Results 11 to 20 of about 59,959 (160)

Wild-type FUS corrects ALS-like disease induced by cytoplasmic mutant FUS through autoregulation [PDF]

, 2021
Mutations in FUS, an RNA-binding protein involved in multiple steps of RNA metabolism, are associated with the most severe forms of amyotrophic lateral sclerosis (ALS).
Sanjuan-Ruiz, Inmaculada, Inmaculada Sanjuan-Ruiz, Lee, Chao-Zong, Qiang Zhu, Noé Govea-Perez, da Cruz, Sandrine, Cleveland, Don, Megat, Salim, Dupuis, Luc, Sylvie Dirrig-Grosch, Melissa McAlonis-Downes, Chao-Zong Lee, Sandrine Da Cruz, Diana Piol, Govea-Perez, Noé, Salim Megat, Don W Cleveland, Dieterle, Stéphane, Stéphane Dieterle, Brian Myers, Dirrig-Grosch, Sylvie, Cleveland, Don W., Gina Picchiarelli, Lagier-Tourenne, Clotilde, Mcalonis-Downes, Melissa, Clotilde Lagier-Tourenne, Luc Dupuis, Piol, Diana, Zhu, Qiang, Picchiarelli, Gina, Myers, Brian, Cleveland, Don W   +31 more
core   +1 more source

Abl kinase-mediated FUS Tyr526 phosphorylation alters nucleocytoplasmic FUS localization in FTLD-FUS [PDF]

, 2023
Nuclear to cytoplasmic mislocalization and aggregation of multiple RNA-binding proteins (RBPs), including FUS, are the main neuropathological features of the majority of cases of amyotrophic lateral sclerosis (ALS) and frontotemporal lobular degeneration
Motaln, Helena, Urša Čerček, Čerček, Urša, Tripathi, Priyanka, Aronica, Eleonora, Alfred Yamoah, Yamoah, Alfred, Boris Rogelj, Goswami, Anand, Helena Motaln, Rogelj, Boris, Priyanka Tripathi, Anand Goswami, Eleonora Aronica   +13 more
core   +1 more source

FOB microscopy - HeLa P525L GFP-FUS

, 2021
Fluorescence, optical diffraction tomography and Brillouin microscopy data of HeLa P525L GFP-FUS cells under control conditions, after arsenite treatment, and after arsenite treatment and chemical fixation.
Jochen Guck (7429550), Raimund Schlüßler (10339790), Martin Nötzel (8065342), Kyoohyun Kim (9084287)   +3 more
core   +1 more source

FUS-SMN Protein Interactions Link the Motor Neuron Diseases ALS and SMA [PDF]

, 2012
Mutations in the RNA binding protein FUS cause amyotrophic lateral sclerosis (ALS), a fatal adult motor neuron disease. Decreased expression of SMN causes the fatal childhood motor neuron disorder spinal muscular atrophy (SMA).
Das, Rita, Maniatis, Tom, Sharma, A, Yan, Biao, Tapia, JC, Gygi, Steve P., Monica A. Carrasco, Shneider, NA, Nishimura, AL, Chen, Shi, Yu, Yong, Sharma, Aarti, Yan, B, Gygi, SP, Christopher E. Shaw, Yamazaki, T, Steve P. Gygi, Siddharthan Chandran, Reed, Robin, Yu, Y, Aarti Sharma, Reed, R, Yong Yu, Rita Das, Das, R, Carrasco, Monica A., Zhai, Bo, Shneider, Neil A., Chen, S, Juan C. Tapia, Tapia, Juan C., Agnes Lumi Nishimura, Lalancette-Hebert, Melanie, Haertlein, TC, Tom Maniatis, Lalancette-Hebert, M, Biao Yan, Carrasco, MA, Neil A. Shneider, Yamazaki, Tomohiro, Nishimura, Agnes Lumi, Sullivan, G, Maniatis, T, Shaw, Christopher E., Shi Chen, Zhai, B, Melanie Lalancette-Hebert, Sullivan, Gareth, Tyler C. Haertlein, Shaw, CE, Chandran, S, Haertlein, Tyler C., Tomohiro Yamazaki, Gareth Sullivan, Robin Reed, Bo Zhai, Chandran, Siddharthan, Sullivan, Gareth; id_orcid   +57 more
core   +1 more source

Effects of retro-nasal aroma release on satiation [PDF]

, 2008
It is suggested that the brain response of a food odour sensed retro-nasally is related to satiation. The extent of retro-nasal aroma release during consumption depends on the physical structure of a food, i.e.
Graaf, C., de, Westerterp-Plantenga, M., Ruijschop, R., Boelrijk, A.E., de Ru, J.A., Boelrijk, A.E.M., de Graaf, C., Ru, J.A., de, Ruijschop, R.M., Westerterp-Plantenga, M.S.   +9 more
core   +1 more source

The Effect of Retro-Cueing on an ERP Marker of VSTM Maintenance [PDF]

, 2009
Previous research has found that Contralateral Delay Activity (CDA) is correlated with the number of items maintained in Visual Short Term Memory from one visual field (VF) (Vogel & Machizawa, 2004).
Alexandra M. Murray, Anna C. Nobre, Bo-Cheng Kuo, Mark G. Stokes   +3 more
core   +1 more source

Solid state NMR spectra of FUS-LC-C, FUS-LC-N, and FUS-LC fibrils

, 2020
2D NCACX and C-C solid state NMR spectra of fibrils formed by the 214-residue low-complexity domain of the FUS protein (FUS-LC), by residues 111-214 (FUS-LC-C), and by residues 2-108 (FUS-LC-N). All samples were uniformly 15N and 13C labeled.
Tycko, R (via Mendeley Data), Tycko, Robert   +1 more
core   +1 more source

FUS ALS-causative mutations impair FUS autoregulation and splicing factor networks through intron retention [PDF]

, 2020
Mutations in the RNA-binding protein FUS cause amyotrophic lateral sclerosis (ALS), a devastating neurodegenerative disease. FUS plays a role in numerous aspects of RNA metabolism, including mRNA splicing.
Jarvis, S, Garone, MG, Jack Humphrey, Eberle, Andrea B, Fisher, Elizabeth M. C., Seth Jarvis, Carmelo Milioto, David Robaldo, Gianni Soraru, Plagnol, Vincent, Schiavo, G, Kräuchi, R, Robaldo, David, Bozzoni, I, Brown, Anna-Leigh, McLaughlin, Martha, Devoy, Anny, Devoy, A, Fisher, EMC, Alessandro Rosa, Pietro Fratta, Fratta, Pietro, Bozzoni, Irene, Humphrey, Jack, Garone, Maria G., Rosa, A, Nicol Birsa, Humphrey, J, Fratta, P, Giampietro Schiavo, Irene Bozzoni, Isaacs, Adrian M, Vincent Plagnol, Plagnol, V, Garone, Maria G, Brown, A-L, Schiavo, Giampietro, Ule, Agnieszka M, Soraru, G, Cristian Bodo, Birsa, Nicol, Ule, Agnieszka M., Soraru, Gianni, Birsa, N, Marc-David Ruepp, Rosa, Alessandro, Milioto, C, Ule, AM, Martha McLaughlin, Adrian M Isaacs, McLaughlin, M, Mühlemann, Oliver, Ruepp, M-D, Jarvis, Seth, Fisher, Elizabeth M C, Andrea B Eberle, Eberle, Andrea B., Kräuchi, Rahel, Oliver Mühlemann, Bodo, Cristian, Rahel Kräuchi, Isaacs, Adrian M., Matthew Bentham, Ruepp, Marc-David, Bentham, M, Isaacs, AM, Bodo, C, Agnieszka M Ule, Elizabeth M C Fisher, Bentham, Matthew, Eberle, AB, Robaldo, D, Anna-Leigh Brown, Milioto, Carmelo, Mühlemann, O, Maria G Garone, Anny Devoy, Humphrey J, Eberle AB, Isaacs AM, Robaldo D, Bodo C, McLaughlin M, Devoy A, Garone MG, Schiavo G, Soraru G, Kräuchi R, Birsa N, Mühlemann O, Ruepp MD, Plagnol V, Milioto C, Fisher EMC, Jarvis S, Bozzoni I, Bentham M, Brown AL, Fratta P, Ule AM, Rosa A   +100 more
core   +2 more sources

Mutant p53R273H disrupts PDPK1 homodimerization and contributes to PDPK1 activation

Molecular Oncology, EarlyView.
How mutant p53R273H drives AKT signaling is unclear. We show that p53R273H, but not wild‐type, directly binds PDPK1 via a mutation‐dependent conformational change. This interaction disrupts inhibitory PDPK1 homodimerization and enhances AKT phosphorylation.
Mei Chee Lim, Alvin Kunyao Guo, Yoko Itahana, Srinivasaraghavan Kannan, Valerie Goh, Mingmin Ong, Terina Yan Wen Tay, Weiying Ye, Sabhashina Radha Krishnan, Jun Nishiyama, Chandra S Verma, Koji Itahana   +11 more
wiley   +1 more source

Delivery of DNA‐encoded vaccines and proteins in mice using cutaneous suction‐mediated transfection

FEBS Open Bio, EarlyView.
Cutaneous suction‐mediated transfection in mice for delivery of DNA‐encoded vaccines and proteins. A critical limitation of DNA vaccines and other therapeutics is transfection in vivo to produce the encoded antigens or therapeutic proteins. Cutaneous suction‐based methods have demonstrated effectiveness in many animal models and have been successfully ...
Emran O. Lallow, Isabel Brandtjen, Yaxin Mo, Melissa Gulley, Louis Osorio, Sagar Kudchodkar, Nandita C. Jhumur, Christine C. Roberts, Lisa K. Denzin, David I. Shreiber, Biju Parekkadan, Hao Lin, Joel N. Maslow   +12 more
wiley   +1 more source