Structural and Biochemical Analysis of DNA Helix Invasion by the Bacterial 8-Oxoguanine DNA Glycosylase MutM (Q27676354)

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English	Structural and Biochemical Analysis of DNA Helix Invasion by the Bacterial 8-Oxoguanine DNA Glycosylase MutM	scientific article

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instance of

scholarly article

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title

Structural and Biochemical Analysis of DNA Helix Invasion by the Bacterial 8-Oxoguanine DNA Glycosylase MutM (English)

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main subject

cell biology

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author name string

Rou-Jia Sung

series ordinal

1

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Michael Zhang

series ordinal

2

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Yan Qi

series ordinal

3

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Gregory L Verdine

series ordinal

4

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language of work or name

English

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publication date

5 April 2013

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published in

Journal of Biological Chemistry

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volume

288

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issue

14

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page(s)

10012-23

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cites work

Sequence-dependent Structural Variation in DNA Undergoing Intrahelical Inspection by the DNA glycosylase MutM

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Encounter and extrusion of an intrahelical lesion by a DNA repair enzyme

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Entrapment and Structure of an Extrahelical Guanine Attempting to Enter the Active Site of a Bacterial DNA Glycosylase, MutM

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Structure of the E. coli DNA Glycosylase AlkA Bound to the Ends of Duplex DNA: A System for the Structure Determination of Lesion-Containing DNA

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20 March 2017

DNA lesion recognition by the bacterial repair enzyme MutM

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20 March 2017

Structural insights into lesion recognition and repair by the bacterial 8-oxoguanine DNA glycosylase MutM

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Instability and decay of the primary structure of DNA

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X-ray structure of a DNA decamer containing 7,8-dihydro-8-oxoguanine

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A new method for sequencing DNA

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20 March 2017

Cloning and expression in Escherichia coli of the OGG1 gene of Saccharomyces cerevisiae, which codes for a DNA glycosylase that excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine

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The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine)

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Single Qdot-labeled glycosylase molecules use a wedge amino acid to probe for lesions while scanning along DNA

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29 September 2017

Analysis of an anomalous mutant of MutM DNA glycosylase leads to new insights into the catalytic mechanism

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29 September 2017

Real-time studies of conformational dynamics of the repair enzyme E. coli formamidopyrimidine-DNA glycosylase and its DNA complexes during catalytic cycle

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29 September 2017

Structure of a DNA glycosylase searching for lesions

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29 September 2017

Repair and genetic consequences of endogenous DNA base damage in mammalian cells

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Thermodynamic, kinetic, and structural basis for recognition and repair of 8-oxoguanine in DNA by Fpg protein from Escherichia coli.

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Single-turnover and pre-steady-state kinetics of the reaction of the adenine glycosylase MutY with mismatch-containing DNA substrates

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29 September 2017

NMR studies of a DNA containing 8-hydroxydeoxyguanosine

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29 September 2017

Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily

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2 June 2018

Stopped-flow kinetic studies of the interaction between Escherichia coli Fpg protein and DNA substrates

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21 January 2018

Influence of the oxidatively damaged adduct 8-oxodeoxyguanosine on the conformation, energetics, and thermodynamic stability of a DNA duplex.

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21 January 2018

Processing of X-ray diffraction data collected in oscillation mode

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Crossref

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21 January 2018

PROCHECK: a program to check the stereochemical quality of protein structures

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Identifiers

DOI

10.1074/JBC.M112.415612

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3465622

OpenCitations bibliographic resource ID

3465622

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3465622

PMC publication ID

3617240

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3465622

PubMed publication ID

23404556

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3465622

 

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