R. Parker. (2022) Nucleic acid-protein condensates in innate immune signaling. EMBO Journal 42:e111870

Reeves, K., Liebig, J., Feula, A., Saldi, T., Lasda, E., Johnson, W., Lilienfeld, J., Maggi, J., Pulley, K., Wilkerson, P.J., Real, B., Zak, G., Davis, J., Fink, M., Gonzales, P, Hager, C., Ozeroff, C., Tat, K., Alkire, M., Butler, C., Coe, E., Darby, J., Freeman, N., Heuer, H., Jones, J.R., Karr, M., Key, S., Maxwell, K., Nelson, L., Saldana, E., Shea, R., Salveson, L., Tomlinson, K., Vargas-Barriga, J., Vigil, B., Brisson, G., Parker, R., Leinwand, L.A., Bjorkman, K., and C. Mansfeldt. (2021) High-resolution within-sewer SARS-CoV-2 surveillance facilitates informed intervention. Water Research 204: 117613.

Corbet, G.A., Burke, J.M. and R. Parker (2021) ADAR1 limits stress granule formation through both translation-dependent and translation-independent mechanisms. Journal of Cell Science134, jcs258783. doi:10.1242/jcs.258783

Corbet, G.A., Wheeler, J.R., Parker, R. and K. Weskamp. (2021) TDP43 ribonucleoprotein granules: physiologic function to pathologic aggregates. RNA Biology Oct 15;18(sup1):128-138. doi:

Yang, Q., Saldi, T.K., Gonzales, P.K., Lasda, E., Decker, C.J., Tat, K.L., Fink, M.R., Hager, C.R., Davis, J.C., Ozeroff, C.D., Muhlrad, D., Clark, S.K., Fattor, W.T., Meyerson, N.R., Paige, C.L., Gilchrist, A.R., Barbachano-Guerrero, A., Worden-Sapper, E.R., Wu, S.S., Brisson, G.R., McQueen, M.B., Dowell, R.D., Leinwand, L., Parker, R., and S.L. Sawyer. (2021) Just 2% of SARS-CoV-2−positive individuals carry 90% of the virus circulating in communities. ÌýPNAS MAY 25, Ìýcommunities. PNASÌýMay 25, 118(21) E2104547118;

Bjorkman, K., Saldi, T., Lasda, E., Bauer, L.C., Kovarik, J., Gonzales, P.K., Fink, M.R., Tat, K.L., Hager, C.R., Davis, J.C., Ozeroff, C.D., Brisson, G.R., Larremore, D.B., Leinwand, L.A., McQueen, M.B. and R. Parker. (2021) Higher viral load drives infrequent SARS-CoV-2 transmission between asymptomatic residence hall roommates. Journal of Infectious Diseases Jul 24;jiab386. doi: 10.1093/infdis/jiab386. Online ahead of print.

Burke, J.M., St Clair, L.A., Perera, R and R. Parker. (2021) SARS-CoV-2 infection triggers widespread host mRNA decay leading to an mRNA export block. RNA Jul 27;rna.078923.121. doi: 10.1261/rna.078923.121. Online ahead of print.Larremore, D., Toomre, D. and R. Parker. (2021) Modeling the effectiveness of olfactory testing to limit SARS-CoV-2 transmission. Nature Communications 12:3664. doi: 10.1038/s41467-021-23315

Burke, J.M., Gilchrist, A.R., Sawyer, S.L. and R. Parker. (2021) RNase L limits host and viral protein synthesis via inhibition of mRNA export. Science Advances 7(23) eabh2479. doi: 10.1126/sciadv.abh2479

Lester, E., Ooi, F.K., Bakkar, N., Ayers, J., Woerman, A.L., Wheeler, J., Bowser, R., Carlson, G.A., Prusiner, S.B. and R. Parker. (2021) Tau aggregates are RNA-protein assemblies that mislocalize multiple nuclear speckle components. Neuron109(10):1675-1691.

Yang, Q., Meyerson, N.R., Clark, S.K., Paige, C.L., Fattor, W.T., Gilchrist, A.R., Barbachanco-Guerrero, A., Healy, B.G., Worden-Sapper, E.R., Wu, S.S., Muhlrad, D., Decker, C.J,, Saldi, T,K., Lasda, E., Gonzales, P.K., Fink, M.R., Tat, K.L, Hager, C.R., Davis, J.C., Ozeroff, C.D., Brisson, G.R., McQueen, M.B., Leinwand, L., Parker, R., and S. Sawyer. (2021) Saliva TwoStep for rapid detection of asymptomatic SARS-C0V-2 carriers. eLife 2021;10:e65113 doi:

Matheny, T., Van Treeck, B., Huynh, T.N. and R. Parker. (2021) RNA partitioning into stress granules is based on the summation of multiple interactions. RNA 27(2):174-189.

Book Chapters & Invited Reviews

Weskamp, K., Olwin, B. and R. Parker. (2021) Post-transcriptional regulation in skeletal muscle development, repair, and disease. Trends in Molecular Medicine, May, 27(5):469. https://www.cell.com/trends/molecular-medicine/pdf/S1471-4914(20)30315-4.pdf

Pratt, J., Lester, E. and R. Parker. (2021) Could SARS-CoV-2 cause tauopathy? The Lancet, July, 20(7):506.

Larremore, D.B., Wilder, B., Lester, E., Shehata, S., Burke, J.M., Hay, J.A., Tambe, M., Mina, M.J. and R. Parker. (2020) Test sensitivity is secondary to frequency and turnaround time for COVID-19 surveillance. Science Advances Jan; 7(1): eabd5393. Ìý

Hoon-Hanks, L.L., Stöhr, A.C., Anderson, A.J., Evans, D.E., Nevarez, J.G., Rodgers, C.P., Cross, S.T., Steiner, H.R., Parker, R. and M.D. Stenglein. (2020) Serpentovirus (nidovirus) and orthoreovirus coinfection associatedÌýwith respiratory disease in captive veiled chameleons (Chamaeleo calyptratus). Viruses 12(11):1329.

Xing, W., Muhlrad, D., Parker, R. and M.K. Rosen. (2020) A quantitative inventory of yeast P body proteins reveals principles of compositional and specificity. eLife 9:e56525.

Shukla, S., Jeong, H.-C., Parker, R. and L.F.Z. Batista. (2020) Chemical inhibition of PAPD5/7 rescues telomerase function and hematopoiesis in dyskeratosis congenita. Blood 4(12):2717-2722.

Moon, S.L., Morisaki, T., Stasevich, T.J., and R. Parker. (2020) Coupling of translation quality control and mRNA targeting to stress granules. Journal of Cell Biology 219(8): e202004120.

Burke, J.M., Lester, E.T., Tauber, D. and R. Parker. (2020) RNase L promotes the formation of unique ribonucleoprotein granules distinct from stress granules. Journal of Biological Chemistry 295(6):1526-1438.

Tauber, D., Tauber, G., Khong, A., Van Treeck, B., Pelletier, J. and R. Parker. (2020) Modulation of RNA condensation by the DEAD-box protein eIF4A. Cell 180:411-426.e16.

Brocard, M., Iadevaia, V., Klein, P., Hall, B., Lewis, G., Lu, J., Burke, J., Wilcocks, M.M., Parker, R., Goodfellow, I.G., Ruggieri, A. and N. Locker. (2020) Norovirus infection results in eIF2a independent host translation shut-off and remodels the G3BP1 interactome evading stress granule formation. PLOS PathogensÌý 16(1):e1008250.

Cirillo, L., Cieren, A., Barbieri, S., Khong, A., Schwager, F., Parker, R. and M Gotta (2019) UBAP2L forms distinct cores that act in nucleating stress granules upstream of G3BP1. Current Biology 30(4):698-707.e6.

Lee, J.E., Cathey, P.I. Wu, H., Parker, R. and G. Voeltz. (2020) Endoplasmic reticulum contact sites regulate the dynamics of membraneless organelles. Science 367(6477): pii: eaay7108.

Book Chapters & Invited Reviews

Mina, M.J., Parker, R. and D. Larremore. (2020) Rethinking Covid-19 Test Sensitivity — A Strategy for Containment. New England Journal of Medicine Nov 26;383(22):e120.

Tauber, D., Tauber, G. and R. Parker. (2020) Mechanisms and Regulation of RNA Condensation Trends in Biochemical Sciences May;45(9):764-778.Khong, A. and R. Parker. (2020) The Landscape of Eukaryotic mRNPs. RNA Mar;26(3):229-239.

Moon, S.L., Morisaki, T., Khong, A., Lyon, K., Parker. R., and T.J. Stasevich. (2019) Multicolor single-molecule tracking of mRNA interactions with RNP granules. Nature Cell Biology February; 21(2):162–168.

Shukla, S., Bjerke, G.A., Muhlrad, D., Yi, R., and R. Parker. (2019) The RNase PARN controls the levels of specific miRNAs that contribute to p53 regulation. Molecular Cell Mar 21;73(6):1204-1216.

Fok, W.C., Shukla, S., Vessoni, A.T., Brenner, K.A., Parker, R., Sturgeon, C.M., Batista, L.F.Z. (2019) Posttranscriptional modulation of TERC by PAPD5 inhibition rescues hematopoietic development in dyskeratosis congenta. Blood Mar 21;133(12):1308-1312.

Tauber D. and R. Parker. (2019) 15-¶Ù±ð´Ç³æ²â-Δ^12,14-prostaglandin J2 promotes phosphorylation of eukaryotic initiation factor 2α and activates the integrated stress response. Journal of Biological Chemistry Apr 19;294(16):6344-6352.

Baron, D.M., Matheny, T., Lin, Y.-C., Leszyk, J.D., Kenna, K., Gall, K.V., Santos, D.P., Tischbein, M., Funes, S., Hayward, L.J., Kiskinis, E., Landers, J.D., Parker. R., Shaffer, S.A., and D.A. Bosco. (2019) Quantitative proteomics identifies proteins that resist transational repression and become dysregulated in ALS-FUS. Human Molecular Genetics Feb 26. Pii: ddz048.

Burke, J.M., Moon, S.L., Matheny, T. and R. Parker (2019) RNase L reprograms translation by widespread mRNA turnover escaped by antiviral mRNAs. Molecular Cell 75:1203-1217.

Decker, C.J., Steiner, H.R., Hoon-Hanks, L.L., Morrison, J.H., Haist, K.C., Stabell, A.C., Poeschla, E.M., Morrison, T.E., Stenglein, M.D., Sawyer, S.L. and R.Parker. (2019) dsRNA-Seq: Identification of viral infection by purifying and sequencing dsRNA. Viruses 11(10): pii: E943.

Matheny, T., Rao, B. and R. Parker (2019) Transcriptome-wide comparison of stress granules and P-bodies reveals that translation plays a major role in RNA partitioning. Molecular and Cellular Biology 39(24): e00313-19.

Book Chapters & Invited Reviews
Corbet G.A. and R. Parker. (2019) ÌýRNP Granule Formation:Ìý Lessons from P-Bodies and Stress Granules ÌýCold Spring Harb Symp Quant Biol.Ìý2019;84:203-215.Ìýdoi: 10.1101/sqb.2019.84.040329.ÌýEpub 2020 Jun 1.

Van Treeck, B., and R. Parker. (2019) Principles of stress granules revealed by imaging approaches. Cold Spring Harbor Perspectives in Biology Feb 1;11(2). pii: a033068.

Cutler, A., Ewachiw, T., Corbet, G., Parker, R., and B. Olwin. (2019) Myo-granules connect physiology and pathophysiology. Journal of Experimental Neuroscience Apr 12;13:1179069519842157.

Tutucci, E., Vera, M., Biswas, J., Garcia, J., Parker, R., and R.H. Singer. (2018) An improved MS2 system for accurate reporting of the mRNA life cycle. Nature Methods 15(1):81-89.

Protter, D.S.W., Rao, B.S., Van Treeck, B., Lin, Y., Mizoue, L., Rosen, M.K.,and R. Parker. (2018) Intrinsically disordered regions can contribute promiscuous interactions to RNP granule assembly. Cell Reports 22(6):1401-1412.

Khong, A., Jain, S., Matheny, T., Wheeler, J.R., and R. Parker. (2018) Isolation of mammalian stress granule cores for RNA-Seq analysis. Methods 137:49-54.

Van Treeck, B., Protter, D.S.W., Matheny, T., Khong, A., Link, C.D., and R. Parker. (2018) RNA self-assembly contributes to stress granule formation and defining the stress granule transcriptome. Proceedings of the National Academy of Science 115(11):2734-2739.

Bakthavachalu, B., Huelsmeier, J., Sudhakaran, I.P., Hillebrand, J., Singh, A., Petrauskas, A., Thiagarajan, D., Sankaranarayanan, M., Mizoue, L., Anderson, E.N., Pandey, U.B., Ross, E., VijayRaghavan, K., Parker, R., and M. Ramaswami. (2018) RNP-granule assembly via ataxin-2 disordered domains is required for long-term memory and neurodegeneration. Neuron 98(4)754-755.

Moon, S.L., and R. Parker. (2018) EIF2B2 mutations in vanishing white matter disease hypersuppress translation and delay recovery during the integrated stress response. RNA 24(6):841-852.

Braselmann, E., Wierzba, A.J., Polaski, J.T., Chromiński, M., Holmes, Z.E., Hung, S.-T., Batan, D., Wheeler, J.R., Parker, R., Jimenez, R., Gryko, D., Batey, R.T, and A.E. Palmer. (2018) A multicolor riboswitch-based platform for imaging of RNA in live mammalian cells. Nature Chemical Biology 10:964-971.

Moon, S.L., and R. Parker. (2018) Analysis of eIF2B bodies and their relationships with stress granules and P-bodies. Scientific Reports 8(1):12264.

Vogler, T.O., Wheeler, J.R., Nguyen, E.D., Hughes, M.P., Britson, K.A., Lester, E., Rao, B., Betta, N.D., Whitney, O.N., Ewachiw, T.E., Gomes, E., Shorter, J., Lloyd, T.E., Eisenberg, D.S., Taylor, J.P., Johnson, A.M., Olwin, B.B., and R. Parker (2018) TDP-43 and RNA form amyloid-like myo-granules in regenerating muscle. Nature 563:508-513.

Khong, A., and R. Parker. (2018) mRNP architecture in translating and stress conditions reveals an ordered pathway of mRNA compaction. Journal of Cell Biology Oct 15. pii: jcb.201806183.

Book Chapters & Invited Reviews
Moon, S.L., Sonenberg, N., and R. Parker. (2018) Neuronal regulation of eIF2a function in health and neurological disorders. Tends in Molecular Medicine 24(6):575-589.

Van Treeck, B., and R. Parker. (2018) Emerging Roles for Intermolecular RNA-RNA Interactions in RNP Assemblies. Cell 174(4):791-802.

Mittag, T., and R. Parker. (2018) Multiple modes of protein-protein interactions promote RNP granule assembly. Journal of Molecular Biology 430(23):4636-4649.

Lester, E., and R. Parker. (2018) The Tau of Nuclear-Cytoplasmic Transport. Neuron 99(5):869-871.

Van Treeck, B., and R. Parker. (2018) Principles of stress granules revealed by imaging approaches. Cold Spring Harbor Perspectives in Biology Feb 1;11(2). pii: a033068.

Walters, R.W., Matheny, T., Mizoue, L.S., Rao, B.S., Muhlrad, D., and R. Parker. (2017) Identification of NAD+ capped mRNAs in Saccharomyces cerevisiae. Proceedings of the National Academy of Science. 114:480-485.

Wheeler, J.R., Jain, S., Khong A., and R. Parker. (2017) Isolation of yeast and mammalian stress granule cores. Methods 126:12-17.

Harigaya, Y. and R. Parker. (2017) The link between adjacent codon pairs and mRNA stability. BMC Genomics 18:364.

Shukla, S. and R. Parker. (2017) PARN modulates Y RNA stability and its 3'-end formation. Molecular and Cellular Biology 37:1-22.

Rao, B.S. and R. Parker. (2017) Numerous interactions act redundantly to assemble a tunable size of P bodies in Saccharomyes cerevisiae. Proceedings of the National Academy of Science 114(45):E9569-E9578.

Khong, A., Matheny, T., Jain, S., Mitchell, S.F., Wheeler, J.R., and R. Parker. (2017) The stress granule transcriptome reveals principles of mRNA accumulation in stress granules. Molecular Cell 68:808-820.

Lasda, E. and R. Parker. (2016) Circular RNAs co-precipitate with extracellular vesicles: A possible mechanism for circRNA clearance. PLOS ONE 11(2):e0148407.

Jain, S., Wheeler, J.R., Walters, R.W., Agrawal, A., Barsic, A., and R. Parker. (2016) ATPase-modulated stress granules contain a diverse proteome and substructure. Cell 164(3):487-498.

Shukla, S., Schmidt, J.C., Goldfarb, K.C., Cech, T.R., and R. Parker. (2016) Inhibition of telomerase RNA decay rescues telomerase deficiency caused by dyskerin or PARN defects. Nature Structural & Molecular Biology 23:286-292.

Garcia, J.F. and R. Parker. (2016) Ubiquitous accumulation of 3' mRNA decay fragments in Saccharomyces cerevisiae mRNAs with chromosomally integrated MS2 arrays. RNA, 22:657-659.

Banani, S.F., Rice, A.M., Peeples, W., Lin, Y., Jain, S., R. Parker, and M.K. Rosen. (2016) Compositional control of phase-separated cellular bodies. Cell, 166:651-663.

Eshleman, N., Liu, G., McGrath, K., Parker, R., and J.R. Buchan. (2016) Defects in THO/TREX-2 function cause accumulation of novel cytoplasmic mRNP granules that can be cleared by autophagy. RNA 22:1200-1214.

Poornima, G., Shah, S., Vignesh, V., Parker R., and Rajyaguru, P.I. (2016) Arginine methylation promotes translation repression activity of eiF4G-binding protein, Scd6. Nucleic Acids Research 44:9358-9368.

Wheeler, J.R., Matheny, T., Jain, S., Abrisch, and R. Parker. (2016) Distinct stages in stress granule assembly and disassembly. eLife Sep 7;5. pii: e18413.

Harigaya, Y. and R. Parker. (2016) Codon optimality and mRNA decay. Cell Research 26:1269-1270.

Harigaya, Y. and R. Parker. (2016) Analysis of the association between codon optimality and mRNA stability in Schizosaccharomyces pombe. BMC Genomics 17:895.

Book Chapters & Invited Reviews
Mitchell, S.F. and R. Parker. (2016) Identification of endogenous mRNA-binding proteins in yeast using crosslinking and polyA enrichment. In: Methods in Molecular Biology, RNA-Protein Complexes and Interactions: Methods and Protocols. (Lin, R-J., ed.) Humana Press, USA, a part of Springer Sciences 1421:153-163.

Protter, D.S.W., and R. Parker. (2016) Principles and properties of stress granules. Trends in Cell Biology 26:668-679.

Shukla, S., and R. Parker (2016) Hypo- and Hyper- assembly diseases of RNA-protein complexes. Trends in Molecular Medicine 22:615-628.

Walters, R., Muhlrad, D., Garcia, J., and R. Parker. (2015) Differential effects of Ydj1 and Sis1 on Hsp70-mediated clearance of stress granules in Saccharomyces cerevisiae. RNA 21:1660-1671.

Garcia, J.F. and R. Parker. (2015) MS2 coat proteins bound to yeast mRNAs block 5' to 3' degradation and trap mRNA decay products: implications for the localization of mRNAs by MS2-MCP system. RNA 8:1393-1395.

Lin, Y., Protter, D.S.W., Rosen, M.K., and R. Parker. (2015) Formation and Maturation of Phase Separated Liquid Droplets by RNA Binding Proteins. Molecular Cell 60:208-219.

Book Chapters & Invited Reviews
Schwartz, J.C., Cech, T.R., and R. Parker. (2015) Biochemical Properties and Biological functions of FET Proteins. Annual Review of Biochemistry 84:355-379.

Mitchell S.F., Parker R. (2015) In Vivo cross-linking followed by PolyA Enrichment to Identify Yeast mRNA Binding Proteins. In: Boudvillain M. (eds) RNA Remodeling Proteins. Methods in Molecular Biology, vol 1259. Humana Press, New York, NY.

Walters, R.W. and R. Parker. (2015) Coupling of Ribostasis and Proteostasis: Hsp70 proteins in mRNA metabolism. Trends in Biochemical Sciences 40:552-559.

Mitchell, S.F. and R. Parker. (2015) Modifications on translation initiation. Cell 163:796-798. doi: 10.1016/j.cell.2015.10.056.

Sudhakaran, I.P., Hillebrand, J., Dervan, A., Das, S., Holohan, E.e., Hülsmeier, J., Sarov, M., Parker, R., Vijayraghavan, K., and M. Ramaswami. (2014) FMRP and Ataxin-2 function together in long-term olfactory habituation and neuronal translational control. Proceedings of the National Academy of Science 111(1):E99-E108.

Wu, D., Muhlrad, D., Bowler, M.W., Liu, Z., Parker, R., and H. Song. (2014) Lsm2 and Lsm3 bridge the interaction of the Lsm1-7 complex with Pat1 for decapping activation. Cell Research, 24:233-246.

Walters, R.W., Shumilin, I.A., Yoon, J-H., Minor, W., and R. Parker. (2014) Edc3 function in yeast and mammals is modulated by interactin with NAD-related compounds. G3 (Bethesda) 4:613-622.

Decker, C.J. and R. Parker. (2014) Analysis of Double-Stranded RNA from Microbial Communities Identifies Double-Stranded RNA Virus-Like Elements. Cell Reports 7:898-906.

Shukla, S. and R. Parker. (2014) Quality control of assembly-defective U1 snRNAs by decapping and 5'-to-3' exonucleolytic digestion. Proceedings of the National Academy of Science 111(32): E3277–E3286.

Book Chapters & Invited Reviews
Walters, R. and R. Parker. (2014) Quality Control: Is there Quality Control of Localized mRNAs? Journal of Cell Biology 204:863-868.

Mitchell, S.F. and R. Parker. (2014) Principles and Properties of Eukaryotic mRNPs. Molecular Cell 54:547-558.

Harigaya, Y. and R. Parker. (2014) Fragile X Mental Retardation Protein and the Ribosome. Molecular Cell 3:330-332.

Lasda, E.L. and R. Parker. (2014) Circular RNAs: Diversity of Form and Function. RNA 20:1829-1842.

Gilbert, J., Ball, M., Blainey, P., Blaser, M., Bohannan, B., Bunge, J., Dominguez, M.G., Epstein, S., Fierer, N., Gevers, D., Grikscheit, T., Hamdan, L., Harvey, J., Huttenhower, C., Kirkup, B., Kong, H., Lauber, C., Lemon, K., Lych, S., Martin, L. Mello, C., Palma, J., Parker, R., Petrosino, J., Segre, J., Vosshall, L., Yi, R. and R. Knight. (2014) Meeting Report for the 1st Skin Microbiota Workshop, Â鶹ӰԺ, CO October 15-16 2012. Standards in Genomic Sciences 9:13:1-7.

Mitchell, S.F., Jain, S., She, M., and R. Parker. (2013) Global Analysis of Yeast mRNPs. Nature Structural and Molecular Biology, 20:127-133.

Buchan, J.R., Kolaitis, R-M., Taylor, J.P, and R. Parker. (2013) Eukaryotic stress granules are cleared by granulophagy and Cdc48/VCP function. Cell, 153:1461-1474.

Book Chapters & Invited Reviews
Jain, S., and R. Parker. (2013) The discovery and analysis of P Bodies. Advances in experimental medicine and biology 768:23-43.

Ramaswami, M., Taylor J.P., and R. Parker. (2013) Altered "Ribostasis": RNA-protein granule formation or persistence in the development of degenerative disorders. Cell 154:727-736.

Rajyaguru, P., She, M., and R. Parker. (2012) Scd6 targets eIF-4G to repress translation: RGG-motif proteins as a class of 4G-binding proteins. Molecular Cell 45:244-254.

Harigaya, Y. and R. Parker. (2012) Global analysis of mRNA decay intermediates in Saccharomyces cerevisiae. Proceedings of the National Academy of Sciences 109:11764-11769.

Parker, R. (2012) Skill Development in Graduate Education. Molecular Cell 46:377-361 PMCID: PMC3873173 Luhtala, N. and R. Parker. (2012) Structure-function analysis of Rny1 in tRNA cleavage and growth inhibition. PLOS ONE 7:e41111. Epub 2012 Jul 19.

Luhtala, N. and R. Parker. (2012) Structure-function analysis of Rny1 in tRNA cleavage and growth inhibition. PLOS ONE 7:e41111. Epub 2012 Jul 19.

Lai, T., Cho, H., Liu, Z., Bowler, M.W., Piao, S., Parker, R., Kim, Y.K., and H. Song. (2012) Structural basis of PNRC2-mediated link between mRNA surveillance and decapping. Structure 20:2025-2037.

Book Chapters & Invited Reviews
Parker, R. (2012) RNA Degradation in Saccharomyces cerevisiae. Genetics 191:671-702.

Buchan, J.R., Capaldi, A.P. and R. Parker. (2012) TOR-tured Yeast Find a New Way to Stand the Heat. Molecular Cell 47:155-157.

Decker, C.J. and R. Parker. (2012) P-Bodies and Stress Granules: Possible Roles in the Control of Translation and mRNA Degradation. Cold Spring Harbor Perspectives in Biology Sep 1;4(9):a012286.

Rajyaguru, P. and R. Parker. (2012) RGG motif proteins: Modulators of mRNA functional states. Cell Cycle 11:2594-2599.Ìý

Buchan, J.R., Yoon, J-H., and R. Parker. (2011) Stress-specific composition, assembly and kinetics of Stress granules in Saccharomyces cerevisiae. Journal of Cell Science 124:228-239.

Balagopal, V., and R. Parker. (2011) Stm1 modulates translation after 80S formation in Saccharomyces cerevisiae. RNA 17:835-842.

Hilliker, A., Gao, Z., Jankowsky, E., and R. Parker. (2011) The DEAD-box protein Ded1 modulates translation by the formation and resolution of an eIF4F-mRNA complex. Molecular Cell 43:962-972.

McCann, C., Holohan E.E., Das, S., Dervan, A., Larkin, A., Lee, J.A., Rodrigues, V., Parker, R., and M. Ramaswami. (2011) The Ataxin-2 protein is required for microRNA function and synapse-specific long-term olfactory habituation. Proceeding of the National Academy of Science 108: E655-662.

Chekulaeva, M., Mathys, H., Zipprich, J.T., Attig, J., Colic, M, Parker, R., and W. Filipowicz. (2011) miRNA repression involves GW182-mediated recruitment of CCR4-NOT through conserved W-containing motifs. Nature Structural & Molecular Biology 18:1218-1226.

Swisher, K. and R. Parker. (2011) Interactions between Upf1 and the decapping factors Edc3 and Pat1 in Saccharomyces cerevisiae. PLOS ONE 6: e26547.

Harigaya, Y., Jones, B.N., Muhlrad, D., Gross, J.D., and R. Parker. (2010) Identification and Analysis of the interaction between Edc3 and Dcp2 in Saccharomyces cerevisiae. Molecular and Cellular Biology 30:1446-1456.

Yoon, J-H., Choi, E-J. and R. Parker. (2010) Dcp2 phosphorylation by Ste20 modulates stress granule assembly and mRNA decay in Saccharomyces cerevisiae. Journal of Cell Biology 189:813-827.

Swisher K.D., and R. Parker. (2010) Localization to, and Effects of Pbp1, Pbp4, Lsm12, Dhh1, and Pab1 on Stress Granules in Saccharomyces cerevisiae. PLOS ONE 5:e10006.

Nissan, T., Rajyaguru, P., She, M., Song, H., and R. Parker. (2010) Decapping activators in Saccharomyces cerevisiae act by multiple mechanisms. Molecular Cell 39:773-783.

Chen, L., Muhlrad, D., Hauryliuk, V., Cheng, Z., Lim, M.K., Shyp, V., Parker, R. and H. Song. (2010) Structure of the Dom34-Hbs1 complex and implications for no-go decay. Nature Structural & Molecular Biology 17:1233-1240.

Hillebrand, J., Pan, K., Kokaram, A, Barbee, S., Parker, R. and M. Ramaswami. (2010) The Me31B DEAD-box helicase localizes to postsynaptic foci and regulates expression of a CaMKII reporter mRNA in dendrites of Drosophila olfactory projection neurons. Frontiers in Neural Circuits 4:121.

Chekulaeva, M., Parker, R., and W. Fillipowicz. (2010) The GW/WG repeats of Drosophila GW182 function as effector motifs for miRNA-mediated repression. Nucleic Acids Research 38:6673-6683.

Book Chapters & Invited Reviews
J. Ross Buchan, Tracy Nissan, and R. Parker. (2010) Analyzing P-Bodies and Stress Granules in Saccharomyces cerevisiae. Methods in Enzymology 470:619-640.

Yoon, J-H. and R. Parker. (2010) Coil-in-to snRNP assembly and Cajal bodies. Nature Structural & Molecular Biology 17:391-393 doi: 10.1038/nsmb0410-391.

Luhtala, N. and R. Parker. (2010) T2 Family ribonucleases: ancient enzymes with diverse roles. Trends in Biochemical Sciences 35:253-259.

Harigaya, Y. and R. Parker. (2010) No-Go Decay: a quality control mechanism for RNA in translation. WIREs RNA, Wiley Interdisciplinary Reviews: RNA, 1:132-141.

Balagopal, V. and R. Parker. (2009) Stm1 modulates mRNA decay and Dhh1 function in Saccharomyces cerevisiae. Genetics 181:93-103.

Thompson, D. and R. Parker. (2009) The RNase Rny1p cleaves tRNAs and promotes cell death during oxidative stress in Saccharomyces cerevisiae. Journal of Cell Biology 185:43-50.

Chekulaeva, M., Filipowicz, W. and R. Parker. (2009) Multiple independent domains of dGW182 function in miRNA-mediated repression in Drosophila RNA 15:794-803.

Passos, D.O., Doma, M.K, Shoemaker, C.J., Muhlrad, D., Green, J., Weissman, J., Hollien, J. and R. Parker. (2009) Analysis of Dom34 and its function in No-Go Decay. Molecular Biology of the Cell 20:3025-3032.

Luhtala, N. and R. Parker. (2009) LSM1 over-expression in Saccharomyces cerevisiae depletes U6 snRNA levels. Nucleic Acids Research 37:5529-5536.

Cziko, A.-M.J., McCann, C.T., Howlett, I.C., Barbee, S.A., Duncan, R.P., Luedemann, R., Zarnescu, D., Zinsmaier, K.E., Parker, R.R., and M. Ramaswami. (2009) Genetic Modifiers of dFMR1 Encode RNA Granule Components in Drosophila. Genetics 182:1051-1060.

Book Chapters & Invited Reviews
Rajyaguru, P. and R. Parker. (2009) Cgh-1 and the Control of Maternal mRNAs. Trends in Cell Biology January 19, 19:24-28.

Balagopal, V. and R. Parker. (2009) Polysomes, P bodies and stress granules: states and fates of eukaryotic mRNAs. Current Opinion in Cell Biology 21:403-408.

Swisher, K.D. and R. Parker. (2009) Related Mechanisms for mRNA and rRNA Quality Control. Molecular Cell May 29, 34:401-402.

Thompson, D.M. and R. Parker. (2009) Stressing out over tRNA cleavage. Cell July 24, 138:215-219.

Buchan, J.R. and R. Parker. (2009) Eukaryotic stress granules: the ins and outs of translation. Molecular Cell 36:932-41.

Pilkington, G.R., and R. Parker. (2008) Pat1 contains distinct functional domains that promote P-body assembly and activation of decapping. Molecular and Cellular Biology 28:1298-1312.

Beckham, C.J., Hilliker, A., Cziko, A.-M., Noueiry, A., Ramaswami, M., and R. Parker. (2008) The DEAD-Box RNA helicase Ded1p affects and accumulates in Saccharomyces cerevisiae P-bodies. Molecular Biology of the Cell 19:984-993.

She, M., Decker, C., Svergun, D.I., Round, A., Chen, N., Muhlrad, D., Parker, R., and H. Song. (2008) Structural basis of Dcp2 recognition and activation by Dcp1. Molecular Cell 29:337-349.

Nissan, T. and R. Parker. (2008) Computational analysis of miRNA-mediated repression of translation: Implications for models of translation initiation inhibition. RNA 14:1480-1491.

Ling, S.H., Decker, C.J., Walsh, M.A., She, M., Parker, R. and H. Song (2008) Crystal structure of human Edc3 and its functional implications. Molecular and Cellular Biology 28:5965-5976.

Pedro-Segura, E., Vergara, S.V., Rodríguez-Navarro, S., Parker, R., Thiele, D.J. and S. Puig (2008) The Cth2 are-binding protein recruits the Dhh1 helicase to promote the decay of succinate dehydrogenase SDH4 mRNA in response to iron deficiency. Journal of Biological Chemistry 283:28527-28535.

Thompson, D.M., Lu, C., Green, P.J. and R. Parker. (2008) tRNA cleavage is a conserved response to oxidative stress in eukaryotes. RNA 14:2095-2103.

Buchan, J.R., Muhlrad, D, and R. Parker. (2008) P-bodies promote Stress Granule assembly in Saccharomyces cerevisiae. Journal of Cell Biology 183:441-455.

Book Chapters & Invited Reviews
Beckham, C.J. and R. Parker. (2008) P Bodies, Stress Granules, and Viral Life Cycles. Cell Host & Microbe 3:206-212.

Hilliker, A., and R. Parker. (2008) "Stressed out? Make some modifications!" Nature Cell Biology 10:1129-1130.

Nissan, T. and R. Parker. (2008) Analyzing P-bodies in Saccharomyces cerevisiae. Methods in Enzymology 448:507-520.

Passos, D.O. and R. Parker. (2008) Analysis of Cytoplasmic mRNA Decay in Saccharomyces cerevisiae. Methods in Enzymology 448:409-427.

Thompson, D. M. and R. Parker. (2007) Cytoplasmic decay of intergenic transcripts in Saccharomyces cerevisiae. Molecular and Cellular Biology 27:92-101.

Cheng, Z., Muhlrad, D., Lim, M.K., Parker, R. and H. Song (2007) Structural and functional insights into the human Upf1 helicase core. EMBO Journal 26:253-64.

Teixeira, D. and R. Parker. (2007) Analysis of P-body Assembly in Saccharomyces cerevisiae. Molecular Biology of the Cell 18:2274-2287.

Brengues, M. and R. Parker. (2007) Accumulation of polyadenylated mRNA, Pab1p, eIF4E, and eIF4G with P-bodies in Saccharomyces cerevisiae. Molecular Biology of the Cell 18:2592-2602.

Beckham, C.J., Light, H.R., Nissan, T.A., Ahlquist, P., Parker, R., and A. Nouiery. (2007) Interactions between Brome Mosaic Virus RNAs and Cytoplasmic Processing Bodies. Journal of Virology 81:9759-9768.

Decker, C.J., Teixeira, D., and R. Parker. (2007) Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae. Journal of Cell Biology 179:437-449.

Book Chapters & Invited Reviews
Parker, R. and U. Sheth. (2007) P Bodies and the Control of mRNA Translation and Degradation. Molecular Cell 25:635-646.

Doma, M.K. and R. Parker. (2007) RNA Quality Control in Eukaryotes. Cell 131:660-668.

Buchan, J.R. and R. Parker. (2007) Molecular Biology: The Two Faces of miRNA. Science 318:1877-1878.

Beliakova-Bethell, N., Beckham, C., Giddings Jr., T.H., Winey, M., Parker, R. and S. Sandmeyer. (2006) Virus-like particles of the Ty3 retrotransposon assemble in association with P-body components. RNA 12:94-101.

She, M., Decker, C.J., Chen, N., Tumati, S., Parker, R. and H. Song. (2006) Crystal structure and functional analysis of Dcp2p from Schizosaccharomyces pombe. Nature Structural and Molecular Biology 13:63-70.

Doma, M.K. and R. Parker. (2006) Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation. Nature 440:561-564.

Sheth, U. and R. Parker. (2006) Targeting of Aberrant mRNAs to Cytoplasmic Processing Bodies. Cell 125:1095-1109.

Hilgers, V., Teixeira, D. and R. Parker. (2006). Translation-independent inhibition of mRNA deadenylation during stress in Saccharomyces cerevisiae. RNA 12:1835-1845.

Segal, S.P., Dunckley, T.C. and R. Parker. (2006) Sbp1p affects translational repression and decapping in Saccharomyces cerevisiae. Molecular and Cellular Biology 26:5120-5130.

Baker, K.E. and R. Parker. (2006) Conventional 3' end formation is not required for NMD substrate recognition in Saccharomyces cerevisiae. RNA 12:1441-1445.

Barbee, S.A., Estes, P.S., Cziko, A-M., Hillebrand, J., Luedeman, R.A., Coller, J.M., Johnson, N., Howlett, I.C., Geng, C., Ueda, R., Brand, A.H., Newbury, S.F., Wilhelm, J.E., Levine, R.B., Nakamura, A., Parker, R., and M. Ramaswami. (2006) Staufen- and FMRP-containing neuronal RNPs are structurally and functionally related to somatic P bodies. Neuron 52:997-1009.

Book Chapters & Invited Reviews
Baker, K.E. and R. Parker. (2006) Features of nonsense-mediated mRNA decay in Saccharomyces cerevisiae. In: Nonsense-mediated mRNA Decay. (Maquat, L., ed.) pp 3-13. Landes Biosciences, Texas.

Valencia-Sanchez, M., Liu, J., Hannon, G.J. and R. Parker. (2006) Control of translation and mRNA degradation by miRNAs and siRNAs. Genes & Development 20:515-524.

Decker, C.J. and R. Parker. (2006) CAR-1 and trailer hitch: Driving mRNP granule function at the ER? Journal of Cell Biology 173:159-163.

Doma, M.K., and R. Parker. (2006) Revenge of the NRD: preferential degradation of nonfunctional eukaryotic rRNA. Developmental Cell 11:757-758.

Chen, N., Walsh, M.A., Liu, Y., Parker, R. and H. Song. (2005) Crystal structures of human DcpS in ligand-free and m⁷GDP-bound forms suggest a dynamic mechanism for scavenger mRNA decapping. Journal of Molecular Biology 347:707-718.

Muhlrad, D. and R. Parker. (2005) The yeast EDC1 mRNA undergoes deadenylation-independent decapping stimulated by Not2p, Not4p and Not5p. EMBO Journal 24:1033-1045.

Teixeria, D., Sheth, U., Valencia-Sanchez, MA, Brengues, M. and R. Parker. (2005) Processing bodies require RNA for assembly and contain non-translating mRNAs. RNA 11:371-382.

Tharun, S., Muhlrad, D., Chowdhury, A. and R. Parker. (2005) Mutations in the Saccharomyces cerevisiae LSM1 gene that affect mRNA decapping and 3' end protection. Genetics 170:33-46.

Cheng, Z., Coller, J., Parker, R. and H. Song. (2005) Crystal structure and functional analysis of DEAD-box protein Dhh1p. RNA 11:1258-1270.

Wilson, M.A., Meaux, S., Parker, R. and A. van Hoof. (2005). Genetic interactions between [PSI⁺] and nonstop mRNA decay affect phenotypic variation Proceeding of the National Academy of Science 102:10244-10249.

Coller, J. and R. Parker. (2005) General Translational Repression by Activators of mRNA Decapping. Cell 122:875-886.

Brengues, M., Teixeria, D. and R. Parker. (2005) Movement of Eukaryotic mRNAs Between Polysomes and Cytoplasmic Processing Bodies. Science 310:486-489.

Liu, J., Valencia-Sanchez, M.A., Hannon, G.J. and Parker, R. (2005). MicroRNA-dependent localization of targeted mRNAs to mammalian P-bodies. Nature Cell Biology 7:719-723.

Liu, J., Rivas, F.V., Wohlschlegel, J., Yates III, J.R., Parker, R. and G.J. Hannon. (2005) A role for the P-body component GW182 in microRNA function. Nature Cell Biology 7:1261-1266.

She, M., Decker, C.J., Sundramurthy, K., Liu, Y., Chen, N., Parker, R. and H. Song. (2004) Crystal Structure of Dcp1p and Its Functional Implications in mRNA Decapping. Nature Structural & Molecular Biology 11:249-256.

Kshirsagar, M. and R. Parker. (2004) Identification of Edc3p as an enhancer of mRNA decapping in Saccharomyces cerevisiae. Genetics166:729-739.

Baker, K.E., Coller, J.M. and R. Parker. (2004) The yeast Apq1p affects nucleocytoplasmic mRNA transport. RNA 10:1352-1358.

Cheng, Z., Liu, Y., Wang, C., Parker R. and H. Song. (2004) Crystal structure of Ski8p, a WD-repeat protein with dual roles in mRNA metabolism and meiotic recombination. Protein Science 13:2673-2684.

Book Chapters & Invited Reviews
Parker, R. and H. Song. (2004) The Enzymes and Control of Eukaryotic mRNA Turnover. Nature Structural and Molecular Biology 11:121-127.

Coller, J. and R. Parker. (2004) Eukaryotic mRNA decapping. Annual Review of Biochemistry 73:861-890.

Baker, K.E., and R. Parker. (2004) Nonsense-mediated mRNA decay: terminating erroneous gene expression. Current Opinion Cell Biology 16:293-299.

Steiger, M., Carr-Schmid, A., Schwartz, D.C., Kiledjian, M. and R. Parker. (2003) Analysis of recombinant yeast decapping enzyme. RNA 9:231-238.

Schwartz, D., Decker, C.J. and R. Parker. (2003) The Enhancer of Decapping Proteins, Edc1p and Edc2p, bind RNA and stimulate activity of the decapping enzyme. RNA 9:239-251.

Sheth, U. and R. Parker. (2003) Decapping and decay of messenger RNA occur in cytoplasmic processing bodies. Science 300:805-808.

Cao, D. and R. Parker. (2003) Computational Modeling and Experimental Analysis of Nonsense-Mediated Decay in Yeast. Cell 113:533-545.

Hilleren, P.J. and R. Parker. (2003) Cytoplasmic Degradation of Splice-Defective pre-mRNAs and Intermediates. Molecular Cell 12:1453-1465.

van Hoof, A., Frischmeyer, P.A., Dietz, H.C. and R. Parker. (2002) Exosome-mediated recognition and degradation of mRNAs lacking a termination codon. Science 295:2262-2264.

Frischmeyer, P.A., van Hoof, A., O’Donnell K., Guerrerio A.L., Parker, R. and H.C. Dietz. (2002) An mRNA Surveillance Mechanism that Eliminates Transcripts Lacking Termination Codons. Science 295:2258-2261.

Book Chapters & Invited Reviews
Wickens, M., Bernstein, D.S., Kimble, J., and R. Parker. (2002) A PUF family portrait: 3' UTR regulation as a way of life. Trends in Genetics 18:150-157.

van Hoof, A., and R. Parker. (2002) Messenger RNA degradation: Beginning at the end. Current Biology 12:R285-R287.

Steiger, M., and R. Parker. (2002) Analyzing mRNA Decay in Saccharomyces cerevisiae Methods in Enzymology 351:648-660.

Decker, C.J. and R. Parker. (2002) mRNA decay enzymes: Decappers conserved between yeast and mammals. Proceeding of the National Academy of Science 99:12512-12514.

Dunckley T., Tucker, M. and R. Parker. (2001) Two related proteins, Edc1p and Edc2p, stimulate mRNA decapping in Saccharomyces cerevisiae. Genetics 157:27-37.

Tucker, M., Valencia-Sanchez M.A., Staples R., Chen J., Denis C.L. and R. Parker. (2001) The transcription factor associated proteins Ccr4 and Caf1 are components of the major cytoplasmic mRNA deadenylase in Saccharomyces cerevisiae. Cell 104:377-386.

Hilleren, P. and R. Parker. (2001) Defects in the mRNA export factors Rat7p, Gle1p, Mex67p and Rat8p cause hyperadenylation during 3' end formation of nascent transcripts. RNA 7:753-764.

He, W. and R. Parker. (2001) The yeast cytoplasmic LsmI/Pat1p complex protects mRNA 3' termini from partial degradation. Genetics 158:1445-1455.

Cao, D. and R. Parker. (2001) Computational modeling of eukaryotic mRNA turnover. RNA 7:1192-1212.

Tharun, S. and R. Parker. (2001) Targeting an mRNA for decapping: displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs. Molecular Cell 8:1075-1083.

Coller, J.M., Tucker, M., Sheth, U., Valencia-Sanchez, M.A. and R. Parker. (2001) The DEAD box helicase, Dhh1p, functions in mRNA decapping and interacts with both the decapping and deadenylase complexes. RNA 7:1717-1727.

Hilleren, P., McCarthy, T., Rosbash, M., Parker, R. and Jensen, T.H. (2001) Quality control of mRNA 3'-end processing is linked to the nuclear exosome. Nature 413:538-542.

Book Chapters & Invited Reviews
Dunckley, T., and R. Parker. (2001) Yeast mRNA Decapping Enzyme. Methods in Enzymology 342:226-233.

Dunckley, T., and R. Parker. (2001) RNA Turnover. In: Encyclopedia of Genetics. (Brenner, S., Miller J.H., eds.) Academic Press, NY, p1748-1751.

van Hoof, A., Lennertz, P. and R. Parker. (2000) Yeast Exosome Mutants Accumulate 3'-Extended Polyadenylated Forms of U4 Small Nuclear RNA and Small Nucleolar RNAs. Molecular and Cellular Biology 20:441-452.

van Hoof, A., Lennertz, P. and R. Parker. (2000) Three conserved members of the RNase D family have unique and overlapping functions in the processing of 5S, 5.8S, U4, U5, RNase MRP and RNase P RNAs in yeast. EMBO Journal 19: 1357-1365.

Tharun, S., He, W., Mayes, A.E., Lennertz, P., Beggs, J.D. and R. Parker. (2000) Yeast Sm-like proteins function in mRNA decapping and decay. Nature 404:515-518.

Jacobs Anderson, J.S. and R. Parker. (2000) Computational Identification of Cis-acting Elements Affecting Post-Transcriptional Control of Gene Expression in Saccharomyces cerevisiae. Nucleic Acids Research 28:1604-1617.

Schwartz, D. and R. Parker. (2000) mRNA decapping in yeast requires dissociation of the cap binding protein, eukaryotic translation initiation factor 4E. Molecular and Cellular Biology 20:7933-7942.

van Hoof, A., Staples, R.R., Baker, R.E. and R. Parker. (2000) Function of the Ski4p (Csl4p) and Ski7p proteins in 3'-to-5' degradation of mRNA. Molecular and Cellular Biology 20:8230-8243.

Olivas, W. and R. Parker. (2000) The Puf3 protein is a transcript-specific regulator of mRNA degradation in yeast. EMBO Journal 19:6602-6611.

Book Chapters & Invited Reviews
He, W., and R. Parker. (2000) Functions of Lsm proteins in mRNA degradation and splicing. Current Opinion in Cell Biology 12:346-350.

Tucker, M., and R. Parker. (2000) Mechanisms and Control of mRNA Decapping in Saccharomyces cerevisiae. Annual Review of Biochemistry 69:571-595.

Schwartz, D.C., and R. Parker. (2000) Interaction of mRNA Translation and mRNA Degradation in Saccharomyces cerevisiae. In: Translational Control of Gene Expression. (Sonenberg, N., Hershey, J.W.B, Matthews, M.B., eds.) pp. 807-825. New York, Cold Spring Harbor Laboratory Press.

LaGrandeur, T. and R. Parker. (1999) The cis acting sequences responsible for the differential decay of the unstable MFA2 and stable PGK1 transcripts in yeast includes the context of the translational short codon. RNA 5:420-433.

Tharun, S. and R. Parker. (1999) Analysis of mutations in the yeast mRNA decapping enzyme. Genetics 151:1273-1285.

Schwartz, D. and R. Parker. (1999) Mutations in Translation Initiation Factors lead to increased rates of deadenylation and decapping of yeast mRNAs. Molecular and Cellular Biology 19:5247-5256.

Dunckley, T. and R. Parker. (1999) The DCP2 protein is required for mRNA decapping in Saccharomyces cerevisiae and contains a functional MutT motif. EMBO Journal 18: 5411-5422.

Muhlrad, D. and R. Parker. (1999) Recognition of Yeast mRNAs as "nonsense containing" leads to both inhibition of mRNA translation and mRNA degradation: Implications for the control of mRNA decapping. Molecular Biology of the Cell 10: 3971-3978.

Muhlrad, D. and R. Parker. (1999) Aberrant mRNAs with extended 3' UTRs are substrates for rapid degradation by mRNA surveillance. RNA 5:1299-1307.

Book Chapters & Invited Reviews
He, W., and R. Parker. (1999) Analysis of mRNA Decay Pathway in S. Cerevisiae. Methods 17:3-10.

Tharun, S., and R. Parker. (1999) Turnover of mRNA in Eukaryotic Cells. In: Comprehensive Natural Products Chemistry, Volume 6: Prebiotic Chemistry, Molecular Fossils, Nucleosides, and RNA. (Barton, Derek H.R., Nakanishi, Koji, Meth-Cohn, Otto, eds.) pp. 205-216. Amsterdam, New York, Elsevier Science, Ltd.

Hilleren, P., and R. Parker. (1999) mRNA Surveillance in Eukaryotes: Kinetic Proofreading of Proper Translation Termination as assessed by mRNP Domain Organization? RNA 5:711-719.

van Hoof, A., and R. Parker. (1999) The exosome: A proteasome for RNA? Cell 99:347-350.

Hilleren, P., and R. Parker. (1999) Mechanisms of mRNA Surveillance in Eukaryotes. Annual Review of Genetics 3:229-260.

Anderson, J.S.J. and R. Parker. (1998) The 3' to 5' degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3' to 5' exonucleases of the exosome complex. EMBO Journal 17:1497-1506.

LaGrandeur, T.E. and R. Parker. (1998) Isolation and Characterization of Dcp1p, the yeast mRNA decapping enzyme. EMBO Journal 17:1487-1496.

Olivas, W. M., Muhlrad, D. and R. Parker. (1997) Analysis of the yeast genome: identification of new non-coding and small ORF-containing RNAs. Nucleic Acids Research 25:4619-4625.

Book Chapters & Invited Reviews
Tharun, S. and R. Parker. (1997) Mechanisms of mRNA Turnover in Eurkaryotic Cells. In: mRNA Metabolism and Post-Transcriptional Gene Regulation. (Morris, D. R. and Harford J. B., eds.), pp. 181-199. New York, Wiley-Liss, Inc.

Hatfield, L., Beelman, C. A., Stevens A. and R. Parker. (1996) Mutations in trans-acting factors that inhibit mRNA decapping in Saccharomyces cerevisiae. Molecular and Cellular Biology 16:5830-5838.

Beelman, C. A., Stevens A., Caponigro G., LaGrandeur, T.E., Hatfield L., Fortner, D. and R. Parker. (1996) An essential component of the decapping enzyme required for normal rates of mRNA decay in yeast. Nature 382:642-646.

Caponigro, G. and R. Parker. (1996) mRNA Turnover in Yeast Promoted by the MATa1 Instability Element. Nucleic Acids Research 24:4304-4312.

Book Chapters & Invited Reviews
Caponigro, G. and R. Parker. (1996) Mechanisms and Control of mRNA Turnover in Saccharomyces cerevisiae. Microbiological Reviews 60:233-249.

Anderson, J.S.J. and R. Parker. (1996) RNA turnover: The helicase story unwinds. Current Biology 6:780-782.

LaGrandeur, T.E. and R. Parker. (1996) mRNA decapping activities and their biological roles. Biochemie 78:1049-1055.

Muhlrad, D., Decker, C. and R. Parker. (1995) Turnover mechanisms of the stable PGK1 mRNA in yeast. Molecular and Cellular Biology 15:2145-2156.

Caponigro, G. and R. Parker. (1995) Multiple functions of the Poly(A) binding protein in mRNA decapping and deadenylation. Genes & Development 9:2421-2432.

Mandart, E. and R. Parker. (1995) Effects of mutations in the RNA14, RNA15, and PAP1 genes on polyadenylation and mRNA metabolism in Saccharomyces cerevisiae. Molecular and Cellular Biology 15:6979-6986.

Book Chapters & Invited Reviews
Beelman, C. and R. Parker. (1995) Degradation of mRNA in Eukaryotes. Cell 81:179-183.

Decker, C.J. and R. Parker. (1995) Diversity of cytoplasmic functions for the 3' untranslated region of eukaryotic transcripts. Current Opinion in Cell Biology 7:386-392.

Beelman, C.A. and R. Parker. (1994) Differential effects of translational inhibition in cis and in trans on the decay of the unstable yeast MFA2 mRNA. Journal of Biological Chemistry 269:9687-9692.

Muhlrad, D., Decker, C. and R. Parker. (1994) Deadenylation of the unstable mRNA encoded by the yeast MFA2 gene leads to decapping followed by 5' to 3' degradation of the transcript. Genes & Development 8:855-866.

Muhlrad, D. and R. Parker. (1994) Premature translational termination triggers mRNA decapping. Nature 370:578-581.

Book Chapters & Invited Reviews
Decker, C. and R. Parker. (1994) Mechanisms of mRNA degradation in eukaryotes. Trends in Biochemical Sciences 19:336-340.

Parker, R. and P. Siliciano. (1993) Evidence for a non-Watson Crick interaction between the first and last nucleotides of a nuclear pre-mRNA intron. Nature 361:660-662.

Decker, C.J. and R. Parker. (1993) A turnover pathway for both stable and unstable mRNAs in yeast: evidence for a requirement for deadenylation. Genes & Development 7:1632-1643.

Caponigro, G., Muhlrad, D. and R. Parker. (1993) A small segment of the MATa1 transcript promotes mRNA decay in yeast: a stimulatory role for rare codons. Molecular and Cellular Biology 13:5141-5148.

Muhlrad, D., Hunter, R. and R. Parker. (1992) A rapid method for the localized mutagenesis of yeast genes. Yeast 8:79-82.

Heaton, B., Decker, C., Muhlrad, D., Donahue, J., Jacobson, A. and R. Parker. (1992) Analysis of chimeric mRNAs identifies multiple regions within yeast mRNAs that regulate mRNA decay. Nucleic Acids Research 20:5365-5373.

Muhlrad, D. and R. Parker. (1992) Mutations affecting stability and deadenylation of the yeast MFA2 transcript. Genes & Development 6:2100-2111.

Book Chapters & Invited Reviews
Parker, R., Muhlrad, D., Deshler, J., Taylor, N. and J. Rossi. (1992) Ribozymes: Principles and designs for their use as antisense and therapeutic agents. In: Gene Regulation: Biology of Antisense RNA and DNA. (R.P. Erickson and J. G. Izant, eds.), pp. 55-70. Raven Press, Ltd., New York.

Parker, R., Herrick, D., Peltz, S. and A. Jacobson. (1991) Measurement of mRNA decay rates in Saccharomyces cerevisiae. Methods in Enzymology 194:415-423.

Parker, R. and A. Jacobson. (1990) Translation and a 42-nucleotide segment within the coding region of the mRNA encoded by the MATa1 gene are involved in promoting rapid mRNA decay in yeast. Proceeding of the National Academy of Science 87:2780-2784.

Herrick, D., Parker, R. and A. Jacobson. (1990) Identification and comparison of stable and unstable mRNAs in Saccharomyces cerevisiae. Molecular and Cellular Biology 10:2269-2284.

Book Chapters & Invited Reviews
Jacobson, A., Herrick, D., Donahue, J., Parker, R. and S. Peltz. (1990) Regulation of mRNA stability in yeast. Post-Transcriptional Control of Gene Expression. (McCarthy, J.E.G., Puitte, M. F., eds.) NATO ASI Series, H9:45-54.

Ruohola, H., Baker, S.M., Parker, R. and T. Platt. (1988) Orientation-dependent function of a short CYC1 DNA fragment in directing mRNA 3' end formation in yeast. Proceeding of the National Academy of Science 85:5041-5045.

Parker, R., Simmons, T., Shuster, E., Siliciano, P. and C. Guthrie. (1988) Genetic analysis of small nuclear RNAs in Saccharomyces cerevisiae: viable sextuple mutant. Molecular and Cellular Biology 8:3150-3159.

Couto, J., Tamm, J., Parker, R. and C. Guthrie. (1987) A trans-acting suppressor restores splicing of a yeast intron with a branch point mutation. Genes & Development 1:445-455.

Parker, R., Siliciano, P. and C. Guthrie. (1987) Recognition of the TACTAAC box during mRNA splicing in yeast involves base-pairing to the U2-like snRNA. Cell 49:229-239.

Book Chapters & Invited Reviews
Parker, R. and B. Patterson. (1987) Architecture of fungal introns: implications for spliceosome assembly. In: Molecular Biology of RNA: New Perspectives (Inouye, M., and Dudock, B.S., Eds.), pp. 133-149. New York: Academic Press.

Cellini, A., Parker, R., McMahon, J., Guthrie, C. and J. Rossi. (1986) Activation of a cryptic TACTAAC box in the yeast actin intron. Molecular and Cellular Biology 6:1571-1578.

Vijayraghavan, U., Parker, R., Tamm, J., Iimura, Y., Rossi, J., Abelson, J.A. and C. Guthrie. (1986) Mutations in conserved intron sequences affect multiple steps in the yeast splicing pathway, particularly assembly of the spliceosome. EMBO Journal 5:1683-1695.

Book Chapters & Invited Reviews
Guthrie, C., Reidel, N., Parker, R., Swerdlow, H. and B. Patterson. (1986) Genetic analyses of snRNAs and RNA processing in yeast. In: Yeast Cell Biology, UCLA Symposia on Molecular Biology, New Series, Vol. 33, pp. 301-321. New York: Alan R. Liss, Inc.

Parker, R. and C. Guthrie. (1985) A point mutation in the conserved hexanu­cleotide at a yeast 5' splice site uncouples recognition, cleavage and ligation. Cell 41:107-118.

Jones, E., Zubenko, G. and R.R. Parker. (1982) PEP4 gene function is required for expression of several vacuolar hydrolases in Saccharomyces cerevisiae. Genetics 102:679-690.

Heffron, F., Kostriken, R., Morita, C. and R. Parker. (1981) Tn3 encodes a site-specific recombination system: identification of essential sequences, genes, and the actual site of recombination. In: Cold Spring Harbor Symposia on Quantitative Biology, Vol. XLV, pp. 259-268.

Jones, E., Zubenko, G., Parker, R., Hemmings, B. and A. Hasik. (1981) Pleiotropic mutations of Saccharomyces cerevisiae which cause deficiency for proteinases and other vacuole enzymes. In: Molecular Genetics in Yeast, Alfred Benzon Symposium, Vol. 16, (von Wettstein, D., Friis, J., Kielland-Brant, M., and Stenderup, A., Eds.), pp. 182-188.