Evidence map›Paper›PMID 38607253›Full record

ArticleThe journal of physical chemistry letters2024

In Solution Identification of the Lysine-Cysteine Redox Switch with a NOS Bridge in Transaldolase by Sulfur K-Edge X-ray Absorption Spectroscopy.

Ashish Tamhankar, Marie Wensien, Sergio A V Jannuzzi, Sayanti Chatterjee, Benedikt Lassalle-Kaiser, Kai Tittmann, Serena DeBeer

Abstract read
In one paragraph

Article in The journal of physical chemistry letters, 2024. 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

7 authors.

Ashish TamhankarMax Planck Institute for Chemical Energy Conversion, Stiftstraße 34-36, 45470 Mülheim an der Ruhr, Germany.ORCID 0009-0000-4010-2501
Marie WensienDepartment of Molecular Enzymology, Göttingen Center of Molecular Biosciences, Georg-August University Göttingen, Julia-Lermonotowa-Weg 3, 37077 Göttingen, Germany.
Sergio A V JannuzziMax Planck Institute for Chemical Energy Conversion, Stiftstraße 34-36, 45470 Mülheim an der Ruhr, Germany.ORCID 0000-0001-7406-6633
Sayanti ChatterjeeMax Planck Institute for Chemical Energy Conversion, Stiftstraße 34-36, 45470 Mülheim an der Ruhr, Germany.ORCID 0000-0002-8030-0753
Benedikt Lassalle-KaiserSynchrotron SOLEIL, L'Orme des Merisiers, Départementale 128, 91190 Saint-Aubin, France.ORCID 0000-0003-2141-2496
Kai TittmannDepartment of Molecular Enzymology, Göttingen Center of Molecular Biosciences, Georg-August University Göttingen, Julia-Lermonotowa-Weg 3, 37077 Göttingen, Germany.ORCID 0000-0001-7891-7108
Serena DeBeerMax Planck Institute for Chemical Energy Conversion, Stiftstraße 34-36, 45470 Mülheim an der Ruhr, Germany.ORCID 0000-0002-5196-3400

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A novel covalent post-translational modification (lysine-NOS-cysteine) was discovered in proteins, initially in the enzyme transaldolase of

Indexed as

Oxidation-ReductionTransaldolaseX-Ray Absorption SpectroscopyCysteineLysineNeisseria gonorrhoeaeProtein Processing, Post-TranslationalSolutionsSulfurCysteineLysineSolutionsSulfurTransaldolase

Identifiers

PMID38607253
PMCPMC11056971

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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.