A mammalian factor that binds telomeric TTAGGG repeats in vitro - Test2 - elhamkhani - TriplyDB

A mammalian factor that binds telomeric TTAGGG repeats in vitro

A mammalian factor that binds telomeric TTAGGG repeats in vitro

http://www.wikidata.org/entity/Q24293724

about

TIN2, a new regulator of telomere length in human cells TIN2 is a tankyrase 1 PARP modulator in the TRF1 telomere length control complex HOT1 is a mammalian direct telomere repeat-binding protein contributing to telomerase recruitment Telomere-binding protein TRF2 binds to and stimulates the Werner and Bloom syndrome helicases Characterization and cell cycle regulation of the related human telomeric proteins Pin2 and TRF1 suggest a role in mitosis TRF1 is a dimer and bends telomeric DNA The human telomere-associated protein TIN2 stimulates interactions between telomeric DNA tracts in vitro Shelterin complex and associated factors at human telomeres Nucleostemin delays cellular senescence and negatively regulates TRF1 protein stability Telomeres-structure, function, and regulation NBS1 and TRF1 colocalize at promyelocytic leukemia bodies during late S/G2 phases in immortalized telomerase-negative cells. Implication of NBS1 in alternative lengthening of telomeres A human interstitial telomere associates in vivo with specific TRF2 and TIN2 proteins A comprehensive model for the recognition of human telomeres by TRF1 Transcriptional activation of TINF2, a gene encoding the telomere-associated protein TIN2, by Sp1 and NF-κB factors Molecular recognition in complexes of TRF proteins with telomeric DNA Malaria parasites possess a telomere repeat-binding protein that shares ancestry with transcription factor IIIA Sequence-specific binding to telomeric DNA by CEH-37, a homeodomain protein in the nematode Caenorhabditis elegans.Molecular Architecture of Full-length TRF1 Favors Its Interaction with DNA TopoIIα prevents telomere fragility and formation of ultra thin DNA bridges during mitosis through TRF1-dependent binding to telomeres Resolution of telomere associations by TRF1 cleavage in mouse embryonic stem cells The Leishmania amazonensis TRF (TTAGGG repeat-binding factor) homologue binds and co-localizes with telomeres Chemistry in human telomere biology: structure, function and targeting of telomere DNA/RNA.Trypanosome telomeres are protected by a homologue of mammalian TRF2.Strand exchange of telomeric DNA catalyzed by the Werner syndrome protein (WRN) is specifically stimulated by TRF2 Human telomeric proteins occupy selective interstitial sites.Telomere Biology-Insights into an Intriguing Phenomenon.Revealing novel telomere proteins using in vivo cross-linking, tandem affinity purification, and label-free quantitative LC-FTICR-MS The terminal DNA structure of mammalian chromosomes.Novel function of the Fanconi anemia group J or RECQ1 helicase to disrupt protein-DNA complexes in a replication protein A-stimulated manner.Gbp1p, a protein with RNA recognition motifs, binds single-stranded telomeric DNA and changes its binding specificity upon dimerization.Chromatin organization and remodeling of interstitial telomeric sites during meiosis in the Mongolian gerbil (Meriones unguiculatus).Telomeres, chromosome instability and cancer Evidence for a HeLa nuclear protein that binds specifically to the single-stranded d(CCCTAA)n telomeric motif.In vitro and in vivo reconstitution and stability of vertebrate chromosome ends.Telomere length modulation in human astroglial brain tumors Telomeres and aging.Activation of telomerase in a human tumor Ku acts in a unique way at the mammalian telomere to prevent end joining.Characterization of recombination in the HLA class II region.Stringent sequence requirements for the formation of human telomeres.

P2860

Q22010863-E7724D11-416E-4981-B374-0101528AC241 Q24292755-4AC0A4BE-9BD4-4F09-9EA6-26DA2E08C0A7 Q24293211-08F06802-347B-4E0E-9E34-2AA49AD2DE6A Q24304488-39221B1E-E743-4C38-B530-CC2BF690BF73 Q24311518-6C39D8D2-748A-4E3A-AA4D-243146674836 Q24318291-F9C5C03B-4B42-454B-9EC7-424EF40B6492 Q24536029-8CA0C30B-B90F-4555-89E1-49EBCCF82F3F Q24601577-F8743E8F-91E2-4655-9812-3CDD38BD3A3B Q24672458-F92AB555-6FC5-4AFD-A405-84E3D899EC1F Q26853108-2F5BEC93-A698-48DD-AE76-5A48918464C0 Q28141883-5C6E3BBC-9C5B-4DE1-AC04-96269D3F590C Q28213455-AFC9B4AF-B331-4F64-B510-5D1D9D9BE8E9 Q28291302-D6B339BC-33B1-491F-B759-116DEE399CF6 Q28478698-286F226C-71B1-4159-9F76-086855BC5326 Q28540156-1DF40179-FF1B-45BC-B836-6FF9FC630E5B Q30041295-9F909CDE-4254-474A-90C0-42561D53C7FF Q30332771-EF1D408E-7F03-4ED4-9EDC-146943A22580 Q30392263-3AA59C11-F59D-46D7-8CDE-1A47CBBF31C8 Q30580233-AF67F4D0-013A-4025-9DD8-5D1413948EEF Q30581726-6F6FF06F-32A0-4966-8736-E666B2583AEA Q33575192-FC7CFC74-00F0-4DBC-AC84-4676948AFFA4 Q33814333-8B6F5B48-1213-43C5-8182-AF8D0478B4FD Q33836828-0E246412-C588-4D44-9B2F-A29E4ADE64D9 Q33843105-431462E1-1E37-4AA6-A044-B12042341637 Q33851199-1617ED26-486A-48E3-81AD-C5DA35E46423 Q33855946-1F144AE4-21E0-4C6F-872B-E597C8CA375F Q33883012-CC8BCF0B-C12B-4FA7-B7D8-0A6A0A8601E4 Q33886897-0B04F531-2B8F-43F9-B9D4-91B57A2CECF3 Q33931112-50682E78-1DF6-4130-AB39-4C82918FD4CF Q33957324-B50983C5-D27E-43A0-86D8-BEA8071ADB90 Q34016558-3617530D-F19A-471D-B541-141773523644 Q34595437-2F8B9AF2-229A-4397-B2B7-3F60097C9103 Q34615196-09507793-AD87-4952-815C-D8B95BB409A2 Q34668792-38055B73-E2BD-42B3-9FCD-4B58F1349B82 Q34731430-90928AB9-252A-4EF7-97CE-2153A0FFA810 Q34768068-9D8DB2D7-C747-4118-889D-76F586231FA6 Q35141128-5363BCD4-7A27-45EC-819D-71462BE7DEDF Q35207184-2141BD7B-5DD1-48C0-B11D-E011F356DCE0 Q35238365-C16FB73A-F24B-442F-9D4A-76CECFA1AD25 Q35751600-595106C2-C420-4FA4-87FC-F846470A9C85

P2860

A mammalian factor that binds telomeric TTAGGG repeats in vitro

http://www.wikidata.org/entity/Q24293724

description

1992 nî lūn-bûn

@nan

1992 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

1992 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

1992年の論文

@ja

1992年論文

@yue

1992年論文

@zh-hant

1992年論文

@zh-hk

1992年論文

@zh-mo

1992年論文

@zh-tw

1992年论文

@wuu

name

A mammalian factor that binds telomeric TTAGGG repeats in vitro

@ast

A mammalian factor that binds telomeric TTAGGG repeats in vitro

@en

A mammalian factor that binds telomeric TTAGGG repeats in vitro

@nl

type

label

A mammalian factor that binds telomeric TTAGGG repeats in vitro

@ast

A mammalian factor that binds telomeric TTAGGG repeats in vitro

@en

A mammalian factor that binds telomeric TTAGGG repeats in vitro

@nl

prefLabel

A mammalian factor that binds telomeric TTAGGG repeats in vitro

@ast

A mammalian factor that binds telomeric TTAGGG repeats in vitro

@en

A mammalian factor that binds telomeric TTAGGG repeats in vitro

@nl

P1433

Q24293724-EE70F7BE-C13D-4CDD-8E24-0103EDD15177

P1476

Q24293724-E71CD2EA-8EA1-4754-A57F-451DE66DF80C

P2093

Q24293724-33D8B75F-25C3-414F-AB06-673BC9949E89

Q24293724-5EDC45CB-C908-40C4-AF96-856CA0E6953A

Q24293724-E3AB26DA-F073-4CA1-86EB-9CF49052E7B7

P2860

Q24293724-01A1EE1A-62BB-4221-B51C-9972108A2B64

Q24293724-027BCA47-D8A2-4D94-8F31-8F237DBEFDA0

Q24293724-04B38B98-16A3-417D-9B9C-3F40A130C5C6

Q24293724-096A4248-D7D2-446A-AA28-8CBFAAF22A3C

Q24293724-0F250CBD-613E-492A-BE79-94FFD8D2ADB7

Q24293724-107FF272-8359-4E61-9D5B-C7AE0E9C26C8

Q24293724-17D145BF-189D-4D0F-95AA-31958F4095FF

Q24293724-185A9A1A-6051-49C5-8A88-A6CAC22121E6

Q24293724-198ACC81-368F-4C72-B0AA-5D52F1540A17

Q24293724-1A3C1C4F-4BD5-4D5B-BDB5-554C7A59E9C2

P304

Q24293724-6A542D50-4BF6-4DE7-9052-FB04E2C770CF

P31

Q24293724-9D60F2DC-C4B7-474B-8DB4-445EEBC29F39

P3181

Q24293724-E00B609C-EE26-4E35-A4AE-1313DECACDAE

P356

Q24293724-4EFBA655-6901-4F78-8937-C1022BC261C7

P407

Q24293724-276576F8-2BA5-4D1A-8032-E2C3651F115B

P433

Q24293724-ED90C2C4-00F3-4FEC-BB0E-799CA061BAEC

P478

Q24293724-62F2CBE4-216F-4BE2-9EC5-ABC5FC207868

P50

Q24293724-0FC9A8A5-5527-413D-BD16-9C32CD160B7F

P577

Q24293724-32680829-4EF1-4382-B6FD-CF726F72A27F

P698

Q24293724-0E0A6EF8-CDA7-4E5E-810D-F1876C36BC9F

P921

Q24293724-BC74FA9E-85E8-4C94-8CDD-485C71C10013

P932

Q24293724-28F95875-D27F-4B78-9040-4D3260A45DA7

P3181

P356

P1433

Molecular and Cellular Biology

P1476

A mammalian factor that binds telomeric TTAGGG repeats in vitro

@en

P2093

L Shiue

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

S Kaplan

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

Z Zhong

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

P2860

Origin of human chromosome 2: an ancestral telomere-telomere fusion

The human telomere terminal transferase enzyme is a ribonucleoprotein that synthesizes TTAGGG repeats

Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes

GCN4, a eukaryotic transcriptional activator protein, binds as a dimer to target DNA

Extensive telomere repeat arrays in mouse are hypervariable

Human telomeres contain at least three types of G-rich repeat distributed non-randomly

Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei

Two DNA-binding factors recognize specific sequences at silencers, upstream activating sequences, autonomously replicating sequences, and telomeres in Saccharomyces cerevisiae

Involvement of the silencer and UAS binding protein RAP1 in regulation of telomere length.

Heat shock factor and the heat shock response

P304

4834-43

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

P31

scholarly article

P3181

1388370

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

P356

10.1128/MCB.12.11.4834

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

P407

P433

11

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

P478

12

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

P50

P577

1992-11-01T00:00:00Z

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

P698

1406665

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

P921

P932

360416

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