Conny WH Yu
@connyyu.bsky.social
Pinned
And it's now live in Nature Structural & Molecular Biology! Many thanks to James and @lapassmore.bsky.social for a great collaboration.
www.nature.com/articles/s41...
www.nature.com/articles/s41...
Reposted by Conny WH Yu
This work is now officially published
@natsmb.nature.com
with some fun new analyses included in the revised version. Congratulations to all the authors! @connyyu.bsky.social @rappsilber.bsky.social @lrsinn.bsky.social @fjoreilly.bsky.social www.nature.com/articles/s41...
@natsmb.nature.com
with some fun new analyses included in the revised version. Congratulations to all the authors! @connyyu.bsky.social @rappsilber.bsky.social @lrsinn.bsky.social @fjoreilly.bsky.social www.nature.com/articles/s41...
November 15, 2025 at 9:51 AM
This work is now officially published
@natsmb.nature.com
with some fun new analyses included in the revised version. Congratulations to all the authors! @connyyu.bsky.social @rappsilber.bsky.social @lrsinn.bsky.social @fjoreilly.bsky.social www.nature.com/articles/s41...
@natsmb.nature.com
with some fun new analyses included in the revised version. Congratulations to all the authors! @connyyu.bsky.social @rappsilber.bsky.social @lrsinn.bsky.social @fjoreilly.bsky.social www.nature.com/articles/s41...
And it's now live in Nature Structural & Molecular Biology! Many thanks to James and @lapassmore.bsky.social for a great collaboration.
www.nature.com/articles/s41...
www.nature.com/articles/s41...
November 6, 2025 at 10:33 AM
And it's now live in Nature Structural & Molecular Biology! Many thanks to James and @lapassmore.bsky.social for a great collaboration.
www.nature.com/articles/s41...
www.nature.com/articles/s41...
A very late repost:
Mad2 is an incredible metamorphic protein capable of adopting multiple conformations. Here we reviewed existing structural data and investigated this ever-changing protein using a combination of real-time NMR and MD simulations (kudos to Joe! @jgreener64.bsky.social)
Mad2 is an incredible metamorphic protein capable of adopting multiple conformations. Here we reviewed existing structural data and investigated this ever-changing protein using a combination of real-time NMR and MD simulations (kudos to Joe! @jgreener64.bsky.social)
Our study of Mad2 conformational changes is out in final form.
A fun collaborative project to work that uses NMR and MD. @connyyu.bsky.social
onlinelibrary.wiley.com/doi/full/10....
A fun collaborative project to work that uses NMR and MD. @connyyu.bsky.social
onlinelibrary.wiley.com/doi/full/10....
Molecular mechanism of Mad2 conformational conversion promoted by the Mad2‐interaction motif of Cdc20
During mitosis, unattached kinetochores trigger the spindle assembly checkpoint by promoting the assembly of the mitotic checkpoint complex, a heterotetramer comprising Mad2, Cdc20, BubR1, and Bub3. ...
onlinelibrary.wiley.com
June 25, 2025 at 3:03 PM
A very late repost:
Mad2 is an incredible metamorphic protein capable of adopting multiple conformations. Here we reviewed existing structural data and investigated this ever-changing protein using a combination of real-time NMR and MD simulations (kudos to Joe! @jgreener64.bsky.social)
Mad2 is an incredible metamorphic protein capable of adopting multiple conformations. Here we reviewed existing structural data and investigated this ever-changing protein using a combination of real-time NMR and MD simulations (kudos to Joe! @jgreener64.bsky.social)
Reposted by Conny WH Yu
🚨 New from PDBe!
Check out the revamped PDBeChem service with enhanced Ligand Pages!
🔍 Explore detailed ligand data, interaction stats, bound structures, related ligands, and more—all in one place.
👉 Read more in the news:
https://buff.ly/4g8eF6E
Check out the revamped PDBeChem service with enhanced Ligand Pages!
🔍 Explore detailed ligand data, interaction stats, bound structures, related ligands, and more—all in one place.
👉 Read more in the news:
https://buff.ly/4g8eF6E
November 27, 2024 at 3:37 PM
🚨 New from PDBe!
Check out the revamped PDBeChem service with enhanced Ligand Pages!
🔍 Explore detailed ligand data, interaction stats, bound structures, related ligands, and more—all in one place.
👉 Read more in the news:
https://buff.ly/4g8eF6E
Check out the revamped PDBeChem service with enhanced Ligand Pages!
🔍 Explore detailed ligand data, interaction stats, bound structures, related ligands, and more—all in one place.
👉 Read more in the news:
https://buff.ly/4g8eF6E
Reposted by Conny WH Yu
Happy to announce that the latest UniProt NAR paper is now out. Find out what we've been up to here academic.oup.com/nar/advance-...
UniProt: the Universal Protein Knowledgebase in 2025
Abstract. The aim of the UniProt Knowledgebase (UniProtKB; https://www.uniprot.org/) is to provide users with a comprehensive, high-quality and freely acce
academic.oup.com
November 18, 2024 at 9:47 AM
Happy to announce that the latest UniProt NAR paper is now out. Find out what we've been up to here academic.oup.com/nar/advance-...
Reposted by Conny WH Yu
In this work, James used NMR with @connyyu.bsky.social , crosslinking mass spec with the Rappsilber lab and biochemical reconstitution to discover that dispersed regions within the IDRs interact with multiple conserved binding sites on Ccr4-Not.
October 21, 2024 at 1:16 AM
In this work, James used NMR with @connyyu.bsky.social , crosslinking mass spec with the Rappsilber lab and biochemical reconstitution to discover that dispersed regions within the IDRs interact with multiple conserved binding sites on Ccr4-Not.
"You cannot by sheer force compel scientific truths to reveal themselves. The major insights come only to the individuals who have the patience to develop an intimate understanding of a problem, who have the space and the freedom to take professional risks and explore apparently bizarre ideas...
December 16, 2023 at 5:11 PM
"You cannot by sheer force compel scientific truths to reveal themselves. The major insights come only to the individuals who have the patience to develop an intimate understanding of a problem, who have the space and the freedom to take professional risks and explore apparently bizarre ideas...