Evidence map›Paper›PMID 37961294›Full record

ArticlebioRxiv : the preprint server for biology2023

Small-molecule binding and sensing with a designed protein family.

Gyu Rie Lee, Samuel J Pellock, Christoffer Norn, Doug Tischer, Justas Dauparas, Ivan Anischenko, Jaron A M Mercer, Alex Kang, Asim Bera, Hannah Nguyen and 9 more

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

19 authors.

Gyu Rie Lee
Samuel J Pellock
Christoffer Norn
Doug Tischer
Justas Dauparas
Jaron A M Mercer
Alex Kang
Asim Bera
Hannah Nguyen
Inna Goreshnik
Dionne Vafeados
Nicole Roullier
Hannah L Han
Brian Coventry
Hugh K Haddox
David R Liu
Andy Hsien-Wei Yeh
David Baker

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Despite transformative advances in protein design with deep learning, the design of small-molecule-binding proteins and sensors for arbitrary ligands remains a grand challenge. Here we combine deep learning and physics-based methods to generate a family of proteins with diverse and designable pocket geometries, which we employ to computationally design binders for six chemically and structurally distinct small-molecule targets. Biophysical characterization of the designed binders revealed nanomolar to low micromolar binding affinities and atomic-level design accuracy. The bound ligands are exposed at one edge of the binding pocket, enabling the

Identifiers

PMID37961294
PMCPMC10635051

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.