Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation. - Wikidata - awgldk - TriplyDB

Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation.

Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation.

http://www.wikidata.org/entity/Q42917499

about

Human Fas-associated factor 1, interacting with ubiquitinated proteins and valosin-containing protein, is involved in the ubiquitin-proteasome pathway The translation initiation factor 3f (eIF3f) exhibits a deubiquitinase activity regulating Notch activation Mutant ubiquitin found in Alzheimer's disease causes neuritic beading of mitochondria in association with neuronal degeneration Mutant ubiquitin (UBB+1) associated with neurodegenerative disorders is hydrolyzed by ubiquitin C-terminal hydrolase L3 (UCH-L3)The HECT domain of TRIP12 ubiquitinates substrates of the ubiquitin fusion degradation pathway The Ubiquitin-Proteasome System: Potential Therapeutic Targets for Alzheimer's Disease and Spinal Cord Injury Misframed ubiquitin and impaired protein quality control: an early event in Alzheimer's disease Structural Basis of E2-25K/UBB+1 Interaction Leading to Proteasome Inhibition and Neurotoxicity Multiple interactions of rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis The Ubiquitin-Proteasome System and Molecular Chaperone Deregulation in Alzheimer's Disease Argyrophilic grain disease The ubiquitin-proteasome system in Alzheimer's disease PKCγ participates in food entrainment by regulating BMAL1 Mutant ubiquitin UBB+1 induces mitochondrial fusion by destabilizing mitochondrial fission-specific proteins and confers resistance to oxidative stress-induced cell death in astrocytic cells Ubiquitin and ubiquitin-derived peptides as substrates for peptidylglycine alpha-amidating monooxygenase Expression of progerin in aging mouse brains reveals structural nuclear abnormalities without detectible significant alterations in gene expression, hippocampal stem cells or behavior.Role of the ubiquitin proteasome system in Alzheimer's disease.Disease-associated mutant ubiquitin causes proteasomal impairment and enhances the toxicity of protein aggregates.Tau interactome mapping based identification of Otub1 as Tau deubiquitinase involved in accumulation of pathological Tau forms in vitro and in vivo.Identification of nitric oxide as an endogenous inhibitor of 26S proteasomes in vascular endothelial cells.Selective Transgenic Expression of Mutant Ubiquitin in Purkinje Cell Stripes in the Cerebellum.Activation of the ubiquitin proteasome pathway in a mouse model of inflammatory myopathy: a potential therapeutic target Ubiquitin/proteasome pathway impairment in neurodegeneration: therapeutic implications Rsp5 ubiquitin ligase modulates translation accuracy in yeast Saccharomyces cerevisiae Role of ubiquitin-proteasome-mediated proteolysis in nervous system disease.HUWE1 and TRIP12 collaborate in degradation of ubiquitin-fusion proteins and misframed ubiquitin.Just one position-independent lysine residue can direct MelanA into proteasomal degradation following N-terminal fusion of ubiquitin.Endoplasmic reticulum stress and unfolded protein response in inclusion body myositis muscle.Proteasome inhibition and aggresome formation in sporadic inclusion-body myositis and in amyloid-beta precursor protein-overexpressing cultured human muscle fibers Identification of Caspase-6-mediated processing of the valosin containing protein (p97) in Alzheimer's disease: a novel link to dysfunction in ubiquitin proteasome system-mediated protein degradation.Accumulation of Basic Amino Acids at Mitochondria Dictates the Cytotoxicity of Aberrant Ubiquitin Extended ubiquitin species are protein-based DUB inhibitors.The ubiquitin proteasome system in synaptic and axonal degeneration: a new twist to an old cycle.The aggravating role of the ubiquitin-proteasome system in neurodegeneration.Enhancement of 26S proteasome functionality connects oxidative stress and vascular endothelial inflammatory response in diabetes mellitus.The role of ubiquitin-protein ligases in neurodegenerative disease.Intermediate filament cytoskeleton of the liver in health and disease Ubiquitin degradation with its substrate, or as a monomer in a ubiquitination-independent mode, provides clues to proteasome regulation.Appetite for destruction: E3 ubiquitin-ligase protection in cardiac disease.Stressing the ubiquitin-proteasome system.

P2860

Q24297296-6B4CDD3D-A5C4-4817-AFDB-049567F28A13 Q24310748-FBC86E8A-440F-418E-9F5B-DDB0FDC11E01 Q24311376-E1F6F875-E4A8-4D2D-95D3-0332121C9FA0 Q24314548-D64D2623-3CFB-410A-B2C0-3302C110E82D Q24317229-BDE03F17-63E9-42FE-B0E7-7A3925163C63 Q26767879-11351D42-91E7-4A82-81B1-E7A0CCF0B8B5 Q26782999-276184DB-19C5-4756-822A-449CDB4D2D73 Q27664383-5CF09887-63B9-4CC0-87BE-2495D6C8B2A8 Q27931879-351A2BFF-48C8-41BA-BEB3-8143AB59355A Q28254943-5B2BF96D-4A40-40F4-BD83-628A8C65C605 Q28266563-E515D799-F02C-4E85-A1B0-167E12191182 Q28268311-159FA130-A2B8-4288-BB53-E69815E13017 Q28509322-339132FC-03CA-4BB3-8E73-266E43577115 Q28539822-65E7BD5F-DFD9-4D8A-85A3-B423C75AC6EA Q28564338-DBD8E144-B923-41F3-80E4-091D87E62928 Q30619979-D10E0E8E-5AE2-4633-958C-9A5973057A15 Q33307872-5F53D28D-571E-489F-B463-7419C5BA9F49 Q33408783-1CEB8F4D-6725-4D87-A65A-C1FC3DE9713D Q33559307-3CCED674-807B-40A0-9D88-C23367831C59 Q33650608-306D02A2-A8B5-4AC9-B6F3-3EF2CAB14C59 Q33665458-413C0BDB-8EE0-45C8-BDCD-1AF166F987E8 Q33842215-12216E0F-E4A5-465D-96AD-0DC2EE67ECB0 Q34012297-051999B8-6051-40BF-AD9D-AE075235CF74 Q34366675-410620C6-9801-46F0-8168-4B9F732BB02E Q34372681-C3521795-22D8-48B7-A0D4-3A5C3FD4253F Q34500475-80FAA3A1-00D4-479B-B6B1-82A3D89A25A4 Q34581001-A844D2A2-CB88-4128-BEE1-CC78857AAE0B Q35083348-1CCE794D-E268-4A68-AD10-B69B0CA972EE Q35085041-D58262BB-6CBB-40C7-8B2A-5B33080D51DE Q35276123-83A65AAC-5553-4580-8CA5-E3944E857E6A Q35529325-074C27D5-205C-4386-9CB6-C5D6C10E500E Q35739138-CAEBB5B1-ECC4-4041-BF66-668FC118C636 Q35739352-1232CFAB-6792-44DA-BE39-C32E2406B99C Q36020204-3A172CED-08BE-4E48-B629-ECB34BE1863F Q36204680-5666C987-FF43-4F9B-8C2A-4AD17F2086B4 Q36565602-AD715EC1-32AD-4366-A00B-D265B9B0C4B1 Q36661678-A3150E98-B02A-41EF-90DA-3FA97BF156F3 Q37274327-40740220-756C-4245-9C15-87B40A841D9F Q37526448-804A8E40-BA9C-44E4-9177-AD2160E35941 Q37562694-BEAA72F3-E97D-4EFB-AEA5-E4022730EB13

P2860

Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation.

http://www.wikidata.org/entity/Q42917499

description

2002 nî lūn-bûn

@nan

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

2002年论文

@zh

2002年论文

@zh-cn

name

Mutant ubiquitin found in neur ...... locks proteasomal degradation.

@en

Mutant ubiquitin found in neur ...... locks proteasomal degradation.

@nl

type

label

Mutant ubiquitin found in neur ...... locks proteasomal degradation.

@en

Mutant ubiquitin found in neur ...... locks proteasomal degradation.

@nl

prefLabel

Mutant ubiquitin found in neur ...... locks proteasomal degradation.

@en

Mutant ubiquitin found in neur ...... locks proteasomal degradation.

@nl

P1433

Q42917499-3070D874-A49F-402B-958D-38A3C45605DA

P1476

Q42917499-E6C07329-6175-4F93-B48F-D17BC3C179CF

P2093

Q42917499-12C53714-AB67-4814-9811-C45E08F0B2D1

Q42917499-17799B01-8688-4638-B236-34513DA5DD3E

Q42917499-19031221-F125-4486-8E25-EBD3CF25B14A

Q42917499-A2655EC0-8045-49E7-A00D-305BF2BA6A95

Q42917499-F53ED092-E5F0-4BCE-879C-00A5AD5B0462

P2860

Q42917499-195E21A5-5BB3-4C97-AC54-AE5BDDFCD337

Q42917499-26D08C4D-8540-484B-8FEB-969F9F83AFFD

Q42917499-34A5090A-0EB1-4952-8D2A-32BCF53D4086

Q42917499-3938719C-DA15-4C5B-8A82-AE0C614C7C9E

Q42917499-3E917251-AFE1-4A99-964E-8CCEA011FDED

Q42917499-45828EA7-F7BF-48C5-BFB2-8DE4843910A9

Q42917499-4954AD9F-CC4F-44B7-9700-430FA1A4928A

Q42917499-4E7E3432-91CC-4EE9-8DD7-5B4CA3CDBA9C

Q42917499-52F48FF7-FFE4-4B51-84DD-A2D2F8F1733A

Q42917499-76502F1E-5BDF-4081-80B2-973C86028B9B

P304

Q42917499-D78461C0-25A4-4398-87F9-56FAB38AFC42

P31

Q42917499-3624743F-26FE-428F-B04C-92DFCD464F38

P356

Q42917499-1D7E3B92-AE98-4F62-8DBB-CF919F460291

P407

Q42917499-B3BCED9F-61A2-44CF-9B95-30A7D50F8E50

P433

Q42917499-D8F4D49D-BBD4-4494-B059-5C9B8EF50D17

P478

Q42917499-5C01B38A-0BC0-4D09-80B2-D58FF0A22130

P50

Q42917499-8D5EC148-8C9F-415C-966A-B33F8FA97F6D

Q42917499-C4CF532B-24A2-4936-90E6-457228D69A11

Q42917499-E03C8C83-4A70-482E-88C2-6B040A56E8C9

P577

Q42917499-7456B7AA-5750-461C-AD8E-3D1A996A2505

P5875

Q42917499-F3CE7E50-9331-4B96-BF7E-E2C0B34064D6

P698

Q42917499-7FD3AEB5-671E-4212-AAAA-2F7199EECF8B

P921

Q42917499-FBE772E8-0B23-4367-9E6C-01FD9AC2C958

P932

Q42917499-C472563E-5523-436B-BD3A-0D7A5FB44D78

P356

P1433

Journal of Cell Biology

P1476

Mutant ubiquitin found in neur ...... locks proteasomal degradation.

@en

P2093

Femke M S de Vrij

http://www.w3.org/2001/XMLSchema#string

Fred W van Leeuwen

http://www.w3.org/2001/XMLSchema#string

Kristina Lindsten

http://www.w3.org/2001/XMLSchema#string

Lisette G G C Verhoef

http://www.w3.org/2001/XMLSchema#string

Nico P Dantuma

http://www.w3.org/2001/XMLSchema#string

P2860

Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism

Metabolism of the polyubiquitin degradation signal: structure, mechanism, and role of isopeptidase T

Recognition of the polyubiquitin proteolytic signal

The N-end rule: functions, mysteries, uses

Structure of tetraubiquitin shows how multiubiquitin chains can be formed

A proteolytic pathway that recognizes ubiquitin as a degradation signal.

A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly.

Frameshift mutants of beta amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients

Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome

In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector

P304

417-427

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1083/JCB.200111034

http://www.w3.org/2001/XMLSchema#string

P407

P433

3

http://www.w3.org/2001/XMLSchema#string

P478

157

http://www.w3.org/2001/XMLSchema#string

P50

David F Fischer

P577

2002-04-29T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

11388403

http://www.w3.org/2001/XMLSchema#string

P698

11980917

http://www.w3.org/2001/XMLSchema#string

P921

neurodegeneration

P932

2173284

http://www.w3.org/2001/XMLSchema#string