LIVIVO - Search results -

Search results

Result 1 - 10 of total 16

Search options

Article ; Online: What is repeated in ALS and FTLD.

Fecto, Faisal / Siddique, Teepu

2012 Volume 11, Issue 1, Page(s) 25–27

MeSH term(s)	Amyotrophic Lateral Sclerosis/genetics ; Chromosomes, Human, Pair 9 ; DNA Repeat Expansion ; Female ; Frontotemporal Lobar Degeneration/genetics ; Humans ; Male ; Promoter Regions, Genetic
Language	English
Publishing date	2012-01
Publishing country	England
Document type	Comment ; Letter
ZDB-ID	2079704-7
ISSN	1474-4465 ; 1474-4422
ISSN (online)	1474-4465
ISSN	1474-4422
DOI	10.1016/S1474-4422(11)70275-7
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Article ; Online: UBQLN2/P62 cellular recycling pathways in amyotrophic lateral sclerosis and frontotemporal dementia.

Fecto, Faisal / Siddique, Teepu

Muscle & nerve

2012 Volume 45, Issue 2, Page(s) 157–162

Abstract: Recent findings highlight a pathologic and functional convergence in amyotrophic lateral sclerosis (ALS) and amyotrophic lateral sclerosis with frontotemporal dementia (ALS-FTD) at the level of protein recycling and disposal. Genes linked to rare cases ... ...

Abstract	Recent findings highlight a pathologic and functional convergence in amyotrophic lateral sclerosis (ALS) and amyotrophic lateral sclerosis with frontotemporal dementia (ALS-FTD) at the level of protein recycling and disposal. Genes linked to rare cases of familial ALS and ALS-FTD, like UBQLN2, OPTN, SQSTM1/p62, and VCP, may converge onto a unifying pathogenic pathway and thereby provide novel therapeutic targets common to a spectrum of etiologically diverse forms of ALS and ALS-FTD. Interactions between these genes need to be further explored to understand their common molecular pathways. Future efforts should be directed toward generation and characterization of in vivo models to dissect the pathogenic mechanisms of ALS and ALS-FTD and the role of protein degradation pathways, both centrally, at the cell body, and peripherally, at the level of the synapse. Such efforts will rapidly accelerate the discovery of new drugs that regulate accumulation of pathogenic proteins and their downstream consequences in ALS and ALS-FTD and, possibly, other neurodegenerative diseases as well.
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/metabolism ; Amyotrophic Lateral Sclerosis/pathology ; Animals ; Brain/metabolism ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Frontotemporal Dementia/genetics ; Frontotemporal Dementia/metabolism ; Frontotemporal Dementia/pathology ; Humans ; Sequestosome-1 Protein ; Ubiquitins/genetics ; Ubiquitins/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Cell Cycle Proteins ; SQSTM1 protein, human ; Sequestosome-1 Protein ; UBQLN2 protein, human ; Ubiquitins
Language	English
Publishing date	2012-02
Publishing country	United States
Document type	Journal Article
ZDB-ID	438353-9
ISSN	1097-4598 ; 0148-639X
ISSN (online)	1097-4598
ISSN	0148-639X
DOI	10.1002/mus.23278
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 1449: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 551: Show issues

Order via subito

Details ▾

Article ; Online: SIGMAR1 mutations, genetic heterogeneity at the chromosome 9p locus, and the expanding etiological diversity of amyotrophic lateral sclerosis.

Fecto, Faisal / Siddique, Teepu

Annals of neurology

2011 Volume 70, Issue 6, Page(s) 867–870

MeSH term(s)	Amyotrophic Lateral Sclerosis/genetics ; Animals ; Female ; Genetic Predisposition to Disease ; Humans ; Male ; Polymorphism, Single Nucleotide/genetics ; Receptors, sigma/genetics ; Sigma-1 Receptor
Chemical Substances	Receptors, sigma
Language	English
Publishing date	2011-12-22
Publishing country	United States
Document type	Editorial ; Comment
ZDB-ID	80362-5
ISSN	1531-8249 ; 0364-5134
ISSN (online)	1531-8249
ISSN	0364-5134
DOI	10.1002/ana.22648
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1370: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 478: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Protein recycling pathways in neurodegenerative diseases.

Fecto, Faisal / Esengul, Y Taylan / Siddique, Teepu

Alzheimer's research & therapy

2014 Volume 6, Issue 2, Page(s) 13

Abstract: Many progressive neurodegenerative diseases, including Alzheimer disease, Parkinson disease, Huntington disease, amyotrophic lateral sclerosis, and frontotemporal lobe dementia, are associated with the formation of insoluble intracellular proteinaceous ... ...

Abstract	Many progressive neurodegenerative diseases, including Alzheimer disease, Parkinson disease, Huntington disease, amyotrophic lateral sclerosis, and frontotemporal lobe dementia, are associated with the formation of insoluble intracellular proteinaceous inclusions. It is therefore imperative to understand the factors that regulate normal, as well as abnormal, protein recycling in neurons. Dysfunction of the ubiquitin-proteasome or autophagy pathways might contribute to the pathology of various neurodegenerative diseases. Induction of these pathways may offer a rational therapeutic strategy for a number of these diseases.
Language	English
Publishing date	2014-03-06
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	2506521-X
ISSN	1758-9193
ISSN	1758-9193
DOI	10.1186/alzrt243
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Making connections: pathology and genetics link amyotrophic lateral sclerosis with frontotemporal lobe dementia.

Fecto, Faisal / Siddique, Teepu

Journal of molecular neuroscience : MN

2011 Volume 45, Issue 3, Page(s) 663–675

Abstract: Over the last couple of decades, there has been a growing body of clinical, genetic, and histopathological evidence that similar pathological processes underlie amyotrophic lateral sclerosis (ALS) and some types of frontotemporal lobe dementia (FTD). ... ...

Abstract	Over the last couple of decades, there has been a growing body of clinical, genetic, and histopathological evidence that similar pathological processes underlie amyotrophic lateral sclerosis (ALS) and some types of frontotemporal lobe dementia (FTD). Even though there is great diversity in the genetic causes of these disorders, there is a high degree of overlap in their histopathology. Genes linked to rare cases of familial ALS and/or FTD, like FUS, TARDBP, OPTN, and UBQLN2 may converge onto a unifying pathogenic pathway and thereby provide novel therapeutic targets common to a spectrum of etiologically diverse forms of ALS and ALS-FTD. Additionally, there are major loci for ALS-FTD on chromosomes 9p and 15q. Identification of causative genetic alterations at those loci will be an important step in understanding the pathogenesis of juvenile- and adult-onset ALS and ALS-FTD. Interactions between TDP-43, FUS, optineurin, and ubiquilin 2 need to be studied to understand their common molecular pathways. Future efforts should also be directed towards generation and characterization of in vivo models to dissect the pathogenic mechanisms of these diseases. Such efforts will rapidly accelerate the discovery of new drugs that regulate accumulation of pathogenic proteins and their downstream consequences.
MeSH term(s)	Adaptor Proteins, Signal Transducing ; Age of Onset ; Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/pathology ; Amyotrophic Lateral Sclerosis/physiopathology ; Autophagy-Related Proteins ; Cell Cycle Proteins/genetics ; DNA-Binding Proteins/genetics ; Frontotemporal Dementia/genetics ; Frontotemporal Dementia/pathology ; Frontotemporal Dementia/physiopathology ; Genetic Predisposition to Disease ; Humans ; Membrane Transport Proteins ; Motor Neurons/pathology ; Pedigree ; Phenotype ; RNA-Binding Protein FUS/genetics ; Transcription Factor TFIIIA/genetics ; Ubiquitins/genetics
Chemical Substances	Adaptor Proteins, Signal Transducing ; Autophagy-Related Proteins ; Cell Cycle Proteins ; DNA-Binding Proteins ; Membrane Transport Proteins ; OPTN protein, human ; RNA-Binding Protein FUS ; Transcription Factor TFIIIA ; UBQLN2 protein, human ; Ubiquitins
Language	English
Publishing date	2011-09-07
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	1043392-2
ISSN	1559-1166 ; 0895-8696
ISSN (online)	1559-1166
ISSN	0895-8696
DOI	10.1007/s12031-011-9637-9
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 3006: 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)

Order via subito

Details ▾

Article ; Online: Mutant TRPV4-mediated toxicity is linked to increased constitutive function in axonal neuropathies.

Fecto, Faisal / Shi, Yong / Huda, Rafiq / Martina, Marco / Siddique, Teepu / Deng, Han-Xiang

The Journal of biological chemistry

2011 Volume 286, Issue 19, Page(s) 17281–17291

Abstract: Mutations in TRPV4 have been linked to three distinct axonal neuropathies. However, the pathogenic mechanism underlying these disorders remains unclear. Both gain and loss of calcium channel activity of the mutant TRPV4 have been suggested. Here, we show ...

Abstract	Mutations in TRPV4 have been linked to three distinct axonal neuropathies. However, the pathogenic mechanism underlying these disorders remains unclear. Both gain and loss of calcium channel activity of the mutant TRPV4 have been suggested. Here, we show that the three previously reported TRPV4 mutant channels have a physiological localization and display an increased calcium channel activity, leading to increased cytotoxicity in three different cell types. Patch clamp experiments showed that cells expressing mutant TRPV4 have much larger whole-cell currents than those expressing the wild-type TRPV4 channel. Single channel recordings showed that the mutant channels have higher open probability, due to a modification of gating, and no change in single-channel conductance. These data support the hypothesis that a "gain of function" mechanism, possibly leading to increased intracellular calcium influx, underlies the pathogenesis of the TRPV4-linked axonal neuropathies, and may have immediate implications for designing rational therapies.
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Axons/metabolism ; Calcium Channels/chemistry ; Cell Cycle Proteins/metabolism ; Cell Membrane/metabolism ; Cell Survival ; Cytoplasm/metabolism ; DNA, Complementary/metabolism ; Electrophysiology/methods ; HeLa Cells ; Humans ; Microscopy, Confocal/methods ; Models, Biological ; Models, Statistical ; Mutation ; Neurodegenerative Diseases/metabolism ; Nuclear Proteins/metabolism ; Transient Receptor Potential Channels/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Calcium Channels ; Cell Cycle Proteins ; DNA, Complementary ; MAD2L1BP protein, human ; Nuclear Proteins ; Transient Receptor Potential Channels
Language	English
Publishing date	2011-03-21
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M111.237685
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.108: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: An unusual case of familial ALS and cerebellar ataxia.

Yasser, Sadia / Fecto, Faisal / Siddique, Teepu / Sheikh, Kazim A / Athar, Parveen

Amyotrophic lateral sclerosis : official publication of the World Federation of Neurology Research Group on Motor Neuron Diseases

2010 Volume 11, Issue 6, Page(s) 568–570

Abstract: We report a case of familial amyotrophic lateral sclerosis (FALS) with clinical signs of cerebellar and posterior column involvement. The patient's work-up showed a known mutation (E100K) in the gene for Cu/Zn superoxide dismutase 1 (SOD1). Our case ... ...

Abstract	We report a case of familial amyotrophic lateral sclerosis (FALS) with clinical signs of cerebellar and posterior column involvement. The patient's work-up showed a known mutation (E100K) in the gene for Cu/Zn superoxide dismutase 1 (SOD1). Our case illustrates that extramotor symptoms, such as prominent cerebellar signs, can be seen in patients with FALS.
MeSH term(s)	Adult ; Amyotrophic Lateral Sclerosis/diagnosis ; Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/physiopathology ; Cerebellar Ataxia/diagnosis ; Cerebellar Ataxia/genetics ; Cerebellar Ataxia/physiopathology ; Female ; Humans ; Mutation ; Superoxide Dismutase/genetics ; Superoxide Dismutase-1
Chemical Substances	SOD1 protein, human ; Superoxide Dismutase (EC 1.15.1.1) ; Superoxide Dismutase-1 (EC 1.15.1.1)
Language	English
Publishing date	2010-12
Publishing country	England
Document type	Case Reports ; Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2264792-2
ISSN	1471-180X ; 1743-4483 ; 1466-0822 ; 1748-2968 ; 1743-4475
ISSN (online)	1471-180X ; 1743-4483
ISSN	1466-0822 ; 1748-2968 ; 1743-4475
DOI	10.3109/17482961003636874
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 5874: 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)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Mutation in the novel nuclear-encoded mitochondrial protein CHCHD10 in a family with autosomal dominant mitochondrial myopathy.

Ajroud-Driss, Senda / Fecto, Faisal / Ajroud, Kaouther / Lalani, Irfan / Calvo, Sarah E / Mootha, Vamsi K / Deng, Han-Xiang / Siddique, Nailah / Tahmoush, Albert J / Heiman-Patterson, Terry D / Siddique, Teepu

Neurogenetics

2014 Volume 16, Issue 1, Page(s) 1–9

Abstract: Mitochondrial myopathies belong to a larger group of systemic diseases caused by morphological or biochemical abnormalities of mitochondria. Mitochondrial disorders can be caused by mutations in either the mitochondrial or nuclear genome. Only 5% of all ... ...

Abstract	Mitochondrial myopathies belong to a larger group of systemic diseases caused by morphological or biochemical abnormalities of mitochondria. Mitochondrial disorders can be caused by mutations in either the mitochondrial or nuclear genome. Only 5% of all mitochondrial disorders are autosomal dominant. We analyzed DNA from members of the previously reported Puerto Rican kindred with an autosomal dominant mitochondrial myopathy (Heimann-Patterson et al. 1997). Linkage analysis suggested a putative locus on the pericentric region of the long arm of chromosome 22 (22q11). Using the tools of integrative genomics, we established chromosome 22 open reading frame 16 (C22orf16) (later designated as CHCHD10) as the only high-scoring mitochondrial candidate gene in our minimal candidate region. Sequence analysis revealed a double-missense mutation (R15S and G58R) in cis in CHCHD10 which encodes a coiled coil-helix-coiled coil-helix protein of unknown function. These two mutations completely co-segregated with the disease phenotype and were absent in 1,481 Caucasian and 80 Hispanic (including 32 Puerto Rican) controls. Expression profiling showed that CHCHD10 is enriched in skeletal muscle. Mitochondrial localization of the CHCHD10 protein was confirmed using immunofluorescence in cells expressing either wild-type or mutant CHCHD10. We found that the expression of the G58R, but not the R15S, mutation induced mitochondrial fragmentation. Our findings identify a novel gene causing mitochondrial myopathy, thereby expanding the spectrum of mitochondrial myopathies caused by nuclear genes. Our findings also suggest a role for CHCHD10 in the morphologic remodeling of the mitochondria.
MeSH term(s)	Chromosomes, Human, Pair 22 ; Family ; Female ; Genes, Dominant ; Humans ; Male ; Mitochondria/genetics ; Mitochondria/ultrastructure ; Mitochondrial Myopathies/genetics ; Mitochondrial Proteins/genetics ; Mutation ; Puerto Rico
Chemical Substances	CHCHD10 protein, human ; Mitochondrial Proteins
Language	English
Publishing date	2014-09-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1339887-8
ISSN	1364-6753 ; 1364-6745
ISSN (online)	1364-6753
ISSN	1364-6745
DOI	10.1007/s10048-014-0421-1
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 5295: 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)

Order via subito

Details ▾

Article ; Online: Dendritic spinopathy in transgenic mice expressing ALS/dementia-linked mutant UBQLN2.

Gorrie, George H / Fecto, Faisal / Radzicki, Daniel / Weiss, Craig / Shi, Yong / Dong, Hongxin / Zhai, Hong / Fu, Ronggen / Liu, Erdong / Li, Sisi / Arrat, Hasan / Bigio, Eileen H / Disterhoft, John F / Martina, Marco / Mugnaini, Enrico / Siddique, Teepu / Deng, Han-Xiang

Proceedings of the National Academy of Sciences of the United States of America

2014 Volume 111, Issue 40, Page(s) 14524–14529

Abstract: Mutations in the gene encoding ubiquilin2 (UBQLN2) cause amyotrophic lateral sclerosis (ALS), frontotemporal type of dementia, or both. However, the molecular mechanisms are unknown. Here, we show that ALS/dementia-linked UBQLN2(P497H) transgenic mice ... ...

Abstract	Mutations in the gene encoding ubiquilin2 (UBQLN2) cause amyotrophic lateral sclerosis (ALS), frontotemporal type of dementia, or both. However, the molecular mechanisms are unknown. Here, we show that ALS/dementia-linked UBQLN2(P497H) transgenic mice develop neuronal pathology with ubiquilin2/ubiquitin/p62-positive inclusions in the brain, especially in the hippocampus, recapitulating several key pathological features of dementia observed in human patients with UBQLN2 mutations. A major feature of the ubiquilin2-related pathology in these mice, and reminiscent of human disease, is a dendritic spinopathy with protein aggregation in the dendritic spines and an associated decrease in dendritic spine density and synaptic dysfunction. Finally, we show that the protein inclusions in the dendritic spines are composed of several components of the proteasome machinery, including Ub(G76V)-GFP, a representative ubiquitinated protein substrate that is accumulated in the transgenic mice. Our data, therefore, directly link impaired protein degradation to inclusion formation that is associated with synaptic dysfunction and cognitive deficits. These data imply a convergent molecular pathway involving synaptic protein recycling that may also be involved in other neurodegenerative disorders, with implications for development of widely applicable rational therapeutics.
MeSH term(s)	Adaptor Proteins, Signal Transducing ; Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/metabolism ; Amyotrophic Lateral Sclerosis/physiopathology ; Animals ; Autophagy-Related Proteins ; Brain/metabolism ; Brain/pathology ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Cognition Disorders/genetics ; Cognition Disorders/physiopathology ; Dementia/genetics ; Dementia/metabolism ; Dementia/physiopathology ; Dendritic Spines/genetics ; Dendritic Spines/metabolism ; Dendritic Spines/pathology ; Dendritic Spines/ultrastructure ; Disease Models, Animal ; Hippocampus/metabolism ; Hippocampus/pathology ; Humans ; Immunohistochemistry ; Inclusion Bodies/metabolism ; Maze Learning/physiology ; Mice, Inbred Strains ; Mice, Transgenic ; Microscopy, Confocal ; Microscopy, Electron ; Motor Activity/genetics ; Motor Activity/physiology ; Mutation ; Proteasome Endopeptidase Complex/metabolism ; Spinal Cord/metabolism ; Spinal Cord/pathology ; Spinal Cord/physiopathology ; Synaptic Transmission/genetics ; Synaptic Transmission/physiology ; Ubiquitins/genetics ; Ubiquitins/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Autophagy-Related Proteins ; Cell Cycle Proteins ; UBQLN2 protein, human ; Ubiquitins ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2014-09-22
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1405741111
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1148: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Differential involvement of optineurin in amyotrophic lateral sclerosis with or without SOD1 mutations.

Deng, Han-Xiang / Bigio, Eileen H / Zhai, Hong / Fecto, Faisal / Ajroud, Kaouther / Shi, Yong / Yan, Jianhua / Mishra, Manjari / Ajroud-Driss, Senda / Heller, Scott / Sufit, Robert / Siddique, Nailah / Mugnaini, Enrico / Siddique, Teepu

Archives of neurology

2011 Volume 68, Issue 8, Page(s) 1057–1061

Abstract: Background: Mutations in optineurin have recently been linked to amyotrophic lateral sclerosis (ALS).: Objective: To determine whether optineurin-positive skeinlike inclusions are a common pathologic feature in ALS, including SOD1 -linked ALS.: ... ...

Abstract	Background: Mutations in optineurin have recently been linked to amyotrophic lateral sclerosis (ALS). Objective: To determine whether optineurin-positive skeinlike inclusions are a common pathologic feature in ALS, including SOD1 -linked ALS. Design: Clinical case series. Setting: Academic referral center. Subjects: We analyzed spinal cord sections from 46 clinically and pathologically diagnosed ALS cases and ALS transgenic mouse models overexpressing ALS-linked SOD1 mutations G93A or L126Z. Results: We observed optineurin-immunoreactive skeinlike inclusions in all the sporadic ALS and familial ALS cases without SOD1 mutation, but not in cases with SOD1 mutations or in transgenic mice overexpressing the ALS-linked SOD1 mutations G93A or L126Z. Conclusion: The data from this study provide evidence that optineurin is involved in the pathogenesis of sporadic ALS and non- SOD1 familial ALS, thus supporting the hypothesis that these forms of ALS share a pathway that is distinct from that of SOD1-linked ALS.
MeSH term(s)	Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/metabolism ; Amyotrophic Lateral Sclerosis/pathology ; Animals ; Cell Cycle Proteins ; Diagnosis, Differential ; Eye Proteins/genetics ; Eye Proteins/metabolism ; Genetic Markers/genetics ; Genetic Predisposition to Disease/genetics ; Humans ; Membrane Transport Proteins ; Mice ; Mice, Transgenic ; Neural Pathways/pathology ; Superoxide Dismutase/genetics ; Superoxide Dismutase-1 ; Transcription Factor TFIIIA/genetics ; Transcription Factor TFIIIA/metabolism
Chemical Substances	Cell Cycle Proteins ; Eye Proteins ; Genetic Markers ; Membrane Transport Proteins ; OPTN protein, human ; Optn protein, mouse ; SOD1 protein, human ; Transcription Factor TFIIIA ; Sod1 protein, mouse (EC 1.15.1.1) ; Superoxide Dismutase (EC 1.15.1.1) ; Superoxide Dismutase-1 (EC 1.15.1.1)
Language	English
Publishing date	2011-08-08
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	80049-1
ISSN	1538-3687 ; 0003-9942
ISSN (online)	1538-3687
ISSN	0003-9942
DOI	10.1001/archneurol.2011.178
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Ui II Zs.191: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

To top

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito