In one paragraphArticle 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. 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 itWhat 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 registryThe 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 literatureWho cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
4 · The recordCorrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
5 · Who and what moneyAuthors and funding
12 authors.
Adam P MoyerDepartment of Biochemistry and Institute for Protein Design, University of Washington, Seattle 98195, Washington, United States.
Theresa A RamelotDepartment of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy 12180, New York, United States.ORCID 0000-0002-0335-1573 Mariano CurtiInstitute of Chemical Research of Catalonia (ICIQ-CERCA), Barcelona Institute of Science and Technology, Av. Països Catalans 16, Tarragona 43007, Spain.ORCID 0000-0002-3721-4358 Margaret A EastmanDepartment of Chemistry, Oklahoma State University, Stillwater, Oklahoma 07478, United States.
Alex KangDepartment of Biochemistry and Institute for Protein Design, University of Washington, Seattle 98195, Washington, United States.
Asim K BeraDepartment of Biochemistry and Institute for Protein Design, University of Washington, Seattle 98195, Washington, United States.
Roberto TejeroDepartment of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy 12180, New York, United States.
Patrick J SalvesonDepartment of Biochemistry and Institute for Protein Design, University of Washington, Seattle 98195, Washington, United States.ORCID 0000-0003-0962-6010 Carles CurutchetDepartament de Farmàcia i Tecnologia Farmacèutica, i Fisicoquímica, Facultat de Farmàcia i Ciències de l'Alimentació, Universitat de Barcelona (UB), Av. Joan XXIII 27-31, Barcelona 08028, Spain.ORCID 0000-0002-0070-1208 Elisabet RomeroInstitute of Chemical Research of Catalonia (ICIQ-CERCA), Barcelona Institute of Science and Technology, Av. Països Catalans 16, Tarragona 43007, Spain.
Gaetano T MontelioneDepartment of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy 12180, New York, United States.ORCID 0000-0002-9440-3059 David BakerDepartment of Biochemistry and Institute for Protein Design, University of Washington, Seattle 98195, Washington, United States.
Funding
User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI MALCOLM S. CAPEL · 2018 to 2026
$34.2MHybrid Methods for Dynamic Structure Analysis of Proteins from Pathogenic MicroorganismsR35GM141818 · NIGMS · RENSSELAER POLYTECHNIC INSTITUTE · PI MONTELIONE, GAETANO T · 2021 to 2025
$3.3MRegional 800 MHz NMR System UpgradeS10OD030482 · OD · RENSSELAER POLYTECHNIC INSTITUTE · PI MONTELIONE, GAETANO T · 2021 to 2021
$1.3MEuropean Research CouncilNIGMS NIH HHS P30 GM124165NIGMS NIH HHS R35 GM141818NIH HHS S10 OD030482
6 · The paper itselfAbstract
Energetically favorable local interactions can overcome the entropic cost of chain ordering and cause otherwise flexible polymers to adopt regularly repeating backbone conformations. A prominent example is the α helix present in many protein structures, which is stabilized by
Indexed as
PeptidesCrystallography, X-RayDipeptidesModels, MolecularProtein Structure, SecondaryDipeptidesPeptides
Identifiers
PMID39231524
PMCPMC11421003
What OpenQuestion holds
Textmetadata
LicenceCC BY-NC-ND
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