Spinocerebellar ataxia with axonal neuropathy: consequence of a Tdp1 recessive neomorphic mutation? - Test2 - elhamkhani - TriplyDB

Spinocerebellar ataxia with axonal neuropathy: consequence of a Tdp1 recessive neomorphic mutation?

Spinocerebellar ataxia with axonal neuropathy: consequence of a Tdp1 recessive neomorphic mutation?

http://www.wikidata.org/entity/Q24298259

about

Optimal function of the DNA repair enzyme TDP1 requires its phosphorylation by ATM and/or DNA-PK The Response to Oxidative DNA Damage in Neurons: Mechanisms and Disease Analysis of the Active-Site Mechanism of Tyrosyl-DNA Phosphodiesterase I: A Member of the Phospholipase D Superfamily Tyrosyl-DNA phosphodiesterase and the repair of 3'-phosphoglycolate-terminated DNA double-strand breaks.Processing of damaged DNA ends for double-strand break repair in mammalian cells TDP2 protects transcription from abortive topoisomerase activity and is required for normal neural function DNA Topoisomerase I Inhibitors: Chemistry, Biology, and Interfacial Inhibition Identification of phosphotyrosine mimetic inhibitors of human tyrosyl-DNA phosphodiesterase I by a novel AlphaScreen high-throughput assay Role of tyrosyl-DNA phosphodiesterase (TDP1) in mitochondria.In vitro complementation of Tdp1 deficiency indicates a stabilized enzyme-DNA adduct from tyrosyl but not glycolate lesions as a consequence of the SCAN1 mutation The DNA binding and 3'-end preferential activity of human tyrosyl-DNA phosphodiesterase.Tyrosyl-DNA-phosphodiesterases (TDP1 and TDP2).Biochemical assays for the discovery of TDP1 inhibitors DNA repair deficiency in neurodegeneration.Colon cancer associated genes exhibit signatures of positive selection at functionally significant positions Neuroprotection and repair of 3'-blocking DNA ends by glaikit (gkt) encoding Drosophila tyrosyl-DNA phosphodiesterase 1 (TDP1).Topoisomerase 1 provokes the formation of short deletions in repeated sequences upon high transcription in Saccharomyces cerevisiae.Neurological disorders associated with DNA strand-break processing enzymes.Poly(ADP-ribose) polymerase and XPF-ERCC1 participate in distinct pathways for the repair of topoisomerase I-induced DNA damage in mammalian cells.Effects of DNA and protein size on substrate cleavage by human tyrosyl-DNA phosphodiesterase 1.Tyrosyl-DNA Phosphodiesterase 1 (Tdp1) inhibitors Exercise Capacity and Response to Training Quantitative Trait Loci in a NZW X 129S1 Intercross and Combined Cross Analysis of Inbred Mouse Strains.Tyrosyl-DNA phosphodiesterase 1 (TDP1) repairs DNA damage induced by topoisomerases I and II and base alkylation in vertebrate cells.Penetrance of biallelic SMARCAL1 mutations is associated with environmental and genetic disturbances of gene expression Oxidative genome damage and its repair: implications in aging and neurodegenerative diseases.TDP2 promotes repair of topoisomerase I-mediated DNA damage in the absence of TDP1.DNA damage and repair: relevance to mechanisms of neurodegeneration Brain capacity for repair of oxidatively damaged DNA and preservation of neuronal function.TDP1 repairs nuclear and mitochondrial DNA damage induced by chain-terminating anticancer and antiviral nucleoside analogs.DNA strand breaks, neurodegeneration and aging in the brain.DNA repair deficiency and neurological disease.4-Pregnen-21-ol-3,20-dione-21-(4-bromobenzenesulfonate) (NSC 88915) and related novel steroid derivatives as tyrosyl-DNA phosphodiesterase (Tdp1) inhibitors.Epigenetic and genetic inactivation of tyrosyl-DNA-phosphodiesterase 1 (TDP1) in human lung cancer cells from the NCI-60 panel PARP1-TDP1 coupling for the repair of topoisomerase I-induced DNA damage.To live or to die: a matter of processing damaged DNA termini in neurons.Oxidative genome damage and its repair in neurodegenerative diseases: function of transition metals as a double-edged sword.When orthologs diverge between human and mouse.Oxidized base damage and single-strand break repair in mammalian genomes: role of disordered regions and posttranslational modifications in early enzymes.Resolution of complex ends by Nonhomologous end joining - better to be lucky than good?Tyrosyl-DNA phosphodiesterase I resolves both naturally and chemically induced DNA adducts and its potential as a therapeutic target.

P2860

2412a9532ae9e6235b2255ae4acd86bd50bd6f58 7897a2265db1859c888b3424c348155aa60ec210 addf9ab6f92c5f0e86ea72c476ae59d491aca91e c46871debac1841035961f59a35a78037c3fe576 d404ce027e6bb1293fa114b00296060988928daa f5990a11f5e1aaf35e9c20c81e170758b436feec

P248

Q24644674-D721AB08-B75C-49A0-B20E-BCEA367F9E95 Q26768287-93C3B2DB-4280-45D6-9428-A2636C0DD869 Q27676072-259011DB-813E-4A4E-8599-5A4D084DD5D2 Q27967652-FBD78429-CC2D-4923-BDE7-A679CE6D0FB3 Q28000148-9837C25F-EDB1-47B8-959F-30086745576A Q28118952-659CF3AC-8EAB-4F4A-955B-47206B3D1590 Q29400901-42C16C75-0970-4561-859D-83D1B0AB93D4 Q33399360-17C1B8D4-45D9-4F41-8B5F-08F1BD9967E4 Q33735624-D1DACF2F-AC5D-4E90-B874-8FF9729B889E Q33747764-E720079F-20B1-4226-9577-F5F3E10B82BC Q33783186-A2B5FB5D-60BC-4A3E-B5D2-BEC324862297 Q33875792-9BCC14C3-9E79-4502-A8FE-9881C817F7EA Q34021070-BD45E6C5-9777-4883-8DFC-F974EDC0D642 Q34183328-600295E2-4F2F-4091-B864-B4FF414B6E70 Q34334316-599E6A22-9A6E-454F-9448-0B7BB5E8A67C Q34480920-BE4F3A5F-B5A4-436A-8A16-928C65CBFFB8 Q34490822-0DE6CC9C-BB9E-4D12-B06F-5722C6792329 Q34535722-4CE4DAF3-701C-4202-9DA1-FDF85B739186 Q34946954-1594C3EE-4F02-4E89-B086-41A2B36B1940 Q35152316-BEF5F81E-D9A2-44A2-BC23-9AC65BD3D0B1 Q35167579-63EE50E2-F039-4CA9-B081-6CB4E805558F Q35879619-CDAE982D-97BD-46D3-8F29-D25E83DF47F3 Q35921514-1FB940F1-47A3-4070-BF4A-8AEC87A07F79 Q35950455-7BEAFDAE-BFBC-458C-B5D2-F15FBDF494A1 Q35957287-C1831AA5-185E-48CD-A211-9819826E2971 Q36280725-C69F9922-E48C-4245-A1C1-ADEAFA584B77 Q36775988-7870EB64-0B9E-4271-899C-DA7E691C1E9E Q37122200-C74DC32B-87CA-437A-AAF6-B9BDC4779AFE Q37148469-2F0A4304-E947-4E6E-9DB9-52885ACB0B9C Q37154126-63316714-BF5E-43F4-908B-A867E79ECB2B Q37368873-F9090670-A16A-423E-889D-5A794CF609BB Q37445367-01E86415-1A2F-479B-A818-DC5176D1D1BC Q37572609-CAE31704-7B73-4E04-969B-57BCE964490B Q37701295-440F408A-E45B-4033-9DB3-4BF215977E9A Q37830005-2342D4FA-8E64-4202-A213-3E4366BB3D3F Q37858347-5CC940E4-1E0E-4F75-A01A-4FB2B8273063 Q37890153-47584BF5-B78D-49FE-AFCD-6A62AAD939A7 Q38022936-822535AC-0285-4474-890B-607DF81BC54D Q38070431-56B726DE-2F56-49B4-A8B9-855F8637626C Q38261264-F06299FE-33E1-4379-A446-4E987903AAED

P2860

Spinocerebellar ataxia with axonal neuropathy: consequence of a Tdp1 recessive neomorphic mutation?

http://www.wikidata.org/entity/Q24298259

description

2007 nî lūn-bûn

@nan

2007 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

name

Spinocerebellar ataxia with ax ...... recessive neomorphic mutation?

@ast

Spinocerebellar ataxia with ax ...... recessive neomorphic mutation?

@en

Spinocerebellar ataxia with ax ...... recessive neomorphic mutation?

@en-gb

Spinocerebellar ataxia with ax ...... recessive neomorphic mutation?

@nl

type

label

Spinocerebellar ataxia with ax ...... recessive neomorphic mutation?

@ast

Spinocerebellar ataxia with ax ...... recessive neomorphic mutation?

@en

Spinocerebellar ataxia with ax ...... recessive neomorphic mutation?

@en-gb

Spinocerebellar ataxia with ax ...... recessive neomorphic mutation?

@nl

prefLabel

Spinocerebellar ataxia with ax ...... recessive neomorphic mutation?

@ast

Spinocerebellar ataxia with ax ...... recessive neomorphic mutation?

@en

Spinocerebellar ataxia with ax ...... recessive neomorphic mutation?

@en-gb

Spinocerebellar ataxia with ax ...... recessive neomorphic mutation?

@nl

P1433

Q24298259-988BE048-DCE1-43DE-9CC2-5AFE23993652

P1476

Q24298259-F18428E3-B795-4926-A56F-3B8704BCBCDA

P2093

Q24298259-2B2135C7-1AC9-4B33-98D4-A60FAA2C4E6C

Q24298259-3CDF2494-B754-490A-AF3D-C27725AE0E52

Q24298259-462F77FF-B22B-4A69-8F4C-8CA73043F89C

Q24298259-4CAC3AEB-9F62-46AE-BC9C-8DC6F0AD7FD4

Q24298259-5257807A-0BCF-4DDF-B2FE-3CECC1A19F06

Q24298259-5784C723-E1C0-48A7-89AF-F456DF7D7617

Q24298259-799305F9-31B1-4FD9-A1EB-1484DBC09C62

Q24298259-88DFFF24-65E6-42C4-9215-B43326AF03EE

Q24298259-92256034-27A0-462B-B21B-7FA33203C8B2

Q24298259-9FDB9B31-0DA9-415F-B153-C44CCF128B0A

P2860

Q24298259-0990D120-0AC9-40B4-8F08-35D6821E3C3B

Q24298259-0D889EA2-16A5-4EED-8064-9FB9DDEF7120

Q24298259-0E6407A6-C583-4AB1-92BA-8A463BB8DA90

Q24298259-178AD1B7-6DBE-4BC2-B14A-CDEC9608AF3E

Q24298259-2AB81967-08B4-4799-AE3A-BE98DBF425B1

Q24298259-2E58BFC6-381F-4693-AEFC-F4A23B0C34D8

Q24298259-31D8F873-CD6F-4BD7-AD80-D603C6847EDE

Q24298259-33939A6F-EAF1-4479-B2D1-F5FA5738C561

Q24298259-38517E4D-B1F5-47C0-97B3-E3745900F3BE

Q24298259-3FF1A44E-8110-4DEE-B080-9ADA04D05E98

P304

Q24298259-B76D105F-1317-4203-8BE5-98D0C425108F

P31

Q24298259-74F96FD3-32D2-4995-BF09-83E2A185D844

P356

Q24298259-7AC67379-3D84-4A5F-8C6E-52B980DADC26

P407

Q24298259-07C31865-9504-449A-A5D0-DB4901BB5E23

P433

Q24298259-C8101C42-05BA-42AB-B5D7-766626322B28

P478

Q24298259-F652FCA2-D62C-47D9-9FDC-E3C5C74C4ACE

P577

Q24298259-5440092D-1BEB-437A-8B69-568D873F742E

P5875

Q24298259-E74D8F93-94FC-4242-BF49-EDF90A08777F

P698

Q24298259-02B2DC45-A41F-4F5C-8359-597E0F8F0534

P921

Q24298259-0520EB4D-7318-4AC6-89FC-FC76CDA6AEE9

Q24298259-524EF5BD-66D6-40A6-8BA7-B9B9664A7AEF

Q24298259-772EC112-C492-4BCC-A818-041D52F9D9A1

Q24298259-DF3703DC-DD48-404E-B414-7132DC87F68C

P932

Q24298259-2E523703-3593-4C6A-A633-BEA217968741

P356

SJ.EMBOJ.7601885

P1433

The EMBO Journal

P1476

Spinocerebellar ataxia with ax ...... recessive neomorphic mutation?

@en

P2093

Cheng Huang

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

Cornelius F Boerkoel

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

Dawna L Armstrong

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

Fujio Umehara

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

Heidrun Interthal

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

Hiroshi Takashima

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

James J Champoux

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

Jennifer L Northrop

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

Ken Inoue

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

Kimiko Deguchi

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

P2860

Defective DNA single-strand break repair in spinocerebellar ataxia with axonal neuropathy-1

Conversion of phosphoglycolate to phosphate termini on 3' overhangs of DNA double strand breaks by the human tyrosyl-DNA phosphodiesterase hTdp1

Identification and characterization of human MUS81-MMS4 structure-specific endonuclease

Human DNA repair excision nuclease. Analysis of the roles of the subunits involved in dual incisions by using anti-XPG and anti-ERCC1 antibodies

The tyrosyl-DNA phosphodiesterase Tdp1 is a member of the phospholipase D superfamily

Deficiency in 3'-phosphoglycolate processing in human cells with a hereditary mutation in tyrosyl-DNA phosphodiesterase (TDP1)

ERCC4 (XPF) encodes a human nucleotide excision repair protein with eukaryotic recombination homologs

Yeast Tdp1 and Rad1-Rad10 function as redundant pathways for repairing Top1 replicative damage.

Repair of topoisomerase I covalent complexes in the absence of the tyrosyl-DNA phosphodiesterase Tdp1.

Tyrosyl-DNA phosphodiesterase (Tdp1) participates in the repair of Top2-mediated DNA damage

P304

4732-43

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

P31

scholarly article

P356

10.1038/SJ.EMBOJ.7601885

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

P407

P433

22

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

P478

26

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

P577

2007-11-14T00:00:00Z

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

P5875

5897723

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

P698

17948061

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

P921

Tyrosyl-DNA phosphodiesterase 1

3'-tyrosyl-DNA phosphodiesterase activity

Tyrosyl-DNA phosphodiesterase 1

P932

2080798

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