(Q38355001)

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Energetics of lesion recognition by a DNA repair protein: thermodynamic characterization of formamidopyrimidine-glycosylase (Fpg) interactions with damaged DNA duplexes.

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12729740%20AND%20SRC:MED&resulttype=core&format=json

3 November 2019

Energetics of lesion recognition by a DNA repair protein: thermodynamic characterization of formamidopyrimidine-glycosylase (Fpg) interactions with damaged DNA duplexes (English)

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12729740%20AND%20SRC:MED&resulttype=core&format=json

3 November 2019

Conceicao Minetti

1

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3 November 2019

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3 November 2019

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Dmitry O Zharkov

3

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3 November 2019

G Eric Plum

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3 November 2019

Francis Johnson

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3 November 2019

Arthur P Grollman

6

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3 November 2019

Kenneth J Breslauer

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3 November 2019

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1 May 2003

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3 November 2019

Journal of Molecular Biology

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3 November 2019

328

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3 November 2019

5

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3 November 2019

1047-1060

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3 November 2019

Chemistry of Glycosylases and Endonucleases Involved in Base-Excision Repair

1 reference

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AP site structural determinants for Fpg specific recognition

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Repair of DNA containing the oxidatively-damaged base, 8-oxoguanine

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NH2-terminal proline acts as a nucleophile in the glycosylase/AP-lyase reaction catalyzed by Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg) protein

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Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8

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Crystal structure of the Lactococcus lactis formamidopyrimidine-DNA glycosylase bound to an abasic site analogue-containing DNA.

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Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNA

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Coupling of local folding to site-specific binding of proteins to DNA

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Heat capacity and entropy changes in processes involving proteins

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Role of the hydrophobic effect in stability of site-specific protein-DNA complexes

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Adenine base unstacking dominates the observed enthalpy and heat capacity changes for the Escherichia coli SSB tetramer binding to single-stranded oligoadenylates

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Structural and thermodynamic strategies for site-specific DNA binding proteins

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A spectroscopic and calorimetric study of the melting behaviors of a "bent" and a "normal" DNA duplex: [d(GA4T4C)]2 versus [d(GT4A4C)]2.

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A terbenzimidazole that preferentially binds and conformationally alters structurally distinct DNA duplex domains: a potential mechanism for topoisomerase I poisoning

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Synthesis of enzymatically noncleavable carbocyclic nucleosides for DNA-N-glycosylase studies

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Single-stranded oligodeoxyribonucleotides are substrates of Fpg protein from Escherichia coli

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Processivity of uracil DNA glycosylase

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Abasic site recognition by two apurinic/apyrimidinic endonuclease families in DNA base excision repair: the 3' ends justify the means

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An ab initio molecular orbital study on the characteristics of 8-hydroxyguanine

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Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA

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Uracil-DNA glycosylase-DNA substrate and product structures: conformational strain promotes catalytic efficiency by coupled stereoelectronic effects

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8-oxoguanine (8-hydroxyguanine) DNA glycosylase and its substrate specificity

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Thermodynamic consequences of an abasic lesion in duplex DNA are strongly dependent on base sequence

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