Evidence map›Paper›PMID 31973069›Full record

ArticleBiomolecules2020

Membrane Binding of Neuronal Calcium Sensor-1: Highly Specific Interaction with Phosphatidylinositol-3-Phosphate.

Viktoriia E Baksheeva, Ekaterina L Nemashkalova, Alexander M Firsov, Arthur O Zalevsky, Vasily I Vladimirov, Natalia K Tikhomirova, Pavel P Philippov, Andrey A Zamyatnin, Dmitry V Zinchenko, Yuri N Antonenko and 2 more

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2020. 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
0.5field-weighted citation impact, top 38% 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, 8 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

12 authors at 4 institutions in 1 country.

Viktoriia E BaksheevaBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119992 Moscow, Russia.
Ekaterina L NemashkalovaInstitute for Biological Instrumentation of the Russian Academy of Sciences, Pushchino, 142290 Moscow Region, Russia.
Alexander M FirsovBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119992 Moscow, Russia.
Arthur O ZalevskyFaculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, 119992 Moscow, Russia.
Vasily I VladimirovBranch of Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences in Pushchino, Pushchino, 142290 Moscow Region, Russia.
Natalia K TikhomirovaBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119992 Moscow, Russia.
Pavel P PhilippovBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119992 Moscow, Russia.
Andrey A ZamyatninBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119992 Moscow, Russia.
Dmitry V ZinchenkoBranch of Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences in Pushchino, Pushchino, 142290 Moscow Region, Russia.
Yuri N AntonenkoBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119992 Moscow, Russia.
Sergey E PermyakovInstitute for Biological Instrumentation of the Russian Academy of Sciences, Pushchino, 142290 Moscow Region, Russia.
Evgeni Yu ZerniiBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119992 Moscow, Russia.
Lomonosov Moscow State University · RUSechenov University · RUInstitute for Biological Instrumentation · RUInstitute of Bioorganic Chemistry · RU

Funding

Российский Фонд Фундаментальных Исследований (РФФИ) 18-04-01250
6 · The paper itself

Abstract

Neuronal calcium sensors are a family of N-terminally myristoylated membrane-binding proteins possessing a different intracellular localization and thereby targeting unique signaling partner(s). Apart from the myristoyl group, the membrane attachment of these proteins may be modulated by their N-terminal positively charged residues responsible for specific recognition of the membrane components. Here, we examined the interaction of neuronal calcium sensor-1 (NCS-1) with natural membranes of different lipid composition as well as individual phospholipids in form of multilamellar liposomes or immobilized monolayers and characterized the role of myristoyl group and N-terminal lysine residues in membrane binding and phospholipid preference of the protein. NCS-1 binds to photoreceptor and hippocampal membranes in a Ca

Indexed as

Binding SitesCalciumHippocampusHumansHydrogen BondingLigandsLightLiposomesLysineMagnesiumMolecular Docking SimulationMutationMyristic AcidNeuronal Calcium-Sensor ProteinsNeuronsNeuropeptidesCalciumfrequenin calcium sensor proteinsLigandsLiposomesLysineMagnesiumMyristic AcidNeuronal Calcium-Sensor ProteinsNeuropeptidesphosphatidylinositol 3-phosphatePhosphatidylinositol Phosphatesmembrane bindingmyristoyl groupNCS-1neuronal calcium sensor-1neuronal calcium sensorsN-terminal myristoylationphosphatidylinositol-3-phosphatephosphoinositidesphospholipid-binding proteinsPI3P

Identifiers

PMID31973069
PMCPMC7072451
OpenAlexW3001735411

What OpenQuestion holds

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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.