Structural bases of dimerization of yeast telomere protein Cdc13 and its interaction with the catalytic subunit of DNA polymerase α - Wikidata - thesis-toulmin - TriplyDB

Structural bases of dimerization of yeast telomere protein Cdc13 and its interaction with the catalytic subunit of DNA polymerase α

Structural bases of dimerization of yeast telomere protein Cdc13 and its interaction with the catalytic subunit of DNA polymerase α

http://www.wikidata.org/entity/Q27664722

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Human single-stranded DNA binding proteins are essential for maintaining genomic stability Finding the end: recruitment of telomerase to telomeres Regulating telomere length from the inside out: the replication fork model Structure and function of the telomeric CST complex Single-stranded DNA-binding proteins: multiple domains for multiple functions Analyses of Candida Cdc13 Orthologues Revealed a Novel OB Fold Dimer Arrangement, Dimerization-Assisted DNA Binding, and Substantial Structural Differences between Cdc13 and RPA70 Cdc13 OB2 Dimerization Required for Productive Stn1 Binding and Efficient Telomere Maintenance Telomere DNA recognition in Saccharomycotina yeast: potential lessons for the co-evolution of ssDNA and dsDNA-binding proteins and their target sites The telomere capping complex CST has an unusual stoichiometry, makes multipartite interaction with G-Tails, and unfolds higher-order G-tail structures CTC1 deletion results in defective telomere replication, leading to catastrophic telomere loss and stem cell exhaustion DNA-induced dimerization of the single-stranded DNA binding telomeric protein Pot1 from Schizosaccharomyces pombe Duplication and functional specialization of the telomere-capping protein Cdc13 in Candida species Insights into Cdc13 dependent telomere length regulation.Structural anatomy of telomere OB proteins The oligonucleotide binding (OB)-fold domain of KREPA4 is essential for stable incorporation into editosomes Human CST has independent functions during telomere duplex replication and C-strand fill-in Archaeology of eukaryotic DNA replication The tenacious recognition of yeast telomere sequence by Cdc13 is fully exerted by a single OB-fold domain.Combinatorial recognition of a complex telomere repeat sequence by the Candida parapsilosis Cdc13AB heterodimer The CDC13-STN1-TEN1 complex stimulates Pol α activity by promoting RNA priming and primase-to-polymerase switch.The telomeric Cdc13 protein interacts directly with the telomerase subunit Est1 to bring it to telomeric DNA ends in vitro.The Telomere Binding Protein Cdc13 and the Single-Stranded DNA Binding Protein RPA Protect Telomeric DNA from Resection by Exonucleases.SUMOylation regulates telomere length homeostasis by targeting Cdc13.Tying up the Ends: Plasticity in the Recognition of Single-Stranded DNA at Telomeres.STN1 OB Fold Mutation Alters DNA Binding and Affects Selective Aspects of CST Function.Everything you ever wanted to know about Saccharomyces cerevisiae telomeres: beginning to end.The Tetrahymena telomerase p75-p45-p19 subcomplex is a unique CST complex Novel phosphorylation sites in the S. cerevisiae Cdc13 protein reveal new targets for telomere length regulation.Telomerase and telomere-associated proteins: structural insights into mechanism and evolution.Telomere-end processing: mechanisms and regulation.Biology of telomeres: lessons from budding yeast.Telomere length regulation in budding yeasts.Spatial Organization and Molecular Interactions of the Schizosaccharomyces pombe Ccq1-Tpz1-Poz1 Shelterin Complex.Progress in Human and Tetrahymena Telomerase Structure Determination.Genome-wide studies of telomere biology in budding yeast A sharp Pif1-dependent threshold separates DNA double-strand breaks from critically short telomeres.Interplay between nonsense-mediated mRNA decay and DNA damage response pathways reveals that Stn1 and Ten1 are the key CST telomere-cap components.Structural Insights into Yeast Telomerase Recruitment to Telomeres.Structural and functional analysis of an OB-fold in human Ctc1 implicated in telomere maintenance and bone marrow syndromes.Structure of the fission yeast S. pombe telomeric Tpz1-Poz1-Rap1 complex.

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Structural bases of dimerization of yeast telomere protein Cdc13 and its interaction with the catalytic subunit of DNA polymerase α

http://www.wikidata.org/entity/Q27664722

description

2011 nî lūn-bûn

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2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի փետրվարին հրատարակված գիտական հոդված

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2011年の論文

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2011年学术文章

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2011年学术文章

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2011年学术文章

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2011年学术文章

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2011年学术文章

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2011年學術文章

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name

Structural bases of dimerizati ...... ic subunit of DNA polymerase α

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Structural bases of dimerizati ...... ic subunit of DNA polymerase α

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Structural bases of dimerizati ...... ic subunit of DNA polymerase α

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Structural bases of dimerizati ...... ic subunit of DNA polymerase α

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Structural bases of dimerizati ...... ic subunit of DNA polymerase α

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Brian C Freeman

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Diane C DeZwaan

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Jia Sun

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Ke Wan

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

Ming Lei

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

Neal F Lue

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

Ninghui Mao

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

Tai-Yuan Yu

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

Yi-Chien Lin

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

Yuting Yang

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

P2860

Human telomerase contains two cooperating telomerase RNA molecules.

Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA

The POT1-TPP1 telomere complex is a telomerase processivity factor

RPA-like mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded DNA and protects telomeres independently of the Pot1 pathway

Conserved telomere maintenance component 1 interacts with STN1 and maintains chromosome ends in higher eukaryotes

Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA

Human telomeres contain two distinct Myb-related proteins, TRF1 and TRF2

TRF1 is a dimer and bends telomeric DNA

OB fold-containing protein 1 (OBFC1), a human homolog of yeast Stn1, associates with TPP1 and is implicated in telomere length regulation

Improved methods for building protein models in electron density maps and the location of errors in these models

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scholarly article

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10.1038/CR.2010.138

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2

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21

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1050614596

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