Evidence map›Paper›PMID 40875121›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2025

Measurement of Substrate SUMOylation in Real Time by Fluorescence Spectroscopy.

Anindita Puri, Vasvi Tripathi, Ranabir Das

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Article in Methods in molecular biology (Clifton, N.J.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

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5 · Who and what money

Authors and funding

3 authors.

Anindita PuriNational Center for Biological Sciences, Tata Institute of Fundamental Research, Bangalore, India.
Vasvi TripathiNational Center for Biological Sciences, Tata Institute of Fundamental Research, Bangalore, India.
Ranabir DasNational Center for Biological Sciences, Tata Institute of Fundamental Research, Bangalore, India. rana@ncbs.res.in.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post-translational modifications, such as SUMOylation, play a crucial role in regulating various cellular processes. Traditionally, in vitro SUMOylation assays are carried out using techniques like SDS-PAGE gels and Western blotting, which are often time consuming. These informative methods, which quantitate the increase in substrate's molecular weight, can introduce potential errors and thus a need arises for a more efficient and accurate alternative. We propose a real-time detection method for SUMOylation that utilizes a fluorescence-tagged substrate, which has been recently developed by our group (Tripathi and Das, CP Protein Sci 101:e111, 2020). We believe this method has the potential to significantly enhance the efficiency and accuracy of SUMOylation assessment, thereby advancing our understanding of SUMO signaling and its function.

Indexed as

Small Ubiquitin-Related Modifier ProteinsSumoylationHumansProtein Processing, Post-TranslationalSpectrometry, FluorescenceSmall Ubiquitin-Related Modifier ProteinsAnisotropyFluorescenceReal-time measurementSpectroscopySUMOylation

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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.