Publisher Correction: PH-domain-binding inhibitors of nucleotide exchange factor BRAG2 disrupt Arf GTPase signaling

March 4th, 2019 by Agata Nawrotek

Publisher Correction: PH-domain-binding inhibitors of nucleotide exchange factor BRAG2 disrupt Arf GTPase signaling

Publisher Correction: PH-domain-binding inhibitors of nucleotide exchange factor BRAG2 disrupt Arf GTPase signaling, Published online: 04 March 2019; doi:10.1038/s41589-019-0255-0

Publisher Correction: PH-domain-binding inhibitors of nucleotide exchange factor BRAG2 disrupt Arf GTPase signaling
  • Posted in Nat Chem Biol, Publications
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A flexible filter maintains a tight grip

March 4th, 2019 by Adrian Gross

A flexible filter maintains a tight grip

A flexible filter maintains a tight grip, Published online: 04 March 2019; doi:10.1038/s41589-019-0248-z

Potassium channels allow the passage of potassium ions across membranes at rates approaching the diffusion limit while maintaining exquisite selectivity between ion species. Single-molecule studies now reveal that the selectivity filter of these proteins transitions between different conformations.

Bidirectional modulation of HIF-2 activity through chemical ligands

February 25th, 2019 by Dalei Wu

Bidirectional modulation of HIF-2 activity through chemical ligands

Bidirectional modulation of HIF-2 activity through chemical ligands, Published online: 25 February 2019; doi:10.1038/s41589-019-0234-5

Structural analysis of HIF-2α in complex with agonists and antagonists reveal that chemical ligands regulate the activity of HIF-2α by affecting the stability of the HIF-2α–ARNT heterodimer via redirecting residues in the PAS-B pocket.

Designing a chemical inhibitor for the AAA protein spastin using active site mutations

February 18th, 2019 by Tommaso Cupido

Designing a chemical inhibitor for the AAA protein spastin using active site mutations

Designing a chemical inhibitor for the AAA protein spastin using active site mutations, Published online: 18 February 2019; doi:10.1038/s41589-019-0225-6

The AAA protein spastin is needed for cell division and organelle transport. Testing spastin constructs with engineered mutations resulted in the identification of a chemical probe to analyze spastin-specific functions in cells.
  • Posted in Nat Chem Biol, Publications
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Tightening a deadly pore former

February 18th, 2019 by Jialing Lin

Tightening a deadly pore former

Tightening a deadly pore former, Published online: 18 February 2019; doi:10.1038/s41589-019-0235-4

A small molecule was identified that binds to a unique site on the pro-apoptotic protein BAX, stabilizing the protein structure allosterically and preventing the conformational activation to a pore former by BH3 proteins.

FTO controls reversible m<sup>6</sup>Am RNA methylation during snRNA biogenesis

February 18th, 2019 by Jan Mauer

FTO controls reversible m6Am RNA methylation during snRNA biogenesis

FTO controls reversible m<sup>6</sup>Am RNA methylation during snRNA biogenesis, Published online: 18 February 2019; doi:10.1038/s41589-019-0231-8

Two different methylation states of the adenosine adjacent to the snRNA cap are found in the biogenesis process of snRNAs, Am and m6Am, whose levels are regulated by FTO and are related to alternative pre-mRNA splicing.
  • Posted in Nat Chem Biol, Publications
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To be or not to be?

February 15th, 2019 by Yiyun Song

To be or not to be?

To be or not to be?, Published online: 15 February 2019; doi:10.1038/s41589-019-0239-0

To be or not to be?

Site-specific ubiquitylation and SUMOylation using genetic-code expansion and sortase

February 15th, 2019 by Maximilian Fottner

Site-specific ubiquitylation and SUMOylation using genetic-code expansion and sortase

Site-specific ubiquitylation and SUMOylation using genetic-code expansion and sortase, Published online: 15 February 2019; doi:10.1038/s41589-019-0227-4

A method combining genetic-code expansion, bioorthogonal Staudinger reduction and sortase-mediated transpeptidation enables site-specific and orthogonal modification of proteins with ubiquitin and SUMO in vitro and in living cells.
  • Posted in Nat Chem Biol, Publications
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A super-powered S-layer

February 15th, 2019 by Caitlin Deane

A super-powered S-layer

A super-powered S-layer, Published online: 15 February 2019; doi:10.1038/s41589-019-0236-3

A super-powered S-layer

Decoding without the cipher

February 15th, 2019 by Amit Kumar Singh Gautam

Decoding without the cipher

Decoding without the cipher, Published online: 15 February 2019; doi:10.1038/s41589-019-0230-9

A new method introduces ubiquitin or ubiquitin-like proteins at specific sites in any protein without the requirement of the cellular ubiquitylation machinery. This will help decipher the code by which these modifications control cellular processes.