“Leo is one of the few founders I’ve worked with to have both the product vision and commercial acumen to build a successful business. It was refreshing to see how quickly and enthusiastically he backed the need for developing a strategic messaging platform that would simultaneously help position their product and accelerate their sales. Since then, he’s led a pivot that’s fueled Ranomics’ growth— all without needing outside capital beyond their initial seed funding, which is especially impressive considering how resource-intensive a startup like theirs is. Leo’s been extremely supportive to me in the time since we’ve worked together, and I’m looking forward working with him again.”
About
I am passionate about turning scientific findings into highly valuable products and services for the world. As an entrepreneur, I have used a combination of strategic management, business development, scientific research and my unique personality to return value for stakeholders and partners. Through this process, I have excelled at connecting with people, identifying areas of common interest and bringing people together in building solutions for the larger goal.
Activity
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We have been recently quiet, because we were very busy scaling THE WORLD'S FIRST AND ONLY BIO-ADIPIC ACID & NYLON66 PRODUCTION! We transitioned from…
We have been recently quiet, because we were very busy scaling THE WORLD'S FIRST AND ONLY BIO-ADIPIC ACID & NYLON66 PRODUCTION! We transitioned from…
Liked by Leo Wan
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We are excited to announce our $325 million #SeriesC financing. This new investment will enable ArsenalBio's ongoing development efforts and scale…
We are excited to announce our $325 million #SeriesC financing. This new investment will enable ArsenalBio's ongoing development efforts and scale…
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💥 Introducing PINDER & PLINDER With existing evals saturating without clear advances in real life downstream tasks, current progress in AI x Bio is…
💥 Introducing PINDER & PLINDER With existing evals saturating without clear advances in real life downstream tasks, current progress in AI x Bio is…
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Experience
Education
Publications
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Dimeric structure of pseudokinase RNase L bound to 2-5A reveals a basis for interferon-induced antiviral activity.
Molecular Cell
RNase L is an ankyrin repeat domain-containing dual endoribonuclease-pseudokinase that is activated by unusual 2,'5'-oligoadenylate (2-5A) second messengers and which impedes viral infections in higher vertebrates. Despite its importance in interferon-regulated antiviral innate immunity, relatively little is known about its precise mechanism of action. Here we present a functional characterization of 2.5 Å and 3.25 Å X-ray crystal and small-angle X-ray scattering structures of RNase L bound to…
RNase L is an ankyrin repeat domain-containing dual endoribonuclease-pseudokinase that is activated by unusual 2,'5'-oligoadenylate (2-5A) second messengers and which impedes viral infections in higher vertebrates. Despite its importance in interferon-regulated antiviral innate immunity, relatively little is known about its precise mechanism of action. Here we present a functional characterization of 2.5 Å and 3.25 Å X-ray crystal and small-angle X-ray scattering structures of RNase L bound to a natural 2-5A activator with and without ADP or the nonhydrolysable ATP mimetic AMP-PNP. These studies reveal how recognition of 2-5A through interactions with the ankyrin repeat domain and the pseudokinase domain, together with nucleotide binding, imposes a rigid intertwined dimer configuration that is essential for RNase catalytic and antiviral functions. The involvement of the pseudokinase domain of RNase L in 2-5A sensing, nucleotide binding, dimerization, and ribonuclease functions highlights the evolutionary adaptability of the eukaryotic protein kinase fold.
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Formin-mediated actin polymerization promotes Salmonella invasion.
Cell Microbiol
Salmonella invade host cells using Type 3 secreted effectors, which modulate host cellular targets to promote actin rearrangements at the cell surface that drive bacterial uptake. The Arp2/3 complex contributes to Salmonella invasion but is not essential, indicating other actin regulatory factors are involved. Here, we show a novel role for FHOD1, a formin family member, in Salmonella invasion. FHOD1 and Arp2/3 occupy distinct microdomains at the invasion site and control distinct aspects of…
Salmonella invade host cells using Type 3 secreted effectors, which modulate host cellular targets to promote actin rearrangements at the cell surface that drive bacterial uptake. The Arp2/3 complex contributes to Salmonella invasion but is not essential, indicating other actin regulatory factors are involved. Here, we show a novel role for FHOD1, a formin family member, in Salmonella invasion. FHOD1 and Arp2/3 occupy distinct microdomains at the invasion site and control distinct aspects of membrane protrusion formation. FHOD1 is phosphorylated during infection and this modification is required for promoting bacterial uptake by host cells. ROCK II, but not ROCK I, is recruited to the invasion site and is required for FHOD1 phosphorylation and for Salmonella invasion. Together, our studies revealan important phospho-dependent FHOD1 actin polymerization pathway in Salmonella invasion.
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Reconstitution and characterization of eukaryotic N6-threonylcarbamoylation of tRNA using a minimal enzyme system.
Nucleic Acids Research
The universally conserved Kae1/Qri7/YgjD and Sua5/YrdC protein families have been implicated in growth, telomere homeostasis, transcription and the N6-threonylcarbamoylation (t6A) of tRNA, an essential modification required for translational fidelity by the ribosome. In bacteria, YgjD orthologues operate in concert with the bacterial-specific proteins YeaZ and YjeE, whereas in archaeal and eukaryotic systems, Kae1 operates as part of a larger macromolecular assembly called KEOPS with Bud32…
The universally conserved Kae1/Qri7/YgjD and Sua5/YrdC protein families have been implicated in growth, telomere homeostasis, transcription and the N6-threonylcarbamoylation (t6A) of tRNA, an essential modification required for translational fidelity by the ribosome. In bacteria, YgjD orthologues operate in concert with the bacterial-specific proteins YeaZ and YjeE, whereas in archaeal and eukaryotic systems, Kae1 operates as part of a larger macromolecular assembly called KEOPS with Bud32, Cgi121, Gon7 and Pcc1 subunits. Qri7 orthologues function in the mitochondria and may represent the most primitive member of the Kae1/Qri7/YgjD protein family. In accordance with previous findings, we confirm that Qri7 complements Kae1 function and uncover that Qri7 complements the function of all KEOPS subunits in growth, t6A biosynthesis and, to a partial degree, telomere maintenance. These observations suggest that Kae1 provides a core essential function that other subunits within KEOPS have evolved to support. Consistent with this inference, Qri7 alone is sufficient for t6A biosynthesis with Sua5 in vitro. In addition, the 2.9 Å crystal structure of Qri7 reveals a simple homodimer arrangement that is supplanted by the heterodimerization of YgjD with YeaZ in bacteria and heterodimerization of Kae1 with Pcc1 in KEOPS. The partial complementation of telomere maintenance by Qri7 hints that KEOPS has evolved novel functions in higher organisms.
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Atomic structure of the KEOPS complex: an ancient protein kinase-containing molecular machine.
Molecular Cell
Kae1 is a universally conserved ATPase and part of the essential gene set in bacteria. In archaea and eukaryotes, Kae1 is embedded within the protein kinase-containing KEOPS complex. Mutation of KEOPS subunits in yeast leads to striking telomere and transcription defects, but the exact biochemical function of KEOPS is not known. As a first step to elucidating its function, we solved the atomic structure of archaea-derived KEOPS complexes involving Kae1, Bud32, Pcc1, and Cgi121 subunits. Our…
Kae1 is a universally conserved ATPase and part of the essential gene set in bacteria. In archaea and eukaryotes, Kae1 is embedded within the protein kinase-containing KEOPS complex. Mutation of KEOPS subunits in yeast leads to striking telomere and transcription defects, but the exact biochemical function of KEOPS is not known. As a first step to elucidating its function, we solved the atomic structure of archaea-derived KEOPS complexes involving Kae1, Bud32, Pcc1, and Cgi121 subunits. Our studies suggest that Kae1 is regulated at two levels by the primordial protein kinase Bud32, which is itself regulated by Cgi121. Moreover, Pcc1 appears to function as a dimerization module, perhaps suggesting that KEOPS may be a processive molecular machine. Lastly, as Bud32 lacks the conventional substrate-recognition infrastructure of eukaryotic protein kinases including an activation segment, Bud32 may provide a glimpse of the evolutionary history of the protein kinase family.
Projects
Honors & Awards
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Vanier Canada Graduate Scholarship
Canadian Institutes of Health Research
The Vanier Canada Graduate Scholarship (Vanier CGS) was created to attract and retain world-class doctoral students and to establish Canada as a global centre of excellence in research and higher learning.
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I'm thrilled to announce that Kano is hiring for a Scientist/Sr. Scientist position in mammalian genome engineering tool development. This is a…
I'm thrilled to announce that Kano is hiring for a Scientist/Sr. Scientist position in mammalian genome engineering tool development. This is a…
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Have a lot of protein structure experience and want to help build better vaccines? Come and join us at Apriori Bio!
Have a lot of protein structure experience and want to help build better vaccines? Come and join us at Apriori Bio!
Liked by Leo Wan
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