Evidence map›Paper›PMID 34467328›Full record

ReviewJACS Au2021

Thiol-Mediated Uptake.

Quentin Laurent, Rémi Martinent, Bumhee Lim, Anh-Tuan Pham, Takehiro Kato, Javier López-Andarias, Naomi Sakai, Stefan Matile

Open access · goldAbstract readReview
In one paragraph

Review in JACS Au, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
11.5field-weighted citation impact, top 1% of its field
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

74 citing papers in PubMed, 165 citations in OpenAlex.

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14 more citing papers are in PubMed but not listed here.

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 at 1 institution in 1 country.

Quentin LaurentDepartment of Organic Chemistry, University of Geneva, 1211 Geneva, Switzerland.
Rémi MartinentDepartment of Organic Chemistry, University of Geneva, 1211 Geneva, Switzerland.
Bumhee LimDepartment of Organic Chemistry, University of Geneva, 1211 Geneva, Switzerland.
Anh-Tuan PhamDepartment of Organic Chemistry, University of Geneva, 1211 Geneva, Switzerland.
Takehiro KatoDepartment of Organic Chemistry, University of Geneva, 1211 Geneva, Switzerland.
Javier López-AndariasDepartment of Organic Chemistry, University of Geneva, 1211 Geneva, Switzerland.
Naomi SakaiDepartment of Organic Chemistry, University of Geneva, 1211 Geneva, Switzerland.ORCID 0000-0002-9460-1944
Stefan MatileDepartment of Organic Chemistry, University of Geneva, 1211 Geneva, Switzerland.ORCID 0000-0002-8537-8349
University of Geneva · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This Perspective focuses on thiol-mediated uptake, that is, the entry of substrates into cells enabled by oligochalcogenides or mimics, often disulfides, and inhibited by thiol-reactive agents. A short chronology from the initial observations in 1990 until today is followed by a summary of cell-penetrating poly(disulfide)s (CPDs) and cyclic oligochalcogenides (COCs) as privileged scaffolds in thiol-mediated uptake and inhibitors of thiol-mediated uptake as potential antivirals. In the spirit of a Perspective, the main part brings together topics that possibly could help to explain how thiol-mediated uptake really works. Extreme sulfur chemistry mostly related to COCs and their mimics, cyclic disulfides, thiosulfinates/-onates, diselenolanes, benzopolysulfanes, but also arsenics and Michael acceptors, is viewed in the context of acidity, ring tension, exchange cascades, adaptive networks, exchange affinity columns, molecular walkers, ring-opening polymerizations, and templated polymerizations. Micellar pores (or lipid ion channels) are considered, from cell-penetrating peptides and natural antibiotics to voltage sensors, and a concise gallery of membrane proteins, as possible targets of thiol-mediated uptake, is provided, including CLIC1, a thiol-reactive chloride channel; TMEM16F, a Ca-activated scramblase; EGFR, the epithelial growth factor receptor; and protein-disulfide isomerase, known from HIV entry or the transferrin receptor, a top hit in proteomics and recently identified in the cellular entry of SARS-CoV-2.

Identifiers

PMID34467328
PMCPMC8395643
OpenAlexW3159607027

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.