Interaction of human DNA polymerase eta with monoubiquitinated PCNA: a possible mechanism for the polymerase switch in response to DNA damage (Q28646728)

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Language	Label	Description	Also known as
English	Interaction of human DNA polymerase eta with monoubiquitinated PCNA: a possible mechanism for the polymerase switch in response to DNA damage	scientific journal article

Statements

scholarly article

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3 February 2017

Interaction of human DNA polymerase eta with monoubiquitinated PCNA: a possible mechanism for the polymerase switch in response to DNA damage (English)

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3 February 2017

author name string

Patricia L. Kannouche

1

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3 February 2017

Jonathan Wing

2

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3 February 2017

Alan R. Lehmann

3

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3 February 2017

publication date

21 May 2004

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3 February 2017

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3 February 2017

14

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3 February 2017

4

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3 February 2017

491–500

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3 February 2017

Yeast DNA repair proteins Rad6 and Rad18 form a heterodimer that has ubiquitin conjugating, DNA binding, and ATP hydrolytic activities

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Structural basis for recruitment of translesion DNA polymerase Pol IV/DinB to the -clamp

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Chemotropic responses of retinal growth cones mediated by rapid local protein synthesis and degradation

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Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA

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Physical and functional interactions of human DNA polymerase eta with PCNA

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Protein regulation by monoubiquitin

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RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO.

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Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair

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hRAD30 mutations in the variant form of xeroderma pigmentosum

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Solution structure of a CUE-ubiquitin complex reveals a conserved mode of ubiquitin binding

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Domain structure, localization, and function of DNA polymerase eta, defective in xeroderma pigmentosum variant cells

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Structural and functional conservation of two human homologs of the yeast DNA repair gene RAD6

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Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA

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Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains

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The XPV (xeroderma pigmentosum variant) gene encodes human DNA polymerase eta

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Mechanisms of accurate translesion synthesis by human DNA polymerase eta

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Preferential cis-syn thymine dimer bypass by DNA polymerase eta occurs with biased fidelity.

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The Y-family of DNA polymerases

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Mechanism of ubiquitin recognition by the CUE domain of Vps9p

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Rad6-dependent ubiquitination of histone H2B in yeast

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A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain

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Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation

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Dysfunction of human Rad18 results in defective postreplication repair and hypersensitivity to multiple mutagens

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Structure of the catalytic core of S. cerevisiae DNA polymerase eta: implications for translesion DNA synthesis

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Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair.

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Sequential assembly of the nucleotide excision repair factors in vivo

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Identifiers

10.1016/S1097-2765(04)00259-X

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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