Longo Lab @ ELSI
@liamlongo.bsky.social
11 followers
9 following
7 posts
Protein Historian
Specially Appointed Associate Professor at the Earth-Life Science Institute, Institute of Science Tokyo
Affiliate Research Scientist at the Blue Marble Space Institute of Science
My academic journey: 🇺🇸 → 🇮🇱 → 🇯🇵
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Longo Lab @ ELSI
@liamlongo.bsky.social
· Jul 21
Longo Lab @ ELSI
@liamlongo.bsky.social
· Jul 21
The History of Enzyme Evolution Embedded in Metabolism
Phylogenetic reconstructions are a primary record of protein evolution. But what other records can attest to the deep history of enzymes, and what tools are needed to decode their meaning? Here, we de...
www.biorxiv.org
Longo Lab @ ELSI
@liamlongo.bsky.social
· Mar 30
Reposted by Longo Lab @ ELSI
Functional Ambidexterity of an Ancient Nucleic Acid-Binding Domain
Now out now in @angewandtechemie.bsky.social
Exciting collaboration with Norman Metanis and Koby Levy
onlinelibrary.wiley.com/doi/10.1002/...
Now out now in @angewandtechemie.bsky.social
Exciting collaboration with Norman Metanis and Koby Levy
onlinelibrary.wiley.com/doi/10.1002/...
Functional Ambidexterity of an Ancient Nucleic Acid‐Binding Domain
The helix-hairpin-helix (HhH) motif is an ancient and ubiquitous nucleic acid-binding element that has emerged as a model system for studying the evolution of dsDNA-binding domains from simple peptid....
onlinelibrary.wiley.com
Longo Lab @ ELSI
@liamlongo.bsky.social
· Mar 28
Redefining the Limits of Functional Continuity in the Early Evolution of P-Loop NTPases
Abstract. At the heart of many nucleoside triphosphatases is a conserved phosphate-binding sequence motif. A current model of early enzyme evolution propos
academic.oup.com
Longo Lab @ ELSI
@liamlongo.bsky.social
· Mar 28
Functional Ambidexterity of an Ancient Nucleic Acid‐Binding Domain
The helix-hairpin-helix (HhH) motif is an ancient and ubiquitous nucleic acid-binding element that has emerged as a model system for studying the evolution of dsDNA-binding domains from simple peptid....
onlinelibrary.wiley.com
Longo Lab @ ELSI
@liamlongo.bsky.social
· Mar 26
A universal polyphosphate kinase powers in vitro transcription
Polyphosphate kinases (PPKs) catalyze phosphoryl transfer between polyphosphates and nucleotides. Polyphosphates are a cost-effective source of phosphorylating power, making polyphosphate kinases an a...
www.biorxiv.org