Evidence map›Paper›PMID 41394289›Full record

ArticleSynlett : accounts and rapid communications in synthetic organic chemistry2025

Hydrophilic α-Aryl-α-Diazoamides for Protein Esterification.

Aniekan Okon, Anton Morgunov, Jinyi Yang, Yana D Petri, Henry R Kilgore, Yanfeng Li, Eric R Strieter, Ronald T Raines

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Synlett : accounts and rapid communications in synthetic organic chemistry, 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

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

8 authors.

Aniekan OkonDepartment of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
Anton MorgunovDepartment of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
Jinyi YangDepartment of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
Yana D PetriDepartment of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
Henry R KilgoreDepartment of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
Yanfeng LiDepartment of Chemistry, University of Massachusetts Amherst, 710 North Pleasant Street, Amherst, MA 01003, USA.
Eric R StrieterDepartment of Chemistry, University of Massachusetts Amherst, 710 North Pleasant Street, Amherst, MA 01003, USA.
Ronald T RainesDepartment of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.

Funding

VIRUS PRODUCTION COREP30CA014051 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI Jacqueline A. Lees · 1985 to 2026
$93.9M
Protein ChemistryR35GM148220 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI Ronald T Raines · 2023 to 2026
$2.2M
Defining the Function of Proteasomal DeubiquitinasesR35GM149532 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI ERIC Robert STRIETER · 2023 to 2026
$1.5M
Molecular probes for allele-specific interdiction of K-Ras G12D signalingF32CA247259 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI OKON, ANIEKAN MATTHEW · 2020 to 2022
$206k
NCI NIH HHS F32 CA247259NCI NIH HHS P30 CA014051NIGMS NIH HHS R35 GM148220NIGMS NIH HHS R35 GM149532
6 · The paper itself

Abstract

Bioreversible protein esterification is a simple, customizable, and traceless strategy for the exogenous delivery of proteins into mammalian cells. Enabling this protein delivery strategy are α-aryl-α-diazoamides bearing a tolyl moiety. The aqueous solubility of the ensuing esterified protein is, however, often compromised, which can result in the loss of soluble esterified protein for downstream applications. Here, we undertook a structure-activity relationship campaign to generate hydrophilic diazoamides for use as protein esterification and cellular delivery agents. We find that the careful adjustment of the hydrogen-bond basicity of α-aryl-α-diazoamides is sufficient to engender soluble esterified proteins, as high hydrogen-bond basicity correlates with high aqueous solubility. Importantly, enhancing aqueous solubility of diazoamides should proceed

Indexed as

celldeliverydiazo compoundsesterificationhydrophilicityhydrophobicityproteinssolubility

Identifiers

PMID41394289
PMCPMC12700464

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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.