Determinants of sequence-specificity within human AID and APOBEC3G - Wikidata - wikimedia - TriplyDB

Determinants of sequence-specificity within human AID and APOBEC3G

Determinants of sequence-specificity within human AID and APOBEC3G

http://www.wikidata.org/entity/Q33885890

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Structure-function analyses point to a polynucleotide-accommodating groove essential for APOBEC3A restriction activities The APOBEC3 family of retroelement restriction factors Suppression of APOBEC3-mediated restriction of HIV-1 by Vif Crystal Structure of the DNA Cytosine Deaminase APOBEC3F: The Catalytically Active and HIV-1 Vif-Binding Domain 1.92 Angstrom Zinc-Free APOBEC3F Catalytic Domain Crystal Structure Base damage within single-strand DNA underlies in vivo hypermutability induced by a ubiquitous environmental agent Rationalisation of the differences between APOBEC3G structures from crystallography and NMR studies by molecular dynamics simulations Regulation of immunoglobulin class-switch recombination: choreography of noncoding transcription, targeted DNA deamination, and long-range DNA repair.High-throughput mutagenesis reveals functional determinants for DNA targeting by activation-induced deaminase.Local sequence targeting in the AID/APOBEC family differentially impacts retroviral restriction and antibody diversification.Identification of a single amino acid required for APOBEC3 antiretroviral cytidine deaminase activity.Sequence and structural determinants of human APOBEC3H deaminase and anti-HIV-1 activities.Recombinase-mediated cassette exchange as a novel method to study somatic hypermutation in Ramos cells Local DNA dynamics shape mutational patterns of mononucleotide repeats in human genomes The somatic autosomal mutation matrix in cancer genomes.Does DNA repair occur during somatic hypermutation?DNA cytosine and methylcytosine deamination by APOBEC3B: enhancing methylcytosine deamination by engineering APOBEC3B.A structural basis for the biochemical behavior of activation-induced deoxycytidine deaminase class-switch recombination-defective hyper-IgM-2 mutants Natural Polymorphisms and Oligomerization of Human APOBEC3H Contribute to Single-stranded DNA Scanning Ability.Crystal Structure of the DNA Deaminase APOBEC3B Catalytic Domain.Efficient deamination of 5-methylcytosines in DNA by human APOBEC3A, but not by AID or APOBEC3G.Strand-biased cytosine deamination at the replication fork causes cytosine to thymine mutations in Escherichia coli.Functional requirements of AID's higher order structures and their interaction with RNA-binding proteins A computational analysis of the structural determinants of APOBEC3's catalytic activity and vulnerability to HIV-1 Vif.Structural analysis of the activation-induced deoxycytidine deaminase required in immunoglobulin diversification Single-Molecule Force Spectroscopy Studies of APOBEC3A-Single-Stranded DNA Complexes.Nuclear Magnetic Resonance Structure of the APOBEC3B Catalytic Domain: Structural Basis for Substrate Binding and DNA Deaminase Activity.Nucleic acid determinants for selective deamination of DNA over RNA by activation-induced deaminase.The local dinucleotide preference of APOBEC3G can be altered from 5'-CC to 5'-TC by a single amino acid substitution.Structural determinants of human APOBEC3A enzymatic and nucleic acid binding properties.Mutator effects and mutation signatures of editing deaminases produced in bacteria and yeast.Structural basis for targeted DNA cytosine deamination and mutagenesis by APOBEC3A and APOBEC3B.A Novel Regulator of Activation-Induced Cytidine Deaminase/APOBECs in Immunity and Cancer: Schrödinger's CATalytic Pocket.APOBECs and virus restriction.Engineering and optimising deaminase fusions for genome editing.Functions and Malfunctions of Mammalian DNA-Cytosine Deaminases D316 is critical for the enzymatic activity and HIV-1 restriction potential of human and rhesus APOBEC3B.A Comparison of Two Single-Stranded DNA Binding Models by Mutational Analysis of APOBEC3G.NMR-based method of small changes reveals how DNA mutator APOBEC3A interacts with its single-stranded DNA substrate.APOBEC Enzymes as Targets for Virus and Cancer Therapy.

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Determinants of sequence-specificity within human AID and APOBEC3G

http://www.wikidata.org/entity/Q33885890

description

2010 nî lūn-bûn

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2010 թուականի Մարտին հրատարակուած գիտական յօդուած

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2010 թվականի մարտին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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Determinants of sequence-specificity within human AID and APOBEC3G

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Determinants of sequence-specificity within human AID and APOBEC3G

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Determinants of sequence-specificity within human AID and APOBEC3G

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Determinants of sequence-specificity within human AID and APOBEC3G

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Determinants of sequence-specificity within human AID and APOBEC3G

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Determinants of sequence-specificity within human AID and APOBEC3G

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Determinants of sequence-specificity within human AID and APOBEC3G

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Ashok S Bhagwat

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Erandi Rajagurubandara

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Michael A Carpenter

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Priyanga Wijesinghe

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P2860

An extended structure of the APOBEC3G catalytic domain suggests a unique holoenzyme model

Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications

Structure, interaction and real-time monitoring of the enzymatic reaction of wild-type APOBEC3G

Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family

Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase

Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G

AID mutates E. coli suggesting a DNA deamination mechanism for antibody diversification

Activation-induced cytidine deaminase deaminates 5-methylcytosine in DNA and is expressed in pluripotent tissues: implications for epigenetic reprogramming

Cytidine deamination of retroviral DNA by diverse APOBEC proteins

An overview of cytidine deaminases.

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