Evidence map›Paper›PMID 37540434›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2023

Using a Modified Proximity Ligation Protocol to Study the Interaction Between Chaperones and Associated Proteins.

Simone Baldan, Anatoli B Meriin, Michael Y Sherman

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2023. 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
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.

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

3 authors.

Simone BaldanMRC Toxicology Unit, University of Cambridge, Cambridge, UK.
Anatoli B MeriinDepartment of Biochemistry, Boston University, Boston, MA, USA. meriin@bu.edu.
Michael Y ShermanDepartment of Molecular Biology, Ariel University, Ariel, Israel.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Molecular chaperones can interact with multiple proteins to form large networks. Understanding these interactions may shed light on the complexity of the chaperone functions. Here we developed a protocol for a modified proximity ligation-based methodology (PLA) for the detection of protein-protein interactions in order to understand how the Hsp70-Bag3 complex interacts with components of the Hippo signaling pathway. These experiments helped to elucidate the mechanisms of transmission of the proteotoxic stress signal to the Hippo pathway. The modified PLA technology has many advantages compared to co-immunoprecipitation protocols. It has higher sensitivity, is quantitative, and can be done in a 96-well format.

Indexed as

HSP70 Heat-Shock ProteinsMolecular ChaperonesHippo Signaling PathwayPolyestersHSP70 Heat-Shock ProteinsMolecular ChaperonesPolyestersBag3Hippo pathwayHsp70LATS1/2Protein complexProximity ligation assayYap

Identifiers

What OpenQuestion holds

Textmetadata
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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.