![High-resolution snapshots of human N-myristoyltransferase in action illuminate a mechanism promoting N-terminal Lys and Gly myristoylation | Nature Communications High-resolution snapshots of human N-myristoyltransferase in action illuminate a mechanism promoting N-terminal Lys and Gly myristoylation | Nature Communications](https://media.springernature.com/m685/springer-static/image/art%3A10.1038%2Fs41467-020-14847-3/MediaObjects/41467_2020_14847_Fig1_HTML.png)
High-resolution snapshots of human N-myristoyltransferase in action illuminate a mechanism promoting N-terminal Lys and Gly myristoylation | Nature Communications
![Exploiting phage receptor binding proteins to enable endolysins to kill Gram-negative bacteria | Scientific Reports Exploiting phage receptor binding proteins to enable endolysins to kill Gram-negative bacteria | Scientific Reports](https://media.springernature.com/full/springer-static/image/art%3A10.1038%2Fs41598-020-68983-3/MediaObjects/41598_2020_68983_Fig1_HTML.png)
Exploiting phage receptor binding proteins to enable endolysins to kill Gram-negative bacteria | Scientific Reports
![Specific length and structure rather than high thermodynamic stability enable regulatory mRNA stem-loops to pause translation | Nature Communications Specific length and structure rather than high thermodynamic stability enable regulatory mRNA stem-loops to pause translation | Nature Communications](https://media.springernature.com/full/springer-static/image/art%3A10.1038%2Fs41467-022-28600-5/MediaObjects/41467_2022_28600_Fig1_HTML.png)
Specific length and structure rather than high thermodynamic stability enable regulatory mRNA stem-loops to pause translation | Nature Communications
![Widespread occurrence of covalent lysine–cysteine redox switches in proteins | Nature Chemical Biology Widespread occurrence of covalent lysine–cysteine redox switches in proteins | Nature Chemical Biology](https://media.springernature.com/full/springer-static/image/art%3A10.1038%2Fs41589-021-00966-5/MediaObjects/41589_2021_966_Figa_HTML.png)
Widespread occurrence of covalent lysine–cysteine redox switches in proteins | Nature Chemical Biology
![NHR-49/PPAR-α and HLH-30/TFEB cooperate for C. elegans host defense via a flavin-containing monooxygenase | eLife NHR-49/PPAR-α and HLH-30/TFEB cooperate for C. elegans host defense via a flavin-containing monooxygenase | eLife](https://iiif.elifesciences.org/lax/62775%2Felife-62775-fig6-v3.tif/full/,1500/0/default.jpg)
NHR-49/PPAR-α and HLH-30/TFEB cooperate for C. elegans host defense via a flavin-containing monooxygenase | eLife
Reversible Dual-Covalent Molecular Locking of the 14-3-3/ERRγ Protein–Protein Interaction as a Molecular Glue Drug Discovery Approach | Journal of the American Chemical Society
![A Genetically Encoded Fluorosulfonyloxybenzoyl-l-lysine for Expansive Covalent Bonding of Proteins via SuFEx Chemistry | Journal of the American Chemical Society A Genetically Encoded Fluorosulfonyloxybenzoyl-l-lysine for Expansive Covalent Bonding of Proteins via SuFEx Chemistry | Journal of the American Chemical Society](https://pubs.acs.org/cms/10.1021/jacs.1c04259/asset/images/medium/ja1c04259_0007.gif)