Article

CryoEM Structure of CtBP2 Confirms Tetrameric Architecture

2020-04-07

Abstract excerpt

C-terminal binding proteins 1 and 2 (CtBP1 and CtBP2) are transcriptional regulators that activate or repress many genes involved in cellular development, apoptosis and metastasis. CtBP proteins are activated under hypoxic conditions where NAD(H) levels tend to be higher. NADH-dependent activation of CtBP2 has direct implication in multiple types of cancers and poor patient prognosis. Previous studies have propose...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 36eb08ec-aee8-56dd-9afd-37746ced3206
DOI: 10.1101/2020.04.06.027573

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

CryoEM Structure of CtBP2 Confirms Tetrameric ArchitectureDOI 10.1101/2020.04.06.027573Read

Cryo-EM structure of CtBP2 confirms tetrameric architecture.Semantic proximity Read

The cryo-electron microscopy structure of human transcription factor IIH.Semantic proximity Read

TFAM organizes DNA into compact higher order structuresSemantic proximity Read

Investigations of the mechanism of mitochondrial complex I by electron cryomicroscopySemantic proximity Read

Substrate binding plasticity revealed by Cryo-EM structures of SLC26A2.Semantic proximity Read

Structural basis of neurofibromin tetramerization and dimer-tetramer equilibriumSemantic proximity Read

A robust workflow for 3D imaging of human mitochondria using cryo-electron tomographySemantic proximity Read

Cryo-EM analysis of human mitochondrial Hsp90 in multiple tetrameric statesSemantic proximity Read

Two p53 tetramers bind one consensus DNA response elementSemantic proximity Read

Quaternary structure of the specific p53-DNA complex reveals the mechanism of p53 mutant dominance.Semantic proximity Read

Structure of the human respiratory complex II.Semantic proximity Read

Structure of the human monomeric NEET protein MiNT and its role in regulating iron and reactive oxygen species in cancer cells.Semantic proximity Read