Evidence map›Paper›PMID 39190920›Full record

ArticleJournal of the American Chemical Society2024

SuFEx Chemistry Enables Covalent Assembly of a 280-kDa 18-Subunit Pore-Forming Complex.

Lee Schnaider, Sophia Tan, Pratik R Singh, Floriana Capuano, Alistair J Scott, Richard Hambley, Lei Lu, Hyunjun Yang, E Jayne Wallace, Hyunil Jo and 1 more

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Sculpting semisynthetic conducting protein pores by de novo design.Nature structural & molecular biology · 2026
    Article
  2. De novo design of semisynthetic conduction pores.Nature structural & molecular biology · 2026
    Article
  3. Article
  4. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors.

Lee SchnaiderDepartment of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, California 94143, United States.ORCID 0000-0002-8505-300X
Sophia TanDepartment of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, California 94143, United States.ORCID 0000-0002-6181-7810
Pratik R SinghOxford Nanopore Technologies Plc, Oxford OX4 4DQ, U.K.
Floriana CapuanoOxford Nanopore Technologies Plc, Oxford OX4 4DQ, U.K.
Alistair J ScottOxford Nanopore Technologies Plc, Oxford OX4 4DQ, U.K.
Richard HambleyOxford Nanopore Technologies Plc, Oxford OX4 4DQ, U.K.
Lei LuDepartment of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, California 94143, United States.ORCID 0000-0001-7097-1505
Hyunjun YangDepartment of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, California 94143, United States.ORCID 0000-0003-2524-2201
E Jayne WallaceOxford Nanopore Technologies Plc, Oxford OX4 4DQ, U.K.
Hyunil JoDepartment of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, California 94143, United States.
William F DeGradoDepartment of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, California 94143, United States.ORCID 0000-0003-4745-263X

Funding

Deciphering the relationship between structure, dynamics and function in helical bundle proteinsR35GM122603 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI WILLIAM DEGRADO · 2017 to 2026
$7.1M
Molecular Biophysics Training GrantT32GM149436 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI Aashish Manglik · 2023 to 2026
$1.6M
Patching Amyloid Surface onto Soluble ProteinK99AG084926 · NIA · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI YANG, HYUNJUN · 2024 to 2024
$119k
Probing the rules of molecular recognition through the de novo design of proteins that bind small-molecule drugs.F32GM143869 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SCHNAIDER, LEE · 2022 to 2022
$68k
NIA NIH HHS K99 AG084926NIGMS NIH HHS F32 GM143869NIGMS NIH HHS R35 GM122603
6 · The paper itself

Abstract

Proximity-enhanced chemical cross-linking is an invaluable tool for probing protein-protein interactions and enhancing the potency of potential peptide and protein drugs. Here, we extend this approach to covalently stabilize large macromolecular assemblies. We used SuFEx chemistry to covalently stabilize an 18-subunit pore-forming complex, CsgG:CsgF, consisting of nine CsgG membrane protein subunits that noncovalently associate with nine CsgF peptides. Derivatives of the CsgG:CsgF pore have been used for DNA sequencing, which places high demands on the structural stability and homogeneity of the complex. To increase the robustness of the pore, we designed and synthesized derivatives of CsgF-bearing sulfonyl fluorides, which react with CsgG in very high yield to form a covalently stabilized CsgG:CsgF complex. The resulting pores formed highly homogeneous channels when added to artificial membranes. The high yield and rapid reaction rate of the SuFEx reaction prompted molecular dynamics simulations, which revealed that the SO

Indexed as

Molecular Dynamics SimulationCross-Linking ReagentsProtein SubunitsCross-Linking ReagentsProtein Subunits

Identifiers

PMID39190920
PMCPMC12360496

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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.