Evidence map›Paper›PMID 35986879›Full record

ArticleBiomolecular NMR assignments2022

Chemical shift assignments of calmodulin bound to a C-terminal site (residues 1120-1147) in 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. 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, top 91% 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, 0 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

2 authors at 1 institution 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.
University of California, Davis · US

Funding

MEMBRANE TARGETING CALCIUM SENSORS IN VISIONR01EY012347 · NEI · UNIVERSITY OF MD BIOTECHNOLOGY INSTITUTE · PI AMES, JAMES B · 1999 to 2023
$6.9M
NEI NIH HHS R01 EY012347NIH HHS R01 EY012347
6 · The paper itself

Abstract

Retinal cyclic nucleotide-gated (CNG) channels consist of two protein subunits (CNGA1 and CNGB1). Calmodulin (CaM) binds to two separate sites within the cytosolic region of CNGB1: CaM binding to an N-terminal site (human CNGB1 residues 565-587, called CaM1) decreases the open probability of CNG channels at elevated Ca

Indexed as

CalmodulinCyclic Nucleotide-Gated Cation ChannelsCalciumHumansNuclear Magnetic Resonance, BiomolecularNucleotides, CyclicProtein SubunitsRetinal Rod Photoreceptor CellsCalciumCalmodulinCNGB1 protein, humanCyclic Nucleotide-Gated Cation ChannelsNucleotides, CyclicProtein SubunitsCalciumCaMCNGB1NMRPhotoreceptorRetina

Identifiers

PMID35986879
PMCPMC9510104
OpenAlexW4294090760

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.