Evidence map›Paper›PMID 35202982›Full record

ArticleJournal of inorganic biochemistry2022

S K-edge XAS of Cu

Yang Ha, Sara A Dille, Augustin Braun, Kyle Colston, Britt Hedman, Keith O Hodgson, Partha Basu, Edward I Solomon

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of inorganic biochemistry, 2022. 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
0.1field-weighted citation impact, top 70% 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

0 citing papers in PubMed, 2 citations in OpenAlex.

No citing paper in PubMed yet.

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 4 institutions in 1 country.

Yang HaDepartment of Chemistry, Stanford University, Stanford, CA 94035, United States; Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA 94025, United States; Advanced Light Source, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA 94720, United States.
Sara A DilleDepartment of Chemistry and Chemical Biology, Indiana University-Purdue University Indianapolis, 402 N Blackford St, Indianapolis, IN 46202, United States.
Augustin BraunDepartment of Chemistry, Stanford University, Stanford, CA 94035, United States; Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA 94025, United States.
Kyle ColstonDepartment of Chemistry and Chemical Biology, Indiana University-Purdue University Indianapolis, 402 N Blackford St, Indianapolis, IN 46202, United States.
Britt HedmanStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA 94025, United States.
Keith O HodgsonDepartment of Chemistry, Stanford University, Stanford, CA 94035, United States; Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA 94025, United States.
Partha BasuDepartment of Chemistry and Chemical Biology, Indiana University-Purdue University Indianapolis, 402 N Blackford St, Indianapolis, IN 46202, United States.
Edward I SolomonDepartment of Chemistry, Stanford University, Stanford, CA 94035, United States; Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA 94025, United States. Electronic address: solomone@stanford.edu.
Indiana University – Purdue University Indianapolis · USStanford Synchrotron Radiation Lightsource · USLawrence Berkeley National Laboratory · USSLAC National Accelerator Laboratory · US

Funding

A Synchrotron Radiation Structural Biology ResourcesP30GM133894 · NIGMS · STANFORD UNIVERSITY · PI Aina E. Cohen, KEITH O HODGSON · 2020 to 2026
$43.3M
Structure/Function Correlations Over Copper EnzymesR01DK031450 · NIDDK · STANFORD UNIVERSITY · PI EDWARD I SOLOMON · 1986 to 2026
$8.7M
SPECTROSCOPIC STUDIES OF COPPER CLUSTERS IN PROTEINSR37DK031450 · NIDDK · STANFORD UNIVERSITY · PI SOLOMON, EDWARD I · 1994 to 2011
$5.7M
MODELS OF NITRATE REDUCTASES AND RELATED ENZYMESR15GM061555 · NIGMS · DUQUESNE UNIVERSITY · PI BASU, PARTHA · 2000 to 2015
$1.4M
NIDDK NIH HHS R01 DK031450NIDDK NIH HHS R37 DK031450NIGMS NIH HHS P30 GM133894NIGMS NIH HHS R15 GM061555
6 · The paper itself

Abstract

Reduced dithiolene ligands are bound to high valent Mo centers in the active site of the oxotransferase family of enzymes. Related model complexes have been studied with great insight by Prof. Holm and his colleagues. This study focuses on the other limit of dithiolene chemistry: an investigation of the 2-electron oxidized dithiolene bound to low-valent late transition metal (TM) ions (Zn

Indexed as

ZincLigandsModels, MolecularOxidation-ReductionX-Ray Absorption SpectroscopyLigandsZincBackbondingDensity functional theory (DFT) calculationsElectronic structuresJahn-Teller distortionOxidized dithioleneS K-edge X-ray absorption spectroscopy (XAS)

Identifiers

PMID35202982
PMCPMC9680909
OpenAlexW4213029454

What OpenQuestion holds

Textmetadata
LicenceTDM
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.