Evidence map›Paper›PMID 34674177›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2022

Using Tandem Affinity Purification to Identify Circadian Clock Protein Complexes from Arabidopsis.

Maria L Sorkin, Dmitri A Nusinow

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Dim green light enables day-and-night monitoring of leaf movements.The Plant journal : for cell and molecular biology · 2026
    Article
  2. Article
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.

Maria L SorkinDonald Danforth Plant Science Center, St. Louis, MO, USA.
Dmitri A NusinowDonald Danforth Plant Science Center, St. Louis, MO, USA. meter@danforthcenter.org.
Donald Danforth Plant Science Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Identification of protein-protein interactions is an effective method of elucidating new roles for circadian clock-associated proteins that can expand beyond the information collected from transcriptional studies and genetic screens. Tandem affinity purification coupled with liquid chromatography mass spectrometry (APMS) utilizes epitope-tagged versions of your protein of interest to co-precipitate direct and indirect protein partners. Here, we provide a protocol and suggestions for proper design of 6x-His-3x-FLAG-tagged clock proteins and isolation of protein-protein interactions using two immunoprecipitation steps for increased specificity.

Indexed as

ArabidopsisCircadian ClocksArabidopsis ProteinsChromatography, LiquidMass SpectrometryTandem Affinity PurificationArabidopsis ProteinsAffinity purificationCircadian clockMass spectrometryProtein-protein interactions

Identifiers

PMID34674177
OpenAlexW3205476975

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.