Solution-state nuclear magnetic resonance studies of the

Rebecca N D'Amico, Somnath Mondal, Dennis S Winston, David D Boehr

Abstract read

In one paragraph

Article in Biochemistry and biophysics reports, 2026. 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

4 authors.

Rebecca N D'AmicoDepartment of Chemistry, The Pennsylvania State University, University Park, PA, 16802, USA.

Somnath MondalDepartment of Chemistry, The Pennsylvania State University, University Park, PA, 16802, USA.

Dennis S WinstonDepartment of Chemistry, The Pennsylvania State University, University Park, PA, 16802, USA.

David D BoehrDepartment of Chemistry, The Pennsylvania State University, University Park, PA, 16802, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tryptophan synthase (TS) is an allosteric bi-enzyme complex that catalyzes the final steps of l-tryptophan biosynthesis through tightly coupled α- and β-subunit reactions. Understanding how conformational dynamics mediate its catalytic efficiency and inter-subunit communication remains a key interest. Here, we establish that

Indexed as

AllosteryEnzyme-enzyme communicationMethyl NMR spectroscopyProtein conformational dynamicsTryptophan synthase

Identifiers

PMID42004543

DOI10.1016/j.bbrep.2026.102586

PMCPMC13091236

What OpenQuestion holds

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Registered trials

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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.