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442 results on '"Richter, Joel D."'

2. FMRP regulation of aggrecan mRNA translation controls perineuronal net development.

Author

van't Spijker, Heleen M. and Richter, Joel D.

Subjects
*FRAGILE X syndrome, *PERINEURONAL nets, *CINGULATE cortex, *NEURAL development, *NEUROPLASTICITY
Abstract

Perineuronal nets (PNNs) are mesh‐like structures on the surfaces of parvalbumin‐expressing inhibitory and other neurons, and consist of proteoglycans such as aggrecan, brevican, and neurocan. PNNs regulate the Excitatory/Inhibitory (E/I) balance in the brain and are formed at the closure of critical periods of plasticity during development. PNN formation is disrupted in Fragile X Syndrome, which is caused by silencing of the fragile X messenger ribonucleoprotein 1 (Fmr1) gene and loss of its protein product FMRP. FXS is characterized by impaired synaptic plasticity resulting in neuronal hyperexcitability and E/I imbalance. Here, we investigate how PNN formation is altered in FXS. PNNs are reduced in Fmr1 KO mouse brain when examined by staining for the lectin Wisteria floribunda agglutin (WFA) and aggrecan. Examination of PNNs by WFA staining at P14 and P42 in the hippocampus, somatosensory cortex, and retrosplenial cortex shows that they were reduced in these brain regions at P14 but mostly less so at P42 in Fmr1 KO mice. However, some differential FMRP regulation of PNN development in these brain regions persists, perhaps caused by asynchrony in PNN development between brain regions in wild‐type animals. During development, aggrecan PNN levels in the brain were reduced in all brain regions in Fmr1 KO mice. Aggrecan mRNA levels were unchanged at these times, suggesting that FMRP is normally an activator of aggrecan mRNA translation. This hypothesis is buttressed by the observations that FMRP binds aggrecan mRNA and that ribosome profiling data show that aggrecan mRNA is associated with reduced numbers of ribosomes in Fmr1 KO mouse brain, indicating reduced translational efficiency. Moreover, aggrecan mRNA poly(A) tail length is also reduced in Fmr1 KO mouse brain, suggesting a relationship between polyadenylation and translational control. We propose a model where FMRP modulates PNN formation through translational up‐regulation of aggrecan mRNA polyadenylation and translation. [ABSTRACT FROM AUTHOR]

Published
2024
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4. Rethinking Unconventional Translation in Neurodegeneration

Author

Gao, Fen-Biao, Richter, Joel D, and Cleveland, Don W

Subjects
Biochemistry and Cell Biology, Biological Sciences, Neurodegenerative, Genetics, Neurosciences, Animals, Codon, Initiator, Frameshifting, Ribosomal, Humans, Neurodegenerative Diseases, Open Reading Frames, Protein Biosynthesis, Regulatory Sequences, Ribonucleic Acid, Trinucleotide Repeat Expansion, ALS, C9ORF72, dipeptide repeat proteins, frontotemporal dementia, near-cognate start codon, repeat expansion, translation, upstream open reading frame, Medical and Health Sciences, Developmental Biology, Biological sciences, Biomedical and clinical sciences
Abstract

Eukaryotic translation is tightly regulated to ensure that protein production occurs at the right time and place. Recent studies on abnormal repeat proteins, especially in age-dependent neurodegenerative diseases caused by nucleotide repeat expansion, have highlighted or identified two forms of unconventional translation initiation: usage of AUG-like sites (near cognates) or repeat-associated non-AUG (RAN) translation. We discuss how repeat proteins may differ due to not just unconventional initiation, but also ribosomal frameshifting and/or imperfect repeat DNA replication, expansion, and repair, and we highlight how research on translation of repeats may uncover insights into the biology of translation and its contribution to disease.

Published
2017

6. Gld2-catalyzed 3′ monoadenylation of miRNAs in the hippocampus has no detectable effect on their stability or on animal behavior

Author

Mansur, Fernanda, Ivshina, Maria, Gu, Weifeng, Schaevitz, Laura, Stackpole, Emily, Gujja, Sharvari, Edwards, Yvonne JK, and Richter, Joel D

Subjects
Biochemistry and Cell Biology, Biological Sciences, Neurosciences, Genetics, Biotechnology, Animals, Behavior, Animal, Hippocampus, Male, Mice, Mice, Inbred C57BL, MicroRNAs, Polynucleotide Adenylyltransferase, RNA 3' End Processing, RNA Stability, Gld2, miRNA, monoadenylation, hippocampus, behavior, Developmental Biology, Biochemistry and cell biology
Abstract

Gld2, a noncanonical cytoplasmic poly(A) polymerase, interacts with the RNA binding protein CPEB1 to mediate polyadenylation-induced translation in dendrites of cultured hippocampal neurons. Depletion of Gld2 from the hippocampus leads to a deficit in long-term potentiation evoked by theta burst stimulation. At least in mouse liver and human primary fibroblasts, Gld2 also 3' monoadenylates and thereby stabilizes specific miRNAs, which enhance mRNA translational silencing and eventual destruction. These results suggest that Gld2 would be likely to monoadenylate and stabilize miRNAs in the hippocampus, which would produce measurable changes in animal behavior. We now report that using Gld2 knockout mice, there are detectable alterations in specific miRNA monoadenylation in the hippocampus when compared to wild type, but that these modifications produce no detectable effect on miRNA stability. Moreover, we surprisingly find no overt change in animal behavior when comparing Gld2 knockout to wild-type mice. These data indicate that miRNA monoadenylation-mediated stability is cell type-specific and that monoadenylation has no measurable effect on higher cognitive function.

Published
2016

10. FMRP deficiency leads to multifactorial dysregulation of splicing and mislocalization of MBNL1 to the cytoplasm.

Author

Jung, Suna, Shah, Sneha, Han, Geongoo, and Richter, Joel D.

Subjects
FRAGILE X syndrome, RNA-binding proteins, CYTOPLASM, KNOCKOUT mice, RNA splicing
Abstract

Fragile X syndrome (FXS) is a neurodevelopmental disorder that is often modeled in Fmr1 knockout mice where the RNA-binding protein FMRP is absent. Here, we show that in Fmr1-deficient mice, RNA mis-splicing occurs in several brain regions and peripheral tissues. To assess molecular mechanisms of splicing mis-regulation, we employed N2A cells depleted of Fmr1. In the absence of FMRP, RNA-specific exon skipping events are linked to the splicing factors hnRNPF, PTBP1, and MBNL1. FMRP regulates the translation of Mbnl1 mRNA as well as Mbnl1 RNA auto-splicing. Elevated Mbnl1 auto-splicing in FMRP-deficient cells results in the loss of a nuclear localization signal (NLS)-containing exon. This in turn alters the nucleus-to-cytoplasm ratio of MBNL1. This redistribution of MBNL1 isoforms in Fmr1-deficient cells could result in downstream splicing changes in other RNAs. Indeed, further investigation revealed that splicing disruptions resulting from Fmr1 depletion could be rescued by overexpression of nuclear MBNL1. Altered Mbnl1 auto-splicing also occurs in human FXS postmortem brain. These data suggest that FMRP-controlled translation and RNA processing may cascade into a general dys-regulation of splicing in Fmr1-deficient cells. This study shows that RNA splicing is widely dysregulated in FMRP-deficient mouse tissues and cells and involves multiple splicing factors, including MBNL1. In FMRP-depleted cells, Mbnl1 RNA is mis-spliced, resulting in improper cytoplasmic localization of MBNL1, which in turn causes impairment of further RNAs. [ABSTRACT FROM AUTHOR]

Published
2023
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15. Reduced Extinction of Hippocampal-Dependent Memories in CPEB Knockout Mice

Author

Zearfoss, N. Ruth, Richter, Joel D., and Berger-Sweeney, Joanne

Abstract

CPEB is a sequence-specific RNA binding protein that regulates translation at synapses. In neurons of CPEB knockout mice, synaptic efficacy is reduced. Here, we have performed a battery of behavioral tests and find that relative to wild-type animals, CPEB knockout mice, although similar on many baseline behaviors, have reduced extinction of memories on two hippocampal-dependent tasks. A corresponding microarray analysis reveals that about 0.14% of hippocampal genes have an altered expression in the CPEB knockout mouse. These data suggest that CPEB-dependent local protein synthesis may be an important cellular mechanism underlying extinction of hippocampal-dependent memories. (Contains 2 tables and 1 figure.)

Published
2006
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25. Genetic and acute CPEB1 depletion ameliorate fragile X pathophysiology

Author

Udagawa, Tsuyoshi, Farny, Natalie G., Jakovcevski, Mira, Kaphzan, Hanoch, Alarcon, Juan Marcos, Anilkumar, Shobha, Ivshina, Maria, Hurt, Jessica A., Nagaoka, Kentaro, Nalavadi, Vijayalaxmi C., Lorenz, Lori J., Bassell, Gary J., Akbarian, Schahram, Chattarji, Sumantra, Klann, Eric, and Richter, Joel D.

Subjects
Fragile X syndrome -- Genetic aspects, Genetic translation -- Research, Physiology, Pathological -- Research, Biological sciences, Health
Abstract

Fragile X syndrome (FXS), the most common cause of inherited mental retardation and autism, is caused by transcriptional silencing of FMR1, which encodes the translational repressor fragile X mental retardation [...]

Published
2013
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26. CPEB and two poly(A) polymerases control miR-122 stability and p53 mRNA translation

Author

Burns, David M., D'Ambrogio, Andrea, Nottrott, Stephanie, and Richter, Joel D.

Subjects
Binding proteins -- Genetic aspects -- Physiological aspects, Fibroblasts -- Genetic aspects, Polymerase chain reaction -- Genetic aspects, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Cytoplasmic polyadenylation-induced translation controls germ cell development (1,2), neuronal synaptic plasticity (3-5) and cellular senescence (6,7), a tumour-suppressor mechanism that limits the replicative lifespan of cells (8,9). The cytoplasmic polyadenylation element binding protein (CPEB) promotes polyadenylation by nucleating a group of factors including defective in germline development 2 (Gld2), a non-canonical poly(A) polymerase (10-12), on specific messenger RNA (mRNA) 3' untranslated regions (UTRs). Because CPEB regulation of p53 mRNA polyadenylation/translation is necessary for cellular senescence in primary human diploid fibroblasts (6), we surmised that Gld2 would be the enzyme responsible for poly(A) addition. Here we show that depletion of Gld2 surprisingly promotes rather than inhibits p53 mRNA polyadenylation/translation, induces premature senescence and enhances the stability of CPEBmRNA. The CPEB3' UTR contains two miR-122 binding sites, which when deleted, elevate mRNA translation, as does an antagomir of miR-122. Although miR-122 is thought to be liver specific, it is present in primary fibroblasts and destabilized by Gld2 depletion. Gld4, a second non-canonical poly(A) polymerase, was found to regulate p53 mRNA polyadenylation/translation in a CPEB-dependent manner. Thus, translational regulation of p53 mRNA and cellular senescence is coordinated by Gld2/miR-122/CPEB/Gld4., Mouse embryo fibroblasts (MEFs) derived from CPEB knockout mice do not senesce as do MEFs derived from wild-type mice, but instead are immortal. Senescence is rescued when ectopic CPEB is [...]

Published
2011
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27. Additional file 1 of Ribosome profiling in mouse hippocampus: plasticity-induced regulation and bidirectional control by TSC2 and FMRP

Author

Hien, Annie, Molinaro, Gemma, Botao Liu, Huber, Kimberly M., and Richter, Joel D.

Abstract

Additional file 1: Fig. S1. Validation of differential expression results from Tsc2+/− versus wild type from Fig. 1. Histogram of the number of differentially expressed genes called from 4990 random permutations of sample labels for the genotype comparison from a RNA-seq and b ribosome profiling. Fig. S2. a Density plot of the length (left) and minimal free energy (MFE) (right) of the 5′UTR of Down and Up RPFs in Tsc2+/− compared to all mRNAs. ns nonsignificant, Wilcoxon rank-sum test with correction by Bonferroni method. b The ratios of phosphorylated/total mTOR, rpS6, and 4EBP1 as determined by western blots of whole hippocampal lysates are unchanged in Tsc2+/− mice as compared to wild-type littermates (n = 13–15 mice/genotype, ns non-significant, unpaired t test). c Total levels of RPL4, RPS25, and LARP1 from hippocampus of wild-type and Tsc2+/− littermates (n = 13–15 mice/genotype, ns = nonsignificant, unpaired t test). d Pearson correlation coefficient was computed for pairs of transcript features including translation efficiency (TE), coding length, and GC content (CDS), 5′ untranslated region length and GC content (5′UTR), 3′ untranslated region length and GC content (3′UTR), and RNA abundance (TPM, transcripts per million). Red indicates a positive correlation, and blue a negative correlation. Gray indicates a correlation of identical parameters. p

Published
2020
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29. CPEB: a life in translation

Author

Richter, Joel D.

Subjects
Oocytes -- Analysis, Cytoplasm -- Analysis, Binding proteins -- Chemical properties, Biochemistry -- Research, Biological sciences, Chemistry
Abstract

Nearly two decades ago, Xenopus oocytes were found to contain mRNAs harboring a small sequence in their 3' untranslated regions that control cytoplasmic polyadenylation and translational activation during development. This cytoplasmic polyadenylation element (CPE) is the binding platform for CPE-binding protein (CPEB), which promotes polyadenylation-induced translation. Since then, the biochemistry and biology of CPEB has grown rather substantially: mechanistically, CPEB nucleates a complex of factors that regulates poly(A) elongation through, of all things, a deadenylating enzyme; biologically, CPEB mediates many processes including germ-cell development, cell division and cellular senescence, and synaptic plasticity and learning and memory. These observations underscore the growing complexities of CPEB involvement in cell function.

Published
2007

30. Regulation of cap-dependent translation by eIF4E inhibitory proteins

Author

Richter, Joel D. and Sonenberg, Nahum

Subjects
Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Author(s): Joel D. Richter (corresponding author) [1]; Nahum Sonenberg [2] A single cell never exploits the full panoply of gene products available for its use; at any one time, the [...]

Published
2005
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37. Translational control of the embryonic cell cycle

Author

Groisman, Irina, Jung, Mi-Young, Sarkissian, Madathia, Cao, Quiping, and Richter, Joel D.

Subjects
Cell research -- Analysis, Genetic translation -- Physiological aspects, Cell cycle -- Genetic aspects, Messenger RNA -- Genetic aspects, Eukaryotic cells -- Genetic aspects, Biological sciences
Abstract

Research has been conducted on the cell cycle progression regulated by the cyclin B translation level. Results demonstrate the importance of cyclin B1 mRNA translation for the embryonic cell cycle.

Published
2002

43. CPEB, maskin, and cyclin B1 mRNA at the mitotic apparatus: implications for local translational control of cell division

Author

Groisman, Irina, Huang, Yi-Shulan, Mendez, Raul, Cao, Quiping, Theurkauf, William, and Richter, Joel D.

Subjects
Xenopus -- Genetic aspects, Cell division -- Research, Developmental cytology -- Research, Oogenesis -- Physiological aspects, Biological sciences
Abstract

CPEB, maskin, and cyclin B1 mRNA have been studied as they relate to the mitotic apparatus, and implications for local translational control of cell division considered. Two mRNAs, Xbub3 and cyclin B1, have been seen to localize with or near CPEB and maskin on spindles and centrosomes in Xenopus embryos. These and other findings indicate that the CPEB-regulated mRNA translation is important for the integrity of the mitotic apparatus and for cell division.

Published
2000

44. Phosphorylation of CPE binding factor by Eg2 regulates translation of c-mos mRNA

Author

Mendez, Raul, Hake, Laura E., Andresson, Thorkell, Littlepage, Laurie E., Ruderman, Joan V., and Richter, Joel D.

Subjects
Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Author(s): Raul Mendez [1]; Laura E. Hake [1, 2]; Thorkell Andresson [3]; Laurie E. Littlepage [3]; Joan V. Ruderman [3]; Joel D. Richter (corresponding author) [1] Full-grown Xenopus oocytes arrest [...]

Published
2000
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45. Genetic Rescue of Fragile X Syndrome Links FMRP Deficiency to Codon Optimality-Dependent RNA Destabilization

Author

Shu, Huan, Donnard, Elisa, Liu, Botao, and Richter, Joel D.

Subjects
congenital, hereditary, and neonatal diseases and abnormalities, nervous system diseases
Abstract

Fragile X syndrome (FXS) is caused by inactivation of FMR1 gene and loss of its encoded product the RNA binding protein FMRP, which generally represses translation of its target transcripts in the brain. In mouse models of FXS (i.e., Fmr1 knockout animals; Fmr1 KO), deletion of Cpeb1 , which encodes a translational activator, mitigates nearly all pathophysiologies associated with the disorder. Here we reveal unexpected wide-spread dys-regulation of RNA abundance in Fmr1 KO brain cortex and its rescue to normal levels in Fmr1/Cpeb1 double KO mice. Alteration and restoration of RNA levels are the dominant molecular events that drive the observed dys-regulation and rescue of translation as measured by whole transcriptome ribosome occupany in the brain. The RNAs down-regulated and rescued in these animal models are highly enriched for FMRP binding targets and have an optimal codon bias that would predict their stability in wild type and possible instability in FMRP knock-out brain. Indeed, whole transcriptome analysis of RNA metabolic rates demonstrates a codon optimality-dependent elevation of RNA destruction in FMRP knock-out cortical neurons. This elevated RNA destruction leads to a massive reshuffling of the identities of stabilizing versus destabilizing codons in neurons upon loss of FMRP. Our results show a widespread RNA instability in FXS, which results from the uncoupling of codon optimality, ribosome occupancy, and RNA degradation mechanisms. Re-establishment of the linkage among these events is likely required by the genetic rescue of the disorder.

Published
2019
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47. Contributors

Author

Abrams, John M., primary, Adelman, John P., additional, Alcorn, Joseph L., additional, Alessi, Dario R., additional, Alexov, Emil, additional, Alford, Simon, additional, Alitalo, Kari, additional, Allison, James P., additional, Almo, Steven C., additional, Alory, Christelle, additional, Al-Shamkhani, Aymen, additional, Amundson, Sally A., additional, Anderson, Carl W., additional, Andersen, Jannik N., additional, Angel, Peter, additional, Appella, Ettore, additional, Arendshorst, William J., additional, Arkinstall, Steve, additional, Audhya, Anjon, additional, Avruch, Joseph, additional, Bader, Gary D., additional, Bagala, Cinzia, additional, Balch, William E., additional, Balsinde, Jesus, additional, Banerjee, Utpal, additional, Barford, David, additional, Bar-Sagi, Dafna, additional, Bartlett, Perry F., additional, Bastiaens, Philippe I.H., additional, Battelli, Chiara, additional, Baudhuin, Linnea M., additional, Beavil, Andrew J., additional, Beavil, Rebecca L., additional, Beavo, Joseph A., additional, Bello-Reuss, Elsa, additional, Bellum, Stephen, additional, Belmonte, Juan Carlos Izpisúa, additional, Bennett, Craig B., additional, Benovic, Jeffrey L., additional, Berridge, Michael J., additional, Beuning, Penny J., additional, Bhandari, Rashna, additional, Bhattacharya, Ananya, additional, Biel, Martin, additional, Bielinski, Vincent A., additional, Bilak, Hana, additional, Birnbaumer, Lutz, additional, Birrell, Geoff, additional, Bishop, Gail A., additional, Blackmer, Trillium, additional, Blackshear, Perry J., additional, Blattner, Christine, additional, Blaustein, Mordecai P., additional, Bokoch, Gary M., additional, Bonewald, Lynda F., additional, Bonomi, Marco, additional, Booden, Michelle A., additional, Boone, Charles, additional, Bootman, Martin D., additional, Bos, Johannes L., additional, Bradbury, Jane M., additional, Bradshaw, Ralph A., additional, Bresnick, Anne R., additional, Brevnova, Lena, additional, Brinkworth, Ross I., additional, Brown, Michael S., additional, Brown, Steven A., additional, Brunet, Anne, additional, Bucki, Robert, additional, Burgoyne, Robert D., additional, Buss, Janice E., additional, Butow, Ronald A., additional, Capdevila, Javier, additional, Carafoli, Ernesto, additional, Carlson, Cathrine R., additional, Carpenter, Graham, additional, Carrillo, Juan J., additional, Casey, Patrick J., additional, Catterall, William A., additional, Cerione, Richard A., additional, Cesareni, Gianni, additional, Chan, Andrew C., additional, Chang, Geoffrey, additional, Chao, Moses V., additional, Charbonneau, Harry, additional, Chen, Philip, additional, Cheng, Alan, additional, Chiu, Chris, additional, Chow, Dar-chone, additional, Chrisman, Ted D., additional, Christensen, Anne Elisabeth, additional, Chung, Jee Y., additional, Churchill, Grant C., additional, Ciechanover, Aaron, additional, Cingolani, Gino, additional, Claeysen, Sylvie, additional, Closset, Jean, additional, Cockcroft, Shamshad, additional, Cohen, Patricia T.W., additional, Cohen, Philip, additional, Colbran, Roger J., additional, Comstock, Clay E.S., additional, Conti, Marco, additional, Corbin, Jackie D., additional, Corda, Daniela, additional, Costagliola, Sabine, additional, Cote, Rick H., additional, Coughlin, Shaun R., additional, Cowart, L. Ashley, additional, Cox, Adrienne D., additional, Cragg, Mark S., additional, Crespo, José L., additional, Crosio, Claudia, additional, Daly, Christopher, additional, Damak, Sami, additional, Dasso, Mary, additional, David, Michael, additional, Davis, Anthony J., additional, Davis, Roger J., additional, Day, Richard N., additional, Degerman, Eva, additional, DeLano, Warren L., additional, Dell'Acqua, Mark L., additional, Délot, Emmanuèle, additional, Demple, Bruce, additional, Dennis, Edward A., additional, Denu, John M., additional, DePaoli-Roach, Anna A., additional, Der, Channing J., additional, de Rooij, Johan, additional, de Sauvage, Frederic, additional, Devreotes, Peter N., additional, Dewaste, Valérie, additional, Dickson, Robert B., additional, Diebold, Becky A., additional, Fiori, Pier Paolo Di, additional, Girolamo, Maria Di, additional, Diplexcito, Julie, additional, Dixon, Jack E., additional, Doms, Robert W., additional, Donoghue, Daniel J., additional, Doolittle, Russell F., additional, Døskeland, Stein Ove, additional, Dostmann, Wolfgang R.G., additional, Dreyer, Matthias K., additional, Du, Guo Guang, additional, Du, Keyong, additional, Duchen, Michael R., additional, Dunphy, William G., additional, Durgan, Joanne, additional, Dustin, Michael L., additional, Edwards, Peter A., additional, Egen, Jackson G., additional, Eiden, Lee E., additional, Elion, Elaine A., additional, Emr, Scott, additional, Engelhardt, Othmar G., additional, Erneux, Christophe, additional, Espenshade, Peter J., additional, Esplin, Edward D., additional, Evers, B. Mark, additional, Eyles, Joanne L., additional, Fame, Sheelagh, additional, Farquhar, Marilyn, additional, Feil, Robert, additional, Feng, Gui-Jie, additional, Fields, Stanley, additional, Fiordalisi, James J., additional, Firtel, Richard A., additional, Fitzgerald, Garret A., additional, Flint, Andrew, additional, Foiani, Marco, additional, Forman, Barry Marc, additional, Fornace, Albert J., additional, Francis, Sharron H., additional, Fritz, Günter, additional, Fruman, David A., additional, Galione, Antony, additional, Gandhi, Chris S., additional, Garbers, David L., additional, Garcia, K. Christopher, additional, Geiger, Benjamin, additional, Gerace, Larry, additional, Gerstner, Andrea, additional, Giaccia, Amato J., additional, Giannattasio, Michele, additional, Giguère, Vincent, additional, Glass, Christopher K., additional, Glennie, Martin J., additional, Glick, Jennifer L., additional, Goldstein, Joseph L., additional, Gopal, Venkatesh, additional, Gorospe, Myriam, additional, Govaerts, Cedric, additional, Graves, Paul R., additional, Gray, Patrick W., additional, Graziani, Irene, additional, Green, Douglas R., additional, Greenberg, Michael E., additional, Greenwald, Iva, additional, Gu, Haihua, additional, Gueven, Nuri, additional, Gutkind, J. Silvio, additional, Haeggström, Jesper Z., additional, Hall, Alan, additional, Hall, Michael N., additional, Haller, Otto, additional, Hamm, Heidi E., additional, Hannun, Yusef A., additional, Hansen, Carl A., additional, Harden, T. Kendall, additional, Hardie, D. Grahame, additional, Hasegawa, Kiminori, additional, Hawkins, Phillip T., additional, Haystead, Timothy A.J., additional, He, Xiao-lin, additional, Heizmann, Claus W., additional, Heldin, Carl-Henrik, additional, Hermiston, Michelle L., additional, Herrlich, Peter, additional, Hewat, Elizabeth A., additional, Hille, Bertil, additional, Hilton, Douglas J., additional, Hinchliffe, K.A., additional, Ho, Steffan N., additional, Ho, Su-Chin, additional, Hochstrasser, Mark, additional, Hofmann, Franz, additional, Hogue, Christopher W., additional, Hol, Wim G.J., additional, Holash, Jocelyn, additional, Holmgren, Robert A., additional, Honig, Barry, additional, Hostager, Bruce S., additional, Hubbard, Stevan R., additional, Huber, Michael, additional, Hunter, Tony, additional, Huttenlocher, Anna, additional, Hymowitz, Sarah G., additional, Ihle, James N., additional, Imler, Jean-Luc, additional, Irvine, R.F., additional, Isacoff, Ehud Y., additional, Iturrioz, Xavier, additional, Iversen, Lars F., additional, Iyengar, Ravi, additional, Jackson, Stephen P., additional, Jan, Lily Yeh, additional, Janiak-Spens, Fabiola, additional, Janmey, Paul A., additional, Jansen, Peter Gildsig, additional, Jarriault, Sophie, additional, Javitch, Jonathan A., additional, Jensen, Elwood V., additional, Jepsen, Kristen, additional, Jones, E. Yvonne, additional, Jones, Katherine A., additional, Jordan, J. Dedrick, additional, Joseph, Jomon, additional, Justement, Louis B., additional, Kafri, Yariv, additional, Kahn, Richard A., additional, Kang, Shin W., additional, Karlin, Arthur, additional, Kast-Woelbern, Heidi R., additional, Kaufman, Randal J., additional, Kazlauskas, Andrius, additional, Keen, James H., additional, Kemler, Rolf, additional, Kemp, Bruce E., additional, Kennedy, Mary B., additional, Kennedy, Matthew A., additional, Kikkawa, Ushio, additional, Kim, Albert H., additional, Kim, Soo-A, additional, Kim, Sung-Hou, additional, Kim, Youngjoo, additional, King-Jones, Kirst, additional, Kintner, Chris, additional, Kivimäe, Saul, additional, Klee, Claude B., additional, Klein, Rüdiger, additional, Kleppisch, Thomas, additional, Kliewer, Steven A., additional, Klinghoffer, Richard A., additional, Knoblich, Juergen A., additional, Kobe, Bostjan, additional, Kochs, George, additional, Kong-Beltran, Monica, additional, König, Rolf, additional, Koong, Albert C., additional, Korc, Murray, additional, Kornitzer, Daniel, additional, Kossiakoff, Anthony A., additional, Kotera, Jun, additional, Kovalenko, M.V., additional, Kozasa, Tohru, additional, Kozlov, Sergei, additional, Kozminski, Keith G., additional, Krugmann, Sonja, additional, Kuriyan, John, additional, Kurokawa, Riki, additional, Kwong, Peter D., additional, Lai, Wi S., additional, Lamar, Elise, additional, Lambert, Millard H., additional, Lambright, David G., additional, Lancet, Doron, additional, Landry, Reiko, additional, Langdon, Wallace Y., additional, Langeberg, Lorene K., additional, Lasko, Paul, additional, Latham, Vaughn, additional, Lavin, Martin F., additional, Lease, Kevin A., additional, Leffler, Hakon, additional, Lemmon, Mark A., additional, Leonard, Ann E., additional, Levitzki, Alexander, additional, Liao, Hong-Jun, additional, Liaw, Lucy, additional, Liberi, Giordano, additional, Lickert, Heiko, additional, Liddington, Robert C., additional, Lincoln, Thomas M., additional, Linder, Jürgen U., additional, Linder, Maurine E., additional, Liu, Hui, additional, Liu, Zhengchang, additional, Lohela, Marja K., additional, Louie, Sarah H., additional, Luttrell, Deirdre K., additional, Luttrell, Louis M., additional, Lyons, Karen M., additional, Macaulay, S. Lance, additional, Maceyka, Michael, additional, Maciag, Thomas, additional, Macian, Fernando, additional, MacKintosh, Carol, additional, MacLennan, David H., additional, Mahmood, Nadir A., additional, Malbon, Craig C., additional, Malik, Sohail, additional, Man, Orna, additional, Manahan, Carol L., additional, Mandinova, Anna, additional, Manganiello, Vincent C., additional, Manley, James L., additional, Mann, Matthias, additional, Manning, Gerald, additional, Manser, Ed, additional, Margeta-Mitrovic, Marta, additional, Margolskee, Robert F., additional, Marinissen, Julia, additional, Mariuzza, Roy A., additional, Marmor, Mina D., additional, Martin, G. Steven, additional, Martin, Karen H., additional, Martinez, Sergio E., additional, Mathews, Michael B., additional, Mayer, Bruce J., additional, Mayer, Mark L., additional, Mazzoni, Maria R., additional, McCormick, Frank, additional, McGowan, Clare H., additional, McKay, Melissa M., additional, McKeehan, Wallace L., additional, McLean, Alison J., additional, Means, Anthony R., additional, Meili, Ruedi, additional, Meng, Jingwei, additional, Merchant, Mark, additional, Mercurio, Frank, additional, Milligan, Graeme, additional, Ming, Guo-Li, additional, Minor, Daniel L., additional, Moghal, Nadeem, additional, Møller, Neils Peter H., additional, Mongillo, Marco, additional, Montminy, Marc, additional, Moon, Randall T., additional, Morimoto, Richard I., additional, Moss, Stephen E., additional, Mott, Helen R., additional, Mouta, Carla, additional, Muda, Marco, additional, Mumby, Marc C., additional, Murphy, Gretchen A., additional, Muzi-Falconi, Marco, additional, Nagaraj, Raghavendra, additional, Nahorski, Stefan R., additional, Nairn, Angus C., additional, Nash, Piers, additional, Neel, Benjamin G., additional, Newton, Alexandra C., additional, Nishizuka, Yasutomi, additional, Noel, Joseph P., additional, Nollen, Ellen A.A., additional, Nooren, Irene M.A., additional, O'Connor, Rodney, additional, Offermanns, Stefan, additional, Olender, Tsviya, additional, Ong, Shao-En, additional, Owen, Darerca, additional, Pagliari, Lisa J., additional, Pao, Lily, additional, Papaconstantinou, John, additional, Pardo, Leonardo, additional, Park, Hay-Oak, additional, Park, Young Chul, additional, Parker, Peter J., additional, Parsons, J. Thomas, additional, Passner, J.M., additional, Pawson, Tony, additional, Pelliccioli, Achille, additional, Perez-Polo, J. Regino, additional, Perrimon, Norbert, additional, Petite, Fabrice G., additional, Petroulakis, Emmanuel, additional, Pfaff, Samuel L., additional, Piehler, Jacob, additional, Pike, Linda J., additional, Pinkoski, Michael J., additional, Pixley, Fiona J., additional, Plevani, Paolo, additional, Poo, Mu-ming, additional, Pozzan, Tullioi, additional, Prescott, Stephen M., additional, Prudovsky, Igor, additional, Putney, James W., additional, Radimerski, Thomas, additional, Radzio-Andzelm, Elzbieta, additional, Ram, Prahlad T., additional, Rameh, Lucia, additional, Ramljak, Danica, additional, Ranscht, Barbara, additional, Rao, Anjana, additional, Raport, Carol J., additional, Reeves, Jacqueline D., additional, Rehman, Holger, additional, Reichman, Trevor W., additional, Reiter, Eric, additional, Resnick, Michael A., additional, Reth, Michael, additional, Rhee, Sue Goo, additional, Richter, Joel D., additional, Rietze, Rodney L., additional, Rini, James M., additional, Ripperger, Jürgen A., additional, Rizo, Josep, additional, Robishaw, Janet D., additional, Roderick, H. Llewelyn, additional, Roeder, Robert G., additional, Rohrschneider, Larry R., additional, Ron, David, additional, Rosenfeld, Michael G., additional, Rosenfeldt, Hans, additional, Rossman, Kent L., additional, Roth, Christopher B., additional, Rudolph, Markus G., additional, Ruppelt, Anja, additional, Saez, Lino, additional, Sakmar, Thomas P., additional, Salvesen, Guy S., additional, Sassone-Corsi, Paolo, additional, Saxe, Charles L., additional, Schäfer, Beat W., additional, Schibler, Ueli, additional, Schindler, Christian W., additional, Schmelzle, Tobias, additional, Schmid, Sandra L., additional, Schmidt, Anja, additional, Schmidt, Eric F., additional, Schreiber, Gideon, additional, Schultz, Joachim E., additional, Schwaller, Beat, additional, Schwamborn, Klaus, additional, Schwartz, Thue, additional, Schwindinger, William F., additional, Scita, Giorgio, additional, Scott, John D., additional, Scott, Shaun, additional, Seebeck, Thomas, additional, Serhan, Charles N., additional, Shabb, John B., additional, Shaw, Andrey S., additional, Shears, Stephen B., additional, Shenolikar, Shirish, additional, Shi, Lei, additional, Shin, Chanseok, additional, Shiozaki, Kazuhiro, additional, Shokat, Kevan M., additional, Shuttleworth, Trevor J., additional, Siderovski, David P., additional, Siegelbaum, Steven A., additional, Silverstein, Adam M., additional, Singer, Robert H., additional, Skinner, Michael K., additional, Slack-Davis, Jill K., additional, Smerdon, Stephen J., additional, Smith, Graeme C.M., additional, Smits, Guillaume, additional, Smolik, Sarah M., additional, Smotrys, Jessica E., additional, Smyth, Emer M., additional, Snyder, Jason T., additional, Sogame, Naoko, additional, Soldi, Raffaella, additional, Sondek, John, additional, Sonenberg, Nahum, additional, Sonneberg, Erica Dutil, additional, Sparrow, Lindsay G., additional, Spiegel, Sarah, additional, Sprang, Stephen R., additional, Srivastava, Deepak, additional, Stanfield, Robyn L., additional, Stanley, E. 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Brad, additional, Thompson, Michael J., additional, Thornton, Janet M., additional, Thummel, Carl S., additional, Togashi, Hideaki, additional, Tong, Amy Hin Yan, additional, Tonks, Nicholas K., additional, Tontonoz, Peter, additional, Topham, M.K., additional, Torgersen, Knut Martin, additional, Tran, Hien, additional, Tremblay, Michel L., additional, Tsai, Ming-Jer, additional, Tsai, Sophia Y., additional, Tsunoda, Susan, additional, Turley, Stewart, additional, Tyson, Darren, additional, Van Etten, Robert L., additional, Vassart, Gilbert, additional, Verveer, Peter J., additional, Vlaeminck, Virginie, additional, de Vos, Abraham M., additional, Voss, Ty C., additional, Walczak, Robert, additional, Walker, Graham C., additional, Walker, John C., additional, Walter, Gernot, additional, Walter, Mark R., additional, Wang, Fen, additional, Wang, Jean Y.J., additional, Wang, Weiru, additional, Ward, Richard J., additional, Wedegaertner, Philip, additional, Wehrle, Christian, additional, Weiss, Arthur, additional, Weiss, Jamie L., additional, Wells, Alan, additional, Werner, Claudia, additional, West, Ann H., additional, Weston, Marie C., additional, Westwick, John K., additional, Wetterholm, Anders, additional, White, Morris F., additional, Whitman, Malcolm, additional, Whorton, Matt R., additional, Wiesmann, Christian, additional, Williams, Roger L., additional, Willis, William D., additional, Willson, Timothy M., additional, Wilson, Ian A., additional, Wiser, Ofer, additional, Wishart, Matthew J., additional, Wittinghofer, Alfred, additional, Woodgett, James R., additional, Worthylake, David K., additional, Wrana, Jeffrey L., additional, Wu, Hao, additional, Xiao, Yijin, additional, Xu, H. Eric, additional, Xu, Yan, additional, Xu, Zheng, additional, Yaffe, Michael B., additional, Yamada, Kenneth M., additional, Yang, Seun-Ah, additional, Yang, Wannian, additional, Yarden, Yosef, additional, Ye, Hong, additional, Ye, Weilan, additional, Yeates, Todd O., additional, Yin, Helen L., additional, York, John D., additional, Young, Edgar C., additional, Young, Kenneth W., additional, Young, Matthew A., additional, Young, Michael W., additional, Yu, Minmin, additional, Zaccai, Nathan R., additional, Zaccolo, Manuela, additional, Zamir, Eli, additional, von Zastrow, Mark, additional, Zhang, Chao, additional, Zhang, Xuewu, additional, Zhang, Zhong-Yin, additional, Zhou, Wenhong, additional, and Zoraghi, Roya, additional

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2003
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