Evidence map›Paper›PMID 35107779›Full record

ArticleBiomolecular NMR assignments2022

Chemical shift assignments of calmodulin bound to the β-subunit of a retinal cyclic nucleotide-gated channel (CNGB1).

Aritra Bej, James B Ames

Open access · hybridAbstract read
In one paragraph

Article in Biomolecular NMR assignments, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.4field-weighted citation impact, top 43% 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

5 citing papers in PubMed, 5 citations in OpenAlex.

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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

2 authors at 2 institutions in 1 country.

Aritra BejDepartment of Chemistry, University of California, Davis, CA, 95616, USA.
James B AmesDepartment of Chemistry, University of California, Davis, CA, 95616, USA. jbames@ucdavis.edu.ORCID 0000-0003-0934-2595
University of California, Davis · USUniversity of California System · US

Funding

MEMBRANE TARGETING CALCIUM SENSORS IN VISIONR01EY012347 · NEI · UNIVERSITY OF MD BIOTECHNOLOGY INSTITUTE · PI AMES, JAMES B · 1999 to 2023
$6.9M
ACQUISITION OF 500 MHZ NMR SPECTROMETERS10RR011973 · NCRR · UNIVERSITY OF CALIFORNIA DAVIS · PI LA MAR, GERD N · 1997 to 1997
–
NCRR NIH HHS S10 RR011973NEI NIH HHS R01 EY012347
6 · The paper itself

Abstract

Rod cyclic nucleotide-gated (CNG) channels are formed by two protein subunits (CNGA1 and CNGB1). Calmodulin (CaM) binds to the cytosolic regulatory domain of CNGB1 and decreases the open probability of CNGA1/CNGB1 channels. The CaM binding site within bovine CNGB1 (residues 679-702) binds tightly to Ca

Indexed as

CalmodulinCyclic Nucleotide-Gated Cation ChannelsAnimalsCalciumCattleNuclear Magnetic Resonance, BiomolecularNucleotides, CyclicRetinal Rod Photoreceptor CellsCalciumCalmodulinCyclic Nucleotide-Gated Cation ChannelsNucleotides, CyclicCalciumCaMCNGB1NMRPhotoreceptorRetina

Identifiers

PMID35107779
PMCPMC9068646
OpenAlexW4210498643

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.