Evidence map›Paper›PMID 31618845›Full record

ArticleInternational journal of molecular sciences2019

Light-Regulation of Tryptophan Synthase by Combining Protein Design and Enzymology.

Andrea C Kneuttinger, Stefanie Zwisele, Kristina Straub, Astrid Bruckmann, Florian Busch, Thomas Kinateder, Barbara Gaim, Vicki H Wysocki, Rainer Merkl, Reinhard Sterner

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.5field-weighted citation impact, top 39% 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

7 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Towards Photochromic Azobenzene-Based Inhibitors for Tryptophan Synthase.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021
    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

10 authors at 2 institutions in 2 countries.

Andrea C KneuttingerInstitute of Biophysics and Physical Biochemistry, University of Regensburg, Universitätsstraße 31, 93053 Regensburg, Germany. Andrea.Kneuttinger@ur.de.ORCID 0000-0002-4341-1593
Stefanie ZwiseleInstitute of Biophysics and Physical Biochemistry, University of Regensburg, Universitätsstraße 31, 93053 Regensburg, Germany. Stefanie.Zwisele@ur.de.
Kristina StraubInstitute of Biophysics and Physical Biochemistry, University of Regensburg, Universitätsstraße 31, 93053 Regensburg, Germany. Kristina.Straub@ur.de.ORCID 0000-0003-4121-7516
Astrid BruckmannInstitute of Biochemistry, Genetics and Microbiology, University of Regensburg, Universitätsstraße 31, 93053 Regensburg, Germany. Astrid.Bruckmann@ur.de.
Florian BuschDepartment of Chemistry and Biochemistry and Resource for Native Mass Spectrometry Guided Structural Biology, The Ohio State University, Columbus, OH 43210, USA. busch.151@osu.edu.
Thomas KinatederInstitute of Biophysics and Physical Biochemistry, University of Regensburg, Universitätsstraße 31, 93053 Regensburg, Germany. Thomas.Kinateder@ur.de.
Barbara GaimInstitute of Biophysics and Physical Biochemistry, University of Regensburg, Universitätsstraße 31, 93053 Regensburg, Germany. Barbara.Gaim@ur.de.
Vicki H WysockiDepartment of Chemistry and Biochemistry and Resource for Native Mass Spectrometry Guided Structural Biology, The Ohio State University, Columbus, OH 43210, USA. wysocki.11@osu.edu.ORCID 0000-0003-0495-2538
Rainer MerklInstitute of Biophysics and Physical Biochemistry, University of Regensburg, Universitätsstraße 31, 93053 Regensburg, Germany. Rainer.Merkl@ur.de.ORCID 0000-0002-3521-2957
Reinhard SternerInstitute of Biophysics and Physical Biochemistry, University of Regensburg, Universitätsstraße 31, 93053 Regensburg, Germany. Reinhard.Sterner@ur.de.
University of Regensburg · DEThe Ohio State University · US

Funding

Waters Select Series Cyclic IMS for P41 Native MS Resource Application to Alzheimer's DiseaseP41GM128577 · NIGMS · OHIO STATE UNIVERSITY · PI SOMOGYI, ARPAD · 2018 to 2022
$7.6M
Deutsche Forschungsgemeinschaft STE 891/12-1NIGMS NIH HHS P41 GM128577NIH HHS P41 GM128577
6 · The paper itself

Abstract

The spatiotemporal control of enzymes by light is of growing importance for industrial biocatalysis. Within this context, the photo-control of allosteric interactions in enzyme complexes, common to practically all metabolic pathways, is particularly relevant. A prominent example of a metabolic complex with a high application potential is tryptophan synthase from

Indexed as

LightProtein EngineeringAllosteric RegulationAmino Acid SequenceBiocatalysisEnzyme ActivationKineticsModels, MolecularMolecular ConformationProtein BindingStructure-Activity RelationshipTryptophan SynthaseTryptophan Synthaseallosterybiocatalysisenzymologyphoto-controlprotein designunnatural amino acids

Identifiers

PMID31618845
PMCPMC6829457
OpenAlexW2981188561

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.