ALS-associated TDP-43 induces endoplasmic reticulum stress, which drives cytoplasmic TDP-43 accumulation and stress granule formation
about
The Unfolded Protein Response and the Role of Protein Disulfide Isomerase in NeurodegenerationAlterations in stress granule dynamics driven by TDP-43 and FUS: a link to pathological inclusions in ALS?Oxidative stress and mitochondrial damage: importance in non-SOD1 ALSProtein Homeostasis in Amyotrophic Lateral Sclerosis: Therapeutic Opportunities?Protein Quality Control and the Amyotrophic Lateral Sclerosis/Frontotemporal Dementia ContinuumEndoplasmic reticulum stress and inflammation in the central nervous systemProgressive Motor Neuron Pathology and the Role of Astrocytes in a Human Stem Cell Model of VCP-Related ALSMyopathy-causing mutations in an HSP40 chaperone disrupt processing of specific client conformers.Aggregation-prone c9FTD/ALS poly(GA) RAN-translated proteins cause neurotoxicity by inducing ER stress.Valproate Attenuates 25-kDa C-Terminal Fragment of TDP-43-Induced Neuronal Toxicity via Suppressing Endoplasmic Reticulum Stress and Activating Autophagy.Altered mRNP granule dynamics in FTLD pathogenesis.Activation of ER Stress and Autophagy Induced by TDP-43 A315T as Pathogenic Mechanism and the Corresponding Histological Changes in Skin as Potential Biomarker for ALS with the MutationGolgi fragmentation in amyotrophic lateral sclerosis, an overview of possible triggers and consequences.Loss of RAD-23 Protects Against Models of Motor Neuron Disease by Enhancing Mutant Protein ClearanceInterplay of endoplasmic reticulum stress and autophagy in neurodegenerative disorders.Activation of HIPK2 Promotes ER Stress-Mediated Neurodegeneration in Amyotrophic Lateral Sclerosis.Protein Quality Control by Molecular Chaperones in Neurodegeneration.Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases.The ER mitochondria calcium cycle and ER stress response as therapeutic targets in amyotrophic lateral sclerosis.Mitochondria and endoplasmic reticulum crosstalk in amyotrophic lateral sclerosis.Ultrastructural features of aberrant glial cells isolated from the spinal cord of paralytic rats expressing the amyotrophic lateral sclerosis-linked SOD1G93A mutation.Translational control by eIF2α in neurons: Beyond the stress response.Stress granules at the intersection of autophagy and ALS.The entangled ER-mitochondrial axis as a potential therapeutic strategy in neurodegeneration: A tangled duo unchained.The cleavage pattern of TDP-43 determines its rate of clearance and cytotoxicity.ER-mitochondria associations are regulated by the VAPB-PTPIP51 interaction and are disrupted by ALS/FTD-associated TDP-43.Protein Disulphide Isomerases: emerging roles of PDI and ERp57 in the nervous system and as therapeutic targets for ALS.The Endoplasmic Reticulum Unfolded Protein Response in Neurodegenerative Disorders and Its Potential Therapeutic SignificanceSubtilase cytotoxin produced by locus of enterocyte effacement-negative Shiga-toxigenic Escherichia coli induces stress granule formation.TDP-43/HDAC6 axis promoted tumor progression and regulated nutrient deprivation-induced autophagy in glioblastoma.Autophagy Dysregulation in ALS: When Protein Aggregates Get Out of Hand.Proteostasis disturbance in amyotrophic lateral sclerosis.Marinesco-Sjögren syndrome protein SIL1 regulates motor neuron subtype-selective ER stress in ALS.Autophagy meets fused in sarcoma-positive stress granules.Omega-3 fatty acids increase the unfolded protein response and improve amyloid-β phagocytosis by macrophages of patients with mild cognitive impairment.Malonate induces the assembly of cytoplasmic stress granules.The roles of intrinsic disorder-based liquid-liquid phase transitions in the "Dr. Jekyll-Mr. Hyde" behavior of proteins involved in amyotrophic lateral sclerosis and frontotemporal lobar degeneration.Capturing intracellular Ca2+ dynamics in computational models of neurodegenerative diseases.Defects in optineurin- and myosin VI-mediated cellular trafficking in amyotrophic lateral sclerosis.Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation
P2860
Q26771343-21577C08-5900-4BD8-8826-441F1E910CE8Q26777971-D3A8431B-9005-43C7-B384-EFCDF45A2C06Q27023941-79FD074C-D83C-4F23-AD45-3B9B1CE892E1Q33621868-CA179539-F770-42BA-B7E9-341EDD8768A8Q33653996-01BB1370-3E52-4AE9-BD0C-32B788BCD191Q33730922-EA3143FE-7A8A-443D-A619-ED07A325B165Q33779813-20648BEC-6DC3-47B0-BF01-4FF2E6CBE506Q33947263-9E4CE297-30DE-4B52-AB3B-35AEDC39971EQ34157304-D8442E3B-3C04-4CE2-8E2F-2823063CCFB8Q35739624-B6545335-D11B-4A2D-83E9-835DE86A6073Q35944221-E835E130-D310-4302-A726-08C82F949D1EQ36002075-8E9EEDB9-5A48-4C8E-9EA4-8C7862E92115Q36211097-C16977BB-E4EA-49A1-811C-D9915597B3CAQ36383297-407FFFED-CCC6-40CD-B0DD-2A8DDE8250EDQ36810822-DAA833D5-AE5F-46D6-8EFE-71090F24C046Q37079670-B3D566E4-8C12-4C05-8056-593B2AB012DEQ37739093-6688BCE4-BF3A-44EB-B6AA-14C0B4E52F34Q38195215-07E8A1C0-BA62-444E-86F0-31CE86781FDDQ38218666-2656C1C8-A272-4F5F-8391-D89C54E66E9CQ38455911-BF0B1E7F-961E-4088-8AB5-DC4D3769DD50Q38597154-3F87AF4E-C4C9-4498-81A8-B80B4E19B5DDQ38781395-B869ADAD-1EAB-4AF8-BD8A-D3DF0AE70DE3Q38835008-F665C096-F17C-420E-9166-6580C25BDCEBQ38841508-C62BFEA7-BFF7-4249-868D-07378BEF6A12Q38915658-97DD0AD4-E0A7-40C6-920E-39EDA6EDF3AEQ38988714-4D5AF8C7-C46C-441A-A000-F1CB42609FA9Q38992384-38AD9A63-AAD2-447E-B0B3-429BDFBA30D4Q39410246-6777D131-1F1E-431A-89BE-91B31BAF74B8Q40839064-2C6E0A78-01B6-4C6E-8E0C-9C274B122224Q41345579-E61ECC60-CA9C-4017-BF71-33DE38A38055Q41525479-1F57877E-36A6-41AD-9D16-879879043C89Q41991266-D7A1B1CC-0E24-4135-90CD-310D3B843529Q42175672-87D12B80-1B1F-40E8-991D-5CFA23A7166DQ43142752-8DE08014-9880-4627-A742-20C48A6BD18FQ46579757-86BFE844-281A-4E00-A703-3539B6E27B64Q46608251-C96ECF2C-A89F-4165-9639-BB32F07545A8Q47693846-42CF6A82-FF6C-49CC-84C0-1DE75B34FE14Q49569836-22D0B862-EC5E-40FE-9AFF-86D704CF0066Q52659046-963E71DE-4882-46FF-AACB-2D8A308BD2BEQ57909514-A9C7693F-FFA8-4D70-9C31-6A99D7368DCE
P2860
ALS-associated TDP-43 induces endoplasmic reticulum stress, which drives cytoplasmic TDP-43 accumulation and stress granule formation
description
2013 nî lūn-bûn
@nan
2013 թուականին հրատարակուած գիտական յօդուած
@hyw
2013 թվականին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
ALS-associated TDP-43 induces ...... n and stress granule formation
@ast
ALS-associated TDP-43 induces ...... n and stress granule formation
@en
ALS-associated TDP-43 induces ...... n and stress granule formation
@nl
type
label
ALS-associated TDP-43 induces ...... n and stress granule formation
@ast
ALS-associated TDP-43 induces ...... n and stress granule formation
@en
ALS-associated TDP-43 induces ...... n and stress granule formation
@nl
prefLabel
ALS-associated TDP-43 induces ...... n and stress granule formation
@ast
ALS-associated TDP-43 induces ...... n and stress granule formation
@en
ALS-associated TDP-43 induces ...... n and stress granule formation
@nl
P2093
P2860
P50
P1433
P1476
ALS-associated TDP-43 induces ...... n and stress granule formation
@en
P2093
Malcolm K Horne
Manal A Farg
P2860
P304
P356
10.1371/JOURNAL.PONE.0081170
P407
P50
P577
2013-11-29T00:00:00Z