Search Results - "Conicella, Alexander E"

ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain by Conicella, Alexander E., Zerze, Gül H., Mittal, Jeetain, Fawzi, Nicolas L.

“…RNA-binding protein TDP-43 mediates essential RNA processing but forms cytoplasmic neuronal inclusions via its C-terminal domain (CTD) in amyotrophic lateral…”
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Mechanistic View of hnRNPA2 Low-Complexity Domain Structure, Interactions, and Phase Separation Altered by Mutation and Arginine Methylation by Ryan, Veronica H., Dignon, Gregory L., Zerze, Gül H., Chabata, Charlene V., Silva, Rute, Conicella, Alexander E., Amaya, Joshua, Burke, Kathleen A., Mittal, Jeetain, Fawzi, Nicolas L.

“…hnRNPA2, a component of RNA-processing membraneless organelles, forms inclusions when mutated in a syndrome characterized by the degeneration of neurons…”
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A single N‐terminal phosphomimic disrupts TDP‐43 polymerization, phase separation, and RNA splicing by Wang, Ailin, Conicella, Alexander E, Schmidt, Hermann Broder, Martin, Erik W, Rhoads, Shannon N, Reeb, Ashley N, Nourse, Amanda, Ramirez Montero, Daniel, Ryan, Veronica H, Rohatgi, Rajat, Shewmaker, Frank, Naik, Mandar T, Mittag, Tanja, Ayala, Yuna M, Fawzi, Nicolas L

“…TDP‐43 is an RNA‐binding protein active in splicing that concentrates into membraneless ribonucleoprotein granules and forms aggregates in amyotrophic lateral…”
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The C‑Terminal Threonine of Aβ43 Nucleates Toxic Aggregation via Structural and Dynamical Changes in Monomers and Protofibrils by Conicella, Alexander E, Fawzi, Nicolas L

“…Recent studies suggest that deposition of amyloid β (Aβ) into oligomeric aggregates and fibrils, hallmarks of Alzheimer’s disease, may be initiated by the…”
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Differential Occupancy of Two GA-Binding Proteins Promotes Targeting of the Drosophila Dosage Compensation Complex to the Male X Chromosome by Kaye, Emily G., Booker, Matthew, Kurland, Jesse V., Conicella, Alexander E., Fawzi, Nicolas L., Bulyk, Martha L., Tolstorukov, Michael Y., Larschan, Erica

“…Little is known about how variation in sequence composition alters transcription factor occupancy to precisely recruit large transcription complexes. A key…”
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TDP-43 α-helical structure tunes liquid–liquid phase separation and function by Conicella, Alexander E., Dignon, Gregory L., Zerze, Gül H., Schmidt, Hermann Broder, D’Ordine, Alexandra M., Kim, Young C., Rohatgi, Rajat, Ayala, Yuna M., Mittal, Jeetain, Fawzi, Nicolas L.

“…Liquid–liquid phase separation (LLPS) is involved in the formation of membraneless organelles (MLOs) associated with RNA processing. The RNA-binding protein…”
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Phosphorylation of the FUS low‐complexity domain disrupts phase separation, aggregation, and toxicity by Monahan, Zachary, Ryan, Veronica H, Janke, Abigail M, Burke, Kathleen A, Rhoads, Shannon N, Zerze, Gül H, O'Meally, Robert, Dignon, Gregory L, Conicella, Alexander E, Zheng, Wenwei, Best, Robert B, Cole, Robert N, Mittal, Jeetain, Shewmaker, Frank, Fawzi, Nicolas L

“…Neuronal inclusions of aggregated RNA‐binding protein fused in sarcoma (FUS) are hallmarks of ALS and frontotemporal dementia subtypes. Intriguingly, FUS's…”
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Mice with endogenous TDP‐43 mutations exhibit gain of splicing function and characteristics of amyotrophic lateral sclerosis by Fratta, Pietro, Sivakumar, Prasanth, Humphrey, Jack, Lo, Kitty, Ricketts, Thomas, Oliveira, Hugo, Brito‐Armas, Jose M, Kalmar, Bernadett, Ule, Agnieszka, Yu, Yichao, Birsa, Nicol, Bodo, Cristian, Collins, Toby, Conicella, Alexander E, Mejia Maza, Alan, Marrero‐Gagliardi, Alessandro, Stewart, Michelle, Mianne, Joffrey, Corrochano, Silvia, Emmett, Warren, Codner, Gemma, Groves, Michael, Fukumura, Ryutaro, Gondo, Yoichi, Lythgoe, Mark, Pauws, Erwin, Peskett, Emma, Stanier, Philip, Teboul, Lydia, Hallegger, Martina, Calvo, Andrea, Chiò, Adriano, Isaacs, Adrian M, Fawzi, Nicolas L, Wang, Eric, Housman, David E, Baralle, Francisco, Greensmith, Linda, Buratti, Emanuele, Plagnol, Vincent, Fisher, Elizabeth MC, Acevedo‐Arozena, Abraham

“…TDP‐43 (encoded by the gene TARDBP ) is an RNA binding protein central to the pathogenesis of amyotrophic lateral sclerosis (ALS). However, how TARDBP…”
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An intrinsically disordered motif regulates the interaction between the p47 adaptor and the p97 AAA+ ATPase by Conicella, Alexander E., Huang, Rui, Ripstein, Zev A., Nguyen, Ai, Wang, Eric, Löhr, Thomas, Schuck, Peter, Vendruscolo, Michele, Rubinstein, John L., Kay, Lewis E.

“…VCP/p97, an enzyme critical to proteostasis, is regulated through interactions with protein adaptors targeting it to specific cellular tasks. One such adaptor,…”
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Lysines in the RNA Polymerase II C‑Terminal Domain Contribute to TAF15 Fibril Recruitment by Janke, Abigail M, Seo, Da Hee, Rahmanian, Vahid, Conicella, Alexander E, Mathews, Kaylee L, Burke, Kathleen A, Mittal, Jeetain, Fawzi, Nicolas L

“…Many cancer-causing chromosomal translocations result in transactivating protein products encoding FET family (FUS, EWSR1, TAF15) low-complexity (LC) domains…”
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Alpha-Helical Structure in TDP-43 Tunes Liquid-liquid Phase Separation and Cellular Function by Conicella, Alexander E., Dignon, Gregory, Zerze, Gül H., Schmidt, Broder, D'Ordine, Alexandra M., Kim, Youngchan, Rohatgi, Rajat, Ayala, Yuna M., Mittal, Jeetain, Fawzi, Nicolas L.

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ALS mutations disrupt phase separation mediated by -helical structure in the TDP-43 low complexity C-terminal domain by Conicella, Alexander E., Zerze, Gül H., Mittal, Jeetain, Fawzi, Nicolas L.

“…RNA-binding protein TDP-43 mediates essential RNA processing but forms cytoplasmic neuronal inclusions via its C-terminal domain (CTD) in amyotrophic lateral…”
Get full text

Mechanistic view of hnRNPA2 low complexity domain structure, interactions, and phase separation altered by disease mutation and arginine methylation by Ryan, Veronica H., Dignon, Gregory L., Zerze, Gul H., Chabata, Charlene V., Silva, Rute, Conicella, Alexander E., Amaya, Joshua, Burke, Kathleen A., Mittal, Jeetain, Fawzi, Nicolas L.

“…nRNPA2, a component of RNA processing membraneless organelles, forms inclusions when mutated in a syndrome characterized by degeneration of neurons (bearing…”
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Mechanistic View of hnRNPA2 Low-Complexity Domain Structure, Interactions, and Phase Separation Altered by Mutation and Arginine Methylation by Ryan, Veronica H., Dignon, Gregory L., Zerze, Gül H., Chabata, Charlene V., Silva, Rute, Conicella, Alexander E., Amaya, Joshua, Burke, Kathleen A., Mittal, Jeetain, Fawzi, Nicolas L.

“…hnRNPA2, a component of RNA-processing membraneless organelles, forms inclusions when mutatedin a syndrome characterized by the degeneration of neurons…”
Get full text

Phosphorylation of the FUS low‐complexity domain disrupts phase separation, aggregation, and toxicity by Monahan, Zachary, Ryan, Veronica H., Janke, Abigail M., Burke, Kathleen A., Rhoads, Shannon N., Zerze, Gül H., O'Meally, Robert, Dignon, Gregory L., Conicella, Alexander E., Zheng, Wenwei, Best, Robert B., Cole, Robert N., Mittal, Jeetain, Shewmaker, Frank, Fawzi, Nicolas L.

“…Neuronal inclusions of aggregated RNA-binding protein fused in sarcoma (FUS) are hallmarks of ALS and frontotemporal dementia subtypes. Intriguingly, FUS's…”
Get full text