Evidence map›Paper›PMID 37191794›Full record

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

In Situ Proximity Ligation Assay to Visualize Protein-Protein Interactions in Tumor Specimens.

Yasuhiro Miki, Erina Iwabuchi, Takashi Suzuki

Abstract read
PubMed Publisher
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. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. Review
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 at 2 institutions in 1 country.

Yasuhiro MikiDepartment of Nursing, Faculty of Medical Science and Welfare, Tohoku Bunka Gakuen University, Sendai, Japan. ymiki@ns.tbgu.ac.jp.
Erina IwabuchiDepartment of Pathology and Histotechnology, Tohoku University Graduate School of Medicine, Sendai, Japan.
Takashi SuzukiDepartment of Pathology and Histotechnology, Tohoku University Graduate School of Medicine, Sendai, Japan.
Tohoku University · JPTohoku Bunka Gakuen University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein-protein interactions (PPI) are the basis of various biological phenomena, such as intracellular signal transduction, gene transcription, and metabolism. PPI are also considered to be involved in the pathogenesis and development of various diseases, including cancer. PPI phenomenon and their functions have been elucidated by gene transfection and molecular detection technologies. On the other hand, in histopathological analysis, although immunohistochemical analyses provide information pertaining to protein expression and their localization in pathophysiological tissues, it has been difficult to visualize the PPI of these proteins. An in situ proximity ligation assay (PLA) was developed as a microscopic visualization technique for PPI in formalin-fixed, paraffin-embedded (FFPE) tissues as well as in cultured cells and frozen tissues. PLA using histopathological specimens enables cohort studies of PPI, which can clarify the significance of PPI in pathology. We have previously shown the dimerization pattern of estrogen receptors and significance of HER2-binding proteins using breast cancer FFPE tissues. In this chapter, we describe a methodology for the visualization of PPI using PLA in pathological specimens.

Indexed as

Breast NeoplasmsProtein Interaction MappingProtein Interaction MapsAntibodiesCell NucleusCohort StudiesErb-b2 Receptor Tyrosine KinasesFemaleFluorescent DyesFormaldehydeHumansParaffin EmbeddingReceptors, EstrogenSignal TransductionTissue FixationAntibodiesERBB2 protein, humanErb-b2 Receptor Tyrosine KinasesFluorescent DyesFormaldehydeReceptors, EstrogenAntibodyCultured cellsFormalin-fixed, paraffin-embedded tissuesFrozen tissuesHistologyImmunohistochemistryIn situ proximity ligation assayPathologyProtein–protein interaction

Identifiers

PMID37191794
OpenAlexW4376643302

What OpenQuestion holds

Textmetadata
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.