Evidence map›Paper›PMID 37607621›Full record

ArticleMethods (San Diego, Calif.)2023

Probing excited state

Ajith Kumar, Kulkarni Madhurima, Athi N Naganathan, Pramodh Vallurupalli, Ashok Sekhar

Open access · greenAbstract read
In one paragraph

Article in Methods (San Diego, Calif.), 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
0.3field-weighted citation impact, top 47% 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, 2 citations in OpenAlex.

  1. Mapping the FF domain folding pathway via structures of transiently populated folding intermediates.Proceedings of the National Academy of Sciences of the United States of America · 2024
    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

5 authors at 3 institutions in 1 country.

Ajith KumarMolecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, Karnataka, India.
Kulkarni MadhurimaMolecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, Karnataka, India.
Athi N NaganathanDepartment of Biotechnology, Bhupat & Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras, Chennai 600036, India.
Pramodh VallurupalliTata Institute of Fundamental Research Hyderabad, 36/P, Gopanpally Village, Serilingampally Mandal, Ranga Reddy District, Hyderabad 500046, India.
Ashok SekharMolecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, Karnataka, India. Electronic address: ashoksekhar@iisc.ac.in.
Indian Institute of Science Bangalore · INIndian Institute of Technology Madras · INTata Institute of Fundamental Research · IN

Funding

DBT-Wellcome Trust India Alliance IA/E/20/1/505675DBT-Wellcome Trust India Alliance IA/I/18/1/503614Wellcome Trust
6 · The paper itself

Abstract

Over 40% of eukaryotic proteomes and 15% of bacterial proteomes are predicted to be intrinsically disordered based on their amino acid sequence. Intrinsically disordered proteins (IDPs) exist as heterogeneous ensembles of interconverting conformations and pose a challenge to the structure-function paradigm by apparently functioning without possessing stable structural elements. IDPs play a prominent role in biological processes involving extensive intermolecular interaction networks and their inherently dynamic nature facilitates their promiscuous interaction with multiple structurally diverse partner molecules. NMR spectroscopy has made pivotal contributions to our understanding of IDPs because of its unique ability to characterize heterogeneity at atomic resolution. NMR methods such as Chemical Exchange Saturation Transfer (CEST) and relaxation dispersion have enabled the detection of 'invisible' excited states in biomolecules which are transiently and sparsely populated, yet central for function. Here, we develop a

Indexed as

Intrinsically Disordered ProteinsAmino Acid SequenceCytidineEukaryotaProteomeCytidineIntrinsically Disordered ProteinsProteomeAlpha protonChemical exchange saturation transferConformational changeIntrinsically disordered proteinsNuclear magnetic resonance spectroscopyProtein dynamics

Identifiers

PMID37607621
PMCPMC7615522
OpenAlexW4386013268

What OpenQuestion holds

Textmetadata
LicenceTDM
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.