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Article ; Online: A fruitful endeavor: modeling ALS in the fruit fly.

Casci, Ian / Pandey, Udai Bhan

2014 Volume 1607, Page(s) 47–74

Abstract: For over a century Drosophila melanogaster, commonly known as the fruit fly, has been instrumental in genetics research and disease modeling. In more recent years, it has been a powerful tool for modeling and studying neurodegenerative diseases, ... ...

Abstract	For over a century Drosophila melanogaster, commonly known as the fruit fly, has been instrumental in genetics research and disease modeling. In more recent years, it has been a powerful tool for modeling and studying neurodegenerative diseases, including the devastating and fatal amyotrophic lateral sclerosis (ALS). The success of this model organism in ALS research comes from the availability of tools to manipulate gene/protein expression in a number of desired cell-types, and the subsequent recapitulation of cellular and molecular phenotypic features of the disease. Several Drosophila models have now been developed for studying the roles of ALS-associated genes in disease pathogenesis that allowed us to understand the molecular pathways that lead to motor neuron degeneration in ALS patients. Our primary goal in this review is to highlight the lessons we have learned using Drosophila models pertaining to ALS research. This article is part of a Special Issue entitled ALS complex pathogenesis.
MeSH term(s)	Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/physiopathology ; Animals ; Animals, Genetically Modified ; Disease Models, Animal ; Drosophila melanogaster/genetics ; Drosophila melanogaster/physiology ; Humans
Language	English
Publishing date	2014-10-05
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1200-2
ISSN	1872-6240 ; 0006-8993
ISSN (online)	1872-6240
ISSN	0006-8993
DOI	10.1016/j.brainres.2014.09.064
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Article ; Online: Unexpected exome sequencing result: de novo TRPS1 mutation in an infant with infantile scoliosis, mild developmental delay, and history of consanguinity.

Casci, Ian / Accousti, William / Lacassie, Yves

American journal of medical genetics. Part A

2014 Volume 164A, Issue 5, Page(s) 1334–1337

MeSH term(s)	Amino Acid Substitution ; Consanguinity ; DNA-Binding Proteins/genetics ; Developmental Disabilities/diagnosis ; Developmental Disabilities/genetics ; Exome ; Genetic Association Studies ; High-Throughput Nucleotide Sequencing ; Humans ; Incidental Findings ; Infant, Newborn ; Mutation ; Phenotype ; Scoliosis/diagnosis ; Scoliosis/genetics ; Syndrome ; Transcription Factors/genetics
Chemical Substances	DNA-Binding Proteins ; TRPS1 protein, human ; Transcription Factors
Language	English
Publishing date	2014-03-19
Publishing country	United States
Document type	Journal Article
ZDB-ID	1493479-6
ISSN	1552-4833 ; 1552-4825
ISSN (online)	1552-4833
ISSN	1552-4825
DOI	10.1002/ajmg.a.36430
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Article ; Online: Muscleblind acts as a modifier of FUS toxicity by modulating stress granule dynamics and SMN localization.

Nature communications

2019 Volume 10, Issue 1, Page(s) 5583

Abstract: Mutations in fused in sarcoma (FUS) lead to amyotrophic lateral sclerosis (ALS) with varying ages of onset, progression and severity. This suggests that unknown genetic factors contribute to disease pathogenesis. Here we show the identification of ... ...

Abstract	Mutations in fused in sarcoma (FUS) lead to amyotrophic lateral sclerosis (ALS) with varying ages of onset, progression and severity. This suggests that unknown genetic factors contribute to disease pathogenesis. Here we show the identification of muscleblind as a novel modifier of FUS-mediated neurodegeneration in vivo. Muscleblind regulates cytoplasmic mislocalization of mutant FUS and subsequent accumulation in stress granules, dendritic morphology and toxicity in mammalian neuronal and human iPSC-derived neurons. Interestingly, genetic modulation of endogenous muscleblind was sufficient to restore survival motor neuron (SMN) protein localization in neurons expressing pathogenic mutations in FUS, suggesting a potential mode of suppression of FUS toxicity. Upregulation of SMN suppressed FUS toxicity in Drosophila and primary cortical neurons, indicating a link between FUS and SMN. Our data provide in vivo evidence that muscleblind is a dominant modifier of FUS-mediated neurodegeneration by regulating FUS-mediated ALS pathogenesis.
MeSH term(s)	Acetyltransferases/genetics ; Acetyltransferases/metabolism ; Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/metabolism ; Animals ; Cytoplasm/metabolism ; Cytoplasmic Granules/metabolism ; Drosophila/genetics ; Drosophila/metabolism ; Drosophila Proteins/metabolism ; Female ; HEK293 Cells ; Humans ; Induced Pluripotent Stem Cells/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Motor Neurons/metabolism ; Mutation ; Nuclear Proteins/metabolism ; Phenotype ; RNA-Binding Protein FUS/genetics ; RNA-Binding Protein FUS/metabolism ; RNA-Binding Protein FUS/toxicity ; SMN Complex Proteins/genetics ; SMN Complex Proteins/metabolism ; Transcription Factors/metabolism
Chemical Substances	Drosophila Proteins ; Membrane Proteins ; Nuclear Proteins ; RNA-Binding Protein FUS ; SMN Complex Proteins ; Transcription Factors ; mbl protein, Drosophila ; Acetyltransferases (EC 2.3.1.-) ; MBOAT1 protein, human (EC 2.3.1.-)
Language	English
Publishing date	2019-12-06
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-019-13383-z
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Article ; Online: Pur-alpha regulates cytoplasmic stress granule dynamics and ameliorates FUS toxicity.

Daigle, J Gavin / Krishnamurthy, Karthik / Ramesh, Nandini / Casci, Ian / Monaghan, John / McAvoy, Kevin / Godfrey, Earl W / Daniel, Dianne C / Johnson, Edward M / Monahan, Zachary / Shewmaker, Frank / Pasinelli, Piera / Pandey, Udai Bhan

Acta neuropathologica

2016 Volume 131, Issue 4, Page(s) 605–620

Abstract: Amyotrophic lateral sclerosis is characterized by progressive loss of motor neurons in the brain and spinal cord. Mutations in several genes, including FUS, TDP43, Matrin 3, hnRNPA2 and other RNA-binding proteins, have been linked to ALS pathology. ... ...

Abstract	Amyotrophic lateral sclerosis is characterized by progressive loss of motor neurons in the brain and spinal cord. Mutations in several genes, including FUS, TDP43, Matrin 3, hnRNPA2 and other RNA-binding proteins, have been linked to ALS pathology. Recently, Pur-alpha, a DNA/RNA-binding protein was found to bind to C9orf72 repeat expansions and could possibly play a role in the pathogenesis of ALS. When overexpressed, Pur-alpha mitigates toxicities associated with Fragile X tumor ataxia syndrome (FXTAS) and C9orf72 repeat expansion diseases in Drosophila and mammalian cell culture models. However, the function of Pur-alpha in regulating ALS pathogenesis has not been fully understood. We identified Pur-alpha as a novel component of cytoplasmic stress granules (SGs) in ALS patient cells carrying disease-causing mutations in FUS. When cells were challenged with stress, we observed that Pur-alpha co-localized with mutant FUS in ALS patient cells and became trapped in constitutive SGs. We also found that FUS physically interacted with Pur-alpha in mammalian neuronal cells. Interestingly, shRNA-mediated knock down of endogenous Pur-alpha significantly reduced formation of cytoplasmic stress granules in mammalian cells suggesting that Pur-alpha is essential for the formation of SGs. Furthermore, ectopic expression of Pur-alpha blocked cytoplasmic mislocalization of mutant FUS and strongly suppressed toxicity associated with mutant FUS expression in primary motor neurons. Our data emphasizes the importance of stress granules in ALS pathogenesis and identifies Pur-alpha as a novel regulator of SG dynamics.
MeSH term(s)	Amyotrophic Lateral Sclerosis/pathology ; Animals ; Anti-Bacterial Agents/pharmacology ; Arsenites/pharmacology ; Brain/cytology ; Carrier Proteins/metabolism ; Cells, Cultured ; Cytoplasmic Granules/drug effects ; Cytoplasmic Granules/metabolism ; DNA Helicases ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Doxycycline/pharmacology ; Embryo, Mammalian ; Enzyme Inhibitors/pharmacology ; Female ; Gene Expression Regulation/drug effects ; Gene Expression Regulation/genetics ; Humans ; Male ; Microtubule-Associated Proteins/metabolism ; Motor Neurons/metabolism ; Poly-ADP-Ribose Binding Proteins ; RNA Helicases ; RNA Recognition Motif Proteins ; RNA, Small Interfering/genetics ; RNA, Small Interfering/metabolism ; RNA-Binding Protein FUS/genetics ; RNA-Binding Protein FUS/metabolism ; Rats ; Rats, Sprague-Dawley ; Sodium Compounds/pharmacology ; Transcription Factors/genetics ; Transcription Factors/metabolism
Chemical Substances	Anti-Bacterial Agents ; Arsenites ; Carrier Proteins ; DNA-Binding Proteins ; Enzyme Inhibitors ; MAP2 protein, human ; Microtubule-Associated Proteins ; PURA protein, human ; Poly-ADP-Ribose Binding Proteins ; RNA Recognition Motif Proteins ; RNA, Small Interfering ; RNA-Binding Protein FUS ; Sodium Compounds ; Transcription Factors ; sodium arsenite (48OVY2OC72) ; DNA Helicases (EC 3.6.4.-) ; G3BP1 protein, human (EC 3.6.4.12) ; RNA Helicases (EC 3.6.4.13) ; Doxycycline (N12000U13O)
Language	English
Publishing date	2016-04
Publishing country	Germany
Document type	Journal Article
ZDB-ID	1079-0
ISSN	1432-0533 ; 0001-6322
ISSN (online)	1432-0533
ISSN	0001-6322
DOI	10.1007/s00401-015-1530-0
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Article ; Online: Isogenic FUS-eGFP iPSC Reporter Lines Enable Quantification of FUS Stress Granule Pathology that Is Rescued by Drugs Inducing Autophagy.

Stem cell reports

2018 Volume 10, Issue 2, Page(s) 375–389

Abstract: Perturbations in stress granule (SG) dynamics may be at the core of amyotrophic lateral sclerosis (ALS). Since SGs are membraneless compartments, modeling their dynamics in human motor neurons has been challenging, thus hindering the identification of ... ...

Abstract	Perturbations in stress granule (SG) dynamics may be at the core of amyotrophic lateral sclerosis (ALS). Since SGs are membraneless compartments, modeling their dynamics in human motor neurons has been challenging, thus hindering the identification of effective therapeutics. Here, we report the generation of isogenic induced pluripotent stem cells carrying wild-type and P525L FUS-eGFP. We demonstrate that FUS-eGFP is recruited into SGs and that P525L profoundly alters their dynamics. With a screening campaign, we demonstrate that PI3K/AKT/mTOR pathway inhibition increases autophagy and ameliorates SG phenotypes linked to P525L FUS by reducing FUS-eGFP recruitment into SGs. Using a Drosophila model of FUS-ALS, we corroborate that induction of autophagy significantly increases survival. Finally, by screening clinically approved drugs for their ability to ameliorate FUS SG phenotypes, we identify a number of brain-penetrant anti-depressants and anti-psychotics that also induce autophagy. These drugs could be repurposed as potential ALS treatments.
MeSH term(s)	Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/metabolism ; Amyotrophic Lateral Sclerosis/pathology ; Animals ; Antidepressive Agents/pharmacology ; Antipyretics/pharmacology ; Autophagy/genetics ; CRISPR-Cas Systems ; Drosophila ; Drosophila Proteins/genetics ; Drug Evaluation, Preclinical ; Green Fluorescent Proteins/genetics ; Heterogeneous-Nuclear Ribonucleoprotein Group F-H/genetics ; Humans ; Induced Pluripotent Stem Cells/metabolism ; Motor Neurons/metabolism ; Motor Neurons/pathology ; Mutation ; Phosphatidylinositol 3-Kinases/genetics ; Proto-Oncogene Proteins c-akt/genetics ; RNA-Binding Protein FUS/genetics ; Signal Transduction/drug effects ; TOR Serine-Threonine Kinases/genetics
Chemical Substances	Antidepressive Agents ; Antipyretics ; Drosophila Proteins ; FUS protein, Drosophila ; FUS protein, human ; Heterogeneous-Nuclear Ribonucleoprotein Group F-H ; RNA-Binding Protein FUS ; Green Fluorescent Proteins (147336-22-9) ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; MTOR protein, human (EC 2.7.1.1) ; TOR Serine-Threonine Kinases (EC 2.7.1.1) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1)
Language	English
Publishing date	2018-01-18
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2720528-9
ISSN	2213-6711 ; 2213-6711
ISSN (online)	2213-6711
ISSN	2213-6711
DOI	10.1016/j.stemcr.2017.12.018
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Article ; Online: Muscleblind acts as a modifier of FUS toxicity by modulating stress granule dynamics and SMN localization

Nature Communications, Vol 10, Iss 1, Pp 1-

2019 Volume 20

Abstract: The exact molecular mechanisms driving FUS-mediated toxicity remain unclear. Here, the authors demonstrate that muscleblind (Mbl) is a novel modifier of FUS-associated ALS, with knockdown of endogenous Mbl suppressing neuromuscular junction defects and ... ...

Abstract	The exact molecular mechanisms driving FUS-mediated toxicity remain unclear. Here, the authors demonstrate that muscleblind (Mbl) is a novel modifier of FUS-associated ALS, with knockdown of endogenous Mbl suppressing neuromuscular junction defects and motor dysfunctions associated with FUS expression in Drosophila, as well as restoring reduced SMN protein levels in mammalian neuronal and human iPSC-derived motor neurons.
Keywords	Science ; Q
Language	English
Publishing date	2019-12-01T00:00:00Z
Publisher	Nature Publishing Group
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Muscleblind acts as a modifier of FUS toxicity by modulating stress granule dynamics and SMN localization

Nature Communications, Vol 10, Iss 1, Pp 1-

2019 Volume 20

Abstract	The exact molecular mechanisms driving FUS-mediated toxicity remain unclear. Here, the authors demonstrate that muscleblind (Mbl) is a novel modifier of FUS-associated ALS, with knockdown of endogenous Mbl suppressing neuromuscular junction defects and motor dysfunctions associated with FUS expression in Drosophila, as well as restoring reduced SMN protein levels in mammalian neuronal and human iPSC-derived motor neurons.
Keywords	Science ; Q
Language	English
Publishing date	2019-12-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Protein arginine methyltransferase 1 and 8 interact with FUS to modify its sub-cellular distribution and toxicity in vitro and in vivo.

Scaramuzzino, Chiara / Monaghan, John / Milioto, Carmelo / Lanson, Nicholas A / Maltare, Astha / Aggarwal, Tanya / Casci, Ian / Fackelmayer, Frank O / Pennuto, Maria / Pandey, Udai Bhan

PloS one

2013 Volume 8, Issue 4, Page(s) e61576

Abstract: Amyotrophic lateral sclerosis (ALS) is a late onset and progressive motor neuron disease. Mutations in the gene coding for fused in sarcoma/translocated in liposarcoma (FUS) are responsible for some cases of both familial and sporadic forms of ALS. The ... ...

Abstract	Amyotrophic lateral sclerosis (ALS) is a late onset and progressive motor neuron disease. Mutations in the gene coding for fused in sarcoma/translocated in liposarcoma (FUS) are responsible for some cases of both familial and sporadic forms of ALS. The mechanism through which mutations of FUS result in motor neuron degeneration and loss is not known. FUS belongs to the family of TET proteins, which are regulated at the post-translational level by arginine methylation. Here, we investigated the impact of arginine methylation in the pathogenesis of FUS-related ALS. We found that wild type FUS (FUS-WT) specifically interacts with protein arginine methyltransferases 1 and 8 (PRMT1 and PRMT8) and undergoes asymmetric dimethylation in cultured cells. ALS-causing FUS mutants retained the ability to interact with both PRMT1 and PRMT8 and undergo asymmetric dimethylation similar to FUS-WT. Importantly, PRMT1 and PRMT8 localized to mutant FUS-positive inclusion bodies. Pharmacologic inhibition of PRMT1 and PRMT8 activity reduced both the nuclear and cytoplasmic accumulation of FUS-WT and ALS-associated FUS mutants in motor neuron-derived cells and in cells obtained from an ALS patient carrying the R518G mutation. Genetic ablation of the fly homologue of human PRMT1 (DART1) exacerbated the neurodegeneration induced by overexpression of FUS-WT and R521H FUS mutant in a Drosophila model of FUS-related ALS. These results support a role for arginine methylation in the pathogenesis of FUS-related ALS.
MeSH term(s)	Adenosine/analogs & derivatives ; Adenosine/pharmacology ; Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/pathology ; Animals ; Arginine/metabolism ; Cytosol/metabolism ; Disease Models, Animal ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Drosophila melanogaster/drug effects ; Drosophila melanogaster/enzymology ; Drosophila melanogaster/genetics ; Enzyme Inhibitors/pharmacology ; Gene Deletion ; Gene Knockdown Techniques ; HEK293 Cells ; Humans ; Inclusion Bodies/drug effects ; Inclusion Bodies/metabolism ; Membrane Proteins/antagonists & inhibitors ; Membrane Proteins/metabolism ; Methylation/drug effects ; Methyltransferases/genetics ; Methyltransferases/metabolism ; Mutant Proteins/metabolism ; Mutation/genetics ; Protein Binding/drug effects ; Protein Transport/drug effects ; Protein-Arginine N-Methyltransferases/antagonists & inhibitors ; Protein-Arginine N-Methyltransferases/metabolism ; RNA-Binding Protein FUS/metabolism ; RNA-Binding Protein FUS/toxicity ; Repressor Proteins/antagonists & inhibitors ; Repressor Proteins/metabolism ; Subcellular Fractions/drug effects ; Subcellular Fractions/metabolism
Chemical Substances	Drosophila Proteins ; Enzyme Inhibitors ; Membrane Proteins ; Mutant Proteins ; RNA-Binding Protein FUS ; Repressor Proteins ; periodate-oxidized adenosine (34240-05-6) ; Arginine (94ZLA3W45F) ; Art1 protein, Drosophila (EC 2.1.1.-) ; Methyltransferases (EC 2.1.1.-) ; PRMT1 protein, human (EC 2.1.1.319) ; PRMT8 protein, human (EC 2.1.1.319) ; Protein-Arginine N-Methyltransferases (EC 2.1.1.319) ; Adenosine (K72T3FS567)
Language	English
Publishing date	2013-04-19
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0061576
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Article ; Online: Isogenic FUS-eGFP iPSC Reporter Lines Enable Quantification of FUS Stress Granule Pathology that Is Rescued by Drugs Inducing Autophagy

Stem Cell Reports, Vol 10, Iss 2, Pp 375-

2018 Volume 389

Abstract: Summary: Perturbations in stress granule (SG) dynamics may be at the core of amyotrophic lateral sclerosis (ALS). Since SGs are membraneless compartments, modeling their dynamics in human motor neurons has been challenging, thus hindering the ... ...

Abstract	Summary: Perturbations in stress granule (SG) dynamics may be at the core of amyotrophic lateral sclerosis (ALS). Since SGs are membraneless compartments, modeling their dynamics in human motor neurons has been challenging, thus hindering the identification of effective therapeutics. Here, we report the generation of isogenic induced pluripotent stem cells carrying wild-type and P525L FUS-eGFP. We demonstrate that FUS-eGFP is recruited into SGs and that P525L profoundly alters their dynamics. With a screening campaign, we demonstrate that PI3K/AKT/mTOR pathway inhibition increases autophagy and ameliorates SG phenotypes linked to P525L FUS by reducing FUS-eGFP recruitment into SGs. Using a Drosophila model of FUS-ALS, we corroborate that induction of autophagy significantly increases survival. Finally, by screening clinically approved drugs for their ability to ameliorate FUS SG phenotypes, we identify a number of brain-penetrant anti-depressants and anti-psychotics that also induce autophagy. These drugs could be repurposed as potential ALS treatments. : Sterneckert and colleagues generate isogenic FUS-eGFP reporter iPSCs that enable the identification of stress granule (SG) phenotypes specifically induced by the ALS mutation FUS P525L. Compound screening shows that modulation of the PI3K/AKT/mTOR pathway regulating autophagy ameliorates SG phenotypes. A second screen identifies similarly acting brain-penetrant US FDA-approved drugs that could be repurposed to treat ALS. Keywords: amyotrophic lateral sclerosis, induced pluripotent stem cells, FUS, stress granules, autophagy, gene editing, CRISPR/Cas9n
Keywords	Medicine (General) ; R5-920 ; Biology (General) ; QH301-705.5
Language	English
Publishing date	2018-02-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Protein arginine methyltransferase 6 enhances polyglutamine-expanded androgen receptor function and toxicity in spinal and bulbar muscular atrophy.

Scaramuzzino, Chiara / Casci, Ian / Parodi, Sara / Lievens, Patricia M J / Polanco, Maria J / Milioto, Carmelo / Chivet, Mathilde / Monaghan, John / Mishra, Ashutosh / Badders, Nisha / Aggarwal, Tanya / Grunseich, Christopher / Sambataro, Fabio / Basso, Manuela / Fackelmayer, Frank O / Taylor, J Paul / Pandey, Udai Bhan / Pennuto, Maria

Neuron

2014 Volume 85, Issue 1, Page(s) 88–100

Abstract: Polyglutamine expansion in androgen receptor (AR) is responsible for spinobulbar muscular atrophy (SBMA) that leads to selective loss of lower motor neurons. Using SBMA as a model, we explored the relationship between protein structure/function and ... ...

Abstract	Polyglutamine expansion in androgen receptor (AR) is responsible for spinobulbar muscular atrophy (SBMA) that leads to selective loss of lower motor neurons. Using SBMA as a model, we explored the relationship between protein structure/function and neurodegeneration in polyglutamine diseases. We show here that protein arginine methyltransferase 6 (PRMT6) is a specific co-activator of normal and mutant AR and that the interaction of PRMT6 with AR is significantly enhanced in the AR mutant. AR and PRMT6 interaction occurs through the PRMT6 steroid receptor interaction motif, LXXLL, and the AR activating function 2 surface. AR transactivation requires PRMT6 catalytic activity and involves methylation of arginine residues at Akt consensus site motifs, which is mutually exclusive with serine phosphorylation by Akt. The enhanced interaction of PRMT6 and mutant AR leads to neurodegeneration in cell and fly models of SBMA. These findings demonstrate a direct role of arginine methylation in polyglutamine disease pathogenesis.
MeSH term(s)	Animals ; COS Cells ; Chlorocebus aethiops ; Drosophila ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; HEK293 Cells ; Humans ; Mice ; Muscular Disorders, Atrophic/enzymology ; Muscular Disorders, Atrophic/genetics ; Muscular Disorders, Atrophic/metabolism ; Nuclear Proteins/metabolism ; PC12 Cells ; Peptides/genetics ; Phosphorylation ; Protein-Arginine N-Methyltransferases/metabolism ; Proto-Oncogene Proteins c-akt/metabolism ; RNA, Messenger/analysis ; Rats ; Real-Time Polymerase Chain Reaction ; Receptors, Androgen/genetics ; Receptors, Androgen/metabolism
Chemical Substances	Drosophila Proteins ; Nuclear Proteins ; Peptides ; RNA, Messenger ; Receptors, Androgen ; polyglutamine (26700-71-0) ; PRMT6 protein, human (EC 2.1.1.319) ; PRMT6 protein, mouse (EC 2.1.1.319) ; Protein-Arginine N-Methyltransferases (EC 2.1.1.319) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1)
Language	English
Publishing date	2014-12-23
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
ZDB-ID	808167-0
ISSN	1097-4199 ; 0896-6273
ISSN (online)	1097-4199
ISSN	0896-6273
DOI	10.1016/j.neuron.2014.12.031
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Zs.A 2496: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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