Article in Nature communications, 2022. 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
0.6field-weighted citation impact, top 35% 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, 7 citations in OpenAlex.
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
17 authors at 8 institutions in 3 countries.
Albert EscobedoInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Baldiri Reixac 10, 08028, Barcelona, Spain. albert.escobedo@crg.eu.ORCID 0000-0001-7295-5111
Jonathan PiccirilloInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Baldiri Reixac 10, 08028, Barcelona, Spain.ORCID 0000-0001-9131-7270
Juan ArandaInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Baldiri Reixac 10, 08028, Barcelona, Spain.ORCID 0000-0001-9385-4651
Tammo DiercksCIC bioGUNE, Basque Research and Technology Alliance (BRTA), Bizkaia Science and Technology Park, 48160, Derio, Spain.
Borja MateosInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Baldiri Reixac 10, 08028, Barcelona, Spain.ORCID 0000-0002-0310-4943
Carla Garcia-CabauInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Baldiri Reixac 10, 08028, Barcelona, Spain.ORCID 0000-0003-0533-0642
Macarena Sánchez-NavarroDepartment of Molecular Biology, Instituto de Parasitología y Biomedicina López Neyra (IPBLN-CSIC), Armilla, Granada, Spain.ORCID 0000-0002-0159-2381
Busra TopalInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Baldiri Reixac 10, 08028, Barcelona, Spain.
Mateusz BiesagaInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Baldiri Reixac 10, 08028, Barcelona, Spain.ORCID 0000-0001-6443-1270
Lasse StabyREPIN and Structural Biology and NMR Laboratory, The Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Ole Maaloes Vej 5, DK-2200, Copenhagen N, Denmark.
Birthe B KragelundREPIN and Structural Biology and NMR Laboratory, The Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Ole Maaloes Vej 5, DK-2200, Copenhagen N, Denmark.ORCID 0000-0002-7454-1761
Jesús GarcíaInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Baldiri Reixac 10, 08028, Barcelona, Spain.ORCID 0000-0003-2961-9790
Oscar MilletCIC bioGUNE, Basque Research and Technology Alliance (BRTA), Bizkaia Science and Technology Park, 48160, Derio, Spain.ORCID 0000-0001-8748-4105
Modesto OrozcoInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Baldiri Reixac 10, 08028, Barcelona, Spain.ORCID 0000-0002-8608-3278
Murray ColesDepartment of Protein Evolution, Max Planck Institute for Biology, Max-Planck-Ring 5, 72076, Tubingen, Germany.ORCID 0000-0001-6716-6150
Ramon CrehuetInstitute for Advanced Chemistry of Catalonia (IQAC), CSIC, Jordi Girona 18-26, 08034, Barcelona, Spain.ORCID 0000-0002-6687-382X
Xavier SalvatellaInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Baldiri Reixac 10, 08028, Barcelona, Spain. xavier.salvatella@irbbarcelona.org.ORCID 0000-0002-8371-4185
Institute for Research in Biomedicine · ESEuskadiko Parke Teknologikoa · ESUniversity of Copenhagen · DKCentro Nacional de Biotecnología · ESInstitució Catalana de Recerca i Estudis Avançats · ESInstitute of Advanced Chemistry of Catalonia · ESInstituto de Parasitología y Biomedicina "López - Neyra" · ESMax Planck Institute for Biology · DE
Funding
No grant is acknowledged in the PubMed record.
6 · The paper itself
Abstract
The binding of intrinsically disordered proteins to globular ones can require the folding of motifs into α-helices. These interactions offer opportunities for therapeutic intervention but their modulation with small molecules is challenging because they bury large surfaces. Linear peptides that display the residues that are key for binding can be targeted to globular proteins when they form stable helices, which in most cases requires their chemical modification. Here we present rules to design peptides that fold into single α-helices by instead concatenating glutamine side chain to main chain hydrogen bonds recently discovered in polyglutamine helices. The resulting peptides are uncharged, contain only natural amino acids, and their sequences can be optimized to interact with specific targets. Our results provide design rules to obtain single α-helices for a wide range of applications in protein engineering and drug design.
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.
A glutamine-based single α-helix scaffold to target globular proteins. · full record | OpenQuestion