Ale Mongera

@mongeralab.bsky.social

Developmental biologist at UCL Multicellular Morphogenesis Lab http://zebrafishucl.org/mongera-lab

We would like to add one or two postdocs to our lab in the next couple of years. If you are close to finishing your PhD and interested in the science we do, feel free to reach out to discuss opportunities.

First published teamwork of the lab 🎉! We wrote a review about emerging concepts of how metabolism promotes, regulates and changes during gastrulation. We hope it will be useful for anyone interested in the emerging field of developmental metabolism. www.sciencedirect.com/science/arti...

A metabolic view of gastrulation: Coordinating signalling, epigenetics and morphogenesis

Gastrulation is the morphogenetic process by which the single-layered pluripotent epiblast is reorganised into the three germ layers and the basic bod…

sciencedirect.com

I won't pay $4,000 for a ticket to see my Knicks play in the NBA Finals for the first time in 27 years, but for some reason I routinely pay three times that much for open access to papers that I wrote myself.

BildBild

Massive congratulations to our Editor-in-Chief for being elected as a Fellow of the Royal Society @royalsociety.org. This is an incredible honour for our journal. @ucl.ac.uk @ucl-cdb.bsky.social

International Society of Developmental Biology@isdb.bsky.social · 5mo ago

‼️MASSIVE‼️ congratulations to Professor Roberto Mayor @mayorlab.bsky.social from UCL, who has been elected as a fellow of The Royal Society @royalsociety.org. Professor Mayor is a Professor of Developmental and Cellular Neurobiology and one of our board of directors. royalsociety.org/news/2026/05...

How much information does it take to fold a protein? Not much, if you use the right information! We find that residue burial, a binary label of core vs surface, encodes a protein's fold highly efficiently and even improves ESM2's structure representation. 1/8 www.biorxiv.org/content/10.6...

Residue burial encodes a protein's fold

Protein structure is controlled by a high-dimensional energy landscape, which is a function of all of the atomic coordinates of the protein. Can this landscape be accurately described by a low-dimensional representation? We find that residue core identity, a binary N-dimensional encoding indicating whether each of the N amino acids in a protein is buried in the core or not, can predict the protein's backbone conformation more efficiently than all other representations that we tested. Core identity is 4 times more efficient than previous estimates of the bits per residue needed to encode a protein's native fold, 2 times more efficient than the Cα contact map, and 1.5 times more efficient than the machine-learned embeddings from FoldSeek's 3Di. Even when the folded structure is unavailable, predicting each residue's burial from sequence yields a more accurate estimate of fold quality than predicting pairwise contacts from the same sequence information. Thus, this work emphasizes that the problem of determining a protein's native fold can be re-framed as predicting each residue's core identity. ### Competing Interest Statement The authors have declared no competing interest. Chan Zuckerberg Initiative (United States), 2023-329572 NIH, T32GM145452

biorxiv.org

🎉 The Developmental Mechanics Seminar Series is back! 🗓️ Thurs, Jan 22 🎙️ Opening talks: 🧬Guy Tanentzapf (UBC) — How cell adhesion molecules wire into the cytoskeleton 🌀Juan Manuel Gomez Elliff (EMBL) @gomezjm-devmech.bsky.social — Mapping tissue mechanics with Brillouin microscopy

International Developmental Mechanics Seminar Series

Please fill out the following survey if you are interested in the 2025-2026 International Zoom Seminars on Developmental Mechanics.

tinyurl.com