Nature Chemical Biology

2011 Nature Chemical Biology

doi: 10.1038/nchembio.554

Weiss, Ingrid M

2011 Nature Chemical Biology

doi: 10.1038/nchembio.550pmid: 21423159

Amorphous mineral phases play important roles in the skeletons of many organisms, but the molecular basis for species-specific control is still under debate. The demonstration that energy-rich metabolites such as phosphoenolpyruvate stabilize amorphous calcium carbonate (ACC) in crayfish inspires speculation about calcium minerals in emerging metabolisms.

Daughdrill, Gary W

2011 Nature Chemical Biology

doi: 10.1038/nchembio.544pmid: 21423160

Detailed biophysical and biochemical studies provide an exquisite example of how conformational flexibility controls the interaction between an intrinsically disordered protein and its numerous binding partners.

Wagner, Bridget K

2011 Nature Chemical Biology

doi: 10.1038/nchembio.540pmid: 21423161

High-throughput screening in Caenorhabditis elegans identified a compound that distinctly regulates fat storage and feeding, highlighting new players in energy homeostasis.

Nielsen, Jens

2011 Nature Chemical Biology

doi: 10.1038/nchembio.548pmid: 21423162

The assembly of chimeric synthetic pathways in cell factories will enable production of novel fuels and chemicals by microbial fermentation. The assembly of five enzymes for production of 1-butanol in Escherichia coli using kinetic considerations provides new lessons regarding these endeavors.

Sato, Ai; Nagasaka, Seiji; Furihata, Kazuo; Nagata, Shinji; Arai, Isao; Saruwatari, Kazuko; Kogure, Toshihiro; Sakuda, Shohei; Nagasawa, Hiromichi

2011 Nature Chemical Biology

doi: 10.1038/nchembio.532pmid: 21336282

The mechanisms and molecules involved in controlling biomineral formation remain unclear, though several proteins have been implicated in the process. Examination of crayfish now surprisingly points to upregulated glycolytic metabolites as playing a critical role in stabilizing amorphous calcium carbonate.[Figure not available: see fulltext.]

Metz, James T; Johnson, Eric F; Soni, Niru B; Merta, Philip J; Kifle, Lemma; Hajduk, Philip J

2011 Nature Chemical Biology

doi: 10.1038/nchembio.530pmid: 21336281

Assisted by 3,800 chemical bioactivities, a bioinformatic analysis explores the inter-relatedness of over 170 kinases and generates a kinase interaction map based on sequence and ligand-binding activity that challenges the robustness of drug interaction networks.[Figure not available: see fulltext.]

Deng, Xianming; Dzamko, Nicolas; Prescott, Alan; Davies, Paul; Liu, Qingsong; Yang, Qingkai; Lee, Jiing-Dwan; Patricelli, Matthew P; Nomanbhoy, Tyzoon K; Alessi, Dario R; Gray, Nathanael S

2011 Nature Chemical Biology

doi: 10.1038/nchembio.538pmid: 21378983

A potent and selective inhibitor of the kinase LRRK2 identified using an in vitro ATP-site competition binding assay also inhibits the G2019S mutant, implicated in Parkinson's disease, as well as the regulatory feedback loop where LRRK2 is phosphorylated and binds 14-3-3 protein.[Figure not available: see fulltext.]

Lemieux, George A; Liu, Jason; Mayer, Nasima; Bainton, Roland J; Ashrafi, Kaveh; Werb, Zena

2011 Nature Chemical Biology

doi: 10.1038/nchembio.534pmid: 21390037

A screen for compounds that alter fat content in C. elegans identifies a novel agonist of an AMP-activated kinase pathway that reduces fat storage as well as implicates the transcription factor K08F8.2 as a regulator of fat metabolism.[Figure not available: see fulltext.]

Wang, Yuefeng; Fisher, John C; Mathew, Rose; Ou, Li; Otieno, Steve; Sublet, Jack; Xiao, Limin; Chen, Jianhan; Roussel, Martine F; Kriwacki, Richard W

2011 Nature Chemical Biology

doi: 10.1038/nchembio.536pmid: 21358637

NMR reveals the dynamic stretching ability of the subdomain LH of the intrinsically disordered p21, providing a physical basis for the binding and functional diversity in its cell cycle regulatory role as a modulator of Cdk–cyclin complexes.[Figure not available: see fulltext.]