Publisher Correction: Structural insights into β-1,3-glucan cleavage by a glycoside hydrolase family

June 25th, 2020 by Camila R. Santos

Nature Chemical Biology, Published online: 25 June 2020; doi:10.1038/s41589-020-0590-1

Publisher Correction: Structural insights into β-1,3-glucan cleavage by a glycoside hydrolase family
  • Posted in Nat Chem Biol, Publications
  • Comments Off on Publisher Correction: Structural insights into β-1,3-glucan cleavage by a glycoside hydrolase family

Groovy RNA polymerase

June 22nd, 2020 by Mirella Bucci

Nature Chemical Biology, Published online: 22 June 2020; doi:10.1038/s41589-020-0582-1

Groovy RNA polymerase

Dissecting the Pol II transcription cycle and derailing cancer with CDK inhibitors

June 22nd, 2020 by Pabitra K. Parua

Nature Chemical Biology, Published online: 22 June 2020; doi:10.1038/s41589-020-0563-4

This Review provides insights into transcriptional regulation, and vulnerabilities of cancer cells to disruption of cyclin-dependent kinase (CDK)-mediated regulation of Pol II transcription, revealed with small-molecule CDK inhibitors.
  • Posted in Nat Chem Biol, Publications
  • Comments Off on Dissecting the Pol II transcription cycle and derailing cancer with CDK inhibitors

Structural insight into the formation of lipoprotein-β-barrel complexes

June 22nd, 2020 by Raquel Rodríguez-Alonso

Nature Chemical Biology, Published online: 22 June 2020; doi:10.1038/s41589-020-0575-0

A structural and biochemical study of bacterial β-barrel assembly machinery component BamA with transport substrate RcsF shows an inward-open conformation with RcsF trapped inside the β-barrel lumen and suggests a push–pull substrate export mechanism.
  • Posted in Nat Chem Biol, Publications
  • Comments Off on Structural insight into the formation of lipoprotein-β-barrel complexes

Spectroscopic coherent Raman imaging of <i>Caenorhabditis elegans</i> reveals lipid particle diversity

June 22nd, 2020 by Wei-Wen Chen

Nature Chemical Biology, Published online: 22 June 2020; doi:10.1038/s41589-020-0565-2

A Raman-based imaging approach that can distinguish closely related chemical species used to characterize the distribution of lipids throughout the body of intact Caenorhabditis elegans worms shows that the epidermis is an important fat-storage reservoir.
  • Posted in Nat Chem Biol, Publications
  • Comments Off on Spectroscopic coherent Raman imaging of <i>Caenorhabditis elegans</i> reveals lipid particle diversity

Discovering Nature’s super glue

June 22nd, 2020 by Zhi Zeng

Nature Chemical Biology, Published online: 22 June 2020; doi:10.1038/s41589-020-0586-x

Molecular glues induce novel protein–protein interactions to modulate protein function and downstream biology. A recent study unveils manumycin polyketides with multiple electrophilic centers as covalent molecular glues between UBR7 and TP53.

Taking out the trash

June 22nd, 2020 by Grant Miura

Nature Chemical Biology, Published online: 22 June 2020; doi:10.1038/s41589-020-0581-2

Taking out the trash

The uninhibited pathway is not worth studying

June 22nd, 2020 by Michael E. Pacold

Nature Chemical Biology, Published online: 22 June 2020; doi:10.1038/s41589-020-0562-5

Glucose 6-phosphate dehydrogenase (G6PD) stands at the head of the pentose phosphate pathway, which is responsible for nucleotide synthesis. The identification and thorough validation of an improved G6PD inhibitor provide a valuable new tool compound for studying metabolism.

Enzymes knuckle down to the job

June 17th, 2020 by Paul H. Walton

Nature Chemical Biology, Published online: 17 June 2020; doi:10.1038/s41589-020-0585-y

A suite of new enzymes reveals more on how Nature breaks down plant-based polysaccharides and how these enzymes might be harnessed in the utilization of plant-based biomass.

Unraveling proteasome engagement

June 15th, 2020 by Cameron G. Roberts

Nature Chemical Biology, Published online: 15 June 2020; doi:10.1038/s41589-020-0573-2

A new study reveals that, in addition to its longstanding role in recruiting proteins to the proteasome, ubiquitination can also induce a structural destabilization that allows the target protein to be efficiently unraveled for degradation.