Article in Journal of the American Chemical Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.4field-weighted citation impact, top 19% 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
4 citing papers in PubMed, 17 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
11 authors at 3 institutions in 1 country.
Kelsey R MillerDepartment of Chemistry, 1102 Natural Sciences II, University of California, Irvine, California 92697, United States.
Saborni BiswasDepartment of Chemistry, Carnegie Mellon University, 4400 Fifth Avenue, Pittsburgh, Pennsylvania 15213, United States.
Andrew JasniewskiDepartment of Molecular Biology and Biochemistry, University of California, Irvine, California 92697, United States.ORCID 0000-0001-7614-0796
Alec H FollmerDepartment of Chemistry, 1102 Natural Sciences II, University of California, Irvine, California 92697, United States.ORCID 0000-0002-6244-6804
Ankita BiswasDepartment of Chemistry, 1102 Natural Sciences II, University of California, Irvine, California 92697, United States.
Therese AlbertDepartment of Biochemistry and Molecular Biology, Oregon Health & Science University, Mail Code HRC3, 3181 SW Sam Jackson Park Road, Portland, Oregon 97239, United States.ORCID 0000-0001-7248-0873
Sinan SabuncuDepartment of Biochemistry and Molecular Biology, Oregon Health & Science University, Mail Code HRC3, 3181 SW Sam Jackson Park Road, Portland, Oregon 97239, United States.ORCID 0000-0001-8346-8175
Emile L BominaarDepartment of Chemistry, Carnegie Mellon University, 4400 Fifth Avenue, Pittsburgh, Pennsylvania 15213, United States.ORCID 0000-0002-5125-265X
Michael P HendrichDepartment of Chemistry, Carnegie Mellon University, 4400 Fifth Avenue, Pittsburgh, Pennsylvania 15213, United States.ORCID 0000-0003-4775-0389
Pierre Moënne-LoccozDepartment of Biochemistry and Molecular Biology, Oregon Health & Science University, Mail Code HRC3, 3181 SW Sam Jackson Park Road, Portland, Oregon 97239, United States.ORCID 0000-0002-7684-7617
A S BorovikDepartment of Chemistry, 1102 Natural Sciences II, University of California, Irvine, California 92697, United States.ORCID 0000-0001-5049-9952
University of California, Irvine · USCarnegie Mellon University · USOregon Health & Science University · US
Funding
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Nitric Oxide Reactions in MetalloenzymesR01GM074785 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI MOENNE-LOCCOZ, PIERRE · 2006 to 2019
$3.8M
EPR and Mossbauer Characterization of Mn and Fe Proteins, Models, IntermediatesR01GM077387 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI HENDRICH, MICHAEL P · 2006 to 2019
$2.9M
Confining Metal Complexes within Protein Hosts: Models for Metalloprotein Active SitesR01GM120349 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI BOROVIK, ANDREW S. · 2017 to 2024
$2.4M
Advanced Spectroscopic and Computational Analysis of Metal Sites in Enzymes, Biomimetic Models, and Catalytic Intermediates.R35GM141948 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI HENDRICH, MICHAEL P · 2021 to 2025
Dinuclear iron centers with a bridging hydroxido or oxido ligand form active sites within a variety of metalloproteins. A key feature of these sites is the ability of the protein to control the structures around the Fe centers, which leads to entatic states that are essential for function. To simulate this controlled environment, artificial proteins have been engineered using biotin-streptavidin (Sav) technology in which Fe complexes from adjacent subunits can assemble to form [Fe
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.
Artificial Metalloproteins with Dinuclear Iron-Hydroxido Centers. · full record | OpenQuestion