Evidence map›Paper›PMID 39975383›Full record

ArticlebioRxiv : the preprint server for biology2025

Identification of actionable targeted protein degradation effector sites through Site-specific Ligand Incorporation-induced Proximity (SLIP).

Zhangping Xiao, Efthymios Spyridon Gavriil, Fangyuan Cao, Xinyue Zhang, Stan Xiaogang Li, Sergei Kotelnikov, Patrycja Michalska, Friederike Marte, Chloe Huang, Yudi Lu and 4 more

Abstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors.

Zhangping XiaoDepartment of Chemistry, Imperial College London, 82 Wood Lane, London W12 0BZ, UK.
Efthymios Spyridon GavriilDepartment of Chemistry, Imperial College London, 82 Wood Lane, London W12 0BZ, UK.
Fangyuan CaoDepartment of Chemistry, Imperial College London, 82 Wood Lane, London W12 0BZ, UK.
Xinyue ZhangDepartment of Chemistry, Imperial College London, 82 Wood Lane, London W12 0BZ, UK.
Stan Xiaogang LiDepartment of Applied Mathematics and Statistics, Stony Brook University, Stony Brook, NY 11794, United States.
Sergei KotelnikovDepartment of Applied Mathematics and Statistics, Stony Brook University, Stony Brook, NY 11794, United States.
Patrycja MichalskaDepartment of Chemistry, Imperial College London, 82 Wood Lane, London W12 0BZ, UK.
Friederike MarteDepartment of Chemistry, Imperial College London, 82 Wood Lane, London W12 0BZ, UK.
Chloe HuangDepartment of Chemistry, Imperial College London, 82 Wood Lane, London W12 0BZ, UK.
Yudi LuDepartment of Chemistry, Imperial College London, 82 Wood Lane, London W12 0BZ, UK.
Yunxuan ZhangDepartment of Chemistry, Imperial College London, 82 Wood Lane, London W12 0BZ, UK.
Erika BernardiniDepartment of Chemistry, Imperial College London, 82 Wood Lane, London W12 0BZ, UK.
Dima KozakovDepartment of Applied Mathematics and Statistics, Stony Brook University, Stony Brook, NY 11794, United States.ORCID 0000-0003-0464-4500
Edward W TateDepartment of Chemistry, Imperial College London, 82 Wood Lane, London W12 0BZ, UK.ORCID 0000-0003-2213-5814

Funding

Enabling the Accelerated Discovery of Novel Chemical Probes by Integration of Crystallographic, Computational, and Synthetic Chemistry ApproachesR01GM140154 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI TROPSHA, ALEXANDER, WILLSON, TIMOTHY M · 2021 to 2024
$2.4M
Simulation of Multi-Protein systemsR01GM140098 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI KOZAKOV, DMYTRO · 2021 to 2024
$1.4M
NIGMS NIH HHS R01 GM140098NIGMS NIH HHS R01 GM140154
6 · The paper itself

Abstract

Targeted protein degradation (TPD) is a rapidly emerging and potentially transformative therapeutic modality. However, the large majority of >600 known ubiquitin ligases have yet to be exploited as TPD effectors by proteolysis-targeting chimeras (PROTACs) or molecular glue degraders (MGDs). We report here a chemical-genetic platform, Site-specific Ligand Incorporation-induced Proximity (SLIP), to identify actionable ("PROTACable") sites on any potential effector protein in intact cells. SLIP uses genetic code expansion (GCE) to encode copper-free "click" ligation at a specific effector site in intact cells, enabling

Indexed as

Genetic code expansioninduced proximitytargeted protein degradation

Identifiers

PMID39975383
PMCPMC11838594

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.