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Niopek Lab

@niopeklab.bsky.social
175 followers 22 following 28 posts

Lab account for AG Niopek at the University of Heidelberg IPMB Protein Engineering | Allostery | CRISPR | Optogenetics | ML Account is managed by PhD Students Niopeklab.de

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Reposted by Niopek Lab
Nicholas Southern @neuroscinikolai.bsky.social · 05/07/2026
New preprint! We used protein domain insertion to tighten the editing window of the TadA8e adenine base editor. Bulky domain insertions concentrated editing around position A5, maintained robust on-target activity, and reduced Cas-independent off-target editing. 🧬 doi.org/10.64898/202...
biorxiv.org
Domain Insertion Improves the Precision of a CRISPR Adenine Base Editor
Adenine base editors (ABEs) enable efficient A:T to G:C conversion, but their broad activity windows frequently cause unintended bystander edits. We hypothesized that insertion of a bulky, inert prote...
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Reposted by Niopek Lab
Nicholas Southern @neuroscinikolai.bsky.social · 15/04/2026
1/28 How do you optimize a dynamic protein property that emerges from multiple states? Our finally published paper in @NatureComms takes on one of the hardest problems in protein engineering with phage assisted evolution: evolving allosteric switches🧵
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Reposted by Niopek Lab
Michael Jendrusch @mjendrusch.bsky.social · 02/03/2026
Are you interested in working with a fresh team on cutting edge protein design? We're hiring a Technical Assistant for our protein design team at DKFZ Heidelberg: jobs.dkfz.de/en/jobs/1683... Please share!
jobs.dkfz.de
Technical Assistant
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Reposted by Niopek Lab
Jan Mathony @jmathony.bsky.social · 12/02/2026
🎉🎉 Our paper on temperature-dependent protein control using AsLOV2 variants is now published at @natchembio.nature.com: www.nature.com/articles/s41... including some new insights from extend variant characterizations.
nature.com
Modular engineering of thermoresponsive allosteric proteins - Nature Chemical Biology
Thermogenetics enables spatiotemporal control of protein activity using temperature. Now, engineering of a compact, insertable thermoresponsive protein module diversifies the classes of proteins amena...
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Niopek Lab @niopeklab.bsky.social · 13/06/2025
Inspired by how nature evolves trigger responsiveness through alternating pressures, we are excited to present POGO-PANCE and RAMPhaGE: Phage-assisted evolution platforms for engineering allosteric protein switches under dynamic selection. Preprint: doi.org/10.1101/2025...
doi.org
Phage-Assisted Evolution of Allosteric Protein Switches
Allostery, the transmission of locally induced conformational changes to distant functional sites, is a key mechanism for protein regulation. Artificial allosteric effectors enable remote manipulation...
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Reposted by Niopek Lab
Dominik Niopek @dominikniopek.bsky.social · 13/06/2025
Check out the new pre-print from our lab on phage-assisted evolution of light-switchable, allosteric proteins. Congrats to first author @neuroscinikolai.bsky.social, co-corresponding author @jmathony.bsky.social and everyone from the @niopeklab.bsky.social involved! www.biorxiv.org/content/10.1...
biorxiv.org
Phage-Assisted Evolution of Allosteric Protein Switches
Allostery, the transmission of locally induced conformational changes to distant functional sites, is a key mechanism for protein regulation. Artificial allosteric effectors enable remote manipulation...
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Niopek Lab @niopeklab.bsky.social · 16/12/2024
Excited to announce our optogenetic transcriptional deactivation toolbox is now out in its final form at Nucleic Acids research: academic.oup.com/nar/advance-....
academic.oup.com
A modular toolbox for the optogenetic deactivation of transcription
Abstract. Light-controlled transcriptional activation is a commonly used optogenetic strategy that allows researchers to regulate gene expression with high
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Niopek Lab @niopeklab.bsky.social · 05/12/2024
We are thrilled to share ProDomino a model for the prediction of domain insertion sites in proteins. Our approach enables the simple and rapid engineering of highly potent switchable proteins, as we exemplify by creating novel inducible variants of Cas9 and Cas12a. www.biorxiv.org/content/10.1...
biorxiv.org
Rational engineering of allosteric protein switches by in silico prediction of domain insertion sites
Domain insertion engineering is a powerful approach to juxtapose otherwise separate biological functions, resulting in proteins with new-to-nature activities. A prominent example are switchable protei...
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Niopek Lab @niopeklab.bsky.social · 26/11/2024
New pre-print from our group reporting engineered, broad-spectrum anti-CRISPR proteins based on AcrIIA5, a type II inhibitor, and AcrVA1, a type V inhibitor, for opto- and chemogenetic control of CRISPR-Cas9 and -Cas12a: www.biorxiv.org/content/10.1... (1/3)
biorxiv.org
A Versatile Anti-CRISPR Platform for Opto- and Chemogenetic Control of CRISPR-Cas9 and Cas12 across a Wide Range of Orthologs
CRISPR-Cas technologies have revolutionized life sciences by enabling programmable genome editing across diverse organisms. Achieving dynamic and precise control over CRISPR-Cas activity with exogenou...
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Niopek Lab @niopeklab.bsky.social · 26/11/2024
Now out in Nucleic Acids Research: A deep mutational scanning platform to characterize the fitness landscape of anti-CRISPR proteins: doi.org/10.1093/nar/... (1/4)
doi.org
A deep mutational scanning platform to characterize the fitness landscape of anti-CRISPR proteins
Abstract. Deep mutational scanning is a powerful method for exploring the mutational fitness landscape of proteins. Its adaptation to anti-CRISPR proteins,
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Reposted by Niopek Lab
Jan Mathony @jmathony.bsky.social · 22/11/2024
Our paper on DMS of anti-CRISPR proteins is out in it's final form Nucleic Acids Research! Many congrats to first authors Tobias and Michael! It was lots of fun to see the story develop. academic.oup.com/nar/advance-...
academic.oup.com
A deep mutational scanning platform to characterize the fitness landscape of anti-CRISPR proteins
Abstract. Deep mutational scanning is a powerful method for exploring the mutational fitness landscape of proteins. Its adaptation to anti-CRISPR proteins,
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