A New BRCT Binding Mode in TopBP1-BLM Helicase Interaction.

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A New BRCT Binding Mode in TopBP1-BLM Helicase Interaction.

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2017 nî lūn-bûn

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2017年学术文章

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A New BRCT Binding Mode in TopBP1-BLM Helicase Interaction.

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A New BRCT Binding Mode in TopBP1-BLM Helicase Interaction.

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A New BRCT Binding Mode in TopBP1-BLM Helicase Interaction.

@en

A New BRCT Binding Mode in TopBP1-BLM Helicase Interaction.

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A New BRCT Binding Mode in TopBP1-BLM Helicase Interaction.

@en

A New BRCT Binding Mode in TopBP1-BLM Helicase Interaction.

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P1476

A New BRCT Binding Mode in TopBP1-BLM Helicase Interaction.

@en

P2093

Georges Mer

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Maria Victoria Botuyan

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P2860

The BRCT domain is a phospho-protein binding domain

Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains

Structure of a Second BRCT Domain Identified in the Nijmegen Breakage Syndrome Protein Nbs1 and its Function in an MDC1-Dependent Localization of Nbs1 to DNA Damage Sites

Structural Insights into Recognition of MDC1 by TopBP1 in DNA Replication Checkpoint Control

Phosphorylation-Dependent Assembly and Coordination of the DNA Damage Checkpoint Apparatus by Rad4TopBP1

BRCT repeats as phosphopeptide-binding modules involved in protein targeting

Interactions between BRCT repeats and phosphoproteins: tangled up in two

MDC1 collaborates with TopBP1 in DNA replication checkpoint control.

TopBP1 interacts with BLM to maintain genome stability but is dispensable for preventing BLM degradation.

TopBP1 controls BLM protein level to maintain genome stability

P304

1471-1472

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P31

scholarly article

P356

10.1016/J.STR.2017.09.011

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P433

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P478

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

P577

2017-10-03T00:00:00Z

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28978405

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P932

5642270

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