Evidence map›Paper›PMID 34094460›Full record

ArticleChemical science2020

Fucosylated ubiquitin and orthogonally glycosylated mutant A28C: conceptually new ligands for

Sakonwan Kuhaudomlarp, Linda Cerofolini, Sabrina Santarsia, Emilie Gillon, Silvia Fallarini, Grazia Lombardi, Maxime Denis, Stefano Giuntini, Carolina Valori, Marco Fragai and 3 more

Open access · diamondAbstract read
In one paragraph

Article in Chemical science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

3 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Review
  3. Druggable Allosteric Sites in β-Propeller Lectins.Angewandte Chemie (International ed. in English) · 2022
    Article
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

13 authors at 6 institutions in 2 countries.

Sakonwan KuhaudomlarpUniversité Grenoble Alpes, CNRS, CERMAV 38000 Grenoble France.
Linda CerofoliniCIRMMP, University of Florence via Sacconi, 6 50019 Sesto F.no FI Italy.ORCID https://orcid.org/0000-0002-0795-9594
Sabrina SantarsiaUniversità di Firenze, Department of Chemistry via della Lastruccia, 3, 13, 50019 Sesto F.no FI Italy cristina.nativi@unifi.it.
Emilie GillonUniversité Grenoble Alpes, CNRS, CERMAV 38000 Grenoble France.
Silvia FallariniUniversità del Piemonte Orientale, Department of Pharmaceutical Sciences 28100 Novara Italy.
Grazia LombardiUniversità del Piemonte Orientale, Department of Pharmaceutical Sciences 28100 Novara Italy.
Maxime DenisUniversità di Firenze, Department of Chemistry via della Lastruccia, 3, 13, 50019 Sesto F.no FI Italy cristina.nativi@unifi.it.
Stefano GiuntiniUniversità di Firenze, Department of Chemistry via della Lastruccia, 3, 13, 50019 Sesto F.no FI Italy cristina.nativi@unifi.it.
Carolina ValoriUniversità di Firenze, Department of Chemistry via della Lastruccia, 3, 13, 50019 Sesto F.no FI Italy cristina.nativi@unifi.it.
Marco FragaiUniversità di Firenze, Department of Chemistry via della Lastruccia, 3, 13, 50019 Sesto F.no FI Italy cristina.nativi@unifi.it.
Anne ImbertyUniversité Grenoble Alpes, CNRS, CERMAV 38000 Grenoble France.ORCID https://orcid.org/0000-0001-6825-9527
Alessandro DondoniInterdisciplinary Center for the Study of Inflammation, University of Ferrara 44121 Ferrara Italy.ORCID https://orcid.org/0000-0003-3454-1983
Cristina NativiUniversità di Firenze, Department of Chemistry via della Lastruccia, 3, 13, 50019 Sesto F.no FI Italy cristina.nativi@unifi.it.ORCID https://orcid.org/0000-0002-6312-3230
University of Florence · ITInstitut des langues et cultures d'Europe, Amérique, Afrique, Asie et Australie · FRUniversità degli Studi del Piemonte Orientale “Amedeo Avogadro” · ITGiotto Biotech (Italy) · ITInteruniversity Consortium for Magnetic Resonance · ITUniversity of Ferrara · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two orthogonal, metal free click reactions, enabled to glycosylate ubiquitin and its mutant A28C forming two protein scaffolds with high affinity for BambL, a lectin from the human pathogen

Identifiers

PMID34094460
PMCPMC8163020
OpenAlexW3093481382

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.