P
Philip A. Romero
Researcher at University of Wisconsin-Madison
Publications - 48
Citations - 2590
Philip A. Romero is an academic researcher from University of Wisconsin-Madison. The author has contributed to research in topics: Biology & Computer science. The author has an hindex of 15, co-authored 38 publications receiving 1945 citations. Previous affiliations of Philip A. Romero include California Institute for Quantitative Biosciences & California Institute of Technology.
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Exploring protein fitness landscapes by directed evolution
TL;DR: Directed evolution studies have shown how rapidly some proteins can evolve under strong selection pressures and, because the entire 'fossil record' of evolutionary intermediates is available for detailed study, they have provided new insight into the relationship between sequence and function.
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Navigating the protein fitness landscape with Gaussian processes
TL;DR: The ability of Gaussian processes to guide the search through protein sequence space by designing, constructing, and testing chimeric cytochrome P450s allowed us to engineer active P450 enzymes that are more thermostable than any previously made by chimeragenesis, rational design, or directed evolution.
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Dissecting enzyme function with microfluidic-based deep mutational scanning
TL;DR: An ultrahigh-throughput method for mapping enzyme sequence–function relationships that combines droplet microfluidic screening with next-generation DNA sequencing is presented and large, unbiased analyses of enzyme function allow the discovery of new biochemical mechanisms that will improve the ability to engineer custom biocatalysts.
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Neutral genetic drift can alter promiscuous protein functions, potentially aiding functional evolution
TL;DR: Investigating how cytochrome P450 enzymes that have evolved neutrally with respect to activity on a single substrate have changed in their abilities to catalyze reactions on five other substrates suggests that initially neutral genetic drift can lead to substantial changes in protein functions that are not currently under selection.
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Directed evolution of a magnetic resonance imaging contrast agent for noninvasive imaging of dopamine.
Mikhail G. Shapiro,Gil G. Westmeyer,Philip A. Romero,Jerzy O. Szablowski,Benedict Küster,Ameer T. Shah,Christopher R. Otey,Robert Langer,Frances H. Arnold,Alan Jasanoff +9 more
TL;DR: The results demonstrate the feasibility of molecular-level functional MRI using neural activity–dependent sensors, and the protein engineering approach can be generalized to create probes for other targets.