Uracil-DNA glycosylase-DNA substrate and product structures: conformational strain promotes catalytic efficiency by coupled stereoelectronic effects (Q22254069)

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

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scholarly article

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

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Uracil DNA glycosylase

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GOA release 2020-03-11

DNA-(apurinic or apyrimidinic site) lyase

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GOA release 2020-03-11

uracil DNA N-glycosylase activity

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GOA release 2020-03-11

Hans Einar Krokan

5

object named as

H E Krokan

author given names

H E

author last names

Krokan

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7 February 2023

4

object named as

G Slupphaug

author given names

G

author last names

Slupphaug

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7 February 2023

7

object named as

J A Tainer

author given names

J A

author last names

Tainer

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7 February 2023

author name string

S S Parikh

1

author given names

S S

author last names

Parikh

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7 February 2023

G Walcher

2

author given names

G

author last names

Walcher

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7 February 2023

G D Jones

3

author given names

G D

author last names

Jones

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7 February 2023

G M Blackburn

6

author given names

G M

author last names

Blackburn

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7 February 2023

language of work or name

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publication date

9 May 2000

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Proceedings of the National Academy of Sciences of the United States of America

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97

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10

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5083-8

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DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination [corrected]

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Crystal structure of wild-type tryptophan synthase complexed with the natural substrate indole-3-glycerol phosphate

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19 March 2017

Heteronuclear NMR and crystallographic studies of wild-type and H187Q Escherichia coli uracil DNA glycosylase: electrophilic catalysis of uracil expulsion by a neutral histidine 187

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X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the alpha-amylase family

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Sugar ring distortion in the glycosyl-enzyme intermediate of a family G/11 xylanase

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Protein mimicry of DNA from crystal structures of the uracil-DNA glycosylase inhibitor protein and its complex with Escherichia coli uracil-DNA glycosylase

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Snapshots along an enzymatic reaction coordinate: analysis of a retaining beta-glycoside hydrolase

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A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA

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The structural basis of specific base-excision repair by uracil-DNA glycosylase

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XtalView/Xfit--A versatile program for manipulating atomic coordinates and electron density

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Quality control by DNA repair

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19 March 2017

Mutation of an active site residue in Escherichia coli uracil-DNA glycosylase: effect on DNA binding, uracil inhibition and catalysis

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27 September 2017

Envisioning the molecular choreography of DNA base excision repair

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27 September 2017

Kinetic mechanism of damage site recognition and uracil flipping by Escherichia coli uracil DNA glycosylase

1 reference

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27 September 2017

Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA.

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Effects of uracil incorporation, DNA mismatches, and abasic sites on cleavage and religation activities of mammalian topoisomerase I.

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In vivo evidence for endogenous DNA alkylation damage as a source of spontaneous mutation in eukaryotic cells

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Conformation and reaction specificity in pyridoxal phosphate enzymes

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Apurinic sites as mutagenic intermediates

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Exonuclease III and endonuclease IV remove 3' blocks from DNA synthesis primers in H2O2-damaged Escherichia coli

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Repair of intrinsic DNA lesions

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Base excision repair enzyme family portrait: integrating the structure and chemistry of an entire DNA repair pathway.

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Properties of a Recombinant Human Uracil-DNA Glycosylase from the UNG Gene and Evidence that UNG Encodes the Major Uracil-DNA Glycosylase

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Abasic sites stimulate double-stranded DNA cleavage mediated by topoisomerase II. DNA lesions as endogenous topoisomerase II poisons

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Identifiers

10.1073/PNAS.97.10.5083

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2000PNAS...97.5083P

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OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

ResearchGate publication ID

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