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05.19.2025 Negative cooperativity controls the activity of Diaphanous related formins.
Greg Theophall from my lab authored a very important paper on the regulatory mechanism of DRFs. It is published in Communications Biology, https://rdcu.be/em0vB, The blog about this paper is published in https://communities.springernature.com/posts/negative-cooperativity-controls-actin-polymerases.
07.19.2024 Ribosome electric field accelerates metabolomic reactions.
My talened graduate student JianChao Yu figured out how Ribosome accelerates metabolic reactions in live cells. It turns out that it does so by using its enourmous electric field. A very detailed paper that describes how it happens is published in the Journal of Physical Chemistry B https://pubs.acs.org/doi/full/10.1021/acs.jpcb.4c00628.
11.03.2023: DIAPH1 LINKS MITO TO ER
Drs. Ravi Ramasamy (NYU) and Ann Marie Schmidt(NYU) together with our team discovered a new way for mitochondria to approach ER, DIAPH1-MFN2 interaction regulates mitochondria-SR/ER contact and modulates ischemic/hypoxic stress | Nature Communications. This work has implications for the treatment of cardiomyopathies and complications of diabetes.
12.05.2022: IN-CELL NMR BIOREACTOR to STUDY mRNA VACCINE
We have published a new paper, Messenger RNA in lipid nanoparticles rescues HEK 293 cells from lipid-induced mitochondrial dysfunction as studied by real time pulse chase NMR, RTPC-NMR, spectroscopy | Scientific Reports (nature.com) that shows the power of the combination of in-cell NMR and a bioreactor to measure metabolic fluxes in live cells. This technology is widely available to study metabolic fluxes in both cell lines and primary cells.
05.13.2022: MICROFLUIDICS RULES IN-CELL NMR.
We have published a new paper (https://www.nature.com/articles/s42003-022-03412-x) about a new way of protein delivery into live cells for in-cell NMR applications. This is a collaborative work with Professor Todd Sulchek's group from Georgia Tech (https://www.me.gatech.edu/faculty/sulchek). We showed that microfluidics can deliver micromolar amounts of labeled proteins into the cytosol without disrupting internal cellular structures. This method is a viable alternative to many previously described methods of protein delivery when long-term (a few days) experiments are desired to follow a particular physiological process.
06.10.2021: RAMBO in biochemistry.
We have published a new paper (https://pubs.acs.org/doi/10.1021/acs.biochem.1c00074?fig=tgr1&ref=pdf) that describes a phenomenon called Ribosome-Amplified MetaBOlism or RAMBO. Because the concentration of ribosomes increases as the cell grows, ribosome binding interactions may regulate metabolic fluxes by altering the distribution of bound and free enzymes. Pyruvate kinase (PK) catalyzes the last step of glycolysis and represents a major drug target for controlling bacterial infections. The binding of metabolic enzymes to ribosomes creates protein quinary structures with altered catalytic activities. NMR spectroscopy and chemical cross-linking combined with high-resolution mass spectrometry were used to establish that PK binds to the ribosome at three independent sites, the L1 stalk, the A site, and the mRNA entry pore. The bioanalytical methodology described characterizes the altered kinetics and confirms the specificity of pyruvate kinase−ribosome interaction, affording an opportunity to investigate the ribosome dependence of metabolic reactions under solution conditions that closely mimic the cytosol. Expanding on the concept of ribosomal heterogeneity, which describes variations in ribosomal constituents that contribute to the specificity of cellular processes, RAMBO firmly establishes the reciprocal process by which ribosome-dependent quinary interactions affect metabolic activity.
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