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

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

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

http://www.wikidata.org/entity/Q24293001

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Human single-stranded DNA binding proteins are essential for maintaining genomic stability Structure of RPA32 bound to the N-terminus of SMARCAL1 redefines the binding interface between RPA32 and its interacting proteins Interaction and colocalization of Rad9/Rad1/Hus1 checkpoint complex with replication protein A in human cells Physical and functional mapping of the replication protein a interaction domain of the werner and bloom syndrome helicases An alternative form of replication protein a prevents viral replication in vitro Evidence for direct contact between the RPA3 subunit of the human replication protein A and single-stranded DNA A naturally occurring human RPA subunit homolog does not support DNA replication or cell-cycle progression Different activities of the largest subunit of replication protein A cooperate during SV40 DNA replication Structural classification of zinc fingers: survey and summary.Domain architecture and biochemical characterization of vertebrate Mcm10 DNA damage-induced ubiquitylation of RFC2 subunit of replication factor C complex Role of the XPA protein in the NER pathway: A perspective on the function of structural disorder in macromolecular assembly RPA homologs and ssDNA processing during meiotic recombination RPA-coated single-stranded DNA as a platform for post-translational modifications in the DNA damage response Multiple facets of TPP1 in telomere maintenance Single-stranded DNA-binding proteins: multiple domains for multiple functions Dynamic binding of replication protein a is required for DNA repair.A metal-binding site in the catalytic subunit of anaerobic ribonucleotide reductase Insights into ssDNA recognition by the OB fold from a structural and thermodynamic study of Sulfolobus SSB protein The structure of SSO2064, the first representative of Pfam family PF01796, reveals a novel two-domain zinc-ribbon OB-fold architecture with a potential acyl-CoA-binding role Structure and Cellular Roles of the RMI Core Complex from the Bloom Syndrome Dissolvasome Crystal structures of RMI1 and RMI2, two OB-fold regulatory subunits of the BLM complex Structural bases of dimerization of yeast telomere protein Cdc13 and its interaction with the catalytic subunit of DNA polymerase α Structures of a key interaction protein from the Trypanosoma brucei editosome in complex with single domain antibodies Structure and conformational change of a replication protein A heterotrimer bound to ssDNA Analyses of Candida Cdc13 Orthologues Revealed a Novel OB Fold Dimer Arrangement, Dimerization-Assisted DNA Binding, and Substantial Structural Differences between Cdc13 and RPA70 Structural basis for Tetrahymena telomerase processivity factor Teb1 binding to single-stranded telomeric-repeat DNA Structure of the Human Telomeric Stn1-Ten1 Capping Complex Reappearance from Obscurity: Mammalian Rad52 in Homologous Recombination Characteristics and concepts of dynamic hub proteins in DNA processing machinery from studies of RPA Nucleic acid recognition by OB-fold proteins Oligonucleotide/oligosaccharide-binding fold proteins: a growing family of genome guardians The telomere capping complex CST has an unusual stoichiometry, makes multipartite interaction with G-Tails, and unfolds higher-order G-tail structures Replication Protein A Presents Canonical Functions and Is Also Involved in the Differentiation Capacity of Trypanosoma cruzi MEIOB targets single-strand DNA and is necessary for meiotic recombination A DNA polymerase-{alpha}{middle dot}primase cofactor with homology to replication protein A-32 regulates DNA replication in mammalian cells A dynamic model for replication protein A (RPA) function in DNA processing pathways Two distinct SSB protein families in nucleo-cytoplasmic large DNA viruses.Saccharomyces cerevisiae replication protein A binds to single-stranded DNA in multiple salt-dependent modes Torsional regulation of hRPA-induced unwinding of double-stranded DNA.

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

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2002 nî lūn-bûn

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2002 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2002 թվականի ապրիլին հրատարակված գիտական հոդված

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2002年の論文

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Structure of the RPA trimeriza ...... p DNA-binding mechanism of RPA

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Structure of the RPA trimeriza ...... p DNA-binding mechanism of RPA

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Structure of the RPA trimeriza ...... p DNA-binding mechanism of RPA

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Structure of the RPA trimeriza ...... p DNA-binding mechanism of RPA

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Structure of the RPA trimeriza ...... p DNA-binding mechanism of RPA

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Structure of the RPA trimeriza ...... p DNA-binding mechanism of RPA

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Structure of the RPA trimeriza ...... p DNA-binding mechanism of RPA

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Structure of the RPA trimeriza ...... p DNA-binding mechanism of RPA

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Structure of the RPA trimeriza ...... p DNA-binding mechanism of RPA

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Structure of the RPA trimeriza ...... p DNA-binding mechanism of RPA

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Elena Bochkareva

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Sergey Korolev

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Susan P Lees-Miller

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P2860

The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding

Replication Protein A (RPA): The Eukaryotic SSB

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

The evolutionarily conserved zinc finger motif in the largest subunit of human replication protein A is required for DNA replication and mismatch repair but not for nucleotide excision repair

The alpha-helical FXXPhiPhi motif in p53: TAF interaction and discrimination by MDM2

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

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Human replication protein A: global fold of the N-terminal RPA-70 domain reveals a basic cleft and flexible C-terminal linker

The solution structure of ribosomal protein L36 from Thermus thermophilus reveals a zinc-ribbon-like fold

Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RAD52 by replication factor RPA

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10.1093/EMBOJ/21.7.1855

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7

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21

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11437029

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11927569

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Replication protein A1

Replication protein A2

Replication protein A3

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125950

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