Is thymidine glycol containing DNA a substrate of E. coli DNA mismatch repair system? - Wikidata - wikimedia - TriplyDB

Is thymidine glycol containing DNA a substrate of E. coli DNA mismatch repair system?

Is thymidine glycol containing DNA a substrate of E. coli DNA mismatch repair system?

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Occurrence, Biological Consequences, and Human Health Relevance of Oxidative Stress-Induced DNA Damage.

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Is thymidine glycol containing DNA a substrate of E. coli DNA mismatch repair system?

http://www.wikidata.org/entity/Q35227178

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2014 nî lūn-bûn

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2014 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

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2014 թվականի օգոստոսին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年论文

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name

Is thymidine glycol containing DNA a substrate of E. coli DNA mismatch repair system?

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Is thymidine glycol containing DNA a substrate of E. coli DNA mismatch repair system?

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Is thymidine glycol containing DNA a substrate of E. coli DNA mismatch repair system?

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Is thymidine glycol containing DNA a substrate of E. coli DNA mismatch repair system?

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Is thymidine glycol containing DNA a substrate of E. coli DNA mismatch repair system?

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Is thymidine glycol containing DNA a substrate of E. coli DNA mismatch repair system?

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JOURNAL.PONE.0104963

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Is thymidine glycol containing DNA a substrate of E. coli DNA mismatch repair system?

@en

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Elena A Kubareva

http://www.w3.org/2001/XMLSchema#string

Elena A Romanova

http://www.w3.org/2001/XMLSchema#string

Peter Friedhoff

http://www.w3.org/2001/XMLSchema#string

Roger J Heinze

http://www.w3.org/2001/XMLSchema#string

Svetlana A Perevozchikova

http://www.w3.org/2001/XMLSchema#string

Tatiana S Oretskaya

http://www.w3.org/2001/XMLSchema#string

P2860

Activation of human MutS homologs by 8-oxo-guanine DNA damage

Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA

The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch

Composite active site of an ABC ATPase: MutS uses ATP to verify mismatch recognition and authorize DNA repair

A structural rationale for stalling of a replicative DNA polymerase at the most common oxidative thymine lesion, thymine glycol

Structures of Escherichia coli DNA mismatch repair enzyme MutS in complex with different mismatches: a common recognition mode for diverse substrates

Structure of the human MutSalpha DNA lesion recognition complex

The cis -(5 R ,6 S )-Thymine Glycol Lesion Occupies the Wobble Position When Mismatched with Deoxyguanosine in DNA

Binding of the human nucleotide excision repair proteins XPA and XPC/HR23B to the 5R-thymine glycol lesion and structure of the cis-(5R,6S) thymine glycol epimer in the 5'-GTgG-3' sequence: destabilization of two base pairs at the lesion site

Magnesium Coordination Controls the Molecular Switch Function of DNA Mismatch Repair Protein MutS

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e104963

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scholarly article

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10.1371/JOURNAL.PONE.0104963

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8

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2014-08-18T00:00:00Z

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264865813

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25133614

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Escherichia coli

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4136841

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