Marcin J. Suskiewicz
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msuskiewicz.bsky.social
Marcin J. Suskiewicz
@msuskiewicz.bsky.social
Structural biologist and biochemist. CNRS researcher at CBM Orléans @cbm-upr4301.bsky.social. Interested in protein modifications & interactions. Also husband, dad of 2, friend, ☧. Personal website: msuskiewicz.github.io
Pinned
Very happy to share our collaborative project on FAM118 proteins - noncanonical sirtuins that form filaments and process NAD in human and other vertebrate cells.
Filament formation and NAD processing by noncanonical human FAM118 sirtuins
Nature Structural & Molecular Biology - Baretić and Missoury et al. identify vertebrate proteins FAM118B and FAM118A as sirtuins similar to bacterial antiphage enzymes and show that...
rdcu.be
Reposted by Marcin J. Suskiewicz
This is excellent.
To “my students and to anyone who might listen, I say: Don’t surrender to AI your ability to read, write and think when others once risked their lives and died for the freedom to do so.”

www.huffpost.com/entry/histor...
I Set A Trap To Catch My Students Cheating With AI. The Results Were Shocking.
"Students are not just undermining their ability to learn, but to someday lead."
www.huffpost.com
November 21, 2025 at 9:42 AM
Reposted by Marcin J. Suskiewicz
Finally out in @nature.com! We uncovered a mechanistic framework for a general and conserved mRNA nuclear export pathway. www.nature.com/articles/s41.... 1/
November 19, 2025 at 11:22 PM
Reposted by Marcin J. Suskiewicz
New preprint 🚨 We systematically measured 17 million phospho-specific dose-response curves (133 kinase inhibitors × 5 cell lines) to decrypt the kinases that shape the human phosphoproteome. We show that drug perturbation potency (not effect size) links kinases to substrates while controlling FDR.
Did you ever come across a phosphosite in your proteomics data for which nothing was known? - I bet so!

We have developed a new strategy termed "potency coherence analysis" that leverages the drug potency dimension in decryptM to decode the kinases that shape the human phosphoproteome.

Read more:
Chemical proteomics decrypts the kinases that shape the dynamic human phosphoproteome
Mass-spectrometry-based phosphoproteomics enables the analysis of thousands of protein phosphorylation events across the human proteome. However, there is a lack of scalable, hypothesis-free, and stat...
doi.org
November 20, 2025 at 11:59 AM
Reposted by Marcin J. Suskiewicz
We just took a deep dive into this tour-de-force chemoproteomics paper from @stephanhacker2.bsky.social and colleagues in our journal club today — really interesting findings about selectivity and coverage of 56 different electrophilic warheads, and great experimental and analysis workflows. Bravo!
How can we study target engagement and selectivity of covalent inhibitors? Which electrophilic probes are best suited to study a certain amino acid?

Our study on "Profiling the proteome-wide selectivity of diverse electrophiles" is published in Nature Chemistry.(1/7)

www.nature.com/articles/s41...
Profiling the proteome-wide selectivity of diverse electrophiles - Nature Chemistry
Covalent inhibitors are powerful entities in drug discovery. Now the amino acid selectivity and reactivity of a diverse electrophile library have been assessed proteome-wide using an unbiased workflow...
www.nature.com
November 20, 2025 at 1:24 AM
Reposted by Marcin J. Suskiewicz
A UBH-UBX module amplifies p97/VCP’s unfolding power to facilitate protein extraction and degradation

www.nature.com/articles/s41...
A UBH-UBX module amplifies p97/VCP’s unfolding power to facilitate protein extraction and degradation - Nature Communications
p97-UFD1L-NPLOC4 unfolds proteins for proteasomal degradation, but whether it suffices to extract proteins from lipid bilayers is unclear. We show that the UBH-UBX module in FAF2 and its homologs doub...
www.nature.com
November 19, 2025 at 3:01 PM
Reposted by Marcin J. Suskiewicz
An open-source computational pipeline to visualize the binding interfaces of protein domains is described
www.science.org/doi/10.1126/...
@uvapress.bsky.social @knaegle.bsky.social
November 19, 2025 at 4:05 PM
Reposted by Marcin J. Suskiewicz
Are you looking for female speakers in CryoEM for seminars and conferences? Are you a woman in CryoEM and not yet on the ‚woman in CryoEM‘ list? Find your speakers and add/update name and affiliation! docs.google.com/spreadsheets...
November 18, 2025 at 10:18 AM
Reposted by Marcin J. Suskiewicz
Please check our collaborative paper with Marcin Suskiewicz and Sebastien Huet labs on FAM118 proteins – non-canonical sirtuins that form filaments and act as NADases in human and other vertebrate cells.
www.nature.com/articles/s41...
Filament formation and NAD processing by noncanonical human FAM118 sirtuins - Nature Structural & Molecular Biology
Baretić and Missoury et al. identify vertebrate proteins FAM118B and FAM118A as sirtuins similar to bacterial antiphage enzymes and show that FAM118A/B processing of NAD involves head-to-tail filament...
www.nature.com
November 17, 2025 at 6:17 PM
Reposted by Marcin J. Suskiewicz
Our new special collection "Protein-Nucleic Acid Interactions: From Origins to Design (2025)" is now published in Current Opinion in Structural Biology. I'm excited to have both co-edited it with Shandar Ahmad and contributed a review!

www.sciencedirect.com/special-issu...
LinkedIn
This link will take you to a page that’s not on LinkedIn
lnkd.in
November 10, 2025 at 5:54 PM
Reposted by Marcin J. Suskiewicz
Akin to bacterial SIR2 antiphage proteins, human SIRal, also known as FAM118b, forms filaments that are essential for its NAD processing activity.

Awesome to see structures of these filaments that differ from bacterial ones.

Congrats to the authors on this beautiful study.
November 17, 2025 at 4:52 PM
Very happy to share our collaborative project on FAM118 proteins - noncanonical sirtuins that form filaments and process NAD in human and other vertebrate cells.
Filament formation and NAD processing by noncanonical human FAM118 sirtuins
Nature Structural & Molecular Biology - Baretić and Missoury et al. identify vertebrate proteins FAM118B and FAM118A as sirtuins similar to bacterial antiphage enzymes and show that...
rdcu.be
November 17, 2025 at 11:37 AM
Reposted by Marcin J. Suskiewicz
MISO: microfluidic protein isolation enables single-particle cryo-EM structure determination from a single cell colony.

Or from a single dish of HEK cell culture in the case of two membrane proteins.

Out in Nature Methods now! lnkd.in/gpyBSceg

Wonderful collaboration with the Efremov lab.
November 14, 2025 at 6:38 PM
Reposted by Marcin J. Suskiewicz
Our nuclease-protease story is out! We explored a fascinating case of coevolution and modularity in prokaryotic immune systems: www.science.org/doi/10.1126/...

Thanks to wonderful coauthors/collaborators/friends, the whole @doudna-lab.bsky.social and everyone at @innovativegenomics.bsky.social
Recurrent acquisition of nuclease-protease pairs in antiviral immunity
Antiviral immune systems diversify by integrating new genes into existing pathways, creating new mechanisms of viral resistance. We identified genes encoding a predicted nuclease paired with a trypsin...
www.science.org
November 13, 2025 at 10:15 PM
Reposted by Marcin J. Suskiewicz
Thrilled to share that the final piece of my PhD work is now on bioRxiv! biorxiv.org/content/10.1... With support from @nvidia and the @NSF, we used AlphaFold to screen 1.6M+ protein pairs, revealing thousands of potential novel PPIs. All data can be viewed at predictomes.org/hp
Proteome-wide in silico screening for human protein-protein interactions
Protein-protein interactions (PPIs) drive virtually all biological processes, yet most PPIs have not been identified and even more remain structurally unresolved. We developed a two-step computational...
biorxiv.org
November 12, 2025 at 9:26 PM
Reposted by Marcin J. Suskiewicz
profaff.fr

The new ProfAff database is up and running. Although there are still many things to improve, it is a major upgrade.
ProfAffv2 - Protein Affinity Database
profaff.fr
October 28, 2025 at 8:04 AM
Reposted by Marcin J. Suskiewicz
Reposted by Marcin J. Suskiewicz
Beautiful review from J. Rudolph on Histone PARylation factor 1: a review of its role in the DNA damage response url: academic.oup.com/nar/article/...
Histone PARylation factor 1: a review of its role in the DNA damage response
Abstract. Although poly-(ADP ribose) polymerase 1 (PARP1) and PARylation of histones have been known for over 50 years and have been successfully targeted
academic.oup.com
November 11, 2025 at 2:49 PM
Reposted by Marcin J. Suskiewicz
People can appreciate science without AI?

Sorry to dunk on this but someone has to break up the chorus - qed isn't ready @biorxivpreprint.bsky.social

Do you implicitly want to send people to AI spin over the paper itself? Not what we're fighting for in #SciPub #AcademicSky #ResearchIntegrity
IT'S HAPPENING! 💥 I'm psyched to launch the collaboration between @qedscience.bsky.social & @openrxiv.bsky.social @biorxivpreprint.bsky.social! Preprint + q.e.d = your science is out there, and anyone can appreciate it. Let's care about making discoveries, and not on “getting published” (1/3) 👇
November 11, 2025 at 7:52 AM
A lovely example of how extensive cryoEM data classification can provide new insights into the recognition of the nucleosome by nucleosome-modifying proteins.
ALC1 Finds a New Foothold on the Nucleosome's Super-Groove https://www.biorxiv.org/content/10.1101/2025.11.10.687450v1
November 11, 2025 at 10:11 AM
Reposted by Marcin J. Suskiewicz
Design stable, folded proteins using only the 10 "ancient" amino acids.

www.biorxiv.org/content/10.1...
October 31, 2025 at 7:40 PM
Reposted by Marcin J. Suskiewicz
Inspired by the AI conference hosted by the Danish Presidency of the EU I've written a probably too long piece about my own shift from a multi-variate/bayesian genomicist to an AI aligned genomicist / biologist.

www.linkedin.com/pulse/though...
Thoughts on AI, Take 2
Further thoughts about AI brought together for me by the AI Science Summit organized by the European Commission and the Danish Presidency of the Council of the EU 2025 - in lovely Copenhagen - this ti...
www.linkedin.com
November 7, 2025 at 5:40 PM
Reposted by Marcin J. Suskiewicz
Here you can read our full review paper on the interplay between ADP-ribosylation and ubiquitination, with special focus on dual, hybrid modification ADPr-Ub:
pubmed.ncbi.nlm.nih.gov/41065402/
October 9, 2025 at 10:07 PM
Reposted by Marcin J. Suskiewicz
Excited to share the peer-reviewed version of our work, now online in @embojournal.org! Big thanks to our reviewers and @hvodermaier.bsky.social for facilitating this process. Looking forward to continuing this fun collaboration with @michaelnadbio.bsky.social!
www.embopress.org/doi/full/10....
October 30, 2025 at 3:33 PM
Reposted by Marcin J. Suskiewicz
this looks very interesting with numerous implications for nuclear biology and gene expression.

Mapping chromatin structure at base-pair resolution unveils a unified model of cis-regulatory element interactions: Cell www.cell.com/cell/fulltex...
Mapping chromatin structure at base-pair resolution unveils a unified model of cis-regulatory element interactions
Li et al. apply base-pair resolution Micro Capture-C ultra to map chromatin contacts between individual motifs within cis-regulatory elements and reveal a unified model of biophysically mediated enhan...
www.cell.com
November 9, 2025 at 5:07 PM